ID Q484F0_COLP3 Unreviewed; 660 AA.
AC Q484F0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Serine protease, trypsin family {ECO:0000313|EMBL:AAZ27366.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:AAZ27366.1};
GN OrderedLocusNames=CPS_1835 {ECO:0000313|EMBL:AAZ27366.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ27366.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ27366.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ27366.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP000083; AAZ27366.1; -; Genomic_DNA.
DR RefSeq; WP_011042659.1; NC_003910.7.
DR AlphaFoldDB; Q484F0; -.
DR STRING; 167879.CPS_1835; -.
DR MEROPS; S01.234; -.
DR KEGG; cps:CPS_1835; -.
DR HOGENOM; CLU_024054_0_0_6; -.
DR Proteomes; UP000000547; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:AAZ27366.1};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:AAZ27366.1};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 42..278
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 660 AA; 71140 MW; 9E01AFAE89FA4392 CRC64;
MKFNTFVIAF VSSAITLYSQ TSSGAPSSDS GDHIKRTATQ RIINGVAAKK DDYPFITGLI
ASSTKEGGEI SPFCGASFIG GHYILTASHC VDGSTASDID VVVGEHNLKD RTTGVRYKVA
QIYMHEDYDS VATNNDIAIL ELETAITNVT PIKPLTVELE SLLKTGDLLT VMGWGNLSVD
DQSFPTVLHK VDVALFDRDK CNAAYGGGLT EQMLCAGFEL GGKDSCQGDS GGPLVINKNG
EWYQAGVVSF GEGCAVAGFP GVYARVSKFL DWIKEKKAGV SYQQKPNPGY VENGYEDIAT
LKFKNLSATE YTITDIKFTD LNKVSQPTVE TNNCNSAALK QNESCEFTVK VTSTELGEGG
FNISVSTTHP ENSLAEQFFA INALEKTSLD MKTLLDINND DIEWYSGGDA VWQAQTTQVL
RGDNAVESGD IINSQNSVLL AIIKNPEVND FSFNYIVQAE EGYDGLKIAL NGRKTEFFAT
GVTQTIFKEE KVVLTPGTDR IAFIFSKDET DDDAEVGFNK AYIDLVQNST TNTAPVINLS
KSIYAVKVQK EVSLDASKSA DEEGDTLHFK WELVGDKLGS VLNNATSAQA TFVAGDKAGN
VTFKVIVTDQ QGATSSKVGS VTITKDTTET KDTVEAKKSG GAGAFILLFS LLFLSLRSRK
//
