ID N1RSM4_FUSC4 Unreviewed; 1559 AA.
AC N1RSM4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Chromodomain helicase hrp3 {ECO:0000313|EMBL:EMT65255.1};
GN ORFNames=FOC4_g10011233 {ECO:0000313|EMBL:EMT65255.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT65255.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the polycystin family.
CC {ECO:0000256|ARBA:ARBA00007200}.
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DR EMBL; KB726990; EMT65255.1; -; Genomic_DNA.
DR STRING; 1229665.N1RSM4; -.
DR HOGENOM; CLU_000315_29_1_1; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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 InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014010; REJ_dom.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51111; REJ; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EMT65255.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..29
FT /note="REJ"
FT /evidence="ECO:0000259|PROSITE:PS51111"
FT DOMAIN 265..336
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 364..424
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 462..633
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 765..926
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1559 AA; 178869 MW; 4606A0BEE8E92C01 CRC64;
MMSTPTLGGP SNGHLSPVDG ISMSFDTGDH ATDSDSHDAP DLTLDQPSPA SSDEANNDSN
IAHDNTHMSA SEQSSEDNAS DDGDFDMEES LPSQNEDAME DRDSSTDSNR ASKRKAPVEE
DEYIKANPEL YGLRRSTRPR EQRKIVESDD SDSEPPVNRR TVKRRRVESS RPSSKIGTPT
LRASTADSDS DSDTYGGARA KSLQKKARMQ REAQPDLAFA EKRWSSRRAA QVQQGAYEES
DVDEDDDDDE LAPMAYTVDY IDDSPYIEKV VRHRLKDGFE ISYGLTKNDF EYFIKWQGKS
HLHDTWETFQ DIRDYRGYRK VENYFRKVIE YEVDIRVGDD IPPETKEQFF LDRERDEEAF
EDYTKVERVV AVRDGEDDTE YLVKWKGLTY EECTWEVASE ISDAFQDQID QYLDRASRSW
QSDRKETNLD TRSRMVKLEE QPDFIKGGEL RNFQLRGLNF LCLNWTKGNN VILADEMGLG
KTVQTVSFLS WLRNARRQEG PSLVVAPLSV IPAWCDTFNH WSPDINYVVY LGPEDARKII
REHELLVDGN PKKPKFNVLV TSYEFILQDW QFLQSIKWQT LAVDEAHRLK NRESQLYNRL
VSFGIPCKIL ITGTPIQNNL AELSALLDFL NPGKVDIDED LDSLSASDAQ EKLQQLHKAI
APFILRRTKE TVESDLPPKT EKIIRVELSD VQLEYYKNIL TRNYTALCDA TNGHKNSLLN
IMMELKKISN HPYMFPGAEE KVLAGSVRRE DQIKGLIASS GKMMLLDQLL SKLNKDGHRV
LIFSQMVKML DILGDYCSLR GYKFQRLDGT IAAGPRRMAI NHFNADDSDD FCFLLSTRAG
GLGINLMTAD TVIIFDSDWN PQADLQAMAR AHRIGQKRPV NIYRLVSKET VEEEVLERAR
NKLLLEYLTI QAGVTDDGKA AFKEELNKKG LRVEGPSSSE DIQMVLKMRS SKMFEQSGNQ
ERLEQLDIDS ILENAEVTKT KVDDKINLSS GGIDWDNFMQ ITDVKVDDIN LDWDQIIPAD
KIAEIKAEEE KKQHEAYVAK VAAESAPRRA AIKSRHRESE RDVRLKKRQK EQQDKEEDDR
RPVPLDPKRP LNDKEQRSLI KAYFRYGSMD DRGDEIIKEA KLKERDPDYV KSVLDEFIKA
AKEAVDDNYA QMVEEEKRLG KTLTKKDRKA VLIDFGDLKK VNAETAIERP KQLQLLRQVI
RSHNDWHTFR LPDATKAASY SCAWGAKEDA MLLVGIDRHG FGAWPQIRDD PDLDMADKLF
LEEHRVEKKE ERSKGNDKMK APGAVHLVRR SEYLLSVLQA KHSNDRGVQR AVENHHRNNK
KSLANGHRGS ATASPAPHNG KKSRDRDRDH LHGDLHRSRS HAEERGTPRP DFKRKHLSHE
DSRSPKHRRI EEHRRSNRER ERERERDRDR ERERERAHDS HPQDERRAKA LRRLDELRRI
GDNKDKRAED NDAMIWFLLK PVRENFERIL STTKDNVKSS KERASIFGVE LVVIGTFLDE
KLAATAADEG LKSNFWDFLA ALWPVDDTSK SVTGKRLSNM YRTLHSRSKG SGSTKTNGA
//
