ID A0A158NJJ4_ATTCE Unreviewed; 1773 AA.
AC A0A158NJJ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
GN Name=105620835 {ECO:0000313|EnsemblMetazoa:XP_012057702.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057702.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012057702.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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DR EMBL; ADTU01017957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01017958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012057702.1; XM_012202312.1.
DR STRING; 12957.A0A158NJJ4; -.
DR EnsemblMetazoa; XM_012202312.1; XP_012057702.1; LOC105620835.
DR GeneID; 105620835; -.
DR KEGG; acep:105620835; -.
DR eggNOG; ENOG502SBKY; Eukaryota.
DR InParanoid; A0A158NJJ4; -.
DR OrthoDB; 2917131at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR039919; ARHGEF10/ARHGEF17.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12877; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR12877:SF15; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 17; 1.
DR Pfam; PF19057; PH_19; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT DOMAIN 889..1077
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1185..1243
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 65..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1773 AA; 193411 MW; 68E82BCFD5BA80E6 CRC64;
MPRAGGGDGG SGPQRTGGGG FGGWLGGAAR AMTGGGVGGG YVVLGGTRYG LRISQENLPP
TVNSREESQE RRRKRNSRES DSRERLTERP VTEKQPIDLA ASIADCCCIG PRSRLPLPRI
PPAIMSSMTT AASSASSSSA SSASCPSIVT GGYPSREIAS DYSSSLPAST TSVAETTPTL
ANNSRGAVQT SVGNIGSTSQ QQQQQQQQPH YHYYQQHYPQ AAVAAVTSSY SPPTTTPCSP
STSLGYSSGV PTTTQTVSVP RQLAQWTKHQ TLKLQEPAVI AVDRLHRFRW SGGGGGSGKK
SSSGPRSEKA ERLRELTEKL KGPAPIPPPR RPSRVQASSP PSSGYQPSSQ NYPQTGSNPS
SGRFEGRSSH RSYTYNEDNH HGNNNQQFQQ HQQQQQENPK TMVRSESVSE ECLSDRSGNS
VYRKPCHDSR KTSRSGSRPE RNSDDVSDLR SKPNASAETA KHLRQYSDSV VDSATSVDDL
CDNLNAASVS GNEGEARDAV TRLEPRGLLA FHRSGAPYRS ASFGQVDFNQ DADFTFSANS
HFPLPANRQK TQPIVTSNRS ETKDIRASTL PRRRGDVTPG TTTPQNSPNR QSPRTSTPSV
DSAVGSAEGL GVSQQGNHEE IRPRSDGSDS LATSSALTSP EPLVPETNQI EPRVETDAPT
VELVGHETVY PIVEGNIVEE TIQKETRIEP HEVIITPPPE EPRLSQASEG SEAPSETPSE
ASSPSGKARR YRGDTSKRRK GVYITQWPEP LDADRNKLSA QSSEERDEPP ATPSDLSDCE
GHTPRRYSKR PLRGPYGQML EAEMAKPRTT DIALEEGLRP RRKISANLSY NASSNNNSGS
EPPTPCHHRT TSSPTKLEGL PGPSPELLAE LLRGSSERVA RAPAHRNDTR THVVVELYDT
ERSYVEALQI LVNKYLQPLK SPENAGLVDA ATVDEIFYQV PALLSHHEIF LEELRRRLDT
WELRQTIGDV FLDVFTKPVV LETYTLFLDN WKSARKAIKT TCQAKPAFAR FLETMEREHK
GKLGLDQLLI KPVQKIPRYE LLIQRLLKHT DPTHPDYELL QAAQKEVHEL VVKINCTERE
SLEWEQQQTT LREVQALVEG LAGIVTNDRA FVRHDLVTIA SNQGTRKERA LFLFSDLLVI
TSIKRRSGTI RKPSTSTCPN SLVGLLDANK YKMLMRISLD DLEVMKAKDE NLRRMAREVD
YLREDCTKLT QLQELAITLH GAKQQLEDLI KDMLSQAQRQ LAERNAAHSQ LACLELTLNT
QAGIENISVM FAKPDKRASW EESFNEAKQK LALSADRRPC PEFVGPLPIR KTRAGLQFTC
AAPTLANGQG SKDVWVCNSD GYVGQVCVLS LSPEPPQVTS CNGVCNARIL CVAGIPACTP
GSNLCMSNNS PFVNSKNSIS ISVQDVDASG GNIQLDSSSS SDDSDSDDIP SADTGSVTLS
GDVSSIDNTI TEEDANQPTM WLGTEDGCIH VYNCNDNIRI KKNKVKIQHG SSVHCIIYLD
NKVFVSLANG DITVYVRDHT GGWNTPDPTT VSVGTVASPV TKMLSVSGKL WCGCHNSVKV
LNTHTLDIEH TFTVSSDTSR AVSCMANSGG LGVWISLHNS AVLRLFHSGT YECLTDINIA
PAVTKMLATG CDDIIRQHKA ACLRVTALLA CNELLWIGTS AGVLLTVPIP HIKPSTQRMS
QPPIVTGIPH GHTGHVRFLT CVETPNPSKP DPRPKVNRYS LKSNKTQQNN INRGKLLVIS
GGDGYEDFRG PQASAELQAG REDSTNHLLL WKV
//
