ID A0A1F3NVN6_9BACT Unreviewed; 679 AA.
AC A0A1F3NVN6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=A3G23_10760 {ECO:0000313|EMBL:OFY69510.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY69510.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY69510.1, ECO:0000313|Proteomes:UP000176497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the peptidase M43B family.
CC {ECO:0000256|ARBA:ARBA00008721}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFY69510.1}.
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DR EMBL; MEPC01000034; OFY69510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3NVN6; -.
DR STRING; 1797365.A3G23_10760; -.
DR Proteomes; UP000176497; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd00146; PKD; 1.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR008754; Peptidase_M43.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR47466; -; 1.
DR PANTHER; PTHR47466:SF1; METALLOPROTEASE MEP1 (AFU_ORTHOLOGUE AFUA_1G07730)-RELATED; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 328..413
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 679 AA; 75570 MW; 9363D0563A34435D CRC64;
MKKTLYLILF TGHLSLLNAQ IQIHESCGFD NYLRQNNISV EKFERTVQNY LRQNKSQRNS
AMPQSLKIIP VVVHVVHNGG TENISDAQIQ SQMDALNEDY RKMPGTAGDG AGADTEIEFR
LAKKDPQGRC TNGIVRIKST LTSHQNYQRA DLAKLSSWDA TRYLNIYVVK TISGGTAGYA
SFPGGPTDQD GIVVMHTYFG RTGTASSSLG RTPTHEAGHW LGVYHTFQNG CGTDTCTEGD
YVCDTPPAAN PNYFCPVINS CSNDFPDVKD QIENYMDYSD DNCKNMFTSG QKERMYATLN
TERITVWQLS NLIATGCDSG YVSAPCNAVA DFTSNAKNIC VGNSVSFVNK SLNNCTTFQW
NFPGGNPETS TQLNPVIKYD STGNYEVSLK ATNSNGTDSV TIENYITVSI PPTGRPVPFI
ENFEEVVFPP QGIILENPDN GITWELDTVA VKFSGYGSAK INNLININYG QADALVFPNM
DLTTFTETPI MTFRWAYARS DANYSDELMV LISTDCGATF KQIFYRTGSQ LTTGTTQTTP
YIPDSSTVWK FAKIQLTPYA FSKNAILKIV NVTDGGNNLY IDSINIGKYP ITSRNNFSNE
NSVLIYPNPF TGNTVVHFTG NFKEKTLVRI FDIFGKEVYY FYFQIASNVF IPERNFKKGI
YIMKIFDNNA VIVKKFIVQ
//
