ID A0A091PPC7_LEPDC Unreviewed; 1245 AA.
AC A0A091PPC7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Rho GTPase-activating protein 29 {ECO:0000256|ARBA:ARBA00040783};
DE AltName: Full=Rho-type GTPase-activating protein 29 {ECO:0000256|ARBA:ARBA00042921};
DE Flags: Fragment;
GN ORFNames=N330_05660 {ECO:0000313|EMBL:KFQ09133.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ09133.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ09133.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ09133.1};
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; KK676301; KFQ09133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PPC7; -.
DR PhylomeDB; A0A091PPC7; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR CDD; cd04409; RhoGAP_PARG1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF7; RHO GTPASE-ACTIVATING PROTEIN 29; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 135..405
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 592..637
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 651..866
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 440..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..352
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 499..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ09133.1"
FT NON_TER 1245
FT /evidence="ECO:0000313|EMBL:KFQ09133.1"
SQ SEQUENCE 1245 AA; 138047 MW; 0DE3402704CEB0DA CRC64;
LLFSENQDGL HQVVHERLGE LLRVLKAVIN KHQTLNSVDI LSAAGTVIAK VKAVNFKEVN
EENKRELFSE IFSSIETLAF TFGNVVSDFL MGDVDNGSSL GLPVSRRSRS FENLSVESGG
SLHERDDIQG HLRAEEVDSM LLRNDSGIES ALSYAKAWSK YTKDVVAWVE KKLSLEVECA
KNLAKMAETA KAVVGHQDYM PFQSIFINAF QNDIENNQLC QQTAAALQSN KFVQPLLGRK
NELDRQRKDI KELWQREQKK MQELEAALRK AKLLYTQRQD EYEKAKSCTA RAEEEHLGSS
GSFVKDFSKQ LEKKRRLEEE ALQKAEEANE HYKASMAEVE EKRNDLESFK SDVLTQLREL
IYQCDLTLKA ATVNLFQLQH AQVVSLPVNC QSLCESAKLY DPGQQYSEFV KSLPKENVPI
ETGSFETQSS QVDGVFNKQS TNSVHTSHGN LSQCSGDFPA QTLDDVGSPI YHRSQKIGEK
RSSSSTDIQA MRGPPPFRSW SVGNQSGGMC SDSESAGGSS ESRSMDSPSA SPGDFKRRLP
RTPSTGTMSS ADDLDEREPP SPSDCGLNDL TSETANSPGP FRNANMSKAA QTHKLRKLRA
PSKCRECDSL VVFHGAECEE CSLACHKKCL ETLAIQCGHK KLHGRLHLFG VEFAQAAKNA
PDGIPFIIKK CTSEIESRAL NVKGIYRVNG AKSRVEKLCQ AFENGKDLVE LSELYAHDIS
NVLKLYLRQL PEPLILFRLY NEFIGLAKES QNVNEELDPK QASPQSKKRQ SICIELNRII
IKIKDLLKQL PVPNYNTLQY LIGHLHRVTE QSDENKMSAS NLGIIFGPTL IRPRQTDATV
SLSSLVDYPY QARVVELLIT YYEKIFDVSL KSLLSTSQSE ETAITVRVAV SAEEREPQQQ
RKSFVAVKEG SLIAPSESRA SETATLVLES NNGKNTKEQL DTSVTGDAAS PASERENDSF
VSLGEDNCKI NLFPGKPNRQ ITKVPLRVPR TKPTTRPVSL PVDRILPPCV LNERNSRNAG
AVSPEKLGRS PTIEEVSEVK ALPAGNTCCR LPCYDTQMLR KTWDKQYKQY DITARTAMIV
TNVPQENRAL ESGTAGALSS SCSSGNNPAD AILPSKPYSV SVRSGRTATE GNGPDANPLA
AFRAPRTLQP PPGTFYKPPS NKSKQNEEGS FAKACAPTSA SSVLHQDNTV KLARSSALLS
GDTEQNTNEQ KTNSEDIHPT DLKPTYQRLR PKRIQELEHR EAHFV
//
