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Database: UniProt
Entry: A0A3Q3KVX8_9TELE
LinkDB: A0A3Q3KVX8_9TELE
Original site: A0A3Q3KVX8_9TELE 
ID   A0A3Q3KVX8_9TELE        Unreviewed;      2572 AA.
AC   A0A3Q3KVX8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
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};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000001246.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000001246.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
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DR   STRING; 205130.ENSMAMP00000001246; -.
DR   Ensembl; ENSMAMT00000001273.2; ENSMAMP00000001246.2; ENSMAMG00000000877.2.
DR   GeneTree; ENSGT00940000158694; -.
DR   Proteomes; UP000261640; Unplaced.
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:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd18026; DEXHc_POLQ-like; 1.
DR   CDD; cd08638; DNA_pol_A_theta; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.20; -; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR046931; HTH_61.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR048960; POLQ-like_helical.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF20470; HTH_61; 1.
DR   Pfam; PF21099; POLQ_helical; 2.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640}.
FT   DOMAIN          74..253
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          292..519
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          871..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1295..1319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1440..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1539..1581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1629..1696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1712..1747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1793..1823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..986
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1053
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1295..1314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1552..1581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1647..1676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2572 AA;  284358 MW;  C7650E006AB3BDA9 CRC64;
     MKRAKLQHSL QNRSASVLTV PSGLDLSTLS DTLPQPGVWY LLLSSWGLPK PVLERYQKHG
     VTHMFEWQAQ CLTVGQVLRG GNLVYSAPTS AGKTLVSELL MLKRVLETKR KALFILPFVS
     VAKEKMHYLQ TVFEEAGVRV EGYMGSTSAA GGFTALDVAV CTIEKANSLV NRLIEEDSMS
     LLGMVVVDEL HMVGDSGRGY LLELLLTKIR YIAQKQNTTG SLSEGVQIVG MSATLPNLSL
     LATWLGAELY QTDYRPVPLQ EHLKVGCNIY DKSLSVVRQF TPALHIKGDD DHIVSLCYET
     VREGHSVLLF CPSKNWCEKL VDSIAREFYN LTHTDCEGSM AIQPVCLDQE GLVDVIAQLK
     RTPAGLDPIL QRTVPWGVAF HHAGLTFDER DVLEGAFRHG MVRVLAATST LSSGVNLPAR
     RVIIRTPTFN GHLLDPLTYK QMVGRAGRKG VDTTGESVLV CKEAERQKGI TLLKGALKPI
     SSCLVRREGE GVTTSMLRAI LEIIVGGVAS TPQDVRLYAS CSLLAASMKS DGKNKSNEEH
     DKGAIETCVE WLMENEFISI QKDGQGTERY CPTQLGAATL SSSLSPPEAL GIFADLQRAM
     KGFVLENDLH ILYLITPLYA EWTTIDWYQF FCLWEQLSSS MKRVAELVGV QEGFLARSVR
     GKIVAKTEKQ HRQMAVHKRL FVSFFLLSLH RFFTTLVLQD LVNEVPLGTV ASKYNCNRGQ
     LQSLQQSAST YAGMVTVFCK RLGWHNMELL LSQYQTRLSF GVQRELVDLV RVSLLNATRA
     RALYAQGLCT VAELARANVA DVEKALRNAV PFKSSKRAVD ESEMEAAERR GIRCVWVTGG
     RALTEQEAAT EIVSEARLLL QEDLAQLGVQ WDPTALPPGA PTVNSPDSHH RSDSDSSSGS
     CVSSKEAKAS NSKVGDRLKK SESSDTGRHR EVTEEEVKRE KRMTQQKIPM PKEEVRREQG
     KSKPLEMEAS RELEEHKKEG RTEAETRQTS SEAPVDTGKV TKIELENTKL YMTNDTDGIR
     QEHTRSEEER EECKKPNEKD SEKNEDADSV RPWGQQEKRP IAKKSLTQEL SDIVSSLPQL
     LSHAQPLPSP VPCPRFRAPV SRVEQQTSVS TKASTGDGTT GLASSPLQPD RLKHSRALSK
     VLHSIQNDKS LQDNTEASCL ASVNNSAPLA KIPASVQVPE PVLQIPHTVS APSNADLNSP
     LPASPASVPL FFPEAKRRRV EGREGDKFSS PELFAGEERD EEAKGVAQKG EESFGDSFEL
     DTQTERIIGQ QTYQHRDGNG RDRNRLVETE TIKEEEKVET ATEMEIDTDE GRSGSEALDN
     ACPRFNISFT DSQMEFFLNT SHQVTDQHHL YNDFKHEIQC NQMFYFCNKK MLLFSQISLG
     PAGDGSMGKD KNEGHSDDNG PPDANQVTSE SANRSSSFLF DSLFDSSLLA DLSPHQILDQ
     SGEEESNGQD VQDKLPLSST QERRLGNLLA NQEAEKQEAI QWGESSFNLS EWGDSLLVGE
     HFLERQSLLR HTERSKKEQE PCDDQAQQPN ADCVLSEQHL PNSQSKPDGG QRGTIKEGES
     LKRVEKENKQ ENKKEEKLNV LLSDKDSENT FHCSPGLQEI FDRWPSMSDQ PSQNTASGHK
     VTQTVKNPAN AVEAPDLPHP SMQMGRQRGK LNVQSAAAEN DSQLVQCSNH DTENVTERPG
     PATDLLPATQ ETPPVTPRVK QTLLPLQKPL TAQPLNQSTP SAVPPQQPAA PKCPKSHPGL
     SSHSSEAVPH KAQLTFTFDH HNKHQLGQEP NILPEHDLKS VLCLSSKTKP VLHTDHNLSP
     PQDCAAPSSP RPKPPFDTES PVADGFTLQL SQDASLCSSK SGGFSIIDVA SDRRLFDTFI
     KEWKTKERYS LALACELREQ GQQPQEEIGG KHMRVSAAHQ KLDSSTDGFP VRDSGGLVLI
     GLSVCWGSRD AYYISLQKEQ SLSSSLAAPP LEEDLPVSER LGQVKTCLSK PSANRRGDVV
     VTYDIIQVYK TLVLSCGISL EGNCEDPKVA CWLVDPGSDE RTLPNMVTVY CPEELPLLDG
     LGNMHAHCPR VRAATKSVLV HAVMNHLTGL LEKDGMLDLF RSIEMPSQVC LALLELNGVG
     FSVEECERQK HVMQAKLAAL ESQAYNLAGH SFSLTSIDDI AQVLFLELHL PPNGDVGGSK
     NKKTLGYTRR GGGRVRLGKQ FSTTKDVLEK LCPLHPLPGV ILEWRRITNA LTKVVFPLQR
     EKKYHHTLAM DRIYPIAQTH TATGRVSFTE PNIQNVPKDF EIYMPVLVGE SPPSQNGFMT
     DKIIRSVMPS VAAGTAQGPA FSVSMRHAFI PFSGGMILAA DYSQLELRVL AHLSRDRRLL
     QVLNGGADVF RCIAAEWKGV DPDAVNDNLR QQAKQICYGI IYGMGAKSLG EQMGVEENDA
     ACYIESFKAR YKGINAFLKE TVKNCIKNGY VQTLMGRRRY LPGITNTNTH IKAHAERQAV
     NTTVQGSAAD IVKLATVNIQ KRLRQTYPAA PLSHQHTRSA NNQCRAGTSH LRGGYFVLQL
     HDELIYETAE EDLIQVAQIV KREMESAVKL YVKLKAKVKV GPSWGNLQDI DL
//
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