ID S7RJR6_GLOTA Unreviewed; 802 AA.
AC S7RJR6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=GLOTRDRAFT_116448 {ECO:0000313|EMBL:EPQ54600.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ54600.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ54600.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ54600.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; KB469303; EPQ54600.1; -; Genomic_DNA.
DR RefSeq; XP_007866881.1; XM_007868690.1.
DR AlphaFoldDB; S7RJR6; -.
DR STRING; 670483.S7RJR6; -.
DR GeneID; 19300185; -.
DR KEGG; gtr:GLOTRDRAFT_116448; -.
DR eggNOG; KOG1547; Eukaryota.
DR HOGENOM; CLU_017509_0_0_1; -.
DR OMA; RSNPCDY; -.
DR OrthoDB; 1699019at2759; -.
DR Proteomes; UP000030669; Unassembled WGS sequence.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 2.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF126; SEPTIN; 1.
DR Pfam; PF00735; Septin; 2.
DR Pfam; PF00172; Zn_clus; 2.
DR PRINTS; PR00755; AFLATOXINBRP.
DR SMART; SM00066; GAL4; 2.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 2.
DR PROSITE; PS51719; G_SEPTIN; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 2.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 2.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..802
FT /note="Zn(2)-C6 fungal-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004556654"
FT DOMAIN 1..391
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT DOMAIN 486..516
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT DOMAIN 678..708
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 239..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPQ54600.1"
SQ SEQUENCE 802 AA; 87436 MW; F63C168DD5D73921 CRC64;
MVAGRRTGKT SFLRLLLDTS FVAPTATSDQ LTSVAKFVQG CSGHTGHIRT VSIDVEHDLG
EQGPTQPLTL TLIDTPSFDF QDDAASDRLC SEIQRHVESR LAESAEDENK ARSGDHHVHL
CVYFLDPDVI VPPSIPTPPV PFVSRARTNS LSHSEPERVI LDPPVTTNPD LCRPVLPVPD
INTIRRLSSR MNVLPVVARA DTLTNERLAA VKMAIRRDLA DAGIGFGIFD APALDGHSQY
PQHKDVGSQP MNGSLPNVLS SHTNRNAPSA APSPPGSPAV TTPLRLPYAL ISPDIYCHND
GVHRPAPSRH ELVLQYTPSN HRTVVKGHSP SCKIEMGRYT RCYRWGSLDV LDPNHSDFLY
LRRAIFHHMQ TLHKYTKEYL LGKFMEGYQP HHATYHPLQQ ISLPPPSRPH PSLSQASRPI
LAIDTAPGPA ATHRQPHLAL PPPSAQEPRR SPLRGPESVV SSSSTKTPPA GTRMSQKQRP
KKITVACNFC RSRKLKCDGG RPACEQCLKR RNPCDYVPNM RRGGARRQRR QDDSESESAS
GDDDQSPEHD SQSPEVPSRP VSRKGNVNMF LTEPLPGSGH LTSPLDRRET VPRLPALVLP
KPNIPGPPSA SYRTDDPSHI AALPTPVTGI SSSSSAHAEL TLPPIRTEPD LPSPSRRRST
VPPRKGHRSL KYGPKVVACN FCRARKTKCD GAHPSCSSCA RRSLQCSYVN DPAGPHGPAR
RKKATTSTSD PSQSSPPTSQ VHTQLPPTTA PPVGYGHMAP PNIGEGEVDL KRNLHDPQQQ
LPPKKMRLEG NASHSVAVAA GP
//
