ID A0A010Q409_9PEZI Unreviewed; 1434 AA.
AC A0A010Q409;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:EXF74567.1};
GN ORFNames=CFIO01_10419 {ECO:0000313|EMBL:EXF74567.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF74567.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF74567.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF74567.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF74567.1}.
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DR EMBL; JARH01000973; EXF74567.1; -; Genomic_DNA.
DR RefSeq; XP_007601770.1; XM_007601708.1.
DR STRING; 1445577.A0A010Q409; -.
DR KEGG; cfj:CFIO01_10419; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_001592_2_0_1; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000020467; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 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; 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; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00487; DEXDc; 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 4: Predicted;
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:UP000020467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 326..526
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1113..1151
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1222..1377
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 161369 MW; 824150A458FE2AFD CRC64;
MARTKMTARR GKLLPKTTAI SFHEPWPVDF IHQLQNLPSN DEAQPQNHDM TEPSAKRLKR
SHEDMKSLLV ADEELEFVRK CPEETLPFTR HNVGPHLQLV KDKSNEFGIA SRIKLSAPWI
NISVTTHSNS INQRLAACLY VFAQKRKKTH GEGDVWAEVD VALRPQGDFL SVVFCFKIYW
NETKTPYSWL RSANERQVSQ RVLNTFLQDE TASSSTQQSW SPLDFYEAAH VPPADDETAL
SIDIPELTAK LYPYQKKTIQ WLLGREGVRW RNSSTESVSD IEELPVSLGT DIAHSFRKVR
TQGEFGQLFY VSDLYHVVTT DLTAFQQAER DIRGGILAEE MGLGKTLEVI GLVTLHRRPP
TDSHIVTQEG DELLTTGATL IVTPESLRNQ WIAELQRHAP HLRVKFYPGR KNVNFDTEDA
LRADLASYDV VITTYPILSA EVHFALKPPD RSRRQERKYE RLVSPLTRIS WWRVCLDEAQ
MIEGGVSGAA IVARVLPRVN VWGVTGTPVK NDVKDLHGLL SFLRYEPYAS SPQIWKALTE
SHKPLFKSLF GSIALRHTKQ LVRHEITVPP QKRYVITLPF TAVEEQYYGE MFKTMAKSCG
LDLLGAPVKP DWTPEKNEAE MRTWLNRLRQ AALHPEIVQI RGTGRKVGPM RTVDEVLDAM
IEQSENDIRA DHRAYLQARL TRGQMLENSP RVKEALEIWE KVKMDAMDLV AECRQEVKTA
VGTLPGEISA AARGGDDSDQ GEGDEGSTNA VVGEARTKLR HALEVLHKAT FFCANAFFQI
KSNTDMTEPD SDDFKKYQKL EDEEYSKAQE VRREILSESH ARAMSLMNSL GRQAETQSFV
EIPELTLSGP KGLESAPTLD TLEELYGVLN EQADRIDEWR EALIGLLCQA LIDEEAENEV
TGEEFTDSTQ IQEELIVHVQ ILRAAIADRQ DAISGLENAL VRHETNVSLT AAENGDGPAP
KKFLALNEAR NSVKPSPVRH GSLRRAIAEL RAIASRLPKD GGGRASLEHG IVTKQIQQTQ
ANITAQTKAA TALERETDRF TSAMNARVEY YRQLQAVSDS VAPYEGPNDG PAVASCIASE
NNYRRKLDSS KAKHRYLLNL KMDGGKSNEP RMCIICQSNF TIGVLTVCGH QFCKDCMKHW
HKAHQNCPMC KRKLRLTELH DITLKPRELK LHDETPVSAS PGVKKDEAAK TNGIYSRFST
EKLAQINDIE LLRMSFGTKV DSIVRHMLWL RESDPGAKSV IFTQYKSFLA ILGEAFNRYQ
IGFSSIDRPG GIMKFQNDAS IECFMLHGRA NSSGLNLVNA SHVFLCEPLL NTALELQAIA
RVDRIGQKNE TTVWLYLIEG SVEESIYNLS VKRRMEHMGQ NSKGKSKEST PEVQEPTLEA
ANTLELEQAH LNQLMSRDKN AGEAVATDDL WECLFGRVSR RITSSVAEEI VAED
//
