ID A0A258YVI9_9PROT Unreviewed; 374 AA.
AC A0A258YVI9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=B7Y21_10720 {ECO:0000313|EMBL:OYZ56664.1};
OS Hydrogenophilales bacterium 16-61-112.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970519 {ECO:0000313|EMBL:OYZ56664.1, ECO:0000313|Proteomes:UP000216368};
RN [1] {ECO:0000313|EMBL:OYZ56664.1, ECO:0000313|Proteomes:UP000216368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-61-112 {ECO:0000313|EMBL:OYZ56664.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYZ56664.1}.
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; NCHD01000060; OYZ56664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258YVI9; -.
DR Proteomes; UP000216368; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR Pfam; PF01400; Astacin; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
FT DOMAIN 54..206
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 41717 MW; FD337BB9A91A5173 CRC64;
MSDSPKAAKP LSKAKPSSKQ AEPAAMRYCS QPVQHPRQFD PAVDALRARA IINGGKKWVN
GTQLTYYCYK SGDSVPAAWH GNAADIREVG AAFQAWFKLG IGISFKEVSR PEDATIRIGF
DSDDGSWSYV GRDILNIRDP FSRTMNFGWA LNTRYGRDTA LHEIGHAIGL EHEHQNPYAG
ITWDTDAVKN YFQGPPNNWG MQEIEWNILR KIPPAEVKGT RWDPDSVMEY HFGSGLIIEP
AAYRNGLMPK GGLSKADKSW IVESYPGTKP KEVIPALEVG LSQRLAIKAG QSRVFNFTPK
RTRTYRIGTF GTSDTVMVLF EIAPAGNVQI AGNDDSGTDL NARINMRLIY GRRYQIGIRL
YYSDMASETS IMVW
//