ID A0A091DFM4_FUKDA Unreviewed; 1502 AA.
AC A0A091DFM4;
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=Rho GTPase-activating protein 5 {ECO:0000313|EMBL:KFO29278.1};
GN ORFNames=H920_09316 {ECO:0000313|EMBL:KFO29278.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO29278.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO29278.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO29278.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN122612; KFO29278.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000018657; -.
DR eggNOG; KOG4271; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd22220; pseudoGTPaseD_p190RhoGAP-B; 1.
DR CDD; cd04373; RhoGAP_p190; 1.
DR Gene3D; 1.10.10.440; FF domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR PANTHER; PTHR46005:SF2; RHO GTPASE-ACTIVATING PROTEIN 5; 1.
DR Pfam; PF01846; FF; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 4.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 267..325
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 366..420
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 427..481
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 482..548
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 590..763
FT /note="PG1 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51852"
FT DOMAIN 779..944
FT /note="PG2 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51853"
FT DOMAIN 1262..1449
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 950..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 172184 MW; 18F3656C216850A5 CRC64;
MMARNKEPRP PSYTISVVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI
DFGGRVVNND HFLYWGDITQ NGEDAVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA
ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV
NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFI
ALVQMLDKTR GKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIS TLPRAFNTLL PSLEEIEHLN
WSEALKLMEK RTDFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH
LISEKRRVEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAFKYITEAD SKEVYSRHQR
EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES
LLLKHIGFVY HPTKETCLSG HNCTDIKVEQ LLASSLLQLD HGRLRLYHDS TNIDKVNLFI
LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYILSQLWT AAFKPHGCFC
VFNSIESLSF IGEFIGKIRT EASQIRKDKY MANLPFTLIL ANQRDSISKN LPILRHQGQQ
LANKLQCPFV DVPTGTYPRK FNETQVKQAL RGVLESVKHN LDVVSPVPTN KDVSEADLRI
VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI
GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDSTRESTHQ
SEDVFLPSPR DCFPYNSYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP
VHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA
HPEDMDSSDN YAEPIDTIFK QKGYSDEIYV VPDDSQPRVN KIRNSFVNNT QGDEENGFSD
RPSKGHGERR PSKYKYKSKT LFSKAKSYYR RTHSDASDDE AFTTSKTKRK GRHRGSEEDP
LLSPVETWKG GIDNPAITSD QEVDDKKMKK KTHKVKEDKK KKKTKNFNPP TRRNWESNYF
GMPLQDLVTA EKPIPLFVEK CVEFIEDTGL CTEGLYRVSG NKTDQDNIQK QFDQDHNINL
VSMEVTVNAV AGALKAFFAD LPDPLIPYSL HPELLEAAKI LDKTERLHAL KEIVKKFHPV
NYDVFRYVIT HLNRVSQQNK INLMTADNLS ICFWPTLMRP DFENREFLST TKIHQSVVET
FIQQCQFFFY NGEIVETANN VAAPLPSNPG QLVESMVPLQ LPPPLQPQLI QPQLQTDPLG
II
//