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HELZ_DANRE
ID   HELZ_DANRE              Reviewed;        1860 AA.
AC   Q6NYU2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Probable helicase with zinc finger domain;
DE            EC=3.6.4.-;
GN   Name=helz; ORFNames=zgc:77407;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a helicase.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR   EMBL; BC066461; AAH66461.1; -; mRNA.
DR   RefSeq; NP_998431.1; NM_213266.1.
DR   AlphaFoldDB; Q6NYU2; -.
DR   STRING; 7955.ENSDARP00000042673; -.
DR   PaxDb; Q6NYU2; -.
DR   PRIDE; Q6NYU2; -.
DR   GeneID; 406550; -.
DR   KEGG; dre:406550; -.
DR   CTD; 9931; -.
DR   ZFIN; ZDB-GENE-040426-2419; helz.
DR   eggNOG; KOG1804; Eukaryota.
DR   InParanoid; Q6NYU2; -.
DR   OrthoDB; 286011at2759; -.
DR   PhylomeDB; Q6NYU2; -.
DR   PRO; PR:Q6NYU2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR10887; PTHR10887; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..1860
FT                   /note="Probable helicase with zinc finger domain"
FT                   /id="PRO_0000354097"
FT   ZN_FING         168..196
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1106..1136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1556..1604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1641..1709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1749..1860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           787..790
FT                   /note="DEAA box"
FT   COMPBIAS        1286..1301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1556..1582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1643..1664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1832..1860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         661..668
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1860 AA;  208033 MW;  1E23D819C86D00FC CRC64;
     MEDRRPQKSC DEAIGSLVRQ EYEAAVAHST EALLAMGPRT PTPSTALLRT RALLYRIAAR
     LQLKDYDQAD EDCKHVFAEE LAKGDGSFRA GLQSLLLDGS LQEVCSVLSK ALYGEPLNGI
     MTKDMTRLKR LLSEIEAARS KVVFSEENEE DVQEGWQFRP PPRGVTSSEE YTLCKRFLEQ
     GLCRYGAQCT SAHSQEELTE WQRRYASRLI RLKQQQEGKH FSENYMEALI EKWINSLTPE
     RVMNDCVDGV TVEHSSDLSI TVNTKKSSHS WTFTLFCKPV RTLQRIALLY DANRPHFSIA
     AVSAGDASAL EPQPVCPGGC QEWSAASPVQ NGMDHCIYTV EIAFSTEIFG TFRQTVVFDL
     GCEPVLMQRV MVDAASIEDL EHLLQARQQL LMTAKRWDSS CKTIVEFVPN ENMDLERSLL
     TRYQIPLSAD QLFTQSVLDK TLTRDNYQPR LHDLLYIEEI AQYKEVTKFN IKVNLQLVTS
     FMLTGISGGA KYAQNGQLFA RFKLTETLSE DTLAGRLVMT KVNSVLLLPV FKERMGQNQP
     AGAKERVYEA LIEEKTKDYI FLRVCKECCD ELGLVADQEL QVELQFQLNR LPLCEMHYAL
     DRVRDNSILF PDISLTPTIP WSPNRQWDEQ LDPRLNAKQK EAILAITTPL SINLPPVLII
     GPYGTGKTFT LAQAVKHILK QPESRVLICT HSNSAADLYI KDYLHPYVEA GNPHARPLRV
     YFRNRWVKTV HPLVQQYCLI SGAHFTFQMP TRQDVERHRV VVVTLSTSQY LCQLDLEPGI
     FTHILLDEAA QAMECETIMP LALAVKSTRV VLAGDHMQLS PFVYSEFARE RNLHVSLLDR
     LYEHYPSEYP CRILLCENYR SHEAIINYTS DLFYEGKLMA SGKQPPHKDF YPLTFFTARG
     EDVQEKNSTA YYNNAEVFEI VERVEEMRKK WPVSWGKLEE GSIGVVSPYA DQVFRIRAEL
     RKKRMSEVSV ERVLNVQGKQ FRVLFLSTVR TRHTCKHKQT AIKRKEQLVE DSTEDLDYGF
     LSNYKLLNTA ITRAQSLVAV VGDPIALCSV GRCRKFWETF ISICHENHSL HGITFEQIKI
     QLEALELKKT YVLNPLAPEF IPRALRSQHP PQQGPGKHQH SPPKAKGQLA NHTEPFPPEG
     FVQPNAAVLM GNPIQAFTPP GAGAPASGKS PSPVQRLDPG ASILYVPAVY GGNMVMPMPL
     PLPWAGYQSR FPMDPRIMSH QAAMYNLNLR PAASRTSPVL YGFSHASPLG LNQQQNTEKE
     LLQEPSGNGK MDINGKAEHC RLLTPERKAP ELKEKQGDLE SVQNKSPEPQ SNMGFPANRL
     IRKDPQRALN FHMAPPHPAF PSHHGTSQFP QQYGLSRPPL RMQTPMHPQA SSFPPSFYSG
     PPMGPRGLQS PVLEGGEDPM GAGMSEDLKG VVRGLPAQMH QQPLRLNSFG EESLDSLLGD
     TLDGQASSGM DALQHQQQAR VGQWGEHTPF LPAGVAPFPL PQQLAHLAQP GLRIPPQILR
     AGWGLGPAAD EEPRPTMPRY PGLLREMLPQ DQQYEQRDPA EMPPPQSRLL QYRQQIQPRS
     PGDLPSPSSS APNHNFPAPA QPSYPDTSRE PPVGFSQAPF PPDHSAGPLP VKYLLQEAHW
     PHPGHMLGHG LPFGLQAMAQ RQDPGPLQHQ QQKQQLQAPQ SSLHSLDEYE PRGPGRPLYQ
     RRISSSSPQP YPDSLEPQDQ PVPSYRYPSA DLWLGGPGPV PGPAPIHNIP CNGASHIGPH
     REILVSKAMS EEQMKAECLQ PPPPPPPHPA SAASLQHHGQ FPPLLPSKQT PPDPGGGGNT
     SPAGHPKPPT MSYASALRAP PKPRPMLPEQ SKKNSDPISL LQELSIGSSN SSNGYYTYFK
 
 
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