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Database: UniProt
Entry: L1LCJ2_THEEQ
LinkDB: L1LCJ2_THEEQ
Original site: L1LCJ2_THEEQ 
ID   L1LCJ2_THEEQ            Unreviewed;      2566 AA.
AC   L1LCJ2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Cytosol aminopeptidase family, catalytic domain containing family {ECO:0000313|EMBL:EKX73061.1};
DE            EC=3.4.11.1 {ECO:0000313|EMBL:EKX73061.1};
GN   ORFNames=BEWA_016220 {ECO:0000313|EMBL:EKX73061.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX73061.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:EKX73061.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:EKX73061.1,
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   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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:EKX73061.1}.
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DR   EMBL; ACOU01000004; EKX73061.1; -; Genomic_DNA.
DR   STRING; 1537102.L1LCJ2; -.
DR   MEROPS; M17.008; -.
DR   EnsemblProtists; EKX73061; EKX73061; BEWA_016220.
DR   VEuPathDB; PiroplasmaDB:BEWA_016220; -.
DR   eggNOG; KOG2597; Eukaryota.
DR   OrthoDB; 2899215at2759; -.
DR   Proteomes; UP000031512; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:EKX73061.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EKX73061.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1442..1463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1475..1495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1937..2118
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00883"
FT   REGION          2339..2363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2346..2363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2566 AA;  289098 MW;  31EC55A920AF7915 CRC64;
     MAKEEERRDG LFFDSLTYFL VGLSVALIYS FADNDHFMFY KVFREAGIHV DFPHYYTRQL
     VVFWGFVASF TFMFVGVFNK KICTFVGWLV PLSYLYIISK VTEYGSVKFG TGMLRAIAVT
     SIVSHIFQTC FVFQIFEETE GLFQRLLSFV GGYFLGYPVV TRLLLRRVLV DGMMDSASIG
     DDLFHFCTTL FFITFTMAAC LTYLFYGMTG GMNTHYWLPA FSPSMGDKIS LGTCVYLWIL
     NPVCISILPQ TLMEQSEYHN HVFIQRVTFA IALLAIPSVV GSMDVSMRCI LTLWKKRTLR
     YLEGLKAAIM VSEELNEMVE EDGREESPLS IVYNSSDIKV PSHIDTWSSI NCDSFSDWEH
     RDVETRDSIL SAILILDLLI KLENTLELGL VEDILKLYCS SKTKDPLVTC TVLLTDNKQV
     LLTVLSRSMG MSKGLLTQVE KIPNCYNGGF GDSTKRCCFK KGVCKGTSLA GTTSNEGTEN
     KTCDCCCPVS IAEIRDFVRE SVSSTEDSIC TMVTRINADT ILSSMEASDL TLDSAKVCVA
     VLKAYYQSCI WLLISILCIE EAILLAVWFC KLCELCKNIC KIIDEKTPKC QCINKSKEGT
     AVTIKTCSVT TLENFDDCDC LCIVSYYGIR TSVETIMTRL HCLRTELVTR ANTTCTFQKV
     ETSDLASEAY LLDSIKAAII LFFGLDSVYK FIVETFKDAC WCCHKDKDPL YPAILSCLLV
     CYRLCSRLFR DASEGTKILE DALLWYKCIF AAKKSSIANV PTKNVENKVE EVKGDKEVKT
     EDCEGGAVAK TRNLKLTITS FETFVKSAQT SLSYFYRTNN RDGEGYAVYY AINVDKTKKA
     VKYLSRLAMT DQKNYTLSSK NLVLREGMSK SGFSSGSCVN IIEDKAKLED QKKESPCKCF
     SSEGEDICAS CEKGEQCNGC KNCECKCKCP ENEGCPCGKT QDKSCKDNVF TRLSQIIECK
     CGTEEKEKKC SNCFNKLCSS LSNLTNKISE VSGSKKEEEK KECEHPGKCG GICCQTRRFS
     HFLKTYVISV FRDIYKELNC KEIKCKCCPC CKKNGELFKC KCQCKEDKKE KECGCKCNCS
     DTEGCSSEGA ECKCECRCEL CWKNFFRCFV ICGLKCGDQC KSEGKGCCKC CCTKTGQEQC
     KCENSHKDDG KCTHKCENCL LCLYTTNMFF CSKCCSQQSE TECKKSAISC KCTCGTGTDK
     CCCKEIAEDK KKEGELASLK LDCCCGDRLG CSIDKITCLL KCFETELPGL YCLASKLDCQ
     LFQFCEQLCS VLDTLEDVKF VLEKAIKIVE CRITKVKCMI KCYSAKFKSL KEQIESIDKK
     DEMYPQVVDL VKKTGKFAVL VTSYSPEIEA TYMKTDFHSE LLKSTTQNLA EVAMRVEDTS
     QLAASTGRSR VALLADSKTV QVDAPNKSEK DNSSILKEYI FIVCRIIFLL LRFQILDPNR
     LWLVKVFTVA FSILSAVYLN LFITELSSDL GKHTGYSINL ILLCGVGTNF IYSWLFHLFD
     YVSIVYPFGN IVSKLETSNP SVDYGKSRYS MFISLISSLR TEFNSIFGIF SDLDTTSSYS
     GIRQNVYPFS TMSKSLISSF RGTLDFTPIL NGPNRSVSAI MDHISFTLLG CHSDDLLTKS
     SGYFGDLNRE MLWHSWYANT VITDTTLFYY YLRRSILFEM SEIARLRPVD KPFSRGFTNS
     RQLWKHFGKI QVDLSFNASL KSPEIEIPRS RHQLNLLRER LYQEYRQKWL VYQLRATKSL
     VNVPLDEHSS TEDLPFLYIK ELDTVHLTAN SLDKLDKKYS DVYRGTKINN CKVLKKEIKT
     WRSSKLGFCE TLSDEGECKR AVNTAVKSLE RFFDTCEDHK PVKDMIEYIT STDYYSTYTH
     GDSDLDTDHK MALFDLTFHQ DGLENNYRIF KGFKNSISHT LDHQLEIAKR NKTTSLIPLG
     IYTLHYGLQI SHNTLEQIEK GLALEFKVLE KDECEELGMG AYLAVSQGSV HPPKFLHATY
     KSDGDIKKKI AFVGKGIMFD AGGYNVKNAT TMIHLMKLDM GGMATVFGAA EAIAKLKPKH
     VEVHFISATC ENMVDANSYR PGDIVTASNG KTIEVINTDC EGRMTLADAL CYAESLGVDV
     VLDTATLTGA QIVALGGDNV QQDENGYFYN SDDGQVNLTE DWYPDPEGIY RKFTHTPKGG
     SIKEILHKGS ALSGINLSSH TSVSVYYWTL DTDYSQPLLI QLGEGINEYY IRSNDDNWTK
     YHDSNSLQKD LDKQNCTRNR AHIVLISDKS DGYQCPGCDT QKINVLTSSP SGYNSHRHSI
     GYSSSISVTT FKDDKNGQVG LPPVKDAQYV IVYRRKSGDT NPLLIYYKQD EEKWFRRNTS
     DGNTWSEVSK DKKPTNPNED TDGKIKDLLQ LSEYHPQITL DLSTSATNYS DSNTGIHITV
     RSSPVEGGYS EFEHSLFGGL FTVKSVMHGT TPLTGITSDG QLDSVTAYYY GDHPSEEKRL
     LLVELRSRGG IKYQYFHRET KDAKDWKEYS ISDQESTRLQ GKYLKTELDK LKKVQFPSGK
     STLRKVLEGC GETGAAGGVG AEAYNFFFNP DKSATRQIIR LLTRLL
//
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