ID R7QU31_CHOCR Unreviewed; 1048 AA.
AC R7QU31;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA replication ATP-dependent helicase/nuclease {ECO:0000256|RuleBase:RU367041};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU367041};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367041};
GN ORFNames=CHC_T00007752001 {ECO:0000313|EMBL:CDF41218.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF41218.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT "Genome structure and metabolic features in the red seaweed Chondrus
RT crispus shed light on evolution of the Archaeplastida.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair.
CC Involved in Okazaki fragments processing by cleaving long flaps that
CC escape FEN1: flaps that are longer than 27 nucleotides are coated by
CC replication protein A complex (RPA), leading to recruit DNA2 which
CC cleaves the flap until it is too short to bind RPA and becomes a
CC substrate for FEN1. Also involved in 5'-end resection of DNA during
CC double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
CC {ECO:0000256|RuleBase:RU367041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU367041};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367041}.
CC Chromosome {ECO:0000256|RuleBase:RU367041}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913, ECO:0000256|RuleBase:RU367041}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG002328; CDF41218.1; -; Genomic_DNA.
DR RefSeq; XP_005711512.1; XM_005711455.1.
DR AlphaFoldDB; R7QU31; -.
DR STRING; 2769.R7QU31; -.
DR EnsemblPlants; CDF41218; CDF41218; CHC_T00007752001.
DR GeneID; 17319229; -.
DR Gramene; CDF41218; CDF41218; CHC_T00007752001.
DR KEGG; ccp:CHC_T00007752001; -.
DR OMA; NYCEAAI; -.
DR OrthoDB; 170190at2759; -.
DR PhylomeDB; R7QU31; -.
DR Proteomes; UP000012073; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR CDD; cd18041; DEXXQc_DNA2; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR026851; Dna2/JHS1_DEXXQ-box.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR10887:SF433; DNA REPLICATION ATP-DEPENDENT HELICASE_NUCLEASE DNA2; 1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 2.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU367041};
KW ATP-binding {ECO:0000256|RuleBase:RU367041};
KW Chromosome {ECO:0000256|RuleBase:RU367041};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367041};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367041};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367041};
KW DNA-binding {ECO:0000256|RuleBase:RU367041};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU367041};
KW Hydrolase {ECO:0000256|RuleBase:RU367041};
KW Iron {ECO:0000256|RuleBase:RU367041};
KW Iron-sulfur {ECO:0000256|RuleBase:RU367041};
KW Metal-binding {ECO:0000256|RuleBase:RU367041};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW ECO:0000256|RuleBase:RU367041}; Nuclease {ECO:0000256|RuleBase:RU367041};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367041};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041};
KW Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT DOMAIN 42..259
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 627..722
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 729..798
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 835..959
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT DOMAIN 967..1021
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
SQ SEQUENCE 1048 AA; 115443 MW; 50F41FCD2631E5B6 CRC64;
MSAVAPNPLP VGPARASSAR LLVLEAVPHP DSKVLRTVDT ITGKQLSVAL CDEWMHSNVN
QNDIVRVLLT RPDGSYLPWD SAPVDEQHPV FVTRDNHLFV HHPDTLVSGT SIADSFLCLR
KSLLTARVPP RSILQSTGGE AALFGSMIHD LFQNLLAIRT LDALDVYESV EIILQQHLED
LYAAKISDAD ARLVLHNVIP SIMEWFKGFA RLDGGENSAG VKVTGGKQTY SMGIGDVYDI
EELVWSPIFG LKGKIDASVI LCSNDEAGGI GVVELKTGSS VGYASVSHSA QVNLYNLLMS
DRYSKHTKGN FTRHPNNKAV SYVRGEVVGL LMQRNEFASY ARFDSDFRRL PPLLQGREDL
CAKCFANDTC MIQHKLLENG SSETVKGGPG PGLFREKAMH LTDEHAAYYM FWRRVLADEE
AHAARPQNEV WNMRGSQREA LGRCLSNLRM VEDSAGSQDG RVNYLLPPGQ RMTVTFQRHH
GDALQAPLND AALAENDFVL VSAESLNTSA GSSQQSIFTW QSALTNGFIQ STSPSSVAVV
IDRSLFAWAR NQAVNVNDII WRIDSVEIHS SHNTAKRTLE NLFCCDETTD LGRLRGLVVD
GTRPRLTEFI IGSQSTTVLK KEFNVTLNDD QDRALQMALR TRDYLLVLGM PGTGKTTTLA
AIVLAYASQG KSVLLCSHTN SAVDNLLQRL LAAGFRDFVR LGRNKRVISK AIHPYHISTL
TADASTTKHL ETVLEQPKVV ATTCLGINHP LLLRRGRFDL VVVDEASQVL QPICLGPLQF
AAGPFILVGD HYQLPPLLRA QQANESIVVV RNAMDASQAC NGTPAIRLNP ENQRNESLFR
RLCEFHPEAM ISLSQQYRMS SEIMRLSNEL VYSGSLSCGS EEIANQRLVT SLAAMEGKAS
WLQAILDQSR AVIFLDMPED CTEDKEPTKN PEKLEKLEAS RRNNLREAGV VCKCVSALEQ
GNGMLDTNVY TIDQYQGRDS DCVIVSFVRC SGSVGPLLKD WRRVNVALTR AKQKLILVGC
SKTLAKGSHF LRGMITLLEN TQSVVPVS
//
