ID A0A1X7RRJ4_ZYMTR Unreviewed; 966 AA.
AC A0A1X7RRJ4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=SNF2 family DNA-dependent ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ZT3D7_G5001 {ECO:0000313|EMBL:SMQ49850.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ49850.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ49850.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; LT853695; SMQ49850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RRJ4; -.
DR STRING; 1276538.A0A1X7RRJ4; -.
DR Proteomes; UP000215127; Chromosome 4.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000215127};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 385..565
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 727..765
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 801..962
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 106511 MW; F270CBDCE1338E47 CRC64;
MAPSSTNNDK RKRVDVDLTG SDDEQTSSRK APRTAAPSSQ ISRSQRPFAA AGSSTSAYSR
PSSSAPTRHV APWSSYNGTH PEAEREAWLA NDIEDDIDEV IASSQDDAAG SDRLRLYGDL
SIKIVGCQYY RGNANPGEHI LMRREPGNPY DTNAIRIDNV SGHQIGHIPR KTAEKLSKYI
DNRWLRCEGQ LAGVKSTFDC PLTVHLFGPD PTSDEGKTLV EKMKVDKLPI RAITDAEKAE
KQRAKAAQEA EKNRLKEARR AAAAGGGSGS ASKGGQPTYA NGHIPNGTQE QQMAEILEAS
ARIHPRGVAA TQQMGMNEDD LKNMPLASQP KGIKTSMLPY QLQALRWLLE HETPALPGPG
TDESVQLWTR SNGGYTNLAS NFTTIQAPPL ASGGILADDM GLGKTLEMIS LIVADAEKFG
RGTTLVVAPL SVMSNWTTQI DAHVKQSSKM SCYTYHGTGR VDSMAAEDFA NYDVVLTTYQ
TLASDFMPRG KDSKQPENKL REKGLYSMEW RRVILDEGHI VRNPQTKGAG AVNNLTSRSR
WVLTGTPIVN SLRDLFSLLR FVGITGGLNQ LDVFNAVLVR PLSNGGAKSE DASILLQAVM
RAFTLRRRKD MAFIDLRLPK LEEFVHRLDF TEKEQTRYDA FRDEAKGLMM KYEQNAAAGA
KTTATYNHVL EVLLRMRQCC NHWGLCKERV SRLLAQLEKQ AVVDLNPENT KALRDILQVQ
IESAEECAIC LETLHEPVIT ACGHSFGKDC IVRVIEGQHK CPMCRAELKD ETCLVKPATE
TGDEKADDEV DLHQSSSKLE GIVKILQATK TDKTIVFSQW TSFLDIVSAR LDKDGVKYCR
LDGTMNVAKR DEAIEALNSD PKTTVMLASL AACSVGLNLT AASNVILSDT WWAPAIEDQA
VDRVHRLGQK KETKVFRLVM EGSIEEETIR IQTDKRKLMA LAFSEKSNKR AAPKTSRIAD
IQRLLA
//
