ID K3VN78_FUSPC Unreviewed; 1589 AA.
AC K3VN78;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chromatin remodeling factor mit1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPSE_03704 {ECO:0000313|EMBL:EKJ76229.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ76229.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ76229.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ76229.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EKJ76229.1}.
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DR EMBL; AFNW01000077; EKJ76229.1; -; Genomic_DNA.
DR RefSeq; XP_009255098.1; XM_009256823.1.
DR EnsemblFungi; EKJ76229; EKJ76229; FPSE_03704.
DR GeneID; 20362323; -.
DR KEGG; fpu:FPSE_03704; -.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_18_0_1; -.
DR OrthoDB; 1384108at2759; -.
DR Proteomes; UP000007978; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd15489; PHD_SF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR041684; Znf-PHD-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF15446; zf-PHD-like; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007978};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 787..959
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1092..1244
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1589 AA; 179898 MW; DA840A879CFEAA38 CRC64;
MMETESMDHD PLQGLVDQDE DAIERSLELL RAELSEQHIP VDVAMMEVEQ TLPNQDNNVR
EENEPDEKEE EILRIEGDIS DKVKPPTKPS YRVQVVVPEI PLEERAQYSF AHSHIVESVL
GEAIHDTVDY RVEFTDGREE LISFTQLVAL DNGRAALARF NQGLGPLDFE IMTGTRKRKY
APEDDWDSEH ESVISDQMDI DDEEDEEPFG TKRMRSSRLR SRENTKQLSR SPSRTDEDEL
DDLEPEPERP TRSLRVRQAR QSTSTSFKNG FGSQDQDELH GDVPPASEEE DDDFMPIVVS
DINPKKGRPN KAHQRLRRLQ TKSMRQKALS QRPSHLKSND SDIEFEAPRR SSRATRNTLN
MQDDDLMDDE SLYTVDDRTP GAPKIVSVRE IFQPLSAESE FATMHMDTCQ SCGGSRHRGQ
MIYCQGCTLS FHRSCIGPRS AREHMVTKVG EDSFVLQCKF CIKIPSKKDN NAPNHDMCQA
CKAPGSSCAP FSEKKTSRQE EKIREENGGV DPVTPVSPKL INNAGHVLFR CVECRRGWHV
EHLPGARSGT IGTDLKSERL KDHSVDWRCK ECATSRHKIH RLVAWRPVRK DLAKQVPRPT
YDEVREDDKE YLVKWDSRSY AHCVWKSGAW VYGKAAATMR ISFSKRDAAE DLLKLNEQDA
IPDEFLMPNI IFNVKTDPSV RKGTREQEMN NLAHVTKIFV KFQGLGYDDV VWDSPPTDED
GEIYASFAEA YYEYVEGKYF SSESQNKIRE RVKAFKAAPF EEINTQPAGL TRGKLMGYQI
EGVNWLLGNY HSGRSVVLAD EMGLGKTVQV VGLVTSLVQD SPKCWPFLIV VPNATCPNWR
REFKQWVPEL RVVAYHGGRE PQALAYNYEL FPNGSTDMKA HVVIMSYDSA QDPATKNLFK
SINWAGLVVD EGQRLKNDQN LLYGSLRSMR IPFRLLLTGT PLQNNKRELF NLLQFIDDKQ
NAAELDLEYE VLDKETLPKL HNKIRPYFLR RTKAGVLKFL PPMTQIILPV TMTVIQEKLS
KSIMAKNPEL IKAMFSNSKM NKKERGSLNN ILMQLRKCLC HPFMYSEAIE ERHHDPTVLQ
RNLVEASAKL LLLQVMLPKL QERGHRVLIF SQFLQQLDIV EDFLSGLSYD CRRLDGSISS
LEKQRRIDAF NAPDSPIFAF LLSTRAGGVG INLATADTVI ILDPDFNPHQ DIQALSRAHR
IGQKKKVLCF QLMTTDSVEE RIMQIGKKKM ALDHALIESM DDDELAGDDL ESILKHGAQA
LFNDDYEKKS IHYDSAAVDA LLDRTVENET KADDGTSFSY AKVWSNDKSG FEAGLATEEM
AEPEAINSSV WDRILAQREA EAQRQAEANQ ETLGRGNRRR QTINYKTEAA INPVLGDPEA
DSADSSDDFA GGDSGDESEE DASVPKGAEA DAILELENPK ARGKKGQQLH SQQVQNANKP
RKETATGQQR QRQWSTWKNG GPQNTNQQGY GQETRIAIPS QNPYQQKGVQ VIPGSSTDSA
RYTMGNHAYQ GYNAPPVPHQ RVVVTQSHPP PPDQITNFRS DRLCSEAEVR LALDYVQHSN
SDTGTKQKHR ALLMDRLRSL TPESAAQHT
//
