ID G4TF77_SERID Unreviewed; 950 AA.
AC G4TF77;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PIIN_03899 {ECO:0000313|EMBL:CCA69959.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA69959.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA69959.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA69959.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
CC -!- SIMILARITY: Belongs to the ARS2 family.
CC {ECO:0000256|ARBA:ARBA00005407}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCA69959.1}.
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DR EMBL; CAFZ01000068; CCA69959.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TF77; -.
DR STRING; 1109443.G4TF77; -.
DR eggNOG; KOG2295; Eukaryota.
DR eggNOG; KOG3334; Eukaryota.
DR HOGENOM; CLU_009652_1_0_1; -.
DR InParanoid; G4TF77; -.
DR OMA; FEDKIMQ; -.
DR OrthoDB; 10695at2759; -.
DR Proteomes; UP000007148; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd00590; RRM_SF; 1.
DR CDD; cd07979; TAF9; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR InterPro; IPR003162; TFIID-31.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13165; ARSENITE-RESISTANCE PROTEIN 2; 1.
DR PANTHER; PTHR13165:SF0; SERRATE RNA EFFECTOR MOLECULE HOMOLOG; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR Pfam; PF02291; TFIID-31kDa; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 307..385
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 599..622
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..902
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 108997 MW; 4850F18B458AC044 CRC64;
MSWDGQDRYG RGSPPRDERR RDSRYGEPTY GSYEDSVRDW EEQERLRQWD EYERARMDWE
RRVNEYKGGD GHRNGYYSGG KRPRSPSPYE RDARPRRDSY DQYGRGGRSR YEDGRRSPRR
RYSPDNRYRR DSNLPNPMDQ DKLVPYRSFL EWYRDAAPDR FFEDEAVTRD NPSDRKVGLK
ARYDEFRADF QAKQVHTLFE KHHKAAWFLE KYDPSEKYAD LRFRVRKQGW NGALDQFISE
LEDGKFDYIF NVGSSNPNEL KPDVKPSEAT SSAEKPVKTE DDEDDGDDDA EGKEGDGDDV
IIPHKGHQVM IKSIPPEIGR LELEPLVDKL SGVASLALGE PVARRNYYRS AWIEFDTEQA
ARDAMEFLSG QEVDNFKLRV TMIRSPLIAK IKRTSVLVSS ERRLEEDLHT IKRLVALLEK
ESHMLANYKP LSQRSTDDTG GDVKMESPVK ESTGDDEQTI HRGAKAVEAR LERLLPPPDS
EEAKSQRLSM TVDLYLAYLR SAFFCCYYCA VIADRADELQ RKCVSHIRTP FNEREMTEIM
RNQKRSDRED HWFLLHDEKI EALVDRDSVD PTRFGGKNVE KELETKLKDQ IRQEDENRFR
CVTCGKMFKS TGYVCKHILN KHPELIGEEF MNHLRIYNNF ALDPHRIQMP PRAPTGAPGR
NGRDGGREDG RHKRRATIDT SENARRKSPP PDAKIDPRAG QRITYQDLDE VAGGEDVALI
YSRQPLLNSA MSALLPEKPA AALPQSARAI ALLLASTPSV VDAPPRVLQM LMEFAHRYTV
QVLMDAQVFA EHAGRPGRII MDDVTLAIQG KVGFEFGGRV PKEYLLAMAA SVNEEPLPPV
QEAFGIRLPP PEHCLVQPDF DLIPNAPPEE DPLYEEIEEE VTDDEEDIAE NDEEDEDDVE
MQEAATNGVR AENGMDIDAD KEGSDLFDGD EDEGAAKDVR RPVNDDDDYD
//
