ID A0A091L6W4_CATAU Unreviewed; 1245 AA.
AC A0A091L6W4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=N323_08251 {ECO:0000313|EMBL:KFP50998.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP50998.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP50998.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP50998.1};
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; KL299481; KFP50998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091L6W4; -.
DR Proteomes; UP000053745; 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; 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; 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:UP000053745};
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 474..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1245
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 1118..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP50998.1"
FT NON_TER 1245
FT /evidence="ECO:0000313|EMBL:KFP50998.1"
SQ SEQUENCE 1245 AA; 138182 MW; C1CE03F112494AB8 CRC64;
LLFSENQDGL HQVVHERLGE LLRVLKAVIN KHQTLNSVDI LSAAGTVIAK VKAVNFKEVN
EENKRELFSE IFSSIETLAF TFGNVVSDFL MGDVDNGSSL GLPVSRRSRS FENLSVESGG
SLHERDDIQG HLRAEDVDSM LLRNDSGIES ALSYAKAWSK YTKDVVAWVE KKLSLELECA
KNVAKMAETA KAVVGHQDYM PFQSIFINAF QNDIENNQLW QQTAAALQSN KFVQPLLGRK
NELDRQRKDI KELWQREQKK MQELEAALRK AKLLYTQRQD EYEKAKSCTA RAEEEHLSSS
GSFVKDFSKQ LEKKRRLEEE ALQKAEEANE HYKASMAEVE EKRNDLESFK SDVLTQLREL
IYQCDLTLKA ATVNLFQLQH AQVVSLPVNC QSLCESAKLY DPGQQYSEFV KSLPKEGVPI
ESGSFETQSS QVDGVFNKQS TNSVHMSHGN LSQCSGDFPT QMLDDAGSPI YHRSQKIGEK
RSSSSTDIQA MRGPPPFRSW SVGNQSGGMC SDSESAGGSS ESRSMDSPSA SPGDFKRRLP
RTPSTGTMSS ADDLDEREPP SPSDCGLNDL TSETANSPGP FRNANMSKAA QTHKLRKLRA
PSKCRECDSL VVFHGAECEE CSLACHKKCL ETLAIQCGHK KLHGRLHLFG VEFAQAAKNV
PDGVPFIIKK CTSEIESRAL NVKGIYRVNG AKSRVEKLCQ AFENGKDLVE LSELYAHDIS
NVLKLYLRQL PEPLILFRLY NEFIGLAKES QNINEELDAK QASPKSKKRQ SICIELNRII
IKIKDLLKQL PVPNYNTLQY LVGHLHRVTE QSDENKMSAS NLGIIFGPTL IRPRQTDATV
SLSSLVDYPY QARVVELLIT YYEKIFDVSL KPLLSTSQSE ETAITVRVAL SAEEREPQQQ
RKSFVAVKET ILIAPSESRA SETAALFLES INSKNTKEQV DASVTGDAVS PPSERDNESF
ASLGEDSCKT NLLPAKPNRQ ITKVPLRVPR TKPATRPVSL PVDRILPPCV LNERNSRNAG
AASPEKLGRS PTIEEVSEVK ALPAVNTCCR LPCYDTQMLR KTWDKQYKQY DITARTAMIM
TNVPQENRAL ESGTAGALSS SCSIGNNSAN AILSSKPYSV SVRSGRTPTE GNSPEANPLA
AFRAPRTLQP PPGTFYKPPS SKSKQNEEGS CAKACAPTSA SSVPHQDDTV KLARSSTLPS
GDTEQNTNEQ KTSSEDIHPT DLKPTYQRLR PKRIQELEHR EAHFV
//
