ID K9J0N6_DESRO Unreviewed; 1590 AA.
AC K9J0N6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Putative guanine nucleotide exchange factor tim {ECO:0000313|EMBL:JAA49961.1};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA49961.1};
RN [1] {ECO:0000313|EMBL:JAA49961.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA49961.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GABZ01003564; JAA49961.1; -; mRNA.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01221; PH_ephexin; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11940; SH3_ARHGEF5_19; 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; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR029212; ARHGEF5/35_N.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR047271; Ephexin-like.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR047270; PH_ephexin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12845:SF2; DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR12845; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF15441; ARHGEF5_35; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1167..1351
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1503..1564
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 163..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..772
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 173356 MW; 5B024544EF12C4C5 CRC64;
MEAEEPQHGA SAPIPATVEF TITPEALMRS SQTPAMGPEA QEDQEPSCKW AEGHPLVETQ
QGDVRDVIDC GTQSVISSPK DGSADVGTSQ EHLAAEVWAT PECQGAVPQS PADRQPRTPA
PLECWACPGQ GEHLPMVPVP SELSSTLEEE SRPELSALLL GTGHAEADET SPRAPAQAAR
LLSREELPAE TGPLRGSEGG TVRQGEELQG AEGTEEQGQE QVGCQEGEPL REAVGLPGEQ
EQVGEQVNGM EEGQRQNQEQ MQGDVMPLKQ GEGEGLNVEL GGLNCDEWYG GTQGHEDLEV
GAQRKREFRG PEEGRVDAQD QENQSLVGRS VNVPGRQEHQ SLPGELMLEE KEEEEVVEDE
EAEDWDGAAL WGEEAERSTE EGEEPDGPPT LAVAALKLSS PRGNLFPDAR HATPGVPGTQ
TELPAEQLPP TALTPTLEPM GCPCQPVSSP SSFSTAGSPD QETAQDSQLE GAELGMWAAS
SRGAEEASAS TSETPLRTPD SAPVTPAAVS PSSTASSSAS PPIAIPRKKT SHTSCSPETS
RASFSISSPS PSGASETLPA ALPGSPSAEA AVDPCDSSNC AGPQSPLASF PGAVPHLRSN
SFPGSQRTQL TPDLAGISLS FSPSELPQRP PKPAVYGSAI SRRDRKSSWH CGSIPESPSS
LSALGQDSRE FTSSPDSPGS PHSHQPWGSP HTAAFAPGSP AYGSSPPLVF VDMRLHEPPP
PALPEKRHVR SSMVETDGHH SGVVPTLRQC SCPPPLAPSP GPRAPRKGPL PEVPDPLVAR
QYRPLPSTPD QPPHTQPSFS TRPRYNKPLP PTPDLFQPRH SLPSDNSPRV YRPPRPDPVA
EPLTEPPPLP PKSRGRTKSV QEALMNSGGQ AKPRPVGQEW TVSSPHSAGR TSWPPAMGRS
TDSLAPTSRS KREVSPGMAF SNVTGLLSPS SPTTPWTLGL QGHTSEPGLS GEAEAPTRGS
LRRIAPREGA NGLKRSDRGQ VRQPEKPSHP HLEKASSWPH RGDPGRLPQG SSGQTAASVE
ASNKPKGWHR QGLRRPSILP EGTPDTRGPA MERAFGSSDT IVFREKKPKE VMGGFSRRCS
KLINSSQLLY QEYSDVVLNK EIQSQQRLDS LAEASGLASP RQPRKALVSS ESYLQRLSMA
STSSLWQEIP VVRNSTVLLS MTHEDQKLQE AKFELIVSEA SYLRSLNIAV DHFQLSAQLR
ATLTNQEHQW LFSRLQDVRD VSSTFLSDLE ENFENNIFTF HVCDVVLNHA SHFRRVYLPY
VTNQTYQERT FQNLLNTNSS FREVLEKLEG DPICQRLSLK SFLILPFQRI TRLKLLLQNI
LKRTQPGSSE EAEATKAHHA LEELIRDCNS NVQRMRHTEE LIYLSQKIEF ECKIFPLISQ
SRWLVKSGEL TALEFSISPG LRRKLNTRPV HLHLFNDCLL LSRPREGSRF LVFDHAPFSA
IRGEKCEMKL HGPHKNLFRL FLLHNTQGTL SEFLFSTETQ SEKLRWISAL AMPGEELDLL
ECCDSPQVQC LRAYKPREND ELALEKADVV MVTQQSNDGW LEGMRLSDGE RGWFPVQQVE
FISNPEVRAR NLKEAHRVKT AKLQLVEQQP
//
