ID   L5JR53_PTEAL            Unreviewed;       469 AA.
AC   L5JR53;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Lactation elevated protein 1 {ECO:0000313|EMBL:ELK00618.1};
GN   ORFNames=PAL_GLEAN10018575 {ECO:0000313|EMBL:ELK00618.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK00618.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family.
CC       {ECO:0000256|ARBA:ARBA00010322}.
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DR   EMBL; KB031156; ELK00618.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5JR53; -.
DR   STRING; 9402.L5JR53; -.
DR   eggNOG; KOG2383; Eukaryota.
DR   InParanoid; L5JR53; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF040713; ZapE; 1.
DR   PANTHER; PTHR12169:SF6; AFG1-LIKE ATPASE; 1.
DR   PANTHER; PTHR12169; ATPASE N2B; 1.
DR   Pfam; PF03969; AFG1_ATPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  53164 MW;  5F43B9688D1D8C93 CRC64;
     MHRASAPPLE GGLSAGDPRG AVRCPPTFLR PPGPGAVGRT PEVVFAASGT AGAKLNAYTV
     QTPESMPPTA ATEAYLKAMA VCHGPLDHYD FLIKSHELKD DEHQRRVIQC LQKLHEDLKG
     YSVEAEGLFS KLFSRSKPPK GLYVYGDVGT GKTMVMDMFY AYVEMKRKKR VHFHGFMLDV
     HKRIHRLKQS LPKRKPGFMS KSYDPIAPIA EEISEEACLL CFDEFQVTDI ADAMILKQLF
     ENLFKNGVVV VATSNRPPED LYKNGLQRAN FVPFISVLKE YCNTVQLDSG VDYRKRRLPA
     AGKLYYLTSE ADVEAVMDKL FDELAQKQND LTRPRILKVQ GRELRLNKAC GTIADCTFEE
     LCERPLGASD YLELSKNFDT IFLRNIPQFT LAKRTQARRF ITLIDNFYDF KCQRNNQMSA
     ELNVKSPLWD DLLEGERGVW CCDRLREEQT YLPGWVVLPR TTCFKIPGL
//