ID T0S0F2_SAPDV Unreviewed; 833 AA.
AC T0S0F2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|Pfam:PF00246};
GN ORFNames=SDRG_04119 {ECO:0000313|EMBL:EQC38408.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC38408.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC38408.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC38408.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; JH767141; EQC38408.1; -; Genomic_DNA.
DR RefSeq; XP_008608000.1; XM_008609778.1.
DR AlphaFoldDB; T0S0F2; -.
DR STRING; 1156394.T0S0F2; -.
DR EnsemblProtists; EQC38408; EQC38408; SDRG_04119.
DR GeneID; 19944846; -.
DR VEuPathDB; FungiDB:SDRG_04119; -.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; T0S0F2; -.
DR OMA; CHALTTY; -.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF45; CYTOSOLIC CARBOXYPEPTIDASE NNA1; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030762}.
FT DOMAIN 324..460
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 678..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 92916 MW; 7AC3F71B28581B3D CRC64;
MEVPSSPKPS PRLSLPRAKL KSLLALSSLA PLPLIQAHHE SINDNDAHVA KAEFNTVLPH
VVHKDIFAAS AEGSPIGSED ESRQLAHLLA EFERRFWKKA NKKATSSLVF RRRSLDPTHV
ATDEAPVVDP TSLTFDSNFE SANLASAYRV HDRNYSFVSQ CTSKHGDTAG PSRVDQEYDL
YCTNDTYTLG HIQWYYFKVT RPPGNGRLRV RFNLRNMMKR DSLYNCGMLP AVYSEAKVNA
GIAGWTHGGE EAFYYQNADV YTRVRRGLRR NFSHYTLSFI YTFEPSEDVV YFAHCFPYTY
TYLQTYLTSL EKCPLRSRNL RRRTLCSTLC GNACDMLTIT EFTSEPQVLR KRTGVVLTAR
VHPGETNGSF LLHGIMEFLT GFSDEAIALR KCYIFKIIPM LNPDGVVHGN YRCSLAGIDL
NRRWSQPSEL YHPTIYAAKK MIALMRQSRK VLLFCDFHGH SRKKNMFTYI AIKMTILSVT
DRNRYGCKPY LSWSRLEDAK VRLFPYVLCK TSSAQAGGYF SFTDCTFNVT RSKRSTGRVA
VWSDIQILNS ITLEASFCGT GDNKARRSIA AFATTTPNHT PRHFTQRDFT CSGEQFCHAL
TTYGALLGIE PIDATTLLGA SAAKHEGVLE LLDLDETPIE PNVRDPTLLT STTAFGANDF
AYSETALSLL DEIASCVPSP SDGAAESENS SGSDSNPSED NYEPEELESN TAWQAFRRNV
VLRRSSSALK SASAGPNSGR TASLTLSSSL AKKSIKLRKK VRRSSTTGTP RVTVSDAPAV
VAKADGGPHR SPRVAPLPLR RVEVKNAGGF AQFHKNMIQR RIHQSQIVMR PPP
//