ID   E2A5C9_CAMFO            Unreviewed;       710 AA.
AC   E2A5C9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:EFN71351.1};
GN   ORFNames=EAG_06077 {ECO:0000313|EMBL:EFN71351.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN71351.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; GL436921; EFN71351.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2A5C9; -.
DR   InParanoid; E2A5C9; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF276; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:EFN71351.1};
KW   Hydrolase {ECO:0000313|EMBL:EFN71351.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000313|EMBL:EFN71351.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT   DOMAIN          16..199
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          302..485
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          564..659
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   710 AA;  84980 MW;  DCB009ED8FF273F8 CRC64;
     MYHHIILDSQ NNITKKLILY RDATIFYNDE LDSDIHKLDV IRRIGYELVH QWFDNLISPV
     HWPDYWLNEG IAILLGTDVI NQDFEDLRMW DLFMVQIQQE ALRFDNSPRD IMKPLTSEIN
     KLSEIDSLFS FSFHIKAPVI LRMLRHFLTD QVFQRGIEIF LSKHKFSSAS IDDFWESMQS
     AHNATNMERI IVREIMNAWT KQKHYPILKV AQIYDYTNFH YVRITVENIE NHWHIPVTIT
     TQTTSNFTIH PWKFFYNWKK SNSTWFMDIA TDGHIDDWII ANLQQIDMYN VNLDSHDNIA
     KKLILYRDAT IFYNDELDPD MHKLDVTRTI GYELVHKWFD NLISPSWWSD YWLNEGIAIL
     LGTDVINKGS EDLRMWDLFV VQIQQESLRL DNFTEGVMKP LRSEINKPSE TDSLFSFSFH
     IKAPVILRML RHFLTDQVFQ NGIEIFLSKH KFSSASIDDF WESMQSAHNA TNMEKIIVRE
     IMNAWTKQKH YPILKVAQIY DYTNFHYVRI TVENIENHWH IPVTITTQTT SNFTIHPWKF
     FYNWKKSNST WFMDIATDGH IGDWIIANLQ QIGYYRVNYE LKNWQNIAKY LNSRNYSKIH
     VLNRAQIIDD AYYFLSSRKL DMSTFLDLAK YLSQETDFVA WYPMIKALEN ISSIFPISDT
     EDIDLFKVNN NRHFINKSVF HILYIRLLHI KYIKNKIVKQ FRKIYIYEKI
//