ID A0A182P105_9DIPT Unreviewed; 1637 AA.
AC A0A182P105;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI000587-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI000587-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI000587-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 199890.A0A182P105; -.
DR EnsemblMetazoa; AEPI000587-RA; AEPI000587-PA; AEPI000587.
DR VEuPathDB; VectorBase:AEPI000587; -.
DR OrthoDB; 2906033at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00176; SPEC; 4.
DR Gene3D; 1.20.58.60; -; 5.
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 InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF210; CRAL-TRIO DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00150; SPEC; 5.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 1266..1440
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1459..1566
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1140..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 510..565
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 596..644
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1203..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1637 AA; 186468 MW; 93F1A4EEA46911B3 CRC64;
MRGNGNTAAS AKMILKVLQE NFGTDVIHQA VIIKPDNFWH KQRSSIASNK YKFETTTISI
QSLGKLVEPS QLTSDFEGFL HYDHAVWIDL RVAFEDFLWQ ASDILDRIDD LQEDLTHSEC
PEDVNGAKHS IDAHNEMKRK ILKLPIEDLD LQGQKLLGKL TTYSNRNDDG CHSAPLPTNC
INPDVTSAMN QVLQQLETTR NAQQQLLNLW QHRKTKLDQC FQLRLFEQDC EKMFDWILHN
RDVFQETYVE IGHNYAIAKN LQEEHQRFAI TSRNVCVNIN RILAVAARLY EGNHYAAAHI
RTLAARLDKT WKDFVTTLDE RTAVLTLSVV FHHKAEQYTE SVSSWAAACE ATIPTPTNVE
SLETAIGTHQ SLYEAMCQAY TEVHSTSKKL LYQLDHLVQV CNQPPIVNTR KNDNSHFNGG
NPAADYSEGA SHVLAVIHQI LGHHRALESK WHAGKLRLHQ KLALRLFQED VKQVLDWLQN
HGDVFLRKNR GIGKSLQKAR IYQTSHEHFE NVAQNTYRNA EKLLAAAEEL ARSGEVSPQE
IFSVAQELET NVASFAERVE KRRRRLDLAV VFYSNEKEIA AWQEQLHAEV TNEESLELAN
EHLEGTERML EQCKEQEENT LKTCMQAIAQ GEALMQELRA IEEEDSSGSL TAVQNALDRI
QKNRLDLEGL WQTRRMKIDL YLRLRIFERD ALEVSSQLEM WSEELQHTEV SRDFQKTEQF
LRLHNESVNQ MQTTTYQVMN QGHELMQLFE SSGLLIMADA NHTAQTRVQC LLEFLHDREL
DLEDMAEAKR IKLEQSMQLC HFQNDANQVI SWIRNGEAML MANFSIPNNF QEAEQLRKEH
EQFQVAIERT HTSAVQVKYR ADALMNANHY DPQSIKDIAE DVTKKWQKLV TCAEERHKLV
TASQNFFKTA EQVCSVLDSL EKEYRREEDW CGGGGSTDKG QQIVQLISKH QEQKEAFLKA
CTLARRTAET FLKYANRSLQ FYHVKSTTVN SESRVKSILE KLLAQETQVL EYWTQRKKRL
DQCQQFVLFE RSAKQAIEWI HDTGEAYLSS RKNKLCSSRE ESELLLREHN EFKSTAKETR
ERVKLLIQLA DTLVEKGHAH ASSIKQWVAT VDYRYKDFSQ RMELYRSNLE KSLGLPGIIQ
QQDDNNLSSS NSSNNSSNSS LNASRSIGMV SSSSGISSGG SFTSVIAVGA SPVPGVLGSG
DGGSGPCSTS STGTGSGSSS GGGSVLEYRH SDPSLETKLN AAAAGAGAVG VVQKEINEEK
RKSARKKEFI MAELLQTERT YVKDLETCIN VFLRELKGGQ QVPQNLLGKE HILFANIEDI
FQFHEKIFLR ELEKYETMPE DVGHCFVTWA TKFDMYVHYC QNKPQSMDYM VQHGGTYFEE
VQRKHKLEHS LPAYLIKPVQ RITKYQLLLK DLQSCCDEGQ GEIKDGLEVM LNVPKKANDV
MHLSLLEQCD MPIDNLGDVV LQDSFLVWDT KQILIKKGRE RHVFLFELYI LFSKEVKDTN
GTVKYIYKNK LLTSDFGVTE HIEGDECKFA IWTGRAPILS DYRIVLKANS LETKQLWVKR
MREVMQETYF SGTSFSLLKS PAKVSGKNLG QRLSKDIDDT LNDNDQDGSS LASFGSGNTT
DSEKVGDTSS SSLESHC
//
