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Database: UniProt
Entry: L2GDU8_COLFN
LinkDB: L2GDU8_COLFN
Original site: L2GDU8_COLFN 
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
//
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