ID A0A0A0BP52_9CELL Unreviewed; 667 AA.
AC A0A0A0BP52;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase M14 {ECO:0000313|EMBL:KGM08874.1};
GN ORFNames=N868_05885 {ECO:0000313|EMBL:KGM08874.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM08874.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM08874.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM08874.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM08874.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM08874.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:KGM08874.1}.
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DR EMBL; AXCY01000146; KGM08874.1; -; Genomic_DNA.
DR RefSeq; WP_052426540.1; NZ_AXCY01000146.1.
DR AlphaFoldDB; A0A0A0BP52; -.
DR OrthoDB; 2874181at2; -.
DR Proteomes; UP000029839; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06228; M14-like; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR11705:SF119; OS02G0119300 PROTEIN; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00327; VWA; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029839}.
FT DOMAIN 471..656
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 122..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 68866 MW; 44E8F172C2544685 CRC64;
MYLDATGIGS ALAALAAAYP TTSELVTTPH PTHEGRTVTL LRVGGRGPHD ADGVLLLGGV
HAREWVPPDA LVSFAADLLE AYATGTGLAY GGASYGAAQV RRVVRTLNLF VLACVNPDGR
AHSQTVDPQW RKNRRPAPAG ATDPACVGVD LNRNFDFLWD HLARFAPDSG VSASADPCHP
TLYRGPSPAS EPETRDVVWV LDTFPRIRWH VDVHSAVPVV LHSWGSDENQ STDPGESFLD
PGLDAVRGRV GDGIGEYLPA QDAAVVVDLA GRIDAGVTAA HGAVYGVEQA MTLYPTSGAS
DDYAFSRHRA VVGTTKVLAW TVECGTSFQP PWSVAEQVVR EVSSGLLALA LAAHEVTDGL
AATLRTPSVA FTHVAEATTT ARAVVVECSG DLDVHLEVTA LSGPFGLPLG PTTTVPAPGR
GATAEGRVWL TWDAGPAGTT ASGSVTVRCV ETDESWTVPV TADAVPRPTT ALALVLDRSG
SMAWDAGDGR SRVEVLREAV SVAVELLRPD DGVGVVRFHH DADTVVPVQQ AGPETFGPGR
SAALAAVAAH VPDPAGATSI GDGVTTAATQ LAAAAGYDGT AMVVLTDGRQ NAPAWVADVA
GSIDGRVFAV GLGAPEAVDP ATLTALVDGT GGWVAVSGVL SVDERFVLAQ YLLQVLAGAT
NDQVVIT
//
