ID B8MD88_TALSN Unreviewed; 1213 AA.
AC B8MD88;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Rho guanyl nucleotide exchange factor (Rom2), putative {ECO:0000313|EMBL:EED17613.1};
GN ORFNames=TSTA_114260 {ECO:0000313|EMBL:EED17613.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17613.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; EQ962655; EED17613.1; -; Genomic_DNA.
DR RefSeq; XP_002481605.1; XM_002481560.1.
DR AlphaFoldDB; B8MD88; -.
DR STRING; 441959.B8MD88; -.
DR GeneID; 8109188; -.
DR VEuPathDB; FungiDB:TSTA_114260; -.
DR eggNOG; KOG4305; Eukaryota.
DR HOGENOM; CLU_001251_6_0_1; -.
DR InParanoid; B8MD88; -.
DR OMA; CFRQKII; -.
DR OrthoDB; 5100844at2759; -.
DR PhylomeDB; B8MD88; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04435; DEP_fRom2; 1.
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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF2; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 513..705
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 890..1188
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 137200 MW; 425EAB3C0BEB3281 CRC64;
MADLGHDRNY RPNTYGQAPN PTRDAAFSDI FGSPAHAAGR SQTMTSQTAP FPNERSRTMT
SHIPPPSMHM QQRGPPHPGA GMRHLSNGYG SQQIPNGNVA QQPHQNYPRP FPRGSPYPGP
VRVGSGPNPH YPNPNFPIPQ GRPGFSPALN SYPDRTRSMA NLPMRPPPQQ TYSQPPVTRD
NHYNSIARTP QGRPVPEKHE DPRTMSLSSY SSSRDHAQTA YGRPVPTRPS RPPSGPDHIP
SQLLPAGPQV QSQTQTQAQG QAFPEQQGQS DGNYHHLRRP SDASMTVRTM SMASTLISDR
TMSLQSQPMQ KQTTQSTNTT AVAPPRKLKP LVYPALLSRV ADVFRERMPL GEYQKNGLSY
QNAFSGSKAV DLIAHIIRTP DRNLALLLGR ALDAQKFFHD VTYDHRLRDS AVEIYQFKET
VTEDSPTSDV NGVFTLLTEC YSPTCTRDNL CYSIACPRRL EQQARLNLKP QPGLRHSSSK
SSLHADDDND NQKLWINMVP KEVSDTLEDR EKKRQEIIFE IMYTERDFVK DLEYLRDFWM
RPLRSAGNTS LSPIPEHRRE KFIRTVFGNC LEVLKVNSAL CEALNARQKE NHVVHTVGDI
FLQHVPRFDP FIKYGANQLY GKYEFEKEKA SNPAFARFVE ETERLKESRK LELNGYLTKP
TTRLARYPLL LEQVAKNTAD DNPDKQDIPK AIGLIKDFLS RVNTESGKAE NHFNLVQLNA
ALKFNPGDYV DLKLTEENRQ MLTKMGFKKG PTDSSEVTAY LFDHAVLLVR IKLINKREEY
RVYKKPIPLE LLVIAQMDEV IPRLGLAKRS SSSLIPGKVI PNNAPIPKEG LPITFRHLGK
GGYDLTLYAT SPTQRKKFIE MVEEQQRKLR ERNSNFYSKT ILCENFFTTA NRVNCLVPID
GGRKLVIGTD DGIYLAERWP KDKNAKPRRI LDATAVTQID TLEEYQLVLV LANKTLSSYP
MEALDVNEGQ NPLARRPKKI QGHANFFKVG IGLGRHLVCS VKTSALSTTI KVFEPMENLA
RGGRKPALGK MFRGGQEALK PFKEYYIPAE SSSVHFLRKT LCVGCARGFE VVSLETTESQ
SLLDQADTSL DFVARKENVK PIHVERMNGE FLLNYSDFSF FVNRNGWRAR PDWLISWEGT
PNAFALSYPY ILAFEPNFIE IRHIETSELI HIMTGKNIRM LHSSTREILY AYEDEEGEDV
VASLDFWSKA TVK
//
