ID A0A0D2DGB6_9EURO Unreviewed; 1076 AA.
AC A0A0D2DGB6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE RecName: Full=R3H domain-containing protein {ECO:0000259|PROSITE:PS51061};
GN ORFNames=PV06_05612 {ECO:0000313|EMBL:KIW42023.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW42023.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW42023.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW42023.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NFX1 family.
CC {ECO:0000256|ARBA:ARBA00007269}.
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DR EMBL; KN847336; KIW42023.1; -; Genomic_DNA.
DR RefSeq; XP_016262239.1; XM_016406635.1.
DR AlphaFoldDB; A0A0D2DGB6; -.
DR STRING; 215243.A0A0D2DGB6; -.
DR GeneID; 27357686; -.
DR VEuPathDB; FungiDB:PV06_05612; -.
DR HOGENOM; CLU_005714_2_0_1; -.
DR OrthoDB; 1412at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd06008; NF-X1-zinc-finger; 6.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 8.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00438; ZnF_NFX; 8.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 774..838
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 119125 MW; 377F2B40CA627795 CRC64;
MESANPQRPA GPSNRGQRSR RRGPPRTPRP AQDTPRVAGT RAFGGQLTQL DAEAPMFVPA
SLPPVPAASS PRPKTSNPRP SRNRNDQRPA APKQPQSQAR RGSLSRSTAP DIASRIHEDI
SSGVYECAIC TNEVTRHSKV WSCRTCWTVF HIGCIKRWSK NEGSAVHRPA GQEEDDSHSG
KQWRCPGCNL PKDTTPSSYT CWCEKELDPK TISGLPPHSC GQTCGRERTF PKPCPHPCEL
LCHAGPCPPC PSMGPTQSCF CGKEETRRRC VETNYETGWS CGSVCGDIMP CGEHTCQRSC
HEGLCGACTT EVEVKCYCGK VEKKLPCHEK GDEKESFSWT GCFDCGQLCG RMMDCGKHHC
EKPCHPQDEK EAHCPRSVDV VKFCPCGKTA LAELDIDTRK SCTDPIPSCQ KECGKTLSCG
HPCRQTCHLD ECEPCTLQVS VNCRCGRNSF EVICHEASED PPQCGRLCKA SLNCGRHECG
QKCCTGERKA AERQATKRKL KPLVAVTRVF DENIEAEHIC TRPCGRRLKC GNHDCIDLCH
RGPCGSCKEA VFDDIACACG RTVLQAPLPC GTQPPPCNFP CTRTKDCGHP QVAHNCHLQD
EECPKCPFLT EKDCLCVKKT LKNQPCWRID VLCGLVCGKA LKCGSHTCRK TCHKAGECED
AHQHCQQECG KAKKTCGHPC EQPCHAPSTC KEDRPCPFKV MITCDCQRKK EEVRCNARSS
NPEPSGRQTS LKCDDECARL ERNRKLAMAL HISDDHTDDH VPYSTATLQM YLEDVAWAHA
QEEALRLFAA DETQKRYGCQ PMKSRQRSFI HSLAEDFGFD SESLDPEPHR HVVLFKTPKF
VAAPMKTLVQ AARVKRAQLN VPAPVQSAPE RKADEVKHEY NGLMLTKPKF ALTEDELRPV
VKKATPTIDL DIVFLPNDEG VALLPSMSWE TPEQLTTLLT SLQPTIAGEV SKHNLAGSVV
LCQFDTTGID IKVVQQQGKP SDNLTNGWSK VAARRAAPVP VPQVRPVGQR PVYTVLGSRL
AEAKKKKEEN EAKLRKRVEA QVVDDWEKEV EEEERNEVDS ERVDTDIPGE PSTSMA
//