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Database: UniProt
Entry: L0AX87_THEEQ
LinkDB: L0AX87_THEEQ
Original site: L0AX87_THEEQ 
ID   L0AX87_THEEQ            Unreviewed;       893 AA.
AC   L0AX87;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Alpha-aminoacylpeptide hydrolase aminopeptidase, putative {ECO:0000313|EMBL:AFZ80197.1};
DE            EC=3.4.11.2 {ECO:0000313|EMBL:AFZ80197.1};
GN   ORFNames=BEWA_030500 {ECO:0000313|EMBL:AFZ80197.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ80197.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:AFZ80197.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:AFZ80197.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; CP001669; AFZ80197.1; -; Genomic_DNA.
DR   RefSeq; XP_004829863.1; XM_004829806.1.
DR   AlphaFoldDB; L0AX87; -.
DR   STRING; 1537102.L0AX87; -.
DR   MEROPS; M01.005; -.
DR   EnsemblProtists; AFZ80197; AFZ80197; BEWA_030500.
DR   GeneID; 15803606; -.
DR   KEGG; beq:BEWA_030500; -.
DR   VEuPathDB; PiroplasmaDB:BEWA_030500; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   OrthoDB; 3256841at2759; -.
DR   Proteomes; UP000031512; Chromosome 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; cd09600; M1_APN; 1.
DR   Gene3D; 2.60.40.1840; -; 1.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR038438; PepN_Ig-like_sf.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR012779; Peptidase_M1_pepN.
DR   InterPro; IPR024601; Peptidase_M1_pepN_C.
DR   InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR   InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02414; pepN_proteo; 1.
DR   PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR   Pfam; PF11940; DUF3458; 1.
DR   Pfam; PF17432; DUF3458_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:AFZ80197.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFZ80197.1};
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:UP000031512};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          102..215
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          254..468
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          473..567
FT                   /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF11940"
FT   DOMAIN          572..889
FT                   /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17432"
SQ   SEQUENCE   893 AA;  100726 MW;  8EC488E42CC7351E CRC64;
     MATTTSTATD ASSVTLKPVK QFVEIFRKDY KPPEFDIENV FMTFKLHETE TKVTSELLMR
     RRPNTGPGNL VLHGDELVCN FISVDGLELS NTPMSGYSLD IDGNMTIPAS FLPKDDSKTF
     TVKTVVTINP KDNLKLCGLY KSSKMFCTQC EPHGFRRITF FLDRPDVLSS YKVRIEADKA
     LYPVLLSNGN KVAAGELGES HFAEFVDPFP KPSYLFALVA GNLSSISSTY RTMSGRDVLV
     QISAEPEDCG KLHWALESVL KSMKWDEEAY GREYDLDVFH VVSVRDFNMG AMENKGLNIF
     NTALLLADVN TTTDAEFVRI MSVVGHEYFH NWTGNRVTCR DWFQLTLKEG LTVFREAEFC
     GTVSSKLSNR IKDVQYLMAV QFAEDSGPMA HPIRPESYIS MDNFYTSTVY DKGSFVIGMY
     KTLLGEEGFR KGMDLYFKRH DLCAVTCDDF RAAMADANGR DFTQFERWYA QSGTPVVEVL
     SAGLTADGFK VHLKQSTPPT PRQEFKLPFH IPIKVGLIGR VSKKDVLDGS TVLELVEDEQ
     EFIIPGVKED CVLSINRDFS APIKVKFEQS EQDLTFLMQY DSDGLNRWDA SQRLSTKFIL
     ARATGNLDAP IGETYLDAFK SLLESDMEQS EKALCLALPD TEILASKMSP YDPGLLHKAL
     RSIKVELSKK FYPQLLELYK KLTLAPGAKD TLDKEDMARR SLRNTLLSYL VASRDAEAVK
     LATEHYKSAK TMTDKYSSFI QLMHMTFDGK QDIVDDFYAF ANGDAQVVDK WFKAQALSEA
     EDSLERVKAL CSHKDFTMSN PNRFNSLVTV FTYSINFHDI SGAGYKFLAD LIIEVDKINP
     QVSARCCNKL LKYSIFDNVR KELMKSHLQR VFNTPGISPN LYEIAQKGLE FTS
//
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