ID A0A0G2HBW2_9PEZI Unreviewed; 838 AA.
AC A0A0G2HBW2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative swi snf family dna-dependent {ECO:0000313|EMBL:KKY32693.1};
GN ORFNames=UCDDA912_g07399 {ECO:0000313|EMBL:KKY32693.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY32693.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY32693.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32693.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY32693.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32693.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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}.
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:KKY32693.1}.
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DR EMBL; LCUC01000292; KKY32693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HBW2; -.
DR STRING; 1214573.A0A0G2HBW2; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 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; IPR000048; IQ_motif_EF-hand-BS.
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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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; PS50096; IQ; 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|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 80..257
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 416..476
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 669..833
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 453..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 95078 MW; 9E6FB52132E7AE31 CRC64;
MDRPVLSLQG RLAAFIRAVE HRFPGAPEKS EAIRFHVLNP IARGTNPEDC LDFVRKFLRK
AKELVVDFED IASLTWLLEQ EKDRQKKGGL LADTMGLGKT VQAMALILAH PSNDPRHKTT
LIVAPLALLR QWEQEILTKV KPRHKLNTLV FHGQVAKYLT VSELLKCDVV LCTYGKLQTE
YKNKFEHKKP EKLRILSDKA KFYRIILDEA HNIRNQTTYC SKAAAELQST YRLCMTGTPF
MNRAEEIFPL IRFLNIPPYN KWDRFSEDIV RPLRNWEGDI QDRGMVKLQA LFRSFTLRRT
KESRLDGKPI IELPPRTDQP AYVEFNDEQR KFYQALEVQQ QLTFNKYLLN GAVMKNYIHI
LILLLRLRQA CDHPFLLKNL GIPEGTKLDE KQMIKLACQL PGDVVQELKR QKRFECLICS
NVTDNPVIVH PCGHHICSSC FTASVTVMET ENFNGNREDD DNSPKKEHRV PCPGDNCEHA
ITPTNIVCYN FLTDVPDSAS ESDNDRMNKD PFCGGSRDDE DDADQHGNLQ GFVVDDEATR
MEDNSDDDES DVDSQDCEDD DEEHEGDGDG RMAYIGGFGS SQTDGAYDDL GTDQTFRTPK
RKPSAATMGG HSGKKSRTSA ESPRKKEKSR SKKKKVLTMA GHRQAAQRSA IAMSRYKARL
RAEWISSAKV DAIMEILEQI RPKQEKTLVF SLWTSFLDLV EIPIERARIK FTRYDGSMTP
SGREAAVKSF MEDPGVRVML VSLTAGNAGL NLTAASQVIV TEPFWNPFVE EQAIDRAHRF
GQERPVTVHR LLIAGTVEDR IVTLQEKKKK LVDAALSERG AANVSRLNVA DLRNLFGL
//
