ID L2GDU8_COLFN Unreviewed; 874 AA.
AC L2GDU8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Snf2 family helicase {ECO:0000313|EMBL:ELA36829.1};
GN ORFNames=CGGC5_456 {ECO:0000313|EMBL:ELA36829.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA36829.1};
RN [1] {ECO:0000313|EMBL:ELA36829.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA36829.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) 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; KB020503; ELA36829.1; -; Genomic_DNA.
DR RefSeq; XP_007274233.1; XM_007274171.1.
DR AlphaFoldDB; L2GDU8; -.
DR STRING; 1213859.L2GDU8; -.
DR EnsemblFungi; ELA36829; ELA36829; CGGC5_456.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
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: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; 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; 2.
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; 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; 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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:ELA36829.1};
KW Helicase {ECO:0000313|EMBL:ELA36829.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000313|EMBL:ELA36829.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 345..513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 669..707
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 96788 MW; 84208CF936237C9E CRC64;
MPPKKRGLDV IDLISSEGEN SSAPPPSKRP AVNRGPSLGQ SSGARVAGSQ PYNTQRTASS
SSFAGPSSQN VYYDRDDADL IDLTQAPDGP ARELYGNLDT KIVGVRYYNG YASQGEVVVC
LREPTNLYDS NAIRVCNVMG IQIGHIPRKV AEKLAPYVDN DDVALEGTLT GEKGVFDCPV
RLHLFGTGDR EQRLQLEDRL KKDKLIKATE LKKTRAEAGA QRKALGIKNS QSTIGLGGSA
SAAPEPEVSL EQLTQASQAL QTHSRGDAVK SLIIDEDTLA AMPMAEQAAV LEAQLLPYQL
QGLAWMTSKE SPQFPPKGTT ESIQLWQRIP KNDKVMSNMA TNFVMNEPKL LSGGILADDM
GLGKTLQVIS LILTGGPGTT LIVAPLSVMS NWEQQMRRHV KKEHLPSIYT YHGSNKVGKD
ELTKYQVVIT SYNTLAMEGP KKSEDSVPKT SPLMQMKWRR VVLDEGHTIR NAKTKAAIAA
TKLTAQSRWA LTGTPIINNI KDFQSLLQFL HITGGVEQPV IFNTVIARPL AQGHQRAETL
LQLLMRDLCL RRKKDMKFVD LKLPPKTEYV HRIQFRPDEK NKYEALLNEA KGALEDYRNQ
TKAGKGQFQS VLERLLRLRQ VCNHWTLCRK RIDDLLKVLE GQSVVSLNPE NVKILQEALR
LYIETQEDCA VCLDTLDSPV ITHCKHVFCR GCITKVIQTQ HKCPMCRNQL EEDSLLEPAP
EGGEEAADDG FDSDGKSSKT EALVKIVQAT TKDPKSKIVI FSQWTSFLNI IQAQIAEAGI
KFCRIDGSMT AAKRDAAIDA LDHDPNTRVM LASLAVCSKR PTTVWRLVME GTVEERVLDI
QHEKRTLVGK AFQEKNKGKK TQETRMADIQ KLLG
//