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Database: UniProt
Entry: S7Z695_PENO1
LinkDB: S7Z695_PENO1
Original site: S7Z695_PENO1 
ID   S7Z695_PENO1            Unreviewed;      1197 AA.
AC   S7Z695;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-FEB-2023, entry version 35.
DE   RecName: Full=R3H domain-containing protein {ECO:0000259|PROSITE:PS51061};
GN   ORFNames=PDE_00588 {ECO:0000313|EMBL:EPS25654.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS25654.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS25654.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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; KB644408; EPS25654.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7Z695; -.
DR   STRING; 933388.S7Z695; -.
DR   eggNOG; KOG1952; Eukaryota.
DR   HOGENOM; CLU_005714_2_1_1; -.
DR   OrthoDB; 1412at2759; -.
DR   PhylomeDB; S7Z695; -.
DR   Proteomes; UP000019376; 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   CDD; cd06006; R3H_unknown_2; 1.
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; IPR034077; R3H_FAP1.
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; 7.
DR   SMART; SM00438; ZnF_NFX; 9.
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:UP000019376};
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          904..967
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          999..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1197 AA;  130295 MW;  9CE73AB67F943A31 CRC64;
     MSGAETAQFD APSSNMQGPD AAAAASTAPT APRARQRRRR PGPAASRVNQ QNGTAQPLNN
     QGADTVQLPV TGSVPTPELA QSSEQTRPQR SSKGRGSGSH RGRGNGPRKG GQGILDTDQA
     EQIPRHQSRG MRARGFAARL TRPHQESGNS HHEPSANGEI DASLRADAPD FVPGPAGTVP
     PASDTRSTNA KGKGKAKPNA PQRPPKVTTK STADDIATRI HEDIAHNLYE CPICTSELGR
     RSKVWACELC WTVFHLSCVK KWSTNEGAAA ARSRQNEEGE MPPVPKAWRC PGCNLSHERF
     PSTYSCWCEK ETDPRPLPGL PPHSCGQTCS RPRKGCPHPC DATCHAGPCA PCTAMGPTQD
     CFCGRNSSTK RCQDTDYDHG WSCGEICGDL LPCGEHTCPL PCHEGLCGAC EVTIEGRCYC
     GKVETEMLCS AKEDEMDSQI IRSDGSSDEW TGCFACHDRC DREFDCGLHS CQKPCHPQDP
     HPTHCPKSPD SVVRCPCGKT KLSDIPDFKP RTSCEDPIPN CREPCGKMLA CGHSCDQICH
     TGPCGMCTRR VPISCQCGRT SGMSVCHQGD VRPPQCFRQC KTTLHCGRHA CAERCCPGEQ
     KAIERQALRR KLKSHLRPTD EDIEAEHICT RICGRLLKCG RHTCPELCHK GACNTCREAI
     FEEIPCNCGR SILYPPQPCG TKPPACPFPC SRPKPCGHPQ TAHNCHLDEE TCPKCPFLTE
     KDCLCGKKVM KNVPCWLTDA RCGQVCGALL KCGSHYCRKD CHRRGECEDA DKPCQQACGK
     TKSLCGHPCE EQCHAPYPCP EKTPCTSTLT VTCSCGRLRQ ERRCGAAKAI TSKGQLQQAE
     RLPSVTPLTC DEECSRLERN RGLASALGVE INQATTVQAI SSTNLPYSAE TLDQYIKLAS
     TVPLSTLQTY EASMHALATD SSSRSFRFPP AKSTLRAYAH SLATDWGFVT ESHDPEPHRH
     VFVLKTLNWT PPVFGVGSGS SIGIGGLSVR ECVKLRERER TKERDAQRAA ALEAKAAREA
     SKTQTGADGW AQVASRAKKP GADGSVTSTR SNTPVQNIFQ SRSIYSALAG GSMPETSRQS
     SKKERLVLRS GVGVGKALRS QPPAEVADSW EEAEEKEELA EKAVQERVQE QVQEQVQEQV
     QEQVQEQVQE QVQEQVQEQK TDAFNPSTLN IFYFAVVSFE EEILPLGLTS YAGGFGM
//
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