ID A0A2T2YI94_9BACT Unreviewed; 508 AA.
AC A0A2T2YI94;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:PSR55217.1};
GN ORFNames=AHMF7605_17735 {ECO:0000313|EMBL:PSR55217.1};
OS Adhaeribacter arboris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Adhaeribacter.
OX NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR55217.1, ECO:0000313|Proteomes:UP000240357};
RN [1] {ECO:0000313|EMBL:PSR55217.1, ECO:0000313|Proteomes:UP000240357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7605 {ECO:0000313|EMBL:PSR55217.1,
RC ECO:0000313|Proteomes:UP000240357};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL Submitted (MAR-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:PSR55217.1}.
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DR EMBL; PYFT01000001; PSR55217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2YI94; -.
DR Proteomes; UP000240357; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 ECO:0000313|EMBL:PSR55217.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:PSR55217.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 346..411
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 508 AA; 56375 MW; 55903354BA6282AE CRC64;
MFKLPSVLKF ILLRANIYVC IIWLLLVVGS VKAQPAKPRP RCATNEVTQR LQQLHPNLLN
QMQKVKVHAQ TYQQQKSKAR LQQPVTVVPV VFHVVYHNSR ENVSTEQLLS QLEVLNEDYR
HQNADSAQTL PQFKKLAADT RIQFCLATRD PNGNATTGIT RKFTSSAEFD IDDAVKFSAF
SGQNAWDSER YLNIWVCNLS GQSLGYSQYP GGPAETDGVV LDYTTIGRAP ANPFASLYNL
GRTGTHEIGH WLGLQHIWGP NDTGCDDSDD IADTPNQDKA SNGCPTGMVT SCNNNPTGNM
YQNYLDYTDD ACMNLFTQDQ AEYMQSILST VRQNILTTAV VCSNPLTANF EVSDTIIVAG
TTVQFQDASI GVRANEWAWI FEGGNVTTST EQNPTVRYDQ PGTYTVSLTA SFNSVTDAVT
KTQYIRVTGP EAIIYPNPAQ QQLSIEAPAS KKLQKIQIIN SVGQVILTQT VQVNFVTLSL
PNVANGIYYC RLWYQDGSFD IKKLVIAR
//
