ID A0A369IAU5_9BACT Unreviewed; 792 AA.
AC A0A369IAU5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=PKD domain-containing protein {ECO:0000313|EMBL:RDB06859.1};
GN ORFNames=DVG78_06125 {ECO:0000313|EMBL:RDB06859.1};
OS Runella aurantiaca.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; Runella.
OX NCBI_TaxID=2282308 {ECO:0000313|EMBL:RDB06859.1, ECO:0000313|Proteomes:UP000253141};
RN [1] {ECO:0000313|EMBL:RDB06859.1, ECO:0000313|Proteomes:UP000253141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX9 {ECO:0000313|EMBL:RDB06859.1,
RC ECO:0000313|Proteomes:UP000253141};
RA Yang X.;
RT "Genome analysis of Runella aurantiaca.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RDB06859.1}.
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DR EMBL; QPIW01000003; RDB06859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369IAU5; -.
DR OrthoDB; 6278496at2; -.
DR Proteomes; UP000253141; 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; 2.60.40.10; 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; PF00801; PKD; 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, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..792
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017033853"
FT DOMAIN 352..438
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 792 AA; 86727 MW; FF4CF535A62D0E4C CRC64;
MLKICTRAFL SLFVLLSFFA QAQRRTEPCA TMEMDSLLRL RNPSEGSLDE FERDLQRKMV
QIKARMASGR GAAEIITIPI VVHVIHSGEA IGTGRNISQA QVQAQIETLN EDFRRRVNTN
GFNSDSRGAD IEIEFCLAQF NPQGQRMAEP GIDRVNGNRA NWVRNDIEGS LKPTTSWDPN
KYYNIWVLDF AAQDDNLLGY AQFPSNSNLS GIPGSGGAAS TDGVVVNYAN FGNAQKGNFS
LLRAPYNLGR TLTHETGHWL GLRHIWGDSN CGDDFCADTP SQASESRGCQ KGRMSCGSAN
MVENYMDYSD DACFNIFTRD QKTRMRAVME ISPRRASLLT SNVCGQLVVG RPTPNFEAEN
RVVLLGAQVK FTDLSTNFPT AWQWEFEGGD PAVATEQNPT VTYRTAGKFR VTLTVSNASG
ASAPLTKTQY IEVVNAGLCA TATNFTGAGT VIRQSTGTGY VSGHNSRRTQ AVAELFPNTL
GYTNLRGASL KFGVAKAARG NETEAVVRVK VWNARGFQGG PGSELTTKEV PLRRILDDVR
NNRATTVVFD QNIDLSRQNN LSFLIGIELD YVAGDTVALT TTLNGESLNA TSWERNSSGN
WDRYIVRTGL NVAHNITAEV GMKASVQIQA SAQFINPGEA VTLQARGASV INWSPSEGLS
ATLGPQVTAR PNRTLTYLVK GTGSDVCLDS ASATIYVRNV QILSNETLPE KDFVISPNPT
DGVAEVSFTN GLRGKVTLRL RSITGQEVWR GEFEKTSDLF RQSINVRTYP AGSYFIDLQL
GDFVDRKRLV KY
//
