ID A0A1H0W1V8_9PSEU Unreviewed; 641 AA.
AC A0A1H0W1V8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative Ig domain-containing protein {ECO:0000313|EMBL:SDP84674.1};
GN ORFNames=SAMN05192558_11722 {ECO:0000313|EMBL:SDP84674.1};
OS Actinokineospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=504798 {ECO:0000313|EMBL:SDP84674.1, ECO:0000313|Proteomes:UP000199651};
RN [1] {ECO:0000313|Proteomes:UP000199651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10655 {ECO:0000313|Proteomes:UP000199651};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNJB01000017; SDP84674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0W1V8; -.
DR STRING; 504798.SAMN05421871_10722; -.
DR Proteomes; UP000199651; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03859; M14_CPT; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR033810; Carboxypeptidase_T.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199651};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..641
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038763367"
FT DOMAIN 521..641
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
SQ SEQUENCE 641 AA; 67729 MW; 78DE554134ABCECA CRC64;
MNRRRISLTA GAAAALAVIV SMSGNPALGD GARGEERATG EYHVANVRTA QQRTAIAKTG
AAVNGTEDSR LLITATPSEV AKIRAQGFTV EAEAAPVTIQ QESTSEAAPQ DFPSSDSGYH
NYSEMVAVIN KAVADHPGII TKQVYGKSHE GRDLYALKIS DNAATDENEP EVLFTHHQHA
REHLTVEMAV YLINELTGKY ATDSRIKGVV DSREIWILPD LNPDGGEFDI STGSYKSWRK
NRQPNPGSTY VGTDMNRNWN YKWGCCGGSS GSFSSDTYRG AAPESAPEVK AVANFVRGRV
IGGKQQITVG IDFHTYSELI LWPFGYTNDD TAPGLTVDDQ RVFSTIGRAM AQTNGYTPEQ
SSDLYITDGS IDDWLWGDQK IYGYTFEMFP SGVLGGGFYP GDEIIARETS RNRAAVLHLL
DFADCPKRSI GQSCSGTGAV TVTDPGAKTS TVGTAISPVQ LQASGGTAPY TWSATGLPAG
LSLNASTGVI SGTPTAAGTF TVTATATASA GGSGSTTFTW TVTASGTCAA MTNGTDVSIP
DRGAAVTSTI DVSCAGTASA TSKVEVHIKH TWRGDLVIDL VAPDGSTYRL KNSSSSDSAD
NVDATYTVNL SAEQRSGAWK LKVQDVASFD TGNIDSWTLT L
//
