LOCUS XP_002114294 3743 aa linear INV 19-JUL-2009
DEFINITION hypothetical protein TRIADDRAFT_57956 [Trichoplax adhaerens].
ACCESSION XP_002114294
VERSION XP_002114294.1 GI:196008857
DBSOURCE REFSEQ: accession XM_002114258.1
KEYWORDS .
SOURCE Trichoplax adhaerens
ORGANISM Trichoplax adhaerens
Eukaryota; Metazoa; Placozoa; Trichoplax.
REFERENCE 1 (residues 1 to 3743)
AUTHORS Srivastava,M., Begovic,E., Chapman,J., Putnam,N.H., Hellsten,U.,
Kawashima,T., Kuo,A., Mitros,T., Salamov,A., Carpenter,M.L.,
Signorovitch,A.Y., Moreno,M.A., Kamm,K., Grimwood,J., Schmutz,J.,
Shapiro,H., Grigoriev,I.V., Buss,L.W., Schierwater,B.,
Dellaporta,S.L. and Rokhsar,D.S.
CONSRTM US DOE Joint Genome Institute (JGI-PGF)
TITLE The Trichoplax genome and the nature of placozoans
JOURNAL Nature 454 (7207), 955-960 (2008)
PUBMED 18719581
REFERENCE 2 (residues 1 to 3743)
AUTHORS Kuo,A., Lucas,S., Glavina del Rio,T., Dahlin,E., Tice,H.,
Pitluck,S., Zhou,K., Srivastava,M., Begovic,E., Chapman,J.,
Putnam,N.H., Hellsten,U., Kawashima,T., Mitros,T., Salamov,A.,
Carpenter,M.L., Signorovitch,A.Y., Moreno,M.A., Kamm,K.,
Grimwood,J., Schmutz,J., Shapiro,H., Grigoriev,I.V., Buss,L.W.,
Schierwater,B., Dellaporta,S.L. and Rokhsar,D.S.
CONSRTM US DOE Joint Genome Institute (JGI-PGF)
TITLE Direct Submission
JOURNAL Submitted (12-JUN-2008) US DOE Joint Genome Institute, 2800
Mitchell Drive B100, Walnut Creek, CA 94598-1698, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from EDV23384.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..3743
/organism="Trichoplax adhaerens"
/strain="Grell-BS-1999"
/db_xref="taxon:10228"
Protein 1..3743
/product="hypothetical protein"
/calculated_mol_wt=424337
Region 44..119
/region_name="DCX"
/note="Ubiquitin-like domain of DCX; cd01617"
/db_xref="CDD:176357"
Site order(48,53..54,58,62,65,76,85,97,110..111,114)
/site_type="other"
/note="XLIS mutations"
/db_xref="CDD:176357"
Site order(48,51,60,75,78,85,87,89,110)
/site_type="other"
/note="SBH mutations"
/db_xref="CDD:176357"
Region 168..251
/region_name="UBQ"
/note="Ubiquitin-like proteins; cl00155"
/db_xref="CDD:212176"
Site order(203,218,245)
/site_type="other"
/note="charged pocket"
/db_xref="CDD:176352"
Site order(220..223,243..244)
/site_type="other"
/note="hydrophobic patch"
/db_xref="CDD:176352"
Region 373..486
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 497..618
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 643..752
/region_name="FGF"
/note="Acidic and basic fibroblast growth factor family;
FGFs are mitogens, which stimulate growth or
differentiation of cells of mesodermal or neuroectodermal
origin. The family plays essential roles in patterning and
differentiation during vertebrate...; cl00060"
/db_xref="CDD:206809"
Site order(648,680,682,684,712,720,723..725,727)
/site_type="other"
/note="receptor interaction site"
/db_xref="CDD:28940"
Site order(743..744,749,753)
/site_type="other"
/note="heparin binding site (glycine box) [chemical
binding]"
/db_xref="CDD:28940"
Region 961..1076
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 1087..1189
/region_name="PLAT_repeat"
/note="PLAT/LH2 domain repeats of family of proteins with
unknown function. In general, PLAT/LH2 consists of an
eight stranded beta-barrel and it's proposed function is
to mediate interaction with lipids or membrane bound
proteins; cd01756"
/db_xref="CDD:28753"
Region 1284..1398
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 1409..1551
/region_name="PLAT_repeat"
/note="PLAT/LH2 domain repeats of family of proteins with
unknown function. In general, PLAT/LH2 consists of an
eight stranded beta-barrel and it's proposed function is
to mediate interaction with lipids or membrane bound
proteins; cd01756"
/db_xref="CDD:28753"
Region 1591..1702
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 1715..>1788
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 1836..1949
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 1963..2085
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 2082..2198
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 2229..>2301
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 2460..>2542
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 2576..2689
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 2820..2937
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 2949..>3033
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 3098..3175
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
Region 3338..3449
/region_name="PLAT"
/note="PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin)
domain or LH2 (Lipoxygenase homology 2) domain. It
consists of an eight stranded beta-barrel. The domain can
be found in various domain architectures, in case of
lipoxygenases, alpha toxin, lipases and...; cl00011"
/db_xref="CDD:206780"
CDS 1..3743
/locus_tag="TRIADDRAFT_57956"
/coded_by="XM_002114258.1:1..11232"
/note="similar to lipoxygenase homology domains 1"
/db_xref="InterPro:IPR001024"
/db_xref="InterPro:IPR003533"
/db_xref="GeneID:6755191"
ORIGIN
1 mdqskrknnd kvktsfasns apaalparpp lyqrsivgak srmvqffkdg ddtfrpvkma
61 insqryrtfd tllddlsqkv plpfgvrniq tplgvhhvys ttqledgksy vcsskkqikq
121 ieysetkqrk gwsyttgpnv krqeigepvp awtkkirava vvntlvrdvr pkvitiyrng
181 aaahnkvkil fnprtmqsye aivkdmansl kvngrqhkly tvegklvsgi sdlihgppey
241 ilcgeealvp latvasvapp qpstvrkrkq qrnkrakkeq vivmsdsdss pevreqhnpq
301 qrqhqkqrqq hhqqrqleee kqqqqpqlrq qarpqqhprk tvdkppqnvn ntdlvedeki
361 eeppvkkgfv lknqweislv tngkrasgtn arvyfsvygd kgsrgpfeig ssfpssstqs
421 nlvsfrdvgk iykirighys skksdswllq nvrlrkrdds edlsfianrw lscyhedgnt
481 qrefpvlrpn qkiiplikyw ltvytgefsg agtssevyvi ingergdtgk rylrslkgkd
541 rkpfqhgkis sfcveavslk tiqnmvvgve nrhdaedaaw ylqkvilktg sdrdanqlvf
601 ycrewldpsd ksertllpds dvtngsrlsa tmdcemsklk egnhvilysk asrkalrvvn
661 nqgldgngdd kdnsntfeii kieddtvafk ncvsqtfiai kkegilsgng kgnsdcifsv
721 ringdltasm eskkladhhv iisnngkamd pklpassaaa rfsiylkgkf rdggkvmlas
781 caanqflsid sngnllccps neeeaifnvi kidkhirafq sasnpdyyir mqgrtvdgkg
841 rgdrpchfri rkncfdgyfv lesvkyngmc lsvqpdmtti vpqvdvgddn vqfrakvvef
901 giksssddeq pqnessdskf rndvekkhsi gingnnnevv qqngideptl aaiipqqepd
961 wtvwvstmdn aiagtnakvt levcghegqs qpllldpsmg ffhpgnterf evyvgpvgki
1021 ykirishdns tdvsdwflnk vkmrhketke elvfickrwl srsrddhdit relpvvranq
1081 svlpvrtymv kvytsdiwga dtdneilini fgklgdtglr elyyssnnee kfhranmdlf
1141 sidavqlgql ikikighnnl nrgegwhldk vvihekskpe leycfpcqrt syaylhilds
1201 nlapmvkmrs ssdqlipven gkknytpepq spdsdsksvl eenqnaegne kiakspdnks
1261 vdqadavnsp eqsnpaqgle nddwqitiat sdkedagtdt qvtlvvygde gistditldq
1321 sgehfqpgdi hqfqvslgpi griykvrlsh nnqgkhtswh vdrlkmrhit thetlmfkfn
1381 rwlsrdkddg ditrelpalr pneiplpvir yhvyvstgdv icggtdtrvy ltiigqrgds
1441 grrelfyshn hankfeqgqt dvfiieavsl ndltsikigh tehgavigmy kklfppnasf
1501 yfntilgagw flakvliteg ddknaknyef pchrwldegq ddgkierely vqepskdaik
1561 eitdqngard dltpdepiee tppepvkegd weikvktsdm psagsyanvy lvayglngks
1621 qvdfdndqdh ftpnqlssfk vhledigely kirighdgvl eeqswhlefv qminlftqet
1681 ynfhfdrwls ryaddsdtcr elsvqiddqf klpnviyrit vytdkgligk kqvwinlygq
1741 hgdcghrlll lseheakfrr nqvdtftiea tslgqldklq mgiknsdked ikshfrkvvv
1801 ttltkindql eevtfgykks syttgpeayl ypnrewllsi ktgdfsssys ntqvaviayg
1861 snsnsgiipl ghgasslfhp nkevkfkipl gylediykir igqaelssec swylqaltlt
1921 nlcteeeyvi kaeswlshyq gtgetwiela taeiqsnllp vlpyvielht nevptsfset
1981 rlyvtlyger gdsgprvlak laepwtqlks nyaneftiha vdlsqlkmlk leygeslnap
2041 awfidkvvvk fgdtnnrtvv lkskinldph ssskkyypeg dwlikirtse irnagtqani
2101 elicygsecv tdkislnnfk nnafsagklt qyknylgsig rpykvrvshd gqnkndgwhl
2161 dyiklfnvct eeefefksnr wiskyednge iirelpvshe ddlytnttyf iqahfregfa
2221 iehlsscvit vygdnsdsge relirslsns pktigdnvte ftieavalgl ldkahlslts
2281 snestewswp ieklvlrdsr npyeektfly kistdsshns vyekdfhpdd qwllnlcalk
2341 isnsncilwl ncygtdgqst laeigklqdl qivnnvakei pikvkdirni ykvrlqtsdd
2401 igslplqvqa ldllhvstgr kyqfavdhls qyqdlqaeyl yqelpaidps ngshlnveiy
2461 evtvflkdqe salesdhrfn iqlfgsngdl geriisnpti dsnsvvqfrl qavdlgnltk
2521 mfvthlssdh nvvlaidkav ikfdnkdilf kpssttdkdv dyshdssmve lrpegtwnil
2581 iktsdienag ttanvylkcy gtegcsdlip ligvylpged vefqtnlsfi gqlykirish
2641 dglkeedswh lhsieltnls tsqlysfshe gwlskykena dvacelavvn edksslsvik
2701 yditlmeldd rfnlnqnwyl iihgeqgdsd ndgrkglscf veavtlqkvk rvtlsctkat
2761 tddhedsqdd nsglpvpcry iniswlddsr kqislkpkfe ettiiendqq iqqfypesdw
2821 iiriytndli ldqisnsdvs illygdikts eplalgtlnp stfkagneae fqvitgnlgk
2881 vykmqiccda iqshfqwhih gvsltniatn eesrydmdcw lsnvqhacqv igelpvgfke
2941 saknlpavvd yiitiyiskn anadiigqmk yitiigdqgd sgkrpfilcd eegfvalnie
3001 ksqlidyknh qirfhlkaid vgqldrinie cddvedlqln idkicltisg nndfietlrk
3061 kksvdherqh vqtylregic liktelndli sesqsqqnys itcygdhgrs ekidldennl
3121 fkesdkesif rietgylgdl fkirldgqdn gqlkanywql ktfqiqnlat edeytanfsq
3181 pplqqmfset dvvrevtiav ddkddyqikl ydiaihgtih qkdteksead qfsleylyln
3241 ifgkisdsge rkimignhdn ndkdtdilge dmfkaasige idkvvlrlmd stssdilanw
3301 pitkitikel gnespiilki keteadnpft reflcedsii iqtstnsvsg teakiklviy
3361 gnnsktneml lqdgnhsdlf qpsqvatfkl qlpdigalyk irlthdsqnk ndgwlpekvt
3421 ikvqhkeyvf scnrwlssve ddgeiirefa vdspngdplp avryqiklpi eidpilddrl
3481 lfnltgdhgd tgdrilkkrk sdiandqyey iieaislrsl kvltvmcdsk iklpfksvvv
3541 lddnhkpitf tlqsssqdqs ssrrgsegdl nnnnnddksp qqsisnddni nnneeklnnn
3601 qadhdgsklk esdqndvina nednlkhdrs dsikdnerny vsyefhpkdi sdsendgsdn
3661 dsdeirnqll gigkklctle gnrilsqdlk tyfmkvsina dvmqkietal dlssdylelq
3721 kfvdvmqkhc eesqidvksl dvl
//
