ID A0A067CLN0_SAPPC Unreviewed; 535 AA.
AC A0A067CLN0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=SPRG_19512 {ECO:0000313|EMBL:KDO31609.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO31609.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO31609.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO31609.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; KK583197; KDO31609.1; -; Genomic_DNA.
DR RefSeq; XP_012197766.1; XM_012342376.1.
DR AlphaFoldDB; A0A067CLN0; -.
DR EnsemblProtists; KDO31609; KDO31609; SPRG_19512.
DR GeneID; 24140863; -.
DR KEGG; spar:SPRG_19512; -.
DR VEuPathDB; FungiDB:SPRG_19512; -.
DR OMA; GYDPCTS; -.
DR OrthoDB; 34788at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF501; CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
KW Hydrolase {ECO:0000256|RuleBase:RU361156};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU361156};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Signal {ECO:0000256|RuleBase:RU361156};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 17..535
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5005103229"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 535 AA; 59146 MW; AA5F262D7DC9D1DA CRC64;
MQIIASLLVV AASAMAADVQ TAHHITDMPN YNDKSPINFN QFAGHMPLPS NGQKMFYWHV
ESQANPATDP LVLWLNGGPG CSSLGGFFTE LGPFVVESDL SVKRNKYGWN RKTNMVFLES
PSGVGFSTPF LNASDYNDAF TTARAREFLA EFLLAYPSYA GRDFYITGES YGGMYIPYLV
DALLTAPIHG LNLKGFAIGN PYTDEAIDNE AYLDYYYTHG MISIEAYADI QAKCNLNGLA
QFAGVFSDRS SNDSCAVAVS EGMVQAETDK LNGYYIYGDV CLLQNDQGNT LQYRDIRPMH
RGPYAPCTDQ FTQSYLRLPQ VQAAIHVSGS HVEWKNCAGH AAIQYTRSKS SLPLYPRILN
ANLKALIYSG DADSVVNFIG TQRWITSSGL KLNVVDKWKA WFGPDKQLAG YTEAYQGLNF
TTVKGAGHMV PAVRPLHALY MFECFVFGQE NCDTFAYPKD NLEYLTGADV TYTNDDDDVT
TQATLSSGES SMNWGLFVVA LLLVGTIISG AVFVMRRRAK KREYADLEEK TPLTC
//