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Database: UniProt
Entry: C3YGD9_BRAFL
LinkDB: C3YGD9_BRAFL
Original site: C3YGD9_BRAFL 
ID   C3YGD9_BRAFL            Unreviewed;       589 AA.
AC   C3YGD9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN   ORFNames=BRAFLDRAFT_92883 {ECO:0000313|EMBL:EEN60660.1};
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:EEN60660.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60660.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN60660.1};
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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; GG666511; EEN60660.1; -; Genomic_DNA.
DR   RefSeq; XP_002604649.1; XM_002604603.1.
DR   AlphaFoldDB; C3YGD9; -.
DR   STRING; 7739.C3YGD9; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   InParanoid; C3YGD9; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR039311; FAM187A/B.
DR   PANTHER; PTHR32178; FAM187; 1.
DR   PANTHER; PTHR32178:SF6; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          368..462
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   DOMAIN          497..561
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
SQ   SEQUENCE   589 AA;  66744 MW;  BBC8D47319FBF343 CRC64;
     MILADVSYSM AAARVLSLFS ILIPIYMSSA VLSASLANLT SSDNSSSNQP YDTQLISPDA
     WSSRRNRAAV TNREIVLGRR NRRAADYCPV IVEKEFYVTQ LLHLRCLCQP INIRHRLLSW
     TVVPRDGQGE KPVLFDEEDR LELGTEFDMT IRHAQVTDSG IYYCRDTSRE RLLVSYDLTV
     KPAKSGVRLS LVALSENPLP NRTAAEMTMF SLWSPWGQCN RCGGSGERAR IGICHVESEN
     FPEHLGTRKV FACDSENLPS FAREVFGEEI RRPGHTIPFY EIRRPDERRV EFCTEPCPIG
     ICHVESENFP EHLGTRKVFA CDSENLPSFA REVFGEEIRR PGHTIPSYEI RRPDERRVEF
     CTEPCPIEHS EDYNVDSSRI GVLGDSSGGN LAAAVALKLN RPEKKNLPPL RFQSLLYPAL
     QALDFRTDSY KRGNSVDILT IDMMAFYWCL YLTGSYVRHP DFFSNNHIPP ELRKRLYTVG
     SVRSKDNNSV MNLPDDMKDI VNPYFAPLVA DDADLRGLPP AYILTCGFDV LRDDGIMYAK
     RLQTVDVPVV HDHLESAFHG IAVMGFKPFS YSLGRESLKK LADILRENL
//
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