UniProt: A0A1L8FMG5

Database: UniProt
Entry: A0A1L8FMG5_XENLA

LinkDB:  A0A1L8FMG5_XENLA 
Original site:  A0A1L8FMG5_XENLA

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (39)   
   InterPro (19)   
   Pfam (8)   
   PROSITE (6)   
   SMART (6)   
All databases (48)   

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ID   A0A1L8FMG5_XENLA        Unreviewed;      1949 AA.
AC   A0A1L8FMG5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=chd5.L {ECO:0000313|RefSeq:XP_041425344.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_041425344.1};
RN   [1] {ECO:0000313|RefSeq:XP_041425344.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041425344.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041425344.1};
RG   RefSeq;
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   RefSeq; XP_041425344.1; XM_041569410.1.
DR   STRING; 8355.A0A1L8FMG5; -.
DR   PaxDb; 8355-A0A1L8FMG5; -.
DR   OMA; KVQKIMH; -.
DR   Proteomes; UP000186698; Chromosome 7L.
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; cd18667; CD1_tandem_CHD3-4_like; 1.
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:SF6; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 5; 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; 1.
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:UP000186698};
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}.
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1318..1373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1509..1657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..30
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..406
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1351..1372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1586..1657
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1949 AA;  223228 MW;  A89BE889CE475E9D CRC64;
     MRGPLGMEED PIEDMENEEM SEEEAGGMEA IDFFSEELPP KRKKSKKSKE GKLSKTKRRK
     KEGSDADVSE NEDELEEKSE SEGSVYAPNK KKKKKLKEKK EKKAKRKKKD DDDDNEDGGI
     KEPKTSAQLM QEWGLENVDY VFSEEDYHTL TNYKAFSQFL RPLIAKKNPK IPMSKMMTVL
     GAKWREFSAN NPLKGSSAAA AAAAVAAAVE TVAVAPPLLV SPPQPVQPAP IRKAKTKEGK
     GPGVRKKSKS SKDSKKKAKG KKVTNLKFKF GGMASKRRKG SSSEEDEREE SDFDSASINS
     SSVRSDISAG LGKRGKRVKK KKKVEEGDGY ETDHQDYCEV CQQGGEIILC DTCPRAYHLV
     CLDPELEKAP EGKWSCPHCE KEGIQWEPKE DDEYEEDGGE EEEEEEDDHM EFCRVCKDGG
     ELLCCDTCPS SYHLHCLNPP LPEIPNGEWL CPRCTCPPLK GKVQRILHWV WREPSPPSIF
     PSDIDPLMPP PKPIEGIPER EFFVKWAGMS YWHCSWVKEL QLELYHTVMF RNYQRKNDMD
     DPPPYDYGSG DEDGKSEKRK NKDPLYAKME EKFYRYGIKA EWMIIHRIMN HSFDKKGDIH
     YLIKWKDLPY DQCTWEIDNI DIPDYETMKQ SYWDHRELML GEDARPLRFK KNRKMKDENL
     EKPPLVPIVD PTVKFDKQAW YIDSTGGTLH PYQLEGLNWL RFSWAQGTDT ILADEMGLGK
     TVQTIVFLYS LYKEGHSKGP YLVSAPLSTI INWEREFEMW APEFYVVTYT GDKDSRAVIR
     ENEFSFEDNA IKSGRKVFRM KKEAQIKFHV LLTSYELITI DHSILGSIEW ACLVVDEAHR
     LKNNQSKFFR VLNSYKIDYK LLLTGTPLQN NLEELFHLLN FLTPERFNNL EGFLEEFADI
     SKEDQIKKLH DLLGPHMLRR LKADVFKNMP AKTELIVRVE LSQMQKKYYK FILTRNFEAL
     NSKGGGNQVS LLNIMMDLKK CCNHPYLFPV AAVEAPVLPN GSYDGNSLVK SSGKLMLLQK
     MLKKLKDGGH RVLIFSQMTK MLDLLEDFLE YEGYKYERID GGITGGLRQE AIDRFNAPGA
     QQFCFLLSTR AGGLGINLAT ADTVIIYDSD WNPHNDIQAF SRAHRIGQNK KVMIYRFVTR
     ASVEERITQV AKRKMMLTHL VVRPGLGSKS GSMTKQELDD ILKFGTEELF KDDVEADHHC
     GTLTVYKKTG DNKDVEDSSV IHYDDAAISK LLDRNQNATE DTEIQNMNEY LSSFKVAQYV
     VREEDGVEEV EREIIKQEEN VDPDYWEKLL RHHYEQQQED LARNLGKGKR IRKQVNYNDA
     SQEDQEWHDD LSDNQSEYSV GSEDEDEDFE EKPEGGRRQS RRQLKSDRDK PLPPLLARVG
     GNIEVLGFNA RQRKAFLNAI MRWGMPPQDA FNSNWLVRDL RGKSEKEFRA YVSLFMRHLC
     EPGADGAETF ADGVPREGLS RQHVLTRIGV MSLVRKKVQE FEQVNGKYST PDLIPESVQN
     KKCFDMVSSD PNTPVAASPA PLPPGTTAMT EKCDAQSVMQ EDSEMVELKL KYPAEAQPTA
     KQEKSEQEEV NEELDMKDVE EDEEKEPADQ NSKAETREEQ EKQSDKSEPC VTPNKLEDKE
     PKTGEDKKPD EKEECETQQN GENDIKQEED EGKKEDKNGK FKFMFNIADG GFTELHTLWQ
     NEERAAISSG KMYDIWHRRH DYWLLAGIVT HGYARWQDIQ NDPRYLILNE PFKSEIHKGN
     YLEMKNKFLA RRFKLLEQAL VIEEQLRRAA YLNMTQDPNH PAMALNARLT EVECLAESHQ
     HLSKESLAGN KPANAVLHKV LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL
     SRLTNRGGDP TLQGTFGSSQ MYNNNFGPNF RGPGPGSIVN YSQMPLGPYM TASNGTHSVY
     PDKKMIDSLK DCASLDRKGR LSDIIFIED
//

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