ID A0A2T4AY06_9HYPO Unreviewed; 1347 AA.
AC A0A2T4AY06;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE SubName: Full=Guanine nucleotide exchange factor {ECO:0000313|EMBL:PTB61939.1};
GN ORFNames=BBK36DRAFT_1173005 {ECO:0000313|EMBL:PTB61939.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB61939.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ680226; PTB61939.1; -; Genomic_DNA.
DR OrthoDB; 1369677at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR10663:SF373; PH AND SEC7 DOMAIN-CONTAINING PROTEIN C11E3.11C; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000241546}.
FT DOMAIN 573..738
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 148103 MW; ABD261EC0F185C25 CRC64;
MADQHASRGR VRDSHDLSLS PRNVTRDSLV NNMLLSLDQF SLGHTTSSST TRSFTGKALT
YDDPRPWAHD SITGSFSHGF RPSVSSPSSS SFRHPQPSRH HYSYSSDYDD DSTRTSVQLP
RARSRSPNRR RSNSSSTFQA SFPKPPAAAD SPIQRARPRA NTGSSTSSVS YDAGYPQNIA
GPASWDRTGF RRSASFDLGP LQAQTQLNAP LVSPFHIDFP NHQLVAPAMA LSDFDAAPAP
SVSYGKSKTE QLAASQSAGG LAQPKEKHGF FRRVFGSSKS TTPAPAETLT SRLTSQVSNV
VAPAPKDVPP QPQQTQPVLQ KKSSSFFRRR KKSVADEAPP LPSDVPPVPS LADANGSLHP
DCDRTTDSPA GSLRQIMTPY LKESAVLSQP LGDITNKAAA RVEDDDDDYR ADIQREFSPD
YELSPNARIR LVQNSDSEQD QLAHDKPGRA PNKLEHRNNS FLDLDGGSDN EEPPVRQRAD
KENDGRLASP TAYKSKDTGG TLRAKKSPHI TDQERFGDEP LRPNMTRPMT ERRSTSYASA
STDDGDYKTA PSAAPSVRVE RSSESSARGP GTLDLLKNRD LDEPEFVIGE PTEDERQKAQ
QIFDGCEDFI PKEKAASWMG EEGPIRQRTL QAYIELYDFT DLSILNALRK VCGRLILRGE
TQQVDRILVA FSKRWCDCNP NHGFKATDVI HTICYSIMLL NTDLHLADIE QKMTRSQFVK
NTLTTITQAV EESVPDAFDR PSILPERGSV LHEAGRAASE PQEKKSFRNS FRPPPRIDTQ
MVDAHDECGP LVKSSFYGSM KAWEEQIEIV LKSIYNSIKE DKLPLFGAEP EKHLHTMPSQ
SNLSVMGMLK RSPSVLSKAP SESQMSTRGR LADNSRNGSS RWASKSRSRT GLGRQGFNSS
RTSFDDTNSL WSPAMSSATW SRYSLGRTQG SMSQDSFGSA MPRGDYQQSI GFANALSQAI
VRSDDANLND GASVMSADVP ATGLLDDESL ELAGPPWIKE GRVMHKHHLD GVGKRAKDRN
WTEVFAVIQR GQMSIFSFNT PKSTRQKSRT RNADKANAPV GGGNWQDNAV NLGTFNLRLT
LASALPSPGY SRSRPYVWAL SLPTGAVHLF QVGTPEIIKE FVSTANYWSS RLSAHPLIGG
ISNIEYGWSD SVINSALAGA NSDNASIMSG GRNSRPGSRA AHGRQPSVQS VNMPSSSIDL
GSGPFTSSGR GKLPGDRITI SEWAPPTQSM RPSHLSEPEQ LEALTAYVKS IEDDLQNHNQ
LRSPMLLAFT PRGSNANKAM ANWERKSAYL LREIVKFRTY VDTLQQAEAR RREIYKERDL
AQRAARGELS DGDMDLSDED GDETLRP
//
