ID A0A091MJF9_9PASS Unreviewed; 740 AA.
AC A0A091MJF9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=ARF GTPase-activating protein GIT2 {ECO:0000313|EMBL:KFP75708.1};
DE Flags: Fragment;
GN ORFNames=N310_02345 {ECO:0000313|EMBL:KFP75708.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP75708.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP75708.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP75708.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK829883; KFP75708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MJF9; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR047161; GIT-like.
DR InterPro; IPR032352; GIT1/2_CC.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR PANTHER; PTHR46097:SF4; ARF GTPASE-ACTIVATING PROTEIN GIT2; 1.
DR PANTHER; PTHR46097; G PROTEIN-COUPLED RECEPTOR KINASE INTERACTING ARFGAP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF16559; GIT_CC; 1.
DR Pfam; PF08518; GIT_SHD; 2.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00555; GIT; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 1..107
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 149..181
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 361..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..461
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP75708.1"
FT NON_TER 740
FT /evidence="ECO:0000313|EMBL:KFP75708.1"
SQ SEQUENCE 740 AA; 82551 MW; C39F26DE72F5C1C8 CRC64;
DPCWASINRG ILICDECCSV HRSLGRHISQ VRHLKHTPWP PTLLQMVETL YNNGANSIWE
HSLLDPASVM SGRRKASPQD KVHPNKAEFI RAKYQMLAFV HRLPCREDDS VTAKDLSKQL
HSSVRTGNLE TCLRLLSLGA QANFFHPEKG NTPLHVAAKA GQTLQAELLA VYGADPGTQD
SNGKTPVDYA RQGGHHELAE RLVEIQYELT DRLAFYLCGR KPEHKTGQHF VIPQMADSSL
DVSELAKAAK KKLQSLSNHL FEELAMDVYD EVDRRETDAV WLATQNHSTL VTETTVVPFL
PVNPEYSSTR NQGRQKLARF NAHEFATLVI DILSDAKRRQ QGNPLTGSKE NVELILKSIS
NQHSSESQDN DQPDYDSVAS DEDTDLETNA AKSNRQKSLD SDLSDGPVTA QEYLQVKNAL
VASEVKIQQL MKVNINLSDE LRIMQKKLQT LQSENTNLRR QATTNIYQVQ SGSEYPDPST
TSSLKRRPSA RGSRPMSMYE TGSGQKPYLP MGEVTYPEES ITRLQPFPPH IGRSAFVTSS
SSLPSFPSTL SWARDESTRR GSKLEKQSSV SESDYDNPPT PQELEESGSG RKGRQRSVIW
QGEGSIPEDA DSAHSSSLPS TEDVIRKTEQ ITKNIQELLR AAQENKHDSY IPCSERIHVA
VTEMAALFPK KPKSELVRTS LRLLTSSAYR LQSECKKALP VETCPTTDLQ LVTQQVIQCA
YDIAKAAKQL VTITTKENNN
//
