GACZ_DICDI
ID GACZ_DICDI Reviewed; 1043 AA.
AC Q55DW9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Rho GTPase-activating protein gacZ;
DE AltName: Full=GTPase activating factor for raC protein Z;
GN Name=gacZ; ORFNames=DDB_G0269496;
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; AAFI02000005; EAL72098.1; -; Genomic_DNA.
DR RefSeq; XP_646012.1; XM_640920.1.
DR AlphaFoldDB; Q55DW9; -.
DR SMR; Q55DW9; -.
DR STRING; 44689.DDB0233848; -.
DR PaxDb; Q55DW9; -.
DR EnsemblProtists; EAL72098; EAL72098; DDB_G0269496.
DR GeneID; 8616960; -.
DR KEGG; ddi:DDB_G0269496; -.
DR dictyBase; DDB_G0269496; gacZ.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_292302_0_0_1; -.
DR InParanoid; Q55DW9; -.
DR OMA; QLDQHVV; -.
DR Reactome; R-DDI-9013148; CDC42 GTPase cycle.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR Reactome; R-DDI-9013409; RHOJ GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q55DW9; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; GTPase activation; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1043
FT /note="Rho GTPase-activating protein gacZ"
FT /id="PRO_0000380223"
FT DOMAIN 855..1043
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 71..107
FT /note="MYND-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 825..852
FT /evidence="ECO:0000255"
FT COMPBIAS 199..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 1043 AA; 113652 MW; B6C7CC1629945E32 CRC64;
MTTTNTSIFG PRVNNSKFNN NNNNNNNNNN NNNNTSNNNN SNIIKPPQVV QETQQQQQAQ
QQPLQTNEEV CVICKSKNVQ VCTGCLMVYY CGAEHQNIDW PNHKSLCSGL NRRNDLLDRA
EKSKDLRKKL QSDIFSSGNR VSNSNNNSSI YSNSTGNINN NNNSNNNNIK GGIGGGAVTN
SSTVMAPERK SIAISNIKHL QQQIQQTQQT QQQPPPTTTS IPTQPNSSSF NKPTAKKPGT
SFKSSSSGDN TPINQSPSSS SSSLVSSTNN NNNNNNNNNN NNNINSNSNN MSGSSGGIKA
LQNQLQNSIN NKPSNTTSNS PNPSPPSSTF VPNSNNNSNS NSSSGSGKSN LNISLKSSTS
SSPVTSTYLY NNNNSNSNSN SNNSSTETTT CISSNSNNSS NIENSDNTNE ENGMKNIKNK
LSQINFGAPP PSFKKPTSKV IENEDNNNSN NDGTLKQSSS SDSIYFNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN SNNNNFDINN SNNIINNKQS
TCSSIDGLSY NNNNSGSSLK NSVPPTTSNT PPRKRSSGGS SSSNNSNIGS NGNRIGFIKE
HKKNQSLPDS FVDFYQSNKN QSNGYESLLD NDDNKTRGYG SFNENDDSHE ECDDDDDDDD
GGGQDGDDGL DGTEFKRGRN RPTGLRTNNN AVFEWESGTI EYSTNNTSQH KKLGVGSRGG
NSFSKDTQSQ STNSTTTDDH QTGSILNSNS GSSDDLQQQQ TQTQQQQSQL SAGVGRIAGK
FRMIGGDIKK KAAIVGTLTK NKVSEVTSKS KSSTSVNNNN NDEVDHNENN NNNNNNINNN
NNNNNNNIEN IIFGIPLEEA VKKSATLHPL IPDVIYKSIE YIREKGIQEE GIFRLSGSAN
AITLLKNEFD RGVNVDLYQQ LDQHVVSGIL KLYLRQIPET LFTQDFGEEL EELRVGGNSS
DAISKRIAGS IILLQRLPES NRCILHYLCN LLNAISFEPS TKMGTVNLAI VFAPTLGVSV
EVMTCLISYY DEIFGIQTYN YNS
