ID A0A1M4RVZ7_9ACTO Unreviewed; 470 AA.
AC A0A1M4RVZ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=ACGLYG10_0362 {ECO:0000313|EMBL:SHE24162.1};
OS Actinomyces glycerinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1892869 {ECO:0000313|EMBL:SHE24162.1, ECO:0000313|Proteomes:UP000184291};
RN [1] {ECO:0000313|Proteomes:UP000184291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Strepis N.;
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQTT01000001; SHE24162.1; -; Genomic_DNA.
DR RefSeq; WP_073327370.1; NZ_FQTT01000001.1.
DR AlphaFoldDB; A0A1M4RVZ7; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000184291; 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 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:UP000184291};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 470 AA; 48764 MW; CA42785C6A9AE42C CRC64;
MTDPETAPAL RDDDAYADSI IDFVTASPTS YHAAAEVARR LDAVGLTAVD EREPWGTDLP
RRGYTRRDGA IIAWLLPEQL DAAAGLRIVG AHTDSPALRL KPRAAMVRDG VQVLNVEVYG
GPLLNAFLDR ELGLAGRLTT FDGTTHLVRT GPIARVAQVA PHLDRSVNES LHLDKQAHLL
PLWTLTSGKA SDAAAAAGTA PAGAATDAAG PGNDAASALP GPDAPEHYLC ELAGIDPADL
AFCDILTYPT EAPARFGRNG EFLASSRLDN LSSVHAALVA LEALAHEGAD AGIAGPIVFI
ANDHEEVGSG TRTGAAGPFL QTVLSRLAGT MGVTGDAYAA LLARSVCVSA DAGHAVHPNY
PQLHDPAVRP VLGGGPLLKI NAQQRYATDA TAVAAWARAC RAAAVPSQDF VSNNAVPCGT
TIGPLTATRL GIPTVDVGQG LLSMHSQREM CAVSDGVRLA RAMHAYWQGA
//