ID Q0YQD0_9CHLB Unreviewed; 1656 AA.
AC Q0YQD0;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=VCBS {ECO:0000313|EMBL:EAT58497.1};
DE EC=3.4.24.40 {ECO:0000313|EMBL:EAT58497.1};
GN ORFNames=CferDRAFT_1073 {ECO:0000313|EMBL:EAT58497.1};
OS Chlorobium ferrooxidans DSM 13031.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=377431 {ECO:0000313|EMBL:EAT58497.1, ECO:0000313|Proteomes:UP000004162};
RN [1] {ECO:0000313|EMBL:EAT58497.1, ECO:0000313|Proteomes:UP000004162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58497.1,
RC ECO:0000313|Proteomes:UP000004162};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM
RT 13031.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT58497.1, ECO:0000313|Proteomes:UP000004162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58497.1,
RC ECO:0000313|Proteomes:UP000004162};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Chlorobium ferroxidans DSM
RT 13031.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase M10B family.
CC {ECO:0000256|ARBA:ARBA00009490}.
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:EAT58497.1}.
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DR EMBL; AASE01000018; EAT58497.1; -; Genomic_DNA.
DR Proteomes; UP000004162; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR040853; RapA2_cadherin-like.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR010221; VCBS_dom.
DR NCBIfam; TIGR01965; VCBS_repeat; 10.
DR Pfam; PF17803; Cadherin_4; 7.
DR Pfam; PF00353; HemolysinCabind; 3.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EAT58497.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004162}.
FT DOMAIN 1007..1189
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 1656 AA; 170664 MW; 495E8072CE1AD452 CRC64;
MIKGNESPMS FIKQADNVGR TGTFTIGTNG VWSYTANSAF DSLNVRESIP ERFSVTLTDG
KTQVERVQIT GTNDAAVISG DVSTTIAETD EALTATGQLA VTDIDNPSLF VAQIETEGIH
GKFSIDESGL WSYIANSAFD ELNEGESLTD SFIVTAADGT TEVVRVTITG TNEILPAGGS
VAESLPVLSS SGNKSVAIIT GDINASALET NAVITATGNL SVASNPLPFV AENGRVGSTG
IFSIGADGLW NFTANSAFDG MNVGETVKES FTVSTVDGMT EVVTVTITGT NDVAVISGDF
NATVLETNAL IAVTGRLSAV DIDNPAIFSA QSGIKGMYGV FDMGSDGAWS YRAGSAFDSL
NIGDTLTESF TASTIDGTSG LVTVTIAGTN DAAVITGDSS ASYVETNAAM TVMGRLLVND
VDNPAAFVAQ SDSKGRTGTF SIGTDGVWSY TANSAFDGLN VGGKVKDLFS VFTSDGTSQV
VSVTITGTND AAIITGDLSP TVFETNTAVS LTGRLRAMDM DNPSIFVAQN GITGLTGTFS
IGMDGAWSYR ANSAFDSLKV GETVTESFSV STVDGTSELV TVIITGTDDA SVVTGNFSAS
VAETDAPITA NGTLTVSDID SPFAFVAQSG TKGTLGLFSI GIDGAWDFRA SSAFDNLNVG
DTLTESFAVT TIDGTSDLVT VTITGTNDAA VITGSLHASE DESDAMITAT GTLHATDVDS
SSAFIAQTDV AGTNGTFSIG TDGVWIFSAN SAFDGLNVDS SVTESFTVTT ADGTSEVVTV
TINGTNDAAV ITGDFSATVA ETNEASTATG HLTVTDLDNP AIFLIQTDNA GFNGSFSIDS
DGLWSYSANS AFDYLNDGDS LVESFIVESA DGTSQIVMLT IMGTNDAAVI TGDFSASVDE
TNVPITATGH LSVTDVDNPA LFVVQTDTGG INGSFSIDAA GLWSYAANSA FDELNAGDTL
TESFTVSTMD GTTEIVTVTI TGTNDALTTS QIVTQLTTSW GSGLTGYTFT WPADLTSISY
AINEGTPTNV DGYTPSEGGT SLVQMSALQV ATARLSFQLL DDIMAKSSGA DHRLVQIADP
SANITLNYSS NTGGGTYTIS FGTVDTVTQS FSITAEQIWL SSAWSSNSDI GMSLGSYGLF
TMIHEIGHAL GLSHPGVYDA GNGGTITYQN NAAFAEDNRK YTVMSYFGGY LPGYGWYPDG
TYSSFIFPQT PMLYDIAAIQ ALHGADTVTR TGDTIYGFNC NLASTDAERP IYDFTSNATP
IFTIWDAGGM DTIDCSGYTT QQIINLNPGT YSSLGGMTEN VAIAFDCTIE RAVGGSGNDV
LIGSAALNYL NGGNAGDFYI VNRAGDHLAA EFADTGTTGS DEVRFASTIE HDTLTLFAGD
TGIERVVIGT GVGISGVTTG TTSLDVDASA VLNPIVITGN AGANKLTGTT YNDVLYGGKG
TDLLNGGNGS DIYHIFSADE HLSAEFSDTG TTGSDDVRFG STIANDTLTL YAGDTGIERV
TATGTATLNI DASGVLNGLL LTGNAGSNTL TGTAYCDTFT GGSGADSFVF TYQLQPVVNK
DTIIDFQSGS DVLAFSKGSF TGITSSAGGL LSSAEFWSEA GATVGHDSDD RIIYDTATGN
LYYDDDGNGS ANARLVALIG TTAHPALLYT DISIIS
//
