ID Q4UIZ5_THEAN Unreviewed; 478 AA.
AC Q4UIZ5;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=TA16610 {ECO:0000313|EMBL:CAI72944.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI72944.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI72944.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
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, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; CR940347; CAI72944.1; -; Genomic_DNA.
DR RefSeq; XP_953622.1; XM_948529.1.
DR AlphaFoldDB; Q4UIZ5; -.
DR STRING; 5874.Q4UIZ5; -.
DR GeneID; 3864019; -.
DR KEGG; tan:TA16610; -.
DR VEuPathDB; PiroplasmaDB:TA16610; -.
DR eggNOG; KOG2596; Eukaryota.
DR InParanoid; Q4UIZ5; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000001950; Chromosome 1 part 1.
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:UP000001950};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 478 AA; 52874 MW; 2B5EF33F54E1F9A1 CRC64;
MSLNSCKLKE AQVLARKFVD FLNATGSPFH TVKQLSLYLT NHLPIKHLNE LRCVTEQFFS
ENWKLENGQS YYVTNNNGTM MAFNIGKKFD PSKGGLILVC SHTDSPCLKL DFKCHVNNKG
FNQLSVTTYG GGLWHTWMDR DLGLAGKVVV KSNGKLEEKL LHVQKPLILL PNLAIHLQNS
TEREALKLNK DNHLKPLIST EVVHNLNSTQ TEPLLKLVSS YHSLAIHLYY IVNIITVIAI
CFSELKCEVE DLVDFELCLM DSNPSCLSGV YEEFVSSGRL DNLGSCFGSI SAFTDFVLNQ
GEDNDAVVVT VSYNYEEIGS SLSYGADSNV TFLWLEKLFG ALGCSLMETR DRALVVSADM
THGVHPNYSE KHISTHSPAF HAGVVLKWNV NGRYATETHS SSLLRTAAAS AGVPLQEFRV
GNETPCGSTV GPILGSRLCV PVADVGFPQL AMHSCREMCS TVDLLNFKLL LQVLLFMV
//
