ID F4WXD0_ACREC Unreviewed; 895 AA.
AC F4WXD0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Leukotriene A-4 hydrolase {ECO:0000313|EMBL:EGI61096.1};
GN ORFNames=G5I_10614 {ECO:0000313|EMBL:EGI61096.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI61096.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; GL888424; EGI61096.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WXD0; -.
DR STRING; 103372.F4WXD0; -.
DR eggNOG; KOG1047; Eukaryota.
DR InParanoid; F4WXD0; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; 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; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 4.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 3.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGI61096.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
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:UP000007755};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 72..180
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 279..326
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 376..533
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 716..825
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
SQ SEQUENCE 895 AA; 105440 MW; E145A124B0DD1375 CRC64;
MDLPCVDPYS YANPDIYQLN EDKMDVSEYF SSDKLKYDVK QTHRSVESEF VIIQIPQKYR
GHFTEFKYKY YKRPYQIKYN CIIKIIYETR KDSPAMYWLR SDQTSDGSHP FLITNNKFTY
ARGIFPCQDS PSIRFTFAAE IFVPNNINSV IICGRTCKRI TEDGCLHKFT FYETFPMPAY
AMIIVVGSLE TIHLDLQHNV SLWAEKKYIE QSKSCFANFH HILTIAKELC GPLYRRKLRE
DVRQYNICVL PPNIPEIELQ CFSMIYVSST LLNEDFFWIF CTVAKKVAQN WAGGLVTCKN
FEHLWLNKSF STFISRKIIY CMYKQNIIPY AMSFLERITA YTLINKFYRL QNYGGYIVCF
HLTSKLVEID IARIIHTHLE LFVDFNETVL RGTAILFIEM EPEYDEIILD IYQLNEDKMD
VLEYFSSDKL KYNVKQNRSV GSKSVIIRIP HKYRGRFTEY KYCNKPYQID YNCAILIMYE
TRKDSPVLYW LRSDQTSDGT HPLLITNNKF TYARGIFPCQ DSPSVRFTFT AEIPQKYRGR
FTEFKYKYCN EPYQIDYNCA ILIMYETRKD SPVLYWLRSD QTSDGTHPLL ITNNKFTYAR
GIFPCQDSPS VRFTFTAEKL KSILTKWIYG PNLRHMPIED ICTLYPELHC LMTKSQGYLL
ATRWITTEAF NNFALLLNEL KFCNNNLERR EFLFHLYASN AILPVAKLWW LRHMFPLDEQ
TCENRYAILI TYETRKDSPV LYWLRSDQTS DGTHPLLITN NKFTYARGIF PCQDSPSVRF
TFTAEISVPN NFNTVIICGR TCRLIINDGD RHIYMCFEMF PMPSYAMIIM VGSLETIHLD
LQHNVSLWAE KKYIEQSKSC FANFHHILTI AKELCGPIYI NDKERYTSMG QGAVS
//
