ID A0A091K270_COLST Unreviewed; 1048 AA.
AC A0A091K270;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=SLIT-ROBO Rho GTPase-activating protein 1 {ECO:0000313|EMBL:KFP30416.1};
DE Flags: Fragment;
GN ORFNames=N325_03865 {ECO:0000313|EMBL:KFP30416.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP30416.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP30416.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP30416.1};
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; KK539344; KFP30416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091K270; -.
DR Proteomes; UP000053615; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07683; F-BAR_srGAP1; 1.
DR CDD; cd04383; RhoGAP_srGAP; 1.
DR CDD; cd11955; SH3_srGAP1-3; 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035648; srGAP1/2/3_SH3.
DR InterPro; IPR037451; srGAP1_F-BAR.
DR PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR14166:SF15; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053615};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..292
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 484..672
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 721..780
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 448..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..357
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 786..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP30416.1"
FT NON_TER 1048
FT /evidence="ECO:0000313|EMBL:KFP30416.1"
SQ SEQUENCE 1048 AA; 120359 MW; 598DA8FB1426CA6B CRC64;
EIRAQLVEQQ KCLEQQTEMR VQLLQDLQDF FRKKSEIEME YSRNLEKLAE RFMAKTRSTK
DHQQYKKDQN LLSPVNCWYL LLNQVRRESK DHATLSDIYL NNVIMRFMQI SEDSTRMFKK
SKEIAFQLHE DLMKVLNELY TVMKTYHMYH AESISAESKL KEAEKQEEKQ IGRSGDPVFH
IRLEERHQRR SSVKKIEKMK EKRQAKYSEN KLKSIKARNE YLLTLEATNA SVFKYYIHDL
SDLIDCCDLG YHASLNRALR TYLSAEYNLE TSRHEGLDII ENAVDSLEPR SDKQRFMEMY
PTAFCPPMKF EFQSHMGDEV CQVTAQQPVQ AELLLRYQQL QSRLATLKIE NEEVKKTTEA
TLQTIQDMVT IEDYDVSECF QHSRSTESVK STVSETYLSK PSIAKRRANQ QETEQFYFMK
FREYLEGSNL ITKLQAKHDL LQRTLGEGHR AEYMTTRPPN LPPKPQKHRK PRPRSQYSAK
LFNGDLESFI KDSGQVIPLI VESCIRFINL YGLQHQGIFR VSGSQVEVND IKNSFERGEN
PLADDQSNHD INSVAGVLKL YFRGLENPVF PKERFNDLIS CIRIDNLYER ALQIRKLLLT
LPRSVLIVMR YLFAFLNHLS QYSDENMMDP YNLAICFGPT LMPVPDMQDQ VSCQAHVNEI
IKTIIIHHEA IFPDAKELDG PVYEKCMAGD DYCDSPYSEH GTLEEVDQDA STEPHTSEDE
CEPIEAIAKF DYVGRSAREL SFKKGASLLL YHRASEDWWE GRHNGIDGLV PHQYIVVQDM
DDTFSDTLSQ KADSEASSGP VTEDKSSSKD MNSPTDRHSD GYLGRQRKRS EPPPPLRRPG
RSSDGHCPVH PPHPLSNSSV ELSSPNLSTH CSPRALLQNR SLNADSPERR RRPGHGSLTN
ISRHDSLKKI DSPPIRRSTS SGQYTGFNDH KPLDPESIAQ DIEETMNTAL NELRELERQS
SAKHAPDVVL DTLEQMKNTP TPASSTESLS PLHSVVLRSS EPQIRRSTSS SSDTMSTFKP
MVAPRMGVQL KPPALRPKPI VLPKTNPS
//
