ID   A0A1V2Q680_9PSEU        Unreviewed;       590 AA.
AC   A0A1V2Q680;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:ONI83594.1};
GN   ORFNames=ALI22I_34545 {ECO:0000313|EMBL:ONI83594.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI83594.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI83594.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI83594.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI83594.1}.
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DR   EMBL; MTQP01000067; ONI83594.1; -; Genomic_DNA.
DR   RefSeq; WP_077009741.1; NZ_MTQP01000067.1.
DR   AlphaFoldDB; A0A1V2Q680; -.
DR   STRING; 1933778.ALI22I_34545; -.
DR   Proteomes; UP000188617; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000834; Peptidase_M14.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 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; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:ONI83594.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..590
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039070798"
FT   DOMAIN          472..590
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          252..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  62067 MW;  F678B564F813F2BF CRC64;
     MKSRRRSLLA LAIAGVAAAA VVTGGTPGTA GPAPEVAAVQ AGPTYVYKVH APLGAAAQNL
     LGRGFDVLED RDGDYLFVLG DATTGQGLKQ AGFTAVIDEV LPAPEWQPPA KKSQSPTFEA
     ADINETYYGG YRTINAHWSH LDLVGQQYPA LTTLVDYGDS WRKTQGSGGY DLRAICITKK
     NAGDCALSPT APKPRFFVMG QLHARELTTG DMAWRWIDHL TTGYGVDAEV TALLDTTEVW
     VVPIANPDGV NIVQQGGNSP RYQRKNANTT NGSNCSGTSS SQVGVDLNRN TDSHWGGAGT
     STDPCAQTYK GPSANSEVET RSLQSLWRNL YRDRRGTGTT DAAPADTTGV VVSMHSYSNL
     ILFPWGWTTA SKAGNDASLR GMAADLASLA GGWQYGQPGE VLYNAAGATD DWVYDDLGVA
     SFVWEVGPSS GTCSGFFPAF SCQTSTFWPK VKPMLMYAAK KATNPYGGGG GNPPVGCAKA
     TNDTDVAIPD NGAAVTSTIT IAGCAGNASS SSQVEVHIVH TYRGDLVIDL VAPDGTAYRL
     KASGNDSADN IDTTYTANVS SEARNGAWTL RVQDVASADT GRINSWSLTV
//