ID S8CA12_DACHA Unreviewed; 918 AA.
AC S8CA12;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE RecName: Full=R3H domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=H072_1501 {ECO:0000313|EMBL:EPS44512.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS44512.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS44512.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS44512.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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}.
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:EPS44512.1}.
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DR EMBL; AQGS01000044; EPS44512.1; -; Genomic_DNA.
DR RefSeq; XP_011107493.1; XM_011109191.1.
DR AlphaFoldDB; S8CA12; -.
DR STRING; 1284197.S8CA12; -.
DR eggNOG; KOG1952; Eukaryota.
DR HOGENOM; CLU_005714_2_3_1; -.
DR OMA; SHECGER; -.
DR OrthoDB; 1412at2759; -.
DR Proteomes; UP000015100; 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; 3.
DR CDD; cd16492; RING-CH-C4HC3_NFX1-like; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 SMART; SM00393; R3H; 1.
DR SMART; SM00438; ZnF_NFX; 3.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 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:UP000015100};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 224..287
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 227..285
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 575..638
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 100530 MW; B79D3EE2F5424F62 CRC64;
MADTANHQSQ HAQSQQSTPT NQSNPNRNRR RRPPRRPRED PQASAESLGN GLSEGQTATE
VSSNPINTHS GHHRSEGAPS SSNRGGRRGG RGGPRQNPRP EARTEEQGAT RETTEPSTRG
TTARQRARRG GSFVPGARQF GGQLTKNEPQ EDRDDADPST LHAEAPNFVP GQSTNIPNTI
VVESGPSATS RPRRNRERHR GAPKTVREAE DLTTRIHTEI SSGEYECMIC YSSVNRKSKV
WDCTRCYAVF HLHCIKKWAK QALEVPGPSN DEIVPQRTWR CPGCQNTSID APNTYTCWCG
KSENPEVARY VPPHSCGQTC GRPREGVSKN CPHGCDLQCH AGPCPPCSAM GPVQPCFCGK
ETSQKRCLDT DYENGWTCGH VCGDFMPCGE HMCERECHGG VCGACEVKEL LKCYCGQEEK
EIRCCDKLDP MLAHGIVDGV ATSWEGYWKC ERKCERAFDC GEHKCQKGCH AQDIEVPHCP
FSPDVVSFCP CGKTELGKKN IRTKCTDPIP HCDKEVTCNT SSKNQSPRRP EIKCIDDCRR
RQLAAAFNID IEKKAAEEAI NTYSDETLEF YMENKAWCVG IEKMAREFCE DKGKIRLAFK
PMKSHLRGFI HGLAEDYGLD SESQDPEPYR SVVMTKNTRW SMPSVGLADA VRARKAEAAA
ASAAQPSGIV PVGTGVQQLR KTTGMQAVNA ILLSGLRVGL LTNELEKELN PVLKQSMLRF
GIRWYGDEEV LLEPLPSSFS MDEVEVELGN VRTNVRRHCT VNRIASSVDL CWVGRDGKVS
NKEGQGWSVV STGKGTRSNA AQQGQSGGSY ANLFGVLRDG PSGSFAAVSA GPKGGLTMKS
DVAKAKVKVL SPVLPKEEPV DDWLEAMENE EREAEAEKAA ASGAASSVED NSEQQSTDEA
EIEPVSKVQE EATASTTA
//
