GACT_DICDI
ID GACT_DICDI Reviewed; 1009 AA.
AC Q54NL0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Rho GTPase-activating protein gacT;
DE AltName: Full=GTPase activating factor for raC protein T;
GN Name=gacT; Synonyms=DG1094; ORFNames=DDB_G0285163;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC transduction pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AAFI02000075; EAL64838.1; -; Genomic_DNA.
DR RefSeq; XP_638352.1; XM_633260.1.
DR AlphaFoldDB; Q54NL0; -.
DR SMR; Q54NL0; -.
DR STRING; 44689.DDB0191387; -.
DR PaxDb; Q54NL0; -.
DR EnsemblProtists; EAL64838; EAL64838; DDB_G0285163.
DR GeneID; 8624977; -.
DR KEGG; ddi:DDB_G0285163; -.
DR dictyBase; DDB_G0285163; gacT.
DR eggNOG; KOG4370; Eukaryota.
DR HOGENOM; CLU_298177_0_0_1; -.
DR InParanoid; Q54NL0; -.
DR OMA; VSPIEPY; -.
DR PRO; PR:Q54NL0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..1009
FT /note="Rho GTPase-activating protein gacT"
FT /id="PRO_0000380217"
FT DOMAIN 163..351
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 580..656
FT /evidence="ECO:0000255"
FT COILED 715..743
FT /evidence="ECO:0000255"
FT COILED 839..952
FT /evidence="ECO:0000255"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 114239 MW; D2557443A252768A CRC64;
MKNIFRRSVQ IFHKDKKEGD KQDYTGSSGS SGNSGTDRSP TSSLSKKDKK HSKHHQNESY
SGDNSPTLSR NHHDEIGHLQ YTANHHIATS HHSHSHNHNH NHNHQLTQPI QQQQQTQHVN
LASNNYYIRH IYTNNQYDET TQIVMNNGIP FIYNPNARKI FGVPLTQVPC RAGSNVPIII
EKLIDHIERT SLNSEGLFRI PGVDLTINQY IKLFDNGEDV DVSPIEPYTA AGLLKRFFRD
LPVFVPQSIN KRVVSLFIDE EGKKKPVDME ILSNLRVLVH QLPTVHFEVM QELTNLLGKL
MSRSDQNKMT ISNIAICLVP TLNCVPAIVT YSIQMHDFFY NEVFPQHHLY YMRPYEEKLV
ESAPTQPINI MTTSGGEKRY SSRPASITIS GLLPSNGQNN SPSSSTITST TITSPHDSTA
PITFTVTTTF SPEQQQQMLQ QQQQQQQQQE KQSSSSLSQS QQSIQPISDT NSTKSDRRTF
RVDPNLDLTQ YIEDTQYNVN RNYLYNGGPS GTTGTTPNGG SLSIGGGNGG NGGSSLSVGS
GGGNGGSSLS VGSNTSVGVG GGGGGNNTTD QSKIYRRSVA YTNNEDTKAA IQQIKEKIDR
YSKEKKTREE KEREKLLRYS IDLERYKDRT INNKQEKRAS RDINKEIERE IEKKRLSPRE
RLNLFGLSSS SSSVNSTLTR STANIISTID GSGGSNRNSK NYGNGSSSSS NRRYSNTINQ
QLQMQLQQLQ IQQQQYQQTQ QSQIPLQYQQ QQQQQQQQTT TTTTTSSGSN RFSSNRYKPV
DLTQSSSNFR YSREIYDDDY YSNNNLMMFG NEQPNQTPIS VSSSSAFTRQ RSQSCFEPEN
LVLLQQQYQQ YQQQQQQQQQ IPFQANPQYS NAVIEQKLDQ IRDTINNLHR DNRVSRDYTH
YLREVEDLRS SLQKETVVSN EFIKNIELED KLRREEEKNQ RLIEEIHLLE TYFILKEKSK
AKRLSTTKDL LTRSRSPTLP SSINMSTSSL GSSSSSAYNN NNNNNNVPK
