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Database: UniProt
Entry: A0A1G9UCJ9_9ACTN
LinkDB: A0A1G9UCJ9_9ACTN
Original site: A0A1G9UCJ9_9ACTN 
ID   A0A1G9UCJ9_9ACTN        Unreviewed;       521 AA.
AC   A0A1G9UCJ9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Zn-dependent amino-or carboxypeptidase, M28 family {ECO:0000313|EMBL:SDM57681.1};
GN   ORFNames=SAMN05444921_11080 {ECO:0000313|EMBL:SDM57681.1};
OS   Streptomyces wuyuanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM57681.1, ECO:0000313|Proteomes:UP000199063};
RN   [1] {ECO:0000313|Proteomes:UP000199063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
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DR   EMBL; FNHI01000010; SDM57681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9UCJ9; -.
DR   STRING; 1196353.SAMN05444921_11080; -.
DR   Proteomes; UP000199063; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd03876; M28_SGAP_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR041756; M28_SGAP-like.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Carboxypeptidase {ECO:0000313|EMBL:SDM57681.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW   Protease {ECO:0000256|ARBA:ARBA00022438};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199063};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..521
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011444289"
FT   DOMAIN          149..237
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          263..481
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   REGION          500..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  53968 MW;  557AE01CE0C79B29 CRC64;
     MNATHRRAVA TVAAAALATP LLLASASPAT AHRHDPAKGA AKDAAKLSKK LVRESSAKDA
     FKHLQKFQQI ADSTGGHRAA GSLGYDASAA YVYQQLKKAG YDVSYQNFDF IYTETQAEKL
     SVVSPAPRDI AISAMTYTKS TPVGGVRADL AAVPVDADGT TGCEPADFAS GTFTGKVALI
     QRGGCTFAAK QENAAAAGAI GAVIYNNTEG ALSGTLGGPE AGKIPTGGIT QAEGAKLAED
     LAKGPVSIDF EIRQLQEKRT TRNVIAETRH GNAANTVMLG AHLDSVTAGP GINDNGSGSA
     GLLEVALEFA KAEKRPANKV RFAWWGAEEN GLLGSEHYVA NLSDLGKKEI KLYLNFDMIA
     SPNYGLFVYD GDNSDGVGAP AGPAGSAQLE RDINEFMDRV GAPHEGTDFT GRSDYGPFVE
     AGIPSGGTFT GAEGIKSAAQ AEKFGGTAGV AYDACYHAKC DDIKNVNMKA FDVNIDIIAN
     AAGTYAHDLS SLRKPVVTVP TDGDTGSGGG LHDGHDHEVT E
//
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