ID D5BDA8_ZUNPS Unreviewed; 590 AA.
AC D5BDA8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=M61 family glycyl aminopeptidase {ECO:0000313|EMBL:ADF54814.1};
GN OrderedLocusNames=ZPR_4513 {ECO:0000313|EMBL:ADF54814.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF54814.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF54814.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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DR EMBL; CP001650; ADF54814.1; -; Genomic_DNA.
DR RefSeq; WP_013073874.1; NC_014041.1.
DR AlphaFoldDB; D5BDA8; -.
DR STRING; 655815.ZPR_4513; -.
DR KEGG; zpr:ZPR_4513; -.
DR eggNOG; COG3975; Bacteria.
DR HOGENOM; CLU_022755_0_0_10; -.
DR OrthoDB; 9778516at2; -.
DR Proteomes; UP000001654; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.3650; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR024191; Peptidase_M61.
DR InterPro; IPR007963; Peptidase_M61_catalytic.
DR InterPro; IPR040756; Peptidase_M61_N.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF05299; Peptidase_M61; 1.
DR Pfam; PF17899; Peptidase_M61_N; 1.
DR PIRSF; PIRSF016493; Glycyl_aminpptds; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:ADF54814.1};
KW Hydrolase {ECO:0000313|EMBL:ADF54814.1};
KW Protease {ECO:0000313|EMBL:ADF54814.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003069754"
FT DOMAIN 20..185
FT /note="Peptidase M61 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17899"
FT DOMAIN 278..395
FT /note="Peptidase M61 catalytic"
FT /evidence="ECO:0000259|Pfam:PF05299"
FT DOMAIN 484..560
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 67227 MW; D5E6E4BEC2076E05 CRC64;
MRLLFIFLFV CTISFAQQNK YQISFENAVH HEVKINIQFP GIKTDTFTVR MSRSSPGRYA
IHEFAKNVYG FKATDSKGKE LKVTRPNPYA WAVTGHDGIV NIEYILFANR GDGTYSQIDP
THAHLNMPAT FMFAEDLQER PIEITYNTEA MPNWKVATQL KHIEGNTFSA PNLQYFMDSP
TEISNFRIKS FEIDGKNVRF VLHDPSSDEL FNEYFERVKK IVEQEMKVYG ELPDFDYGEY
TFLACYIPNV SGDGMEHRNS TILTDVETLA NGGMKGNIGT VSHEFFHAWN VERIRPQSLE
PFDFTEANMS GALWFAEGFT SYYTNLILCR AGIISENDYI DGLNGSFNYV WNSPALQYFN
PIEMSYQAPF VDAATSLDPV NRENTFISYY SYGSVLGLAL DLHLRDKGLN LDDFMKLVWH
SYGKPEVPYE IKDIENLLKQ YAGEDIAKNF FNKYIYNSNM PDYKQLFANV GVDLSRKANE
SFLDISVENS ENGLVMTNNP KIGAPSYKAG LDKGANIISI NTIPVTSVEE FNEITSELKP
GQKISLKFSN YGEEKTVEVG VDKNPSYQIN IDPKPKKKAL KNRENWLSAK
//
