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Database: UniProt
Entry: A0A2Y9T823_PHYMC
LinkDB: A0A2Y9T823_PHYMC
Original site: A0A2Y9T823_PHYMC 
ID   A0A2Y9T823_PHYMC        Unreviewed;      1938 AA.
AC   A0A2Y9T823;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Probable helicase with zinc finger domain isoform X2 {ECO:0000313|RefSeq:XP_023985792.1};
GN   Name=HELZ {ECO:0000313|RefSeq:XP_023985792.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023985792.1};
RN   [1] {ECO:0000313|RefSeq:XP_023985792.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023985792.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_023985792.1; XM_024130024.3.
DR   Proteomes; UP000248484; Chromosome 14.
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_023985792.1};
KW   Helicase {ECO:0000313|RefSeq:XP_023985792.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nucleotide-binding {ECO:0000313|RefSeq:XP_023985792.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
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          1247..1461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1579..1598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1608..1643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1703..1722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1730..1848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1871..1938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1358..1372
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1373..1388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1408
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1409..1434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1557..1572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1619..1638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1755..1822
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1871..1888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1913..1938
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1938 AA;  217593 MW;  6F2445DB871744FD CRC64;
     MEDRRAEKSC EQACESLKRQ DYEMTLKHCT EALLSLGQYS MADFTGPCPL EIESIKIESL
     LYRIASFLQL KNYGQADEDC RHVLGEGLAK GDGTFQAVLC CMQLKGKLQP VSSILARSLT
     GESLNGMVTK DLTRLKILLT ETETATGNVL SGYHVEDLEE GSCNGWHFRP PPRGITSSEE
     YTLCKRFLEQ GICRYGAQCT SAHSQEELAE WQKRYASRLI KLKQQNENKQ LSGSYMETLI
     EKWMNSLSPE KVLSECIEGV KVEHNPDLSV TVNTKKSHQT WTFALTCKPA RMLYRVALLY
     DAHRPHFSII AISAGDSATQ VSQEVPENCQ EWIGGKMAQN GLDHYVYKVG IAFNTEIFGT
     FRQTIVFDFG LEPVLMQRVM IDAASTEDLE YLMHAKQQLV TTAKRWDSSS KTIIDFEPNE
     TTDLEKSLLI RYQIPLSADQ LFTQSVLDKS LTKTNYQSRL HDLLYIEEIA QYKEVSKFNL
     KVQLQILASF MLTGVSGGAK YAQNGQLFGR FKLSETLSED TLAGRLVMTK VNAVYLLPVP
     KEKLVQTQGT KEKVYEATIE EKTKEYIFLR ISRECCEELH LRPDYDTQVE LQFQLNRLPL
     CEMHYALDRI KDNGVLFPDI TMTPTIPWSP NRQWDEQLDP RLNAKQKEAV LAVTTPLSVQ
     LPPVLIIGPY GTGKTFTLAQ AVKHILQQQE TRILICTHSN SAADLYIKDY LHPYVEAGNP
     QARPLRVYFR NRWVKTVHPV VHQYCLISSA HSTFQMPQKE DILKHRVVVV TLNTSQYLCQ
     LDLEPGFFTH VLLDEAAQAM ECETIMPLAL ATKDTRVVLA GDHMQLSPFV YSEFARERNL
     HVSLLDRLYE HYPAEFPCRI LLCENYRSHE AIINYTSELF YEGKLMASGK QPAHKDFYPL
     TFFTARGEDV QEKNSTAFYN NAEVFEVVER VEELRRKWPV AWGKLDDGSI GVVTPYADQV
     FRIRAELRKK RLSDVNVERV LNVQGKQFRV LFLSTVRTRH TCKHKQTPIK KKEQLLEDST
     EDLDYGFLSN YKLLNTAITR AQSLVAVVGD PIALCSIGRC RKFWERFIAL CHENNSLHGI
     TFEQIKAQLE ALELKKTYVL NPLAPEFIPR ALRVQHTGNT NRLQQSPPKG KSLHHIQNDH
     FQNDGIVQPN PSVLIGNPIR AYTPPPPLGP HPNLGKSPSP VQRIDPHTGT SILYVPAVYG
     GNVVMSVPLP VPWTGYQGRF AVDPRIITHQ AAMAYNMNLL QTHGRGSPIP YGLGHHPPVS
     IGQTQNQHPE KDQHEQSRNG KSDTNNPGPE INKIRTPEKK PTESKQMDLE SNPQNRSPES
     RPGVVYPKFH RKDNPNPRHV TLPLPAPHAQ CAVPGRHFHP LPPLPRPPFP IPQQHASSNQ
     QQNNLPEQPN QMPPHPNQGA PRQSPLGQPP PQLSAACQAG PSSAFFNNAV SHRPQSPPAE
     AAIPEQQPPP MLQGGHSPLR AIAQPGPILP SHLNNFTDEN PPGLPVGEAL DRVHGSVALE
     ALRQQQVRLQ QWSEHHACLS QGSAPYPHHH HPHPHLQHLP QPPIGYHQPP VRADWKLPGS
     AEDEAETTDS RLQDLIRELS NRDQSETREL AEMPPPQSRL LQYRQIQTRS PPAVPSPPSS
     ADHSTHFSTF SDSSRDLEVA SNPAFPPRLP PQLFSSPFSL PSEHLAPPPL KCLAPDGAWT
     FANLQQNRLM GPGFPYGLPP LPPRPPQTPF VHMQSHQPAV SQEPFHPLSA RTVSSSSLPS
     LEEYEPRGPG RPLYQRRISS SSVQPCPEEV STPQDSLAQC KELQDHNNQS SFNFSSPESW
     VNTTSSTPYQ NIPCNGSSRT AQPRELIAPP KTVKPPEDHL KPENLEGSSS FNYSVLQHLG
     QFPPLMPNKQ IAESAHSSSQ QSCGGSRPAM SYASALRAPP KPRPPPEQAK KSSDPLSLFQ
     ELSLGSSSGS NGFYSYFK
//
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