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Database: UniProt
Entry: E9B2P8_LEIMU
LinkDB: E9B2P8_LEIMU
Original site: E9B2P8_LEIMU 
ID   E9B2P8_LEIMU            Unreviewed;       404 AA.
AC   E9B2P8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   03-MAY-2023, entry version 52.
DE   SubName: Full=Putative ADP-ribosylation factor GTPase activating protein 1 {ECO:0000313|EMBL:CBZ29511.1};
GN   ORFNames=LMXM_31_1230 {ECO:0000313|EMBL:CBZ29511.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ29511.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|EMBL:CBZ29511.1, ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29511.1,
RC   ECO:0000313|Proteomes:UP000007259};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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DR   EMBL; FR799584; CBZ29511.1; -; Genomic_DNA.
DR   RefSeq; XP_003877967.1; XM_003877918.1.
DR   AlphaFoldDB; E9B2P8; -.
DR   GeneID; 13453556; -.
DR   KEGG; lmi:LMXM_31_1230; -.
DR   VEuPathDB; TriTrypDB:LmxM.31.1230; -.
DR   OMA; CDVMHGT; -.
DR   OrthoDB; 389572at2759; -.
DR   PhylomeDB; E9B2P8; -.
DR   Proteomes; UP000007259; Chromosome 31.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   CDD; cd08830; ArfGap_ArfGap1; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   PANTHER; PTHR46395; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR46395:SF1; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 1; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          12..131
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          152..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  42983 MW;  495110AF0DF4B339 CRC64;
     MAGRHYVSPE DERAFVSIFA KDPECSECFE CGAPSPQWCD VMHGTFICLN CSGQHRGLGV
     HLSFVRSSTM DGWMKWKPEK LRQMELGGNR RARLYFEAHK VPKTPLKARY ESLPALRYAD
     MLESEALGRP FNEASWQPPA WYTRLKAAAS LSGPSPTSSY PQTDPSRFAG VGSNGHPHVM
     PGSGGGDSEW YSALYSGWSA VSQKTAELAQ HATKAVQSAD VEGMRSTLAQ KWAGVSATVS
     TYAADLQQRI AQGSARDNDD GLDRMIQNAR QAQRESGVDS SAAVQRRYGH IQGSSGDGPG
     LGVAVQAKPV GAASLESSTV YQGRVLWQSA SASSPTESAT ASVSSGWGSP TRASPSTALP
     QIQPTTSRPV NPLGGGGGGG GGSSSPPASQ LTKKDEWAWD DENI
//
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