ID A0A163C4E3_DIDRA Unreviewed; 1315 AA.
AC A0A163C4E3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=ST47_g6687 {ECO:0000313|EMBL:KZM22200.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM22200.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM22200.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM22200.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
CC -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by
CC homologous recombination and in genome maintenance. Capable of
CC unwinding D-loops. Plays a role in limiting crossover recombinants
CC during mitotic DNA double-strand break (DSB) repair. Component of a
CC FANCM-MHF complex which promotes gene conversion at blocked replication
CC forks, probably by reversal of the stalled fork.
CC {ECO:0000256|ARBA:ARBA00003813, ECO:0000256|RuleBase:RU367027}.
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:RU367027};
CC -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC MHF complex. {ECO:0000256|ARBA:ARBA00011390,
CC ECO:0000256|RuleBase:RU367027}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367027}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889,
CC ECO:0000256|RuleBase:RU367027}.
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:KZM22200.1}.
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DR EMBL; JYNV01000223; KZM22200.1; -; Genomic_DNA.
DR STRING; 5454.A0A163C4E3; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
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:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR Gene3D; 1.20.1320.20; hef helicase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 358..526
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 699..862
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1099
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1315 AA; 146015 MW; ECC06D1AE8F05215 CRC64;
MSDDDDYGDG YDDTEFLNAA TQVEVEKENT PAFRPSPRPT KRRKVSQACE KAKPIPSRKT
PVRRRQPFAA SSNHDESDVA ADNESFGVNG KDDSPATSEE PQEKQPSSRK KRAASKQQND
VVDEDEDASP ARTTIAQKRR DRIHIPTTEL DMTDIFFTQP PQEHSPPWKP RGAIWAKPTS
IGVHKPLAEP TKWTGLDAMK TMALPGRQSI SSRPKAITPV AVDEPESPIE DDRILQSPSI
IGAQVAYDYA QDLADLPSDA FSSSTASPQK QDGDGDIIML AESRKRIAPP QGSLRQTTLF
GRQGASGQIP PSQANKRYNF IVDQRQEPPT HHKLDHEALK TWVYPTNLGT IRDYQFNIVQ
RGLFHNLLVA LPTGLGKTFI AATIMLNWYR WTTESQIVFV APTKPLVSQQ VGACFGIAGI
PRSATTMLTG GIQPGLRSEE WKSKRVFFMT PQTLLNDLKN GYADPKKIVL LVVDEAHRAT
GSYAYVEVVS FLRRFNQSFR VLALTATPGA DVESVQKVID GLDISRVEIR TENSMDICNY
VHQRTVEKRV FQNSDEMEMC MDLYSQALQP LVNQVAGLGA YWSNDPRTLT PFGCTQAASK
WTNEAGRHAN PGVKNMVRTI LTLLASIAHG MDLLKFHGMA PFYTKLKDFR DDSHKTKSKY
RKQVLDSDAF KKLMARLDTW VNDENFAGHP KLEYVQECIL EHFVNAGEGP NASQTRIMVF
AHFRDSAEEI VRILKKHEPM IRPRVFVGQS TAKNSEGMNQ KEQLEVIDKF KAGTFNTLIA
TSIGEEGLDI GEVDLIICYD SKASPIRMLQ RMGRTGRKRE GKIIMLQMQG KEENDANKAK
DSYEKMQELI ANGSHFTFHD EISRRIVPSD VKPVVDRRAI EIPPENSQQG WLPEPKKSGR
TKKPPKKFHM PDGVLTGFVT AGCMGEEIVP KGRGKKAPAI MYPSEEVLEV PSLELVLLDG
SATNDLERRF QTVYDDDDAP MVGALDLSQH ADHQRTLTHT ELLSRPGQKT RNFVSTMQRI
HAMNSDRIEL FKRNLHHSDY ESDCVGDDVL TANTDLRPLI CEDMWAEDGP TSEELTTTKA
KPKAKSKAPP KPKAKSVPKP KTKAPRETPA PRGRPRKETA ATAAAVETPI RPPKAKSQTP
RTRTPNWKVS ALAGEGEESS PPPTDPRFCV ASQADTIGSD DTNDGEEEDP SLWKLDSELN
SFIVDGTVEE EDEVPASSLP GLDFNGLGKA TQAMIRSATK PKRSVKAEKL FTSDITDDDA
VVSSDSDDDA PLVKLGGDAN GKLAFVVASD SEEESAPVVP RKRARRVIDD DEDDE
//
