ID C3YJK8_BRAFL Unreviewed; 403 AA.
AC C3YJK8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=CUB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_119701 {ECO:0000313|EMBL:EEN59315.1};
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:EEN59315.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59315.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN59315.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; GG666520; EEN59315.1; -; Genomic_DNA.
DR RefSeq; XP_002603304.1; XM_002603258.1.
DR AlphaFoldDB; C3YJK8; -.
DR STRING; 7739.C3YJK8; -.
DR eggNOG; KOG3627; Eukaryota.
DR eggNOG; KOG4292; Eukaryota.
DR InParanoid; C3YJK8; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR PANTHER; PTHR24250:SF29; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..403
FT /note="CUB domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935320"
FT DOMAIN 19..128
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 169..401
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 403 AA; 42895 MW; F9C4516D8A507683 CRC64;
MIWFLCVLSL ASYAKAQSCG GTFSGSSGTA ASPNYPNSYG NDLNCEYSFP ANGQLLQITF
NSFQLEAASS WTGSCYDTVT VYDGGVRVGE YCGTNRPANI ATRSEVTIEF TSDYSVAASG
FSLSFSRGGE IITTTTLPPP TYAPGSCGTP AIQPRSSEML RYDQAEGRIV NGDDATPHSW
PWQVSLQTST GWHYCGGSIV NENWVITAAH CDPTISSDYV ILGEHNKGGG TESIQRVRIS
RKICHQQYNS NTIDYDICLL KLATPAVFSD KVHPVCMANS GDDSSFPAGM RCYTSGWGKT
SASSSGTPDI LQQAMIPLIS TSQCQAAWGS VNTITDRMVC AGADGATSCM GDSGGPLVCQ
KDGAWNLIGV VSWGSSQCST STPAVYARVT NLRQWLDSTM ANN
//
