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}.
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; 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
//