ID   A0A136NJ30_9BACT        Unreviewed;       710 AA.
AC   A0A136NJ30;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Pregnancy-associated plasma protein-A {ECO:0000313|EMBL:KXK46184.1};
GN   ORFNames=UZ10_BCD003001390 {ECO:0000313|EMBL:KXK46184.1};
OS   Bacteroidetes bacterium OLB10.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617421 {ECO:0000313|EMBL:KXK46184.1, ECO:0000313|Proteomes:UP000070480};
RN   [1] {ECO:0000313|EMBL:KXK46184.1, ECO:0000313|Proteomes:UP000070480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB10 {ECO:0000313|EMBL:KXK46184.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK46184.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNBX01000030; KXK46184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136NJ30; -.
DR   STRING; 1617421.UZ10_BCD003001390; -.
DR   PATRIC; fig|1617421.3.peg.1448; -.
DR   Proteomes; UP000070480; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
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..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..710
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007476855"
FT   DOMAIN          385..444
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   710 AA;  78082 MW;  28F71A21BF56F4A6 CRC64;
     MVNQIKSHNF ITMKKFFTRS LLILTAMTWG YASAQTPLTH WCATDDVCNA RENSDPVVRQ
     QRQQLEAFTQ QYVSSFQPSY FRTTGTPVYV IPVVFHVVHN WGPENISDEQ IYDAVRVLNR
     DYNLQRTDTA NIIPSFKALN ADVQIEFRLA HLDPLGNCTN GIDRIASTLT YDADDNSKLN
     PWPYNKYLNI WTISNFGASH AGAAAYAYKP GTAPSGKDGI ISLSNYVGSI GTSNTTNQYT
     LTHEIGHWLN LNHTWGGTNQ PGVSCGDDNV TDTPVTKGFL SCPQPANADV CNPGIIENYQ
     NYMDYSYCYY MFTLGQKARM WAALNSAIGF RNQVHTTSNL NATGTNGNAT TCVPVASFSS
     IQKVICEGGV ANFSDASGNL DTVGITYLWD FPGGVPSSST DKNPTGIVYP TAGAYDVTLT
     VTSSAGFDTH TEIENVVVRP GTTNLFVPFS ESFESITFPS ADWLTESDDG DGWELTSNAA
     HTGFNSVSIN NYSGNTTSSK DVFITPGFNL TNTTQTQFKF WVAFALKNTA GTDQLKVYAS
     NNCGQLWNLR LTKSGTSLAT VNNAVTSNFV PTSAQWRQET VSLTSGQYST RPNVSLKFEY
     TNDMGNNIYI DDINLSGVVG INDFPLSQED VTIVPNPAYD KSTVNFELSK PENVLITVVD
     MLGNEVHRIA DERLDAGEYQ YEVNTKWAKG IYMVRITAGN QIITKKLVVQ
//