ID M4YLN2_THEXX Unreviewed; 474 AA.
AC M4YLN2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:AGI48094.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:AGI48094.1};
GN ORFNames=TALC_01105 {ECO:0000313|EMBL:AGI48094.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI48094.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI48094.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI48094.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290}.
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DR EMBL; CP002916; AGI48094.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YLN2; -.
DR KEGG; tar:TALC_01105; -.
DR PATRIC; fig|1054217.5.peg.1049; -.
DR eggNOG; arCOG01518; Archaea.
DR HOGENOM; CLU_590123_0_0_2; -.
DR Proteomes; UP000012076; 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 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:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 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:0000313|EMBL:AGI48094.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGI48094.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000012076};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 474 AA; 52856 MW; 7C8AE2C5151A735F CRC64;
MVSKKDDKSA GQKLEEKLLM KSEILAASNS KLLDESMAYG EEYKTFLCHK TEREIVDYTL
PIAKKKGYKE FKYGTKYKAG DKVFFNNRGK NLILCTIGKQ PVSEGVRVSV AHADSPRLDF
KPNPLFETTD MAYFKTHYYG GIKKYQWMTI PLSLHGVVTL SNGKSVTVRI GEDAEDPLFC
ISDLLVHLAG NQVKKPMYEA IDAEQMNILV GSWPVDDEKV KEKIKLNIMQ ILNKKYGIKE
KDFLSAELCA CPAYQPRDLG LDRSMVAAYG QDDKVCAFAQ FKAEIDTVSP EFTTMMVFAD
KEETGSDGPT GMRSVFWKDF LEDLAEAYGF NVRHVLRKSI CLSCDVNAAV DPGWPEAFEP
TNCSFLGRGP VVSKYTGARG KYSTNDASAE VMGYLRRILE EADIPWQVGE LGRVDVGGGG
TIASEISVHN IDTVDMGVPV LSMHAPMEVT SKTDDYMLYK AVFAFFNSKL PKTI
//
