ID A0A0U1LWK4_TALIS Unreviewed; 1793 AA.
AC A0A0U1LWK4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Rho1 guanine nucleotide exchange factor 3 {ECO:0000313|EMBL:CRG87166.1};
GN ORFNames=PISL3812_04183 {ECO:0000313|EMBL:CRG87166.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG87166.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG87166.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG87166.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CVMT01000003; CRG87166.1; -; Genomic_DNA.
DR STRING; 28573.A0A0U1LWK4; -.
DR OMA; DMFYHPG; -.
DR OrthoDB; 2734900at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
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; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF1; RHO1 GUANINE NUCLEOTIDE EXCHANGE FACTOR TUS1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 960..1152
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1422..1735
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1793 AA; 197613 MW; D6BF9CAD39A0FA8E CRC64;
MSHYQSSHQA YYGQQNHPTA SSQNNTSHRQ YSAYSSQPDQ VTPLRRMPSY VAGDDANYAP
GANGEGGYGP QGHAPAGTVY NNLNHTAQAN LGSRHSQFSV GSSQQSNPSR ASSHGSSATS
TYHTQAYHTS VPPPTSPNAY NPQQYARPHS LSQPPAMGYN PQAYTSVGGN SQYMNAPTPY
QPYNPAAYQP NPALHRQPTD STARYQQLAT YGMPSPQAQA PPLPPRGADH PYGPRQSQLS
AETSPNPNYG HSPSNQVSPS LSYHSSIHHA GQPSPGFASN QSYVSSSPNS LPSRQPSRTS
PALPQVPSML SSPTIEEQPP VPPAHQSHGD LGYDNYNSAA VSRNSGSSPT YQSSVPRRTD
TLTRHPQSRP LPGPPPDADA EAEAQNGTLT TYDDLMKEVE EAVQGRSEMR NSNSRWVSHT
EGRTGEDEPR PLFTGDSAAS QLSPDEHHTH TNGSVATGTG QYVNYDAYSD ESDAEAAAGI
AMMQMADEEE RAEAERRRSR AGTSVSLFSS QEPQQPTPGL FTSFQEASSD SDYAHYDLAG
YGGGYEAPMH YGDTFAPGTE TKLPRVSNSL RSSGDASYTN ENSHTFSSHG STGYPHPTPA
RVDTGGTGGL AMPGTNMGHR MSFDDADEDV VLPMPDIDTP SRSQSPEKVE PADLFYHPGM
RPLPPAPVEP ANILSHLIPA GTYRHDQPGD HGETDQFRPL PPISTNTYEQ SLSNPHQVPR
SSSLSSHSST PRTETPIRSK TDADRVKYKQ QQEFLRQQAQ DPTGALGYSA SPEPSAITLD
LPTLPASRRK KFNPAKLSSE QFRKCSEPWA LSAIVAWVKE LSEDETDLKE HVVVNAIVAL
FTHKVPTMNT ADAETLGASV VNSMLSEGAL IRDEEWVKFS NKSLSGVLFQ ITGSGCYSSR
LHVQETEGFG RCYSHHCMRT LKKINLKAQV MEPQKKAQDW VTFYSIPKEV WETHSKKEID
RQNNLHEIVT TEDSFIGQLD VLRELYRDQL AKMQPSIITP KRLDKFLRDV FGKVDQVKKV
NEDYLLAQLK YRQKEQGPFI VGFSDIFREW IRKAKAAYID YAATFPNANY LVRKEAERNA
LFKQFLNQAR DNKLSNRLSW DTYLKAPITR IQRYTLLLST VHKNMIKDSE EKHNLALAIE
EIKVVALECD NKVGEMSKKV DLMELSARLQ LRPEMRNEVE LNLEHLGREI IFQGDLQRPG
TRTRFNLVDT HAVLFDHYLV LAKAMQGRDI TRSVYDVSKL PIPMDLLVLE SMNDDPVVKS
SVKGISTVAP PAAAAAAARG PGAGALTHTS SANSTASTGA ASTKSFVATT VLESSKDDKI
LYPFKVKHLG KTGTYTLFAP SAQNRQDWCE KIIEAKTKHA ASLFAQNAEP FRLRVLADAA
FSYSEAPGAK TVMINGTPLD RAIQDVEGKF ANIGIRPNPV CRAAVNCATV FQQQSGQLMC
AIGTDAGVFI SRYDDPRGWT RTITISRVTQ IAVFEEFNLL ILIADKSLIA YHLDVVCPNS
GMPSQTSQHD SARRAPQKIS GNREVGFFSI GRMKDRVLVF YKKRDGISST FKVIEPVLHK
STASRSRIFS SRRGQTEFFR EYDEFYIPTE SYHINLFHTS LAISTQRGIE VLTLDKKQPW
SVPNLSSESP EAQPYLTSIA ARIKDLRPLG MFRLSDSEFL LAYSECAVYV NKLGDVSRSV
VMEFVGRAHT ACLYGKFLIL LNDDFIEVRN AMNGRLRQVI PGRNVVCLDD GGNMEGNAPI
NSSSFAGSGA NGHTSLTRDL ARVGRTIKIC MQHPQYDRSQ VVVELIENEG QKD
//
