ID A0A1V8TZQ5_9PEZI Unreviewed; 839 AA.
AC A0A1V8TZQ5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN ORFNames=B0A51_16557 {ECO:0000313|EMBL:OQO16766.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO16766.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC transmission and normal cell cycle progression in G(2)/M (By
CC similarity). May have a role in changing DNA topology to allow the
CC loading of proteins involved in maintaining sister chromatid cohesion
CC in the vicinity of the centromeres (By similarity). Has a specific role
CC in chromosome segregation during meiosis II.
CC {ECO:0000256|ARBA:ARBA00025396}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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:OQO16766.1}.
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DR EMBL; NAEU01001144; OQO16766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TZQ5; -.
DR STRING; 1974281.A0A1V8TZQ5; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 3..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 111..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 92641 MW; 27BC68E8BA98FA9E CRC64;
MAPSKDFHHP YQPYEIQQQF MQAVYDCIED GKVGIFESPT GTGKSLSLIC GALTWLREHK
GKMFDEAMQS VQIDDDEPEW MLEHARSSKR SEALQMRADF EERLALVREK DRKTREHAAK
ATHLQKRRKQ GDGKTDLDDA YVEQFALNDY ESDKDGNGGE MSKYSAGTTD VLKKLGLLGA
EDQDARPTEM DEELKIFFCS RTHSQLSQFV GELQRARLPP GLPPGDSIST GTTSTYEEVK
QISLGSRKNL CINPEVNKLE SQTAINERCA ELQQSKTPSA KKCSFLPNKD NEELVLDFRD
HALASIHDIE DLAAVGKKLG ICPYYASRSA VDPAEIVTLP YPLMLQKSAR EALGISLRGH
VVIIDEAHNL MDAVESTHSA QITEVQLRFG REALMIYLQK FRNKLKDGNR LYVTQLVRVI
DSLLLAVTQV QAVSGAGGVL DASALLAGKA VDQINMSKLA KYISESRIAR KVEGYAAHLK
QTDVVNGGVE QASGVSDTPI LTHVQNFLTT LANPSKEGRF FWSRDESDKS ITLRYLLLNP
SEHFRDIVAE ARTVILAGGT MSPMEDYTAQ LFPYLTSASI STLSCGHIIP ASHLFVRTIT
SDASTSPLNF TYKTRSDTTL IRRLGNMLLE LLPKITGGTV IFFTSYAYLS QIQTQWSADS
TLTKLAALSK PLFFDSRSSP AEATFASYST AIHSNPTRGA VLFSVLGGKL SEGINFSDAL
GRCVIVVGLP FPNLETPEWK AKAEFLDRQP GAKPGAGRLH AENICMRVVN QAVGRVIRHK
GDWAGVVLVD GRFGQERILR KLPGWIKRSL PEGGGSGRVR DVSEGLGEFF NERTAKQVA
//
