ID M1UF86_9CORY Unreviewed; 420 AA.
AC M1UF86;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=H924_06880 {ECO:0000313|EMBL:AGG66820.1};
OS Corynebacterium callunae DSM 20147.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121353 {ECO:0000313|EMBL:AGG66820.1, ECO:0000313|Proteomes:UP000011760};
RN [1] {ECO:0000313|EMBL:AGG66820.1, ECO:0000313|Proteomes:UP000011760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20147 {ECO:0000313|EMBL:AGG66820.1,
RC ECO:0000313|Proteomes:UP000011760};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium callunae DSM 20147.";
RL Submitted (FEB-2013) 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}.
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DR EMBL; CP004354; AGG66820.1; -; Genomic_DNA.
DR RefSeq; WP_015651251.1; NZ_ATVF01000004.1.
DR AlphaFoldDB; M1UF86; -.
DR STRING; 1121353.H924_06880; -.
DR KEGG; ccn:H924_06880; -.
DR PATRIC; fig|1121353.3.peg.1402; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000011760; Chromosome.
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 420 AA; 45005 MW; 97247F65CD23FD55 CRC64;
MHATDDFRSF IAHSPSSYHA ADTVATELET VGFIRQDETK TWDATPGGHF LVRGGAIIAW
WVPEDASVDS GFRIIGSHTD SPGFKLKPKG DLPNAHFQQA GVEVYGGPIF NSWLDRELSL
AGRVVLADGS VRLLNTGPIL RIPNLAIHLD RTLNSTFALN PQHHLQPIFA VGDPHVSIME
VIAEAADVES ADILSHDLIT VDVQEAEVFG AHGDFFAAGR LDNLSSVYPS LKALIKAASG
EDNSSDILIM AAFDHEEVGS NSPTGAAGPL LEDVLIRTAT ALGADEETRR QMFQRSSMVS
ADAAHSIHPN FPQKHDPVNY PVIGRGPVLK VNANQRYASD ALSSGVWLRA CQMAGVPHQV
FAGNNEVPCG STIGPISATG LGISTVDVGI PLLSMHSARE MAGVKDLLWF EKALESYLVN
//