ID A0A3Q4A8K7_MOLML Unreviewed; 1794 AA.
AC A0A3Q4A8K7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000000145.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000000145.1}
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR STRING; 94237.ENSMMOP00000000145; -.
DR Ensembl; ENSMMOT00000000145.1; ENSMMOP00000000145.1; ENSMMOG00000000073.1.
DR OMA; KAKSRFM; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 278..325
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 355..402
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 390..448
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 485..520
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 602..786
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 918..1067
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1794 AA; 204053 MW; 755EE62796F15D5E CRC64;
MDVGGAEDAD DGGPGQRSDS EGSDYTPGRK KKKRAGSGKE KKRSSAGAER SASKKKDPEP
EEDDDDDDDD GLEPKSSSQL LDDWGMEDID HVFTEEDYRS LTNYKAFSQF VRPLIAAKNP
KIAVSKMMMV LGAKWREFST NNPLRGAAAA NAALATANVP SAVENMVAKT KEGKGPNARR
KSKPAPKPQE KKNNAKTKKV APLKIKLGGF NSKRKRSSSE EDEPDVDSDF EDGSMNSVSV
SEGSNSRSSR SKKKPSKSKP KKKKAEAEDG DGYETDHQDY CEVCQQGGEI ILCDTCPRAY
HMVCLDPDME KAPEGTWSCP HCEKEGIQWE AREEASEGEE DNGDAGEMEE DDHHMEFCRV
CKDGGELLCC DSCPSSYHIH CLNPPLPEIP NGEWICPRWR PEREFFAKWC NMSYWHCSWV
TELQLELHCQ VMFRNYQRKN DMDEPPPIDF GEGEEDKSVK RKNKDPMYAQ LEEKYLRFGI
KMEWLMIHRI LNHSVDRKNN VHYLIKWREL PYDQATWEAE DMDVPEFDIY KAQYWNHREL
MMGEDGRPGK KIKVKGRVKR PDRPPENPVV DPTIKFERQP EYLDSTGGTL HPYQLEGLNW
LRFSWAQGTD TILADEMGLG KTVQTAVFLY SLYKEGHSKG PFLVSAPLST IINWEREFEM
WAPDMYVVTY VGDKDSRAII RENEFSFEDN AIRGGKKASR MKKDSSIKFH VLLTSYELIT
IDMAILGSID WACLVVDEAH RLKNNQSKFF RVLNNYPLQH KLLLTGTPLQ NNLEELFHLL
NFLTPERFSK LEIFLEEFAD IAKEDQIKKL HDMLGPHMLR RLKADVFKHM PSKTELIVRV
ELSPMQKKYY KFILTKNFEA LNTKGGGNQV SLLNVVMDLK KCCNHPYLFP AAAIEAPKMP
NGMYDGSALT KSSGKLLLLQ KMMRKLKEGG HRVLIFSQMT KMLDLLEDFL ENEGYKYERI
DGGITGGMRQ EAIDRFNAPG AQQFAFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA
FSRAHRIGQN KKVMIYRFVT KASVEERITQ VAKKKMMLTH LVVRPGLGSK TGSMSKQELD
DILKFGTEEL FKDEGEGDNK EEDSSIIHYD DKAIDRLLDR NQDATDDTEL QSMNEYLSSF
KVAQYVVKDE EDEEEEVQRE IIKQEESVDP DYWEKLLRHH YEQQQEDLAR NLGKGKRIRK
QVNYNDGSQE DRADWQDDQS DGQSDYSVAS EEGDEDFDER TEANSRRPNR KGLRNDKDKP
LPPLLARVGG NIEVLGFNSR QRKAFLNAVM RYGMPPQDAF TTQWLVRDLR GKSEKEFKAY
VSLFMRHLCE PGADGAETFA DGVPREGLSR QHVLTRIGVM SLIRKKVQEF EHVNGQWSMP
WMAELEESKK AAQPDSPGKT PSTGTPADTQ PNTPAPVDDS SSKSDEAEKE VKKEGEAEKN
GKETVISIPD DDEKSPPSEQ ESKKNGEEPM ETDKPSNGDS EGVKEKEGES EKKSPEGVEE
TKTEGSEVNP EEPEGKAEEK KEEKMDTAPP ADEKKDLKEE KEAQKPEEAT KLQNGDSNKE
SGAPAAAASE EKKKAKTRFM FNIADGGFTE LHSLWQNEER AATVTKKTNE IWHRRHDYWL
LTGIIQHGYA RWQDIQNDVK FAILNEPFKG EMNRGNFLEI KNKFLARRFK LLEQALVIEE
QLRRAAYLNM SEDPSHPSMA LNTRFSEVEC LAESHQHLSK ESMSGNKPAN AVLHKVLKQL
EELLSDMKAD VTRLPATIAR IPPVAVRLQM SERNILSRLA SRGPETQTQQ TQQQ
//
