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Database: UniProt
Entry: A0A2Y9PJW5_DELLE
LinkDB: A0A2Y9PJW5_DELLE
Original site: A0A2Y9PJW5_DELLE 
ID   A0A2Y9PJW5_DELLE        Unreviewed;      1941 AA.
AC   A0A2Y9PJW5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Probable helicase with zinc finger domain isoform X1 {ECO:0000313|RefSeq:XP_022445575.1, ECO:0000313|RefSeq:XP_022445576.1};
GN   Name=HELZ {ECO:0000313|RefSeq:XP_022445575.1,
GN   ECO:0000313|RefSeq:XP_022445576.1, ECO:0000313|RefSeq:XP_022445577.1,
GN   ECO:0000313|RefSeq:XP_022445578.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022445576.1};
RN   [1] {ECO:0000313|RefSeq:XP_022445575.1, ECO:0000313|RefSeq:XP_022445576.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022445575.1,
RC   ECO:0000313|RefSeq:XP_022445576.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022445575.1; XM_022589867.2.
DR   RefSeq; XP_022445576.1; XM_022589868.2.
DR   RefSeq; XP_022445577.1; XM_022589869.2.
DR   RefSeq; XP_022445578.1; XM_022589870.2.
DR   STRING; 9749.A0A2Y9PJW5; -.
DR   Ensembl; ENSDLET00000015809; ENSDLEP00000014322; ENSDLEG00000010531.
DR   KEGG; dle:111182922; -.
DR   OrthoDB; 5405202at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005524; F:ATP binding; 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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18077; DEXXQc_HELZ; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR049569; HELZ_DEAD-box_1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF365; HELICASE WITH ZINC FINGER DOMAIN-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|RefSeq:XP_022445575.1,
KW   ECO:0000313|RefSeq:XP_022445576.1};
KW   Helicase {ECO:0000313|RefSeq:XP_022445575.1,
KW   ECO:0000313|RefSeq:XP_022445576.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723};
KW   Nucleotide-binding {ECO:0000313|RefSeq:XP_022445575.1,
KW   ECO:0000313|RefSeq:XP_022445576.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          178..206
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         178..206
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1248..1344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1522..1547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1611..1647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1733..1851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1867..1941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1390..1409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1416..1435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1622..1643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1758..1825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1873..1891
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1916..1941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1941 AA;  218080 MW;  98235BDA5486C68F CRC64;
     MEDRRAEKSC EQACESLKRQ DYEMTLKHCT EALLSLGQYS MADFTGPCPL EIESIKIESL
     LYRIASFLQL KNYGQADEDC RHVLGEGLAK GDGTFQAVLC CMQLKGKLQL VSSILAKSLT
     GESLNGMVTK DLTRLKILLT ETETATGNVL PGYHVEDLEE GSCNGWHFRP PPRGITSSEE
     YTLCKRFLEQ GICRYGAQCT SAHSQEELAE WQKRYASRLI KLKQQNENKQ LSGSYMETLI
     EKWMNSLSPE KVLSECIEGV KVEHNPDLSV TVNTKKSHQT WTFALTCKPA RMLYRVALLY
     DAHRPHFSIV AISAGDSATQ VSQEVPENCQ EWIGGKMAQN GLDHYVYKVG IAFNTEIFGT
     FRQTIVFDFG LEPVLMQRVM IDAASTEDLE YLMHAKQQLV TTAKRWDSSS KTIIDFEPNE
     TTDLEKSLLI RYQIPLSADQ LFTQSVLDKS LTKTNYQSRL HDLLYIEEIA QYKEVSKFNL
     KVQLQILASF MLTGVSGGAK YAQNGQLFGR FKLTETLSED TLAGRLVMTK VNAVYLLPVP
     KEKLVQTQGT KEKVYEATIE EKTKEYIFLR ISRECCEELN LRPDYDTQVE LQFQLNRLPL
     CEMHYALDRI KDNGVLFPDI TMTPTIPWSP NRQWDEQLDP RLNAKQKEAV LAVTTPLSIQ
     LPPVLIIGPY GTGKTFTLAQ AVKHILQQQE TSRILICTHS NSAADLYIKD YLHPYVEAGN
     PQARPLRVYF RNRWVKTVHP VVHQYCLISS AHSTFQMPQK EDILKHRVVV VTLNTSQYLC
     QLDLEPGFFT HVLLDEAAQA MECETIMPLA LATKDTRVVL AGDHMQLSPF VYSEFARERN
     LHVSLLDRLY EHYPAEFPCR ILLCENYRSH EAIINYTSEL FYEGKLMASG KQPAHKDFYP
     LTFFTARGED VQEKNSTAFY NNAEVFEVVE RVEELRRKWP VAWGKLDDGS IGVVTPYADQ
     VFRIRAELRK KRLSDVNVER VLNVQGKQFR VLFLSTVRTR HTCKHKQTPI KKKEQLLEDS
     TEDLDYGFLS NYKLLNTAIT RAQSLVAVVG DPIALCSIGR CRKFWERFIA LCHENNSLHG
     ITFEQIKAQL EALELKKTYV LNPLAPEFIP RALRVQHTGN TNRLQQSPPK GKSLHHIQND
     HFQNDGIVQP NPSVLIGNPI RAYTPPPPLG PHPNLGKSPS PVQRIDPHTG TSILYVPAVY
     GGNVVMSVPL PVPWTGYQGR FAVDPRIITH QAAMAYNMNL LQTHGRGSPI PYGLGHHPPV
     SIGQTQNQHQ EKDQHEQSRN GKSDTNNPGP EINKIRTPEK KPTESKQMDL ESNPQNRSPE
     SRPGVVYPKF HRKDNLNPRH INLPVPAPHA QYAVPSRHFH PLPQLPRPPF AIPQQHALSS
     QQQNNLPEQP NQMPPHPNQG VPQQDPLGQP PPQLSAACQA GPNSAFFNTP VSHRPQSPPA
     EAALPEQQPP PMLQGGHSPL RAIAQPGPIL PSHLNNFADE NPPGLPVGEA LDRVHGSVAL
     EALRQQQARL QQWSEHHAYL SQGSVPYPHH HHPHPHPHLQ HLPQPPIGLH QPPVRADWKL
     PSSAEDEAET ADSRFQDLIR ELSNRDQSET RELAEMPPPQ SRLLQYRQIQ TRSPPAVPSP
     PSSADHSTHF SNFSDSSRDL EVASNPAFPQ RLPPQLFNSP FSLPSEHLAP PPLKCLAPDG
     AWTFANLQQN RLMGPGFPYG LPPLPPRPPQ TPFVHMQSHQ PAVSQEPFHP LSARTVSSSS
     LPSLEEYEPR GPGRPLYQRR ISSSSVQPCS EEVSTPQDSL AQCKELQDHN NQSSFNFSSP
     ESWVNTTSST PYQNIPCNGS SRTAQPRELI APPKTGKPPE DHLKPENLEG SSSFNYSVLQ
     HLGQFPPLMP NKQIAESASS SSQQSCGGSK PAMSYASALR APPKPRPPPE QAKKSSDPLS
     LFQELSLGSS SGSNGFYSYF K
//
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