ID A0A0U4C742_9BACT Unreviewed; 731 AA.
AC A0A0U4C742;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=AUC43_14250 {ECO:0000313|EMBL:ALW86152.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW86152.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW86152.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW86152.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M43B family.
CC {ECO:0000256|ARBA:ARBA00008721}.
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DR EMBL; CP013909; ALW86152.1; -; Genomic_DNA.
DR RefSeq; WP_068194959.1; NZ_CP013909.1.
DR AlphaFoldDB; A0A0U4C742; -.
DR STRING; 1411621.AUC43_14250; -.
DR KEGG; hyg:AUC43_14250; -.
DR OrthoDB; 6278496at2; -.
DR Proteomes; UP000059542; Chromosome.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..731
FT /note="PKD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006847590"
FT DOMAIN 382..441
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 731 AA; 77702 MW; 500426846F5412C3 CRC64;
MLKRILPSLL TAAMALASLG ATAQSMADER GRNWCGAVAE QERYFSQHPD AAEAQKALYR
KLEAREQIVQ RSTAGTSSAD VTIPVVVHVI HSGGADNISD RQIYSAIEQL NLDYQKQNSD
TANTLAQFRP IAASLGFQFR LAKKDPNGNC TTGITRHYAP NLTNDDYSGA VQAVSVWDRN
RYLNIWVVGS IGTPTAGGGI ILGYSNLPQN STATRDGFVV RGDWFGNQGT SNPTRALSRT
ATHEIGHYFG LLHPWGGNNN PEVPGYCSDT DFVADTPPTN GTFSCNLNYA PCGDVANVQN
FMDYATCPTM FTQGQKARMR DVLNTIRTGL TTPANLVATG TNDGYAAPDC APIAAFAAVP
GASTNVCVNT PVSLRDYSSN FSSTGGTLTY TWSFPGGNPS TATGQNVTVS YPTAGYYPVT
ETVSNSIGTS SSTVTDYIRV EGPSGGETAP FAESFENSNF PNLFNAPTLR NYTVTGATSS
GTAANFRWAW QAALPAADGS AYLVVNNRSY PAGAVTTLIT PNINLSAVSN TAVLSFSRAF
ALRSAGANDQ LRISFSNDCG VNWSSPTVLD VTQLTTQGLT PIDGYVPASS SEWQQLVVPI
PAQFQGSGLF KVRLQMVNST TQGNSFYLDN LRVSAPLATK ADALANHGIS VYPNPLTNET
AVHLNLTGTT QVGLSLTDVL GRNVLNLPTK MYGAGQQSLP LQTAGRALRA GVYVVRISLN
GETYTSKLTV N
//
