ID A0A1G3MNN6_9SPIR Unreviewed; 439 AA.
AC A0A1G3MNN6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=A2004_09485 {ECO:0000313|EMBL:OHD31609.1};
OS Spirochaetes bacterium GWC1_61_12.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802180 {ECO:0000313|EMBL:OHD31609.1, ECO:0000313|Proteomes:UP000178922};
RN [1] {ECO:0000313|EMBL:OHD31609.1, ECO:0000313|Proteomes:UP000178922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHD31609.1}.
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DR EMBL; MIAU01000068; OHD31609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3MNN6; -.
DR Proteomes; UP000178922; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 439 AA; 46757 MW; 895D18FC4C29764B CRC64;
MPTQHGRALC EFIDASPTAF HAVDSAEAML KAWGGQRLSE KEVWDLQPQQ LYYLVRDDAS
LIAFRLGTAP LATAGFLLAG AHTDAPGLRA RIDKAVAAKG LERVAVEVYG GPINATWLDR
PLSLAGRVLL QAAAGRVVSR LVNFSRPLAI IPNLAIHLNR DLNKGFEYPM HTAMLPLVAA
NGAAPAGEGV QGSWLLSALA RELAVDPAAI LSAELTFYEA APSVIFGEHD ELLAASRIDN
LEGCHAILSA FCACRATAHT QVAVLFDNEE IGSTSTRGAN SALLRDVLER IVLAQASTAQ
DFYRAAASSL LLSVDGAQAF HPGYADKFDP DYAPVLNKGP AIKLNANIRY ATEAKGEAYI
RSLCTRHQLP CQRFVMRADL SPGSTIGPMT SANTGIRTID IGLPMLAMHS VRETAGTVDH
DSLIALLQAA YMEGPAVAD
//