ID A0A177BXS6_9PLEO Unreviewed; 962 AA.
AC A0A177BXS6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SNF2 family helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC84DRAFT_1168441 {ECO:0000313|EMBL:OAG00324.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG00324.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG00324.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG00324.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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; KV441559; OAG00324.1; -; Genomic_DNA.
DR RefSeq; XP_018030689.1; XM_018179395.1.
DR AlphaFoldDB; A0A177BXS6; -.
DR STRING; 1460663.A0A177BXS6; -.
DR GeneID; 28762881; -.
DR InParanoid; A0A177BXS6; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
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; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16509; RING-HC_HLTF; 1.
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 InterPro; IPR017907; Znf_RING_CS.
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; PS00518; ZF_RING_1; 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:UP000077069};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 369..548
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 707..745
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 786..940
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 106371 MW; A675538D5D2A86A9 CRC64;
MAGQKRPSCD DHGGYEPPRT PLGASASRGY APARASSAAR APKSARTGYD SLPARTAPGS
SQYDPLVIDD ESDEDDASQE VQDSSQSVGE TDMSYVLYGV ISTKIVGVRY YTGHANVGEI
AIPRREPNNQ YDRNAIQVLN VHRQQIGHIP KTQAAKLAAF MDCHSLIVEA TISGRKQYFE
CPLMLRIYGP SDPNTRQLLV ENMRNAGLPP SSWKDATQRQ KAEREREKIA AQAAKRAKKQ
GGAVVGVGRG QQHENGLAEY AAGSSQGVEQ GLSLEDIIGG SERFNPRNAE QFVEEFGIKE
SDLAAMPKAS QPQALSTELH DFQLQGLHWL LDKESPKLPA QGTRDVVQLW KPHPEMRGAF
INIATNFSVT NPALASGGIL ADDMGLGKTI QVISLIMADR ELGRRASDAC NATLILAPVS
VMSNWSTQIK KHIKEEHALR VMFYHSNRKE PITPKSIANF DVVISTYDSV SSEWHSQKST
ALPRKSGVFS VKWRRVILDE GHNIRNPKAK KTIAASNLLA QSRWALTGTP IINNLKDLFS
LVRFLRLSGG LNSLDIFHAA IMRPVMAGDA LGNQALQMLM AGICLRRKKE MSFIDLRLPE
LAEYVHKVTL LPHEQEKYDA FEAQAKGTLD LYRKEARGRN ASDTYRHLLE VLLRMRQLCN
HWKMISEERI DSIMQQLEAK GTVDLTEENK ATLQKMLQLS IDSQEDCPVC LDSYKDPVIT
KCAHIFCTAC IERVIETQHK CPMCRAELES LATTTVKPPK ELAVLPAPTQ EQLADKKSLE
SNASSKVNAL MSILTASAQD PANKTIVFSQ WTTFLTLLEP HLRAANMGYT RIDGSMPATA
RDAALEQFDS SPTCTIMLAS LSVCSVGLNL VAANQVVLSD SWWAPAIEDQ AVDRVHRLGQ
KRETKVFRLV VEGSIEERVL GIQEDKRKLM GLAFAEKESG KKRRAAGVAD LERLLGTQPR
KW
//
