Hey KrZ...I just did a translated blast search (protein-->nucleotide)...lots o' hits, your second sequence tended to have higher homology with INMTs...some are just general aromatic amino acid decarboxylases, some hits were also for the similar Tyr/Dopa decarboxylases, which are specific to these two substrates (eg. from Papaver somniferum)...you should also consider up-regulating production of S-adenosylmethionine if you are going to express the INMT at high levels, otherwise it might become a limiting factor in the reaction...anyways, here's the top hits(1st 5 from your first sequence, 2nd 5 from your second AA sequence)...now just look for conserved sequences between the enzymes that you are most interested in and see if there are any losses of this conservation in the Tyr/Dopa decarboxylases...hope this helps:
1: P17770 AROMATIC-L-AMINO-ACID DECARBOXYLASE (DOPA DECARBOXYLASE) (TRYPTOPHAN DECARBOXYLASE) BLink, PubMed, Related Sequences, Taxonomy, LinkOut
LOCUS DCD_CATRO 500 aa PLN 01-NOV-1995
DEFINITION AROMATIC-L-AMINO-ACID DECARBOXYLASE (DOPA DECARBOXYLASE)
(TRYPTOPHAN DECARBOXYLASE).
ACCESSION P17770
PID g118306
VERSION P17770 GI:118306
DBSOURCE swissprot: locus DCD_CATRO, accession P17770;
class: standard.
created: Aug 1, 1990.
sequence updated: Aug 1, 1990.
annotation updated: Nov 1, 1995.
xrefs: gi: gi: 167489, gi: gi: 167490, gi: gi: 18225, gi: gi:
18226, gi: gi: 1247291, gi: gi: 1247292, gi: gi: 68027, gi: gi:
100170, gi: gi: 542023
xrefs (non-sequence databases): PFAM PF00282, PROSITE PS00392
KEYWORDS Lyase; Decarboxylase; Pyridoxal phosphate.
SOURCE Madagascar periwinkle.
ORGANISM Catharanthus roseus
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons; core
eudicots; Asteridae; euasterids I; Gentianales; Apocynaceae;
Catharanthus.
REFERENCE 1 (residues 1 to 500)
AUTHORS De Luca,V., Marineau,C. and Brisson,N.
TITLE Molecular cloning and analysis of cDNA encoding a plant tryptophan
decarboxylase: comparison with animal dopa decarboxylases
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 86 (
, 2582-2586 (1989)
MEDLINE 89202373
REMARK SEQUENCE FROM N.A.
REFERENCE 2 (residues 1 to 500)
AUTHORS Goddijn,O.J., Lohman,F.P., de Kam,R.J., Schilperoort,R.A. and
Hoge,J.H.
TITLE Nucleotide sequence of the tryptophan decarboxylase gene of
Catharanthus roseus and expression of tdc-gusA gene fusions in
Nicotiana tabacum
JOURNAL Mol. Gen. Genet. 242 (2), 217-225 (1994)
MEDLINE 94211212
REMARK SEQUENCE FROM N.A.
STRAIN=CV. MORNING MIST; TISSUE=LEAF
COMMENT -------------------------------------------------------------------
This SWISS-PROT entry is copyright. It is produced through a
collaboration between the Swiss Institute of Bioinformatics and
the EMBL outstation - the European Bioinformatics Institute.
The original entry is available from
http://www.expasy.ch/sprot
and
http://www.ebi.ac.uk/sprot
------------------------------------------------------------------.
[CATALYTIC ACTIVITY] L-TRYPTOPHAN = TRYPTAMINE + CO(2) (ALSO ACTS
ON 5-HYDROXY-L-TRYPTOPHAN AND DIHYDROXY-L-PHENYLALANINE (DOPA)).
[COFACTOR] PYRIDOXAL PHOSPHATE.
[SUBUNIT] HOMODIMER.
[SIMILARITY] BELONGS TO GROUP II DECARBOXYLASES (DDC, GAD, HDC AND
TYRDC).
FEATURES Location/Qualifiers
source 1..500
/organism="Catharanthus roseus"
/db_xref="taxon:4058"
1..500
Protein 1..500
/product="AROMATIC-L-AMINO-ACID DECARBOXYLASE"
/EC_number="4.1.1.28"
Site 319
/site_type="binding"
/note="PYRIDOXAL PHOSPHATE (BY SIMILARITY)."
ORIGIN
1 mgsidstnva msnspvgefk pleaeefrkq ahrmvdfiad yyknvetypv lsevepgylr
61 kripetapyl peplddimkd iqkdiipgmt nwmspnfyaf fpatvssaaf lgemlstaln
121 svgftwvssp aatelemivm dwlaqilklp ksfmfsgtgg gviqnttses ilctiiaare
181 raleklgpds igklvcygsd qthtmfpktc klagiypnni rlipttvetd fgispqvlrk
241 mveddvaagy vplflcatlg ttsttatdpv dslseianef giwihvdaay agsacicpef
301 rhyldgierv dslslsphkw llayldctcl wvkqphlllr alttnpeylk nkqsdldkvv
361 dfknwqiatg rkfrslklwl ilrsygvvnl qshirsdvam gkmfeewvrs dsrfeivvpr
421 nfslvcfrlk pdvsslhvee vnkklldmln stgrvymtht ivggiymlrl avgsslteeh
481 hvrrvwdliq kltddllkea
//
1: AAB39709 tryptophan decarboxylase [Camptotheca acuminata] BLink, Related Sequences, Nucleotide, Taxonomy
LOCUS AAB39709 498 aa PLN 02-JAN-1997
DEFINITION tryptophan decarboxylase [Camptotheca acuminata].
ACCESSION AAB39709
PID g1763279
VERSION AAB39709.1 GI:1763279
DBSOURCE locus CAU73657 accession U73657.1
KEYWORDS .
SOURCE Camptotheca acuminata.
ORGANISM Camptotheca acuminata
Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
Magnoliophyta; eudicotyledons; core eudicots; Asteridae; Cornales;
Cornaceae; Nyssoideae; Camptotheca.
REFERENCE 1 (residues 1 to 498)
AUTHORS Lopez-Meyer,M. and Nessler,C.L.
TITLE Tryptophan decarboxylase is encoded by two autonomously regulated
genes in Camptotheca acuminata which are differentially expressed
during development and stress
JOURNAL Unpublished
REFERENCE 2 (residues 1 to 498)
AUTHORS Lopez-Meyer,M. and Nessler,C.L.
TITLE Direct Submission
JOURNAL Submitted (08-OCT-1996) Biology, Texas A&M University, College
Station, TX 77843-3258, USA
FEATURES Location/Qualifiers
source 1..498
/organism="Camptotheca acuminata"
/db_xref="taxon:16922"
/tissue_type="leaf"
Protein 1..498
/function="converts tryptohan to tryptamine"
/product="tryptophan decarboxylase"
/EC_number="4.1.1.28"
CDS 1..498
/gene="tdc2"
/coded_by="U73657.1:1576..3072"
/note="TDC"
ORIGIN
1 mgsidsnydt esagqcrple peefrkqahq mvdfiadyyk niesypvlsq vepgylqsrl
61 petapyrpep fesilkdvhk diipgvthwl spnffayfpa tvssaafvge mlctcfnavg
121 fnwlaspael elemvvmdwl asmlklpnsf tflgtgggvi qgttseailc tliaardral
181 esigvdsihk lvvygsdqth styakacnla gilpcnirsi rteavanfsl spdslhreie
241 advaagmvpl ylcatvgtts ttaidslspl advandyglw fhvdaayags acicpefrhy
301 ldgieradsl slsphkwlls yldccclwvk rpsvlvkals tdpeylknkp sesnsvvdfk
361 dwqvgtgrrf kalrlwfvmr sygvanlqsh irsdiqmakm feefvnsdpr feivvprvfs
421 lvcfrlnpfs ksdpcntell nrkllewvns tgqvyithtk vggvymlrfa vgatlteehh
481 vsaawklire gadallcs
//
1: AAB39708 tryptophan decarboxylase [Camptotheca acuminata] BLink, Related Sequences, Nucleotide, Taxonomy
LOCUS AAB39708 502 aa PLN 02-JAN-1997
DEFINITION tryptophan decarboxylase [Camptotheca acuminata].
ACCESSION AAB39708
PID g1763277
VERSION AAB39708.1 GI:1763277
DBSOURCE locus CAU73656 accession U73656.1
KEYWORDS .
SOURCE Camptotheca acuminata.
ORGANISM Camptotheca acuminata
Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
Magnoliophyta; eudicotyledons; core eudicots; Asteridae; Cornales;
Cornaceae; Nyssoideae; Camptotheca.
REFERENCE 1 (residues 1 to 502)
AUTHORS Lopez-Meyer,M. and Nessler,C.L.
TITLE Tryptophan decarboxylase is encoded by two autonomously regulated
genes in Camptotheca acuminata which are differentially expressed
during development and stress
JOURNAL Unpublished
REFERENCE 2 (residues 1 to 502)
AUTHORS Lopez-Meyer,M. and Nessler,C.L.
TITLE Direct Submission
JOURNAL Submitted (08-OCT-1996) Biology, Texas A&M University, College
Station, TX 77843-3258, USA
FEATURES Location/Qualifiers
source 1..502
/organism="Camptotheca acuminata"
/db_xref="taxon:16922"
/dev_stage="7-day-old seedlings"
Protein 1..502
/function="converts tryptophan into tryptamine"
/product="tryptophan decarboxylase"
/EC_number="4.1.1.28"
CDS 1..502
/gene="tdc1"
/coded_by="U73656.1:189..1697"
/note="TDC"
ORIGIN
1 mgsldsnydt espasvgqfn pldpeefrkq ahcivdfiad yykniesypv lsqvdpgyrh
61 srlgknapyr sepfesilkd vqkdiipgmt hwmspnffah fpatvssaaf vgemlctcfn
121 svgfnwlasp aatelemvvi dwlanmlklp ksfmfsgtgg gvlqgttsea ilctliaasp
181 mhfeivgvkt stsfvvygsd qthstyakac klagilpcni rsipttadsn fsvsplllrr
241 aieadkaagm vplyicatvg ttsttaidpl ssladvandy gvwfhvdaay agsacicpef
301 rhyldgiera dslslsphkw llsyldcccl wvkspsllvk alstdpeylk nqpsesksvv
361 dykdwqvgtg rrfkalrlwf vmrsygvanl qshirtdvqm akmfegfvks dprfeilvpr
421 vfslvcfrln pisgsdptgt ealnrklldw vnstgrvymt htkvggiyml rfavgatlte
481 krhvssawkl ikegadvllk ed
//
1: AAG60665 tyrosine/dopa decarboxylase [Thalictrum flavum subsp. glaucum] BLink, Related Sequences, Nucleotide, Taxonomy
LOCUS AF314150_1 518 aa PLN 31-JAN-2001
DEFINITION tyrosine/dopa decarboxylase [Thalictrum flavum subsp. glaucum].
ACCESSION AAG60665
PID g12620328
VERSION AAG60665.1 GI:12620328
DBSOURCE locus AF314150 accession AF314150.1
KEYWORDS .
SOURCE Thalictrum flavum subsp. glaucum.
ORGANISM Thalictrum flavum subsp. glaucum
Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
Magnoliophyta; eudicotyledons; Ranunculales; Ranunculaceae;
Thalictrum.
REFERENCE 1 (residues 1 to 518)
AUTHORS Samanani,N. and Facchini,P.J.
TITLE Cloning and characterization of a tyrosine/dopa decarboxylase cDNA
from the meadow rue, Thalictrum flavum ssp. glaucum
JOURNAL Unpublished
REFERENCE 2 (residues 1 to 518)
AUTHORS Samanani,N. and Facchini,P.J.
TITLE Direct Submission
JOURNAL Submitted (16-OCT-2000) Department of Biological Sciences,
University of Calgary, 2500 University Drive N.W., Calgary, Alberta
T2N 1N4, Canada
COMMENT Method: conceptual translation supplied by author.
FEATURES Location/Qualifiers
source 1..518
/organism="Thalictrum flavum subsp. glaucum"
/sub_species="glaucum"
/db_xref="taxon:150095"
/note="cell suspension culture"
Protein 1..518
/product="tyrosine/dopa decarboxylase"
/EC_number="4.1.1.25"
CDS 1..518
/gene="TYDC1"
/coded_by="AF314150.1:116..1672"
ORIGIN
1 mgslhvedld niskctvenp ldpeefrrqg hmmidflady yrdiekypvr sqvepgylrk
61 eipdsapynp esietiledv hkqiipgith wqspnyfayf pssgsvagfl gemlstgfnv
121 vgfnwmsspa atelesivmd wlgkmlklpk sflfsgnggg vlqgttceai lctltaardr
181 mlnkigreni cklvvygsdq thcalqkaaq iagihpnnfr avpttkandy glsasalrst
241 iledieaglv plflcatvgt tsstavdpig plckvasdys iwvhvdaaya gsacicpefr
301 hfidgvenad sfslnahkwf fttldccclw vkepsalika lstnpeylrn kateshqvvd
361 ykdwqialsr rframklwlv lrsygvanlr nflrshvkma knfegfiald krfeivvprt
421 famvcfrllp prspliiktn gyqngngvyh kdesraneln rrllesinas gsaymthsmv
481 ggvymirfav gaslteerhv ilawkvvqeh adavlatf
//
1: P54769 TYROSINE/DOPA DECARBOXYLASE 2 [INCLUDES: DOPA DECARBOXYLASE (DDC); TYROSINE DECARBOXYLASE ] BLink, PubMed, Related Sequences, Taxonomy, LinkOut
LOCUS TYD2_PAPSO 531 aa PLN 15-JUL-1999
DEFINITION TYROSINE/DOPA DECARBOXYLASE 2 [INCLUDES: DOPA DECARBOXYLASE (DDC);
TYROSINE DECARBOXYLASE ].
ACCESSION P54769
PID g1717826
VERSION P54769 GI:1717826
DBSOURCE swissprot: locus TYD2_PAPSO, accession P54769;
class: standard.
created: Oct 1, 1996.
sequence updated: Oct 1, 1996.
annotation updated: Jul 15, 1999.
xrefs: gi: gi: 607746, gi: gi: 607747
xrefs (non-sequence databases): PFAM PF00282, PROSITE PS00392
KEYWORDS Lyase; Decarboxylase; Pyridoxal phosphate; Multigene family.
SOURCE opium poppy.
ORGANISM Papaver somniferum
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons;
Ranunculales; Papaveraceae; Papaver.
REFERENCE 1 (residues 1 to 531)
AUTHORS Facchini,P.J. and De Luca,V.
TITLE Differential and tissue-specific expression of a gene family for
tyrosine/dopa decarboxylase in opium poppy
JOURNAL J. Biol. Chem. 269 (43), 26684-26690 (1994)
MEDLINE 95014524
REMARK SEQUENCE FROM N.A.
STRAIN=CV. MARIANNE
COMMENT -------------------------------------------------------------------
This SWISS-PROT entry is copyright. It is produced through a
collaboration between the Swiss Institute of Bioinformatics and
the EMBL outstation - the European Bioinformatics Institute.
The original entry is available from
http://www.expasy.ch/sprot
and
http://www.ebi.ac.uk/sprot
------------------------------------------------------------------.
[FUNCTION] MARGINALLY HIGHER SUBSTRATE SPECIFICITY FOR L-DOPA OVER
L-TYROSINE.
[CATALYTIC ACTIVITY] L-TYROSINE = TYRAMINE + CO(2).
[COFACTOR] PYRIDOXAL PHOSPHATE.
[SUBUNIT] HOMODIMER (BY SIMILARITY).
[TISSUE SPECIFICITY] PREDOMINANTLY EXPRESSED IN THE ROOTS AND
STEMS, WHILE A LOWER LEVEL EXPRESSION IS SEEN IN THE SEPALS AND
CARPELS OF FULLY EXPANDED FLOWERS.
[SIMILARITY] BELONGS TO GROUP II DECARBOXYLASES (DDC, GAD, HDC AND
TYRDC).
FEATURES Location/Qualifiers
source 1..531
/organism="Papaver somniferum"
/db_xref="taxon:3469"
1..531
Protein 1..531
/product="TYROSINE/DOPA DECARBOXYLASE 2 [INCLUDES: DOPA
DECARBOXYLASE"
/EC_number="4.1.1.28"
/EC_number="4.1.1.25"
Site 319
/site_type="binding"
/note="PYRIDOXAL PHOSPHATE (BY SIMILARITY)."
ORIGIN
1 mgslntedvl enssafgvtn pldpeefrrq ghmiidflad yyrdvekypv rsqvepgylr
61 krlpetapyn pesietilqd vtteiipglt hwqspnyyay fpssgsvagf lgemlstgfn
121 vvgfnwmssp aatelesvvm dwfgkmlnlp esflfsgsgg gvlqgtscea ilctltaard
181 rklnkigreh igrlvvygsd qthcalqkaa qvaginpknf raiktfkens fglsaatlre
241 viledieagl iplfvcptvg ttsstavdpi spicevakey emwvhvdaay agsacicpef
301 rhfidgveea dsfslnahkw ffttldcccl wvkdpsalvk alstnpeylr nkatesrqvv
361 dykdwqials rrfrslklwm vlrsygvtnl rnflrshvkm aktfeglicm dgrfeitvpr
421 tfamvcfrll ppktikvydn gvhqngngvv plrdenenlv lanklnqvyl etvnatgsvy
481 mthavvggvy mirfavgstl teerhviyaw kilqehadli lgkfseadfs s
//
1: AAC97491 indolethylamine N-methyltransferase [Oryctolagus cuniculus] BLink, PubMed, Related Sequences, Nucleotide, Taxonomy
LOCUS AAC97491 263 aa MAM 22-DEC-1998
DEFINITION indolethylamine N-methyltransferase [Oryctolagus cuniculus].
ACCESSION AAC97491
PID g4039109
VERSION AAC97491.1 GI:4039109
DBSOURCE locus AF077826 accession AF077826.1
KEYWORDS .
SOURCE rabbit.
ORGANISM Oryctolagus cuniculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus.
REFERENCE 1 (residues 1 to 263)
AUTHORS Thompson,M.A. and Weinshilboum,R.M.
TITLE Rabbit lung indolethylamine N-methyltransferase. cDNA and gene
cloning and characterization
JOURNAL J. Biol. Chem. 273 (51), 34502-34510 (1998)
MEDLINE 99069450
REFERENCE 2 (residues 1 to 263)
AUTHORS Thompson,M.A. and Weinshilboum,R.M.
TITLE Direct Submission
JOURNAL Submitted (13-JUL-1998) Pharmacology, Mayo Clinic/Mayo Foundation,
200 1st St. SW, Rochester, MN 55905, USA
COMMENT Method: conceptual translation supplied by author.
FEATURES Location/Qualifiers
source 1..263
/organism="Oryctolagus cuniculus"
/db_xref="taxon:9986"
/tissue_type="lung"
Protein 1..263
/function="catalyzes the N-methylation of tryptamine"
/product="indolethylamine N-methyltransferase"
CDS 1..263
/gene="INMT"
/coded_by="AF077826.1:16..807"
ORIGIN
1 meggftggde yqkhflprdy lntyysfqsg pspeaemlkf nleclhktfg pgglqgdtli
61 digsgptiyq vlaacesfkd itlsdftdrn reelakwlkk epgaydwtpa lkfacelegn
121 sgrwqekaek lratvkrvlk cdanlsnplt pvvlppadcv ltllamecac csldayraal
181 rnlasllkpg ghlvttvtlq lssymvgere fscvalekee veqavldagf dieqllyspq
241 sysastapnr gvcflvarkk pgs
//
1: XP_004862 indolethylamine N-methyltransferase [Homo sapiens] BLink, Related Sequences, Nucleotide, Taxonomy, LinkOut
LOCUS XP_004862 263 aa PRI 09-FEB-2001
DEFINITION indolethylamine N-methyltransferase [Homo sapiens].
ACCESSION XP_004862
PID g11420979
VERSION XP_004862.1 GI:11420979
DBSOURCE REFSEQ: accession XM_004862.1
KEYWORDS .
SOURCE human.
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 263)
AUTHORS NCBI Annotation Project.
TITLE Direct Submission
JOURNAL Submitted (04-FEB-2001) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
COMMENT GENOME ANNOTATION REFSEQ: This reference sequence was derived by
automated computational analysis of NCBI genomic sequence contig
NT_007825 using gene prediction method: Acembly.
Supporting evidence includes similarity to: 71 proteins, 1 mRNAs
See details in AceView
Method: conceptual translation supplied by author.
FEATURES Location/Qualifiers
source 1..263
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="7"
Protein 1..263
/product="indolethylamine N-methyltransferase"
Region 4..259
/region_name="NNMT/PNMT/TEMT family"
/db_xref="CDD:pfam01234"
/note="NNMT_PNMT_TEMT"
CDS 1..263
/gene="INMT"
/db_xref="LocusID:11185"
/db_xref="MIM:604854"
/coded_by="TR00067273:1..792"
ORIGIN
1 mkggftggde yqkhflprdy latyysfdgs pspeaemlkf nleclhktfg pgglqgdtli
61 digsgptiyq vlaacdsfqd itlsdftdrn reelekwlkk epgaydwtpa vkfacelegn
121 sgrweekeek lraavkrvlk cdvhlgnpla pavlpladcv ltllamecac csldayraal
181 cnlasllkpg ghlvttvtlr lpsymvgkre fscvalekee veqavldagf dieqllhspq
241 sysvtnaann gvcfivarkk pgp
//
1: NP_006765 indolethylamine N-methyltransferase; thioester S-methyltransferase-like [Homo sapiens] BLink, PubMed, Related Sequences, Nucleotide, Taxonomy, OMIM, LinkOut
LOCUS NP_006765 263 aa PRI 03-FEB-2001
DEFINITION indolethylamine N-methyltransferase; thioester
S-methyltransferase-like [Homo sapiens].
ACCESSION NP_006765
PID g10092584
VERSION NP_006765.2 GI:10092584
DBSOURCE REFSEQ: accession NM_006774.2
KEYWORDS .
SOURCE human.
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 263)
AUTHORS Thompson,M.A., Moon,E., Kim,U.J., Xu,J., Siciliano,M.J. and
Weinshilboum,R.M.
TITLE Human indolethylamine N-methyltransferase: cDNA cloning and
expression, gene cloning, and chromosomal localization
JOURNAL Genomics 61 (3), 285-297 (1999)
MEDLINE 20021766
PUBMED 10552930
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from AF128848.1,
AF128847.1.
On Sep 12, 2000 this sequence version replaced gi:5803044.
FEATURES Location/Qualifiers
source 1..263
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="7"
/map="7p15.3-p15.2"
Protein 1..263
/product="indolethylamine N-methyltransferase"
/note="thioester S-methyltransferase-like"
Region 4..259
/region_name="NNMT/PNMT/TEMT family"
/db_xref="CDD:pfam01234"
/note="NNMT_PNMT_TEMT"
CDS 1..263
/gene="INMT"
/db_xref="LocusID:11185"
/db_xref="MIM:604854"
/coded_by="NM_006774.2:1..792"
ORIGIN
1 mkggftggde yqkhflprdy latyysfdgs pspeaemlkf nleclhktfg pgglqgdtli
61 digsgptiyq vlaacdsfqd itlsdftdrn reelekwlkk epgaydwtpa vkfacelegn
121 sgrweekeek lraavkrvlk cdvhlgnpla pavlpladcv ltllamecac csldayraal
181 cnlasllkpg ghlvttvtlr lpsyvvgkre fscvalekee veqavldagf dieqllhspq
241 sysvtnaann gvccivarkk pgp
//
1: AAF18305 indolethylamine N-methyltransferase [Homo sapiens] BLink, PubMed, Related Sequences, Nucleotide, Taxonomy, OMIM, LinkOut
LOCUS AF128847_1 263 aa PRI 16-DEC-1999
DEFINITION indolethylamine N-methyltransferase [Homo sapiens].
ACCESSION AAF18305
PID g6580817
VERSION AAF18305.1 GI:6580817
DBSOURCE locus AF128847 accession AF128847.1
KEYWORDS .
SOURCE human.
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 263)
AUTHORS Thompson,M.A., Moon,E., Kim,U.J., Xu,J., Siciliano,M.J. and
Weinshilboum,R.M.
TITLE Human indolethylamine N-methyltransferase: cDNA cloning and
expression, gene cloning, and chromosomal localization
JOURNAL Genomics 61 (3), 285-297 (1999)
MEDLINE 20021766
PUBMED 10552930
REFERENCE 2 (residues 1 to 263)
AUTHORS Thompson,M.A., Moon,E., Kim,U.-J., Xu,J., Siciliano,M.J. and
Weinshilboum,R.M.
TITLE Direct Submission
JOURNAL Submitted (17-FEB-1999) Pharmacology, Mayo Clinic, 200 1st St. SW,
Rochester, MN 55905, USA
COMMENT Method: conceptual translation supplied by author.
FEATURES Location/Qualifiers
source 1..263
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="7"
/map="7p15.2-p15.3"
Protein 1..263
/product="indolethylamine N-methyltransferase"
/name="INMT"
CDS 1..263
/gene="INMT"
/coded_by="AF128847.1:17..808"
ORIGIN
1 mkggftggde yqkhflprdy latyysfdgs pspeaemlkf nleclhktfg pgglqgdtli
61 digsgptiyq vlaacdsfqd itlsdftdrn reelekwlkk epgaydwtpa vkfacelegn
121 sgrweekeek lraavkrvlk cdvhlgnpla pavlpladcv ltllamecac csldayraal
181 cnlasllkpg ghlvttvtlr lpsymvgkre fscvalekge veqavldagf dieqllhspq
241 sysvtnaann gvccivarkk pgp
//
1: BAB28594 putative [Mus musculus] BLink, PubMed, Related Sequences, Nucleotide, Taxonomy, LinkOut
LOCUS BAB28594 264 aa ROD 08-FEB-2001
DEFINITION putative [Mus musculus].
ACCESSION BAB28594
PID g12850108
VERSION BAB28594.1 GI:12850108
DBSOURCE locus AK013010 accession AK013010.1
KEYWORDS .
SOURCE house mouse.
ORGANISM Mus musculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus.
REFERENCE 1 (sites)
AUTHORS Carninci,P. and Hayashizaki,Y.
TITLE High-efficiency full-length cDNA cloning
JOURNAL Methods Enzymol. 303, 19-44 (1999)
REFERENCE 2 (sites)
AUTHORS Carninci,P., Shibata,Y., Hayatsu,N., Sugahara,Y., Shibata,K.,
Itoh,M., Konno,H., Okazaki,Y., Muramatsu,M. and Hayashizaki,Y.
TITLE Normalization and subtraction of cap-trapper-selected cDNAs to
prepare full-length cDNA libraries for rapid discovery of new genes
JOURNAL Genome Res. 10 (10), 1617-1630 (2000)
MEDLINE 20499374
REFERENCE 3 (sites)
AUTHORS Shibata,K., Itoh,M., Aizawa,K., Nagaoka,S., Sasaki,N., Carninci,P.,
Konno,H., Akiyama,J., Nishi,K., Kitsunai,T., Tashiro,H., Itoh,M.,
Kikuchi,N., Ishii,Y., Nakamura,S., Hazama,M., Nishine,T.,
Harada,A., Yamamoto,R., Matsumoto,H., Sakaguchi,S., Ikegami,T.,
Kashiwagi,K., Fujiwake,S., Inoue,K., Togawa,Y., Izawa,M., Ohara,E.,
Watahiki,M., Yoneda,Y., Ishikawa,T., Ozawa,K., Tanaka,T.,
Matsuura,S., Okazaki,Y., Muramatsu,M., Inoue,Y. and Hayashizaki,Y.
TITLE RIKEN integrated sequence analysis (RISA) system--384-format
sequencing pipeline with 384 multicapillary sequencer
JOURNAL Genome Res. 10 (11), 1757-1771 (2000)
MEDLINE 20530913
REFERENCE 4 (sites)
AUTHORS The RIKEN Genome Exploration Research Group Phase II Team and
FANTOM Consortium.
TITLE Functional annotation of a full-length mouse cDNA collection
JOURNAL Nature 409, 685-690 (2001)
REFERENCE 5 (residues 1 to 264)
AUTHORS Adachi,J., Aizawa,K., Akahira,S., Akimura,T., Aono,H., Arai,A.,
Arakawa,T., Carninci,P., Fukuda,S., Fukunishi,Y., Furuno,M.,
Hanagaki,T., Hara,A., Hayatsu,N., Hiramoto,K., Hiraoka,T., Hori,F.,
Imotani,K., Ishii,Y., Itoh,M., Izawa,M., Kato,H., Kawai,J.,
Kojima,Y., Konno,H., Kouda,M., Koya,S., Kurihara,C., Matsuyama,T.,
Miyazaki,A., Nishi,K., Nomura,K., Numazaki,R., Ohno,M., Okazaki,Y.,
Okido,T., Owa,C., Saito,H., Saito,R., Sakai,C., Sakai,K., Sano,H.,
Sasaki,D., Shibata,K., Shibata,Y., Shinagawa,A., Shiraki,T.,
Sogabe,Y., Suzuki,H., Tagami,M., Tagawa,A., Takahashi,F.,
Tanaka,T., Tejima,Y., Toya,T., Yamamura,T., Yasunishi,A.,
Yoshida,K., Yoshino,M., Muramatsu,M. and Hayashizaki,Y.
TITLE Direct Submission
JOURNAL Submitted (10-JUL-2000) Yoshihide Hayashizaki, The Institute of
Physical and Chemical Research (RIKEN), Laboratory for Genome
Exploration Research Group, RIKEN Gemomic Sciences Center (GSC),
RIKEN Yokohama Institute; 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama,
Kanagawa 230-0045, Japan (E-mail:genome-res@gsc.riken.go.jp,
URL:
http://genome.gsc.riken.go.jp/
, Tel:81-45-503-9222,
Fax:81-45-503-9216)
COMMENT Please visit our web site (
http://genome.gsc.riken.go.jp/
) for
further details.
cDNA library was prepared and sequenced in Mouse Genome
Encyclopedia Project of Genome Exploration Research Group in Riken
Genomic Sciences Center and Genome Science Laboratory in RIKEN.
Division of Experimental Animal Research in Riken contributed to
prepare mouse tissues. First strand cDNA was primed with a primer
[5' GAGAGAGAGAAGGATCCAAGAGCTCTTTTTTTTTTTTTTTTVN 3'], cDNA was
prepared by using trehalose thermo-activated reverse transcriptase
and subsequently enriched for full-length by cap-trapper. cDNA went
through one round of normalization to Rot = 7.5 and subtraction to
Rot = 37.5. Second strand cDNA was prepared with the primer adapter
of sequence [5'
GAGAGAGAGATTCTCGAGTTAATTAAATTAATCCCCCCCCCCCCC 3']. cDNA was cleaved
with XhoI and SstI. Cloning sites, 5' end: XhoI; 3' end: SstI.
Host: SOLR.
FEATURES Location/Qualifiers
source 1..264
/organism="Mus musculus"
/strain="C57BL/6J"
/db_xref="taxon:10090"
/db_xref="MGD:MGI:102963"
/db_xref="MGD:MGI:1898920"
/clone="2810406G07"
/clone_lib="RIKEN full-length enriched mouse cDNA library"
/dev_stage="10, 11 days embryo"
Protein 1..264
/name="putative"
CDS 1..264
/coded_by="AK013010.1:45..839"
ORIGIN
1 megkvyigge dyekeftpkd ylttyysfhs gpvaeqeivk fslqnlyqtf stggvggdvl
61 idigsgptiy qllsacevfr eiivtdytpq nmqelqkwlk kepgaydwss ivqhaceleg
121 drsrwqekea klrrtvtrvl rcdvtktppl gsaqvpladc vltflameca cpdidtyraa
181 lrrlagllkp gghlvtlvtl rfqhymvgpk kfsgvyleke vvekaiqdag cqvlkcncvs
241 lsyseaycsh dglcfvvark gpsa
//
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