GenomeNet

Database: UniProt
Entry: C3XWY5_BRAFL
LinkDB: C3XWY5_BRAFL
Original site: C3XWY5_BRAFL 
ID   C3XWY5_BRAFL            Unreviewed;      1615 AA.
AC   C3XWY5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
DE   Flags: Fragment;
GN   ORFNames=BRAFLDRAFT_71196 {ECO:0000313|EMBL:EEN67245.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN67245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67245.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN67245.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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DR   EMBL; GG666471; EEN67245.1; -; Genomic_DNA.
DR   RefSeq; XP_002611235.1; XM_002611189.1.
DR   STRING; 7739.C3XWY5; -.
DR   eggNOG; ENOG502QT6K; Eukaryota.
DR   InParanoid; C3XWY5; -.
DR   Gene3D; 1.20.1480.30; Designed four-helix bundle protein; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR24543:SF326; METALLOENDOPEPTIDASE; 1.
DR   PANTHER; PTHR24543; MULTICOPPER OXIDASE-RELATED; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          1505..1615
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1249..1276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1476..1517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          330..498
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          610..637
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        151..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..567
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..825
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1040
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1136..1160
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1273
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1476..1514
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEN67245.1"
SQ   SEQUENCE   1615 AA;  174937 MW;  393805DF5F6F0843 CRC64;
     DAQEAAQEAY SEFETAVETG ENVEEAAAVL EEEMEDLNTE IETAQEDAIG AEAAEVAEEQ
     ASENLEAIQA GLAAGNPAQV AAAAEGIGEN VDDILEAAAD VGLDSPALED AEEAVQEAEA
     AVETALQTGD REAVAAAAEV LEEELQDLQE GVDQAQEQQE QAEETEAAQG EISETIHELE
     ELVEGEDIAA EETVFQELVE QADELETALQ DSNLDSPAVE AALDAAHGAQ EDVEAAIQNE
     NQEEIAAALT ELGSAMDELD TAAGEAQEDV AAEQAAEAAE DQASETLEDI QAGLAAGNPA
     EVAAGLDDVG ENVADILEAA GDAGLDSPVL DEAETAIQEA EEAVQTALET GDREDVEEAV
     ERLEEEFKDL QEGVDEAQEV QEQADETEAV QEQLSETISE MEDLVAEGDI SAEETVIEEF
     EEQAEELQAA LESAELDSPA VEAAIEGVQE AQEEVQTAIQ NEDEEEIAAA LTELGSQVEE
     LDTAAAEAQQ DAEAEQAAEA AETAVETAAE AFEEVVEAGG STSEEEEALE TLEERVDYFN
     QQFEEETEQA EQEEEQAVAQ EGAEDALEDV LEDLSEGDTG QAEETVEQII EDIAQVASVA
     EDAGADTPQV DFVQAEIEEV AGEMKEAIQE ENTERAEQLA EVLETKMETF EHVVETAVEE
     AEEQQTAEDT ASELQELIPD LTSLGEGDEE EVQQAVEEIK AEFEQIVAGE AGDILNEQQP
     GLVSEVEAAI LEVEQAAESG DSEEIKEAAQ TLEQELVVVQ EEAEYSACGG CEGEGAPQII
     NNQIIAFKGR RPQPMLQRPA VGIGESAESE EEQEQIEEAQ EEAEEAQDVV AEGADDLLEA
     VQTGDIGEVE DLTEDLTEQV EELESVFEEA DIDNQEVVEL QDEVIEKIEE VESVMQSGTP
     EEQEQAAAEL IEAVDELKET AAAQVAEGTQ DEVEENADDI LEAVQTGDSE EVEELTENIV
     EQVEELDTVL EEAGVDTEEV AELKEEIIEK AEEVESVMQS GTSEEQEQAA AELIEAVDEL
     KETAEEAQEE QEVEAAAEDV EETQGEVKET ADDILEAVQT GDTDEVEELT ENIEEQVEEL
     DTVLEEAGVD TQEVVELKEE IIEKAEEVES VMQSGTQEEQ EQAAAELIEA VDELKETAEE
     AQEEQEGEEA AEEVDETQDD VVETADDIMQ AAQTGDTEEL EELTESIAEE VQELETALEG
     AGVDTEDVGE LEEVMEQVEE MQSVIESGTQ EEQEQAAAEL IEVVDELKDT AEEAQEEQEG
     EEAAEDVEET QQEMTETLSE VGDILQEGTQ EEKVEVVEEL EETVDTLFED IAEASVESET
     IDEVKDELEE QVAALEEAVE SGDTAAQETI QEEIEETIQE VAEVVEEVQE TQEGEEAAAV
     VVRTEEEITE TLDEVEEVLQ EGTQEEKQEV VDELESNVET LIEDIEEANV ESETVDEARD
     QLEEQVEALQ EAVESGDTAA QVAIQGTIEE TVQEVEEAVN EAAGVEEPEE EEEPEEEEEP
     EEEPEEEPEE EGETVSVIES IPREAFTASS TLDEQHSSYY AVIGKTYEDG SPAFWAPGTD
     DTDQYLQIDM GQPTQLSTVE TQGAAGRFVT TFLLRYSVDG VTWITYKGDD GEDMV
//
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