ID A0A1F1L5R3_9CORY Unreviewed; 424 AA.
AC A0A1F1L5R3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=HMPREF3067_01920 {ECO:0000313|EMBL:OFS23208.1};
OS Corynebacterium sp. HMSC04H06.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581050 {ECO:0000313|EMBL:OFS23208.1, ECO:0000313|Proteomes:UP000177657};
RN [1] {ECO:0000313|EMBL:OFS23208.1, ECO:0000313|Proteomes:UP000177657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC04H06 {ECO:0000313|EMBL:OFS23208.1,
RC ECO:0000313|Proteomes:UP000177657};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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:OFS23208.1}.
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DR EMBL; LWPR01000016; OFS23208.1; -; Genomic_DNA.
DR RefSeq; WP_070768050.1; NZ_KV823406.1.
DR AlphaFoldDB; A0A1F1L5R3; -.
DR STRING; 1581050.HMPREF3067_01920; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000177657; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000177657};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 424 AA; 45572 MW; A00CECD55035E800 CRC64;
MTSTQDFLDF IDASPSSYHA AANVERELVA AGFQRQREED AWDVSPGGHV VVRGGAVMAY
IVPPRLAEGA GEKLRGFRIV GSHTDSPGFT VKPEPDFQQA GWDQIGVEVY GGPILHSWFD
RELTLAGQVT LRDQSTHLVN TGPILRIPNL AIHMVRKDEF TPDRQFHLQP VWQLSANGKY
ASLGEYVAEQ LGVQATDIAA FNLITAAAQP AGLFGPANEF IAAGRMDNLS SVHASLEAFK
AAAQDYDGSD VLVMAAFDHE EVGSNSRYGA AGPILADILQ RTAVALGSTG DDLFRVFAHS
HCVSADAAHS VHPNYAQKHD PHHQPLIGHG PVTKINGKQG YASDSESITR WENACRRAGV
PFQRFVANND VPCGSTIGPI TATRLGIETV DIGVPMLSMH SAREMVGVSD QATLFGALLE
YLVG
//
