ID A0A401RM13_CHIPU Unreviewed; 2084 AA.
AC A0A401RM13;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=chiPu_0018264 {ECO:0000313|EMBL:GCC19202.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC19202.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC19202.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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:GCC19202.1}.
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DR EMBL; BEZZ01001519; GCC19202.1; -; Genomic_DNA.
DR STRING; 137246.A0A401RM13; -.
DR OMA; EDCIEWI; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd18016; DEXHc_RecQ2_BLM; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR012532; BDHCT.
DR InterPro; IPR032437; BLM_N.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF08072; BDHCT; 1.
DR Pfam; PF16202; BLM_N; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
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:UP000287033}.
FT DOMAIN 716..891
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 906..1064
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1253..1333
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 135..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1649..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1391
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2084 AA; 231249 MW; 5FC061F27B70E2EC CRC64;
MYFIIDRAFT FKKILPGTVG TPSFQGLNNT CALKDRDVNA FKNVIVSKPQ LNLHSTKPKE
QQPKINNILK QTTKQSELTS QTAFPLLSSS PALRHAAITS PVSQKLDPEQ SFSSVINLDD
WDDLDDFETP WKESSRLKVT SPSSTEPTVQ KTNNLKNINS SGLTSPKIGS DQYLKNAASE
EIKDNPARLS PREPGAELKD VNNIAICLGS SQKELLHSDD EDCIKSFPSR RKSSSSAVRI
ILSDDESDGS RKEVEEEKID LTDADRLLSS QPQLDTIPTA CSQSRDLENE GYESDCIPPS
PESDQISLPS FIKCLSDSAE TVRSKERSKS LACSRPEENE HSEEPMCTSD NPRDKDTPVG
YSNQLIQVME NICRLVEQIP ASELQHLSCA SQLLQQRELR RKLLADQNEA QSTLNGGIST
AVTLSKQSSA VSNISTDRVT SPISVNSSQG SGSPKTFTFK KSSLKTTGMP RDNFFSTEDF
FAVDQTSAHT GKKSATSDNC KSLLSKSCFQ RKLDLSTGGN KASPPSTPQS KYSSLNCISY
GSSDAASRND LDKSTRVSAA GMHTAADQKR FVEDSRSCMA EEDLMFDDID IDNFDIDDLD
VEEVPECFLN SPSQPAGNIS HGAIQPIREG GTKTAWRKTP AQDGSEHTSR PSATASIKKS
QALLGSSEAS HEQGHSRSPV LERFRGFHFP HSKEMMRIFH KKFGLHQFRT NQLEAINAAL
LNEDCFVLMP TGGGKSLCYQ LPACLTQGVT VVISPLRSLI LDQVQKLTLF DIPATHLTAS
KSDSEVASTY MQLSKKDPIV KLLYCTPEKV SASNRLIAAL VNLYERKLLS RFVIDEAHCV
SQWGHDFRPD YKKLNELRSR FPTIPMMALT ATATPRVQKD ILNQLKMLKP QVFTMSFNRH
NLKYEVLPKK PKKIAEDCIE WIRRNYPRDS GIIYCLSRHE CDTVAETLKR NGIAAMAYHA
GLQDSNRDFI QNRWINQEDC QVICATIAFG MGIDKPDVRY VIHATLPKSM EGYYQESGRA
GRDGETSHCV LFYSYSDVTR IRRIIQMEKD GNQFTKQTHF NNLYNMVHYC ENVVECRRIQ
LLAYFGENGF NSQFCKEHPE VACDNCLRKK NYKTRNVTGE VKNIVQFVQK HCASANGRIH
SASQPSSRLT LNMLVDIFLG CKNARIQSGI FGTGAAYSRH NVERLFRKLV LDRILREDLY
ITANDQAVAY VTAGEKAQQV LKGLHQVDFQ ETDNASSIRK QRNSMAKNVS KREEMVKQCL
TDLTELCKKL GKTFGVHYFN IFNTATIKRI AESLSSDPEV LLQIDGVTED KLDKYGGELI
EVLQKYSEWQ LPEEEAFEAR TSDSWIDCGK SQEEEEEQCE ETSVYFNKSK NTNNRKRKKG
SYYRRTKKRK TGYNNQQSSK SSNTKFATTS KHSNPRPATG NRRPGLLFSR ASYPRGRCGF
QDGGCESALS LVAGNGGREM SPFMSQISCS APGSGRSAPG TAASFPSKAM KPGARGTALG
RQPTAAGSVN RKRRLGPGGG GGETPGPETP GRETPGRGTP GRETPGPETP GRGTPGRSSN
RRVRQDGADQ RQVPAAQGDI PPGPTSPAEP GMAPSDSDGF STDDEFPLSF HRQSEGLSLY
EKKRLKNIQE NARFFASLNM QETAAKLREI GKRRQTKRPN ASKRKKLQSS GVQPIVRRSM
RLLRLDPTGT PLPEIPIEIQ KESEERISGP VKMVQDDEDD SKETPHLMKI WLEMSQGEVH
TKKKQPVELK TYKSTLHRMT MQEGFVAKVT PSRVGSLAFH PSPRNFLVAA GSTYGHIGLW
DLSSQEGTVH QFKPHCNTIN CLHFSPSNSA ELLSLSNEGS IRCGNVAAAV FDEVYTSDTW
ATSSFDFLAE DGSTLIVSHW DGNVAVVDRR TPSTSGELDA DLGVNHFRTV GVHPMHRQYF
VAAGTRCAAI YDVRNLKASP KKAVASLGIH TKNVSSAYFS SLTGNKVVTT CMDDRIRIFD
TSAIIPKIPV VASIIHNNCT GRWLTKFRAV WDPKRDDCFV VGSMARPRQI EVFHFTGSKV
REFRDMEWLG SVCSINVMHP TRNVLVGGNS SGRLHVFTDG ALSG
//
