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Database: UniProt
Entry: A0A3B4UB44_SERDU
LinkDB: A0A3B4UB44_SERDU
Original site: A0A3B4UB44_SERDU 
ID   A0A3B4UB44_SERDU        Unreviewed;      2061 AA.
AC   A0A3B4UB44;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Helicase with zinc finger {ECO:0000313|Ensembl:ENSSDUP00000015597.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000015597.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000015597.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 41447.ENSSDUP00000015597; -.
DR   Ensembl; ENSSDUT00000015884.1; ENSSDUP00000015597.1; ENSSDUG00000011381.1.
DR   GeneTree; ENSGT00940000156686; -.
DR   OMA; KREMAPE; -.
DR   OrthoDB; 5405202at2759; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0004386; F:helicase 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; 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; 2.
DR   Pfam; PF13087; AAA_12; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723};
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          182..210
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         182..210
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1124..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1586..1709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1722..1741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1762..1916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1955..2040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1383..1405
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1626..1655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1670..1699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1722..1739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1764..1823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1847..1873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1955..1981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1982..1999
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2061 AA;  230343 MW;  E88E8A7F846ACDE5 CRC64;
     MADRRAEKSC EEASRSLVRR EYEAAVSHST DALVVLVPQA PSSGTPVPPS PPSLTATGPL
     RSRALLYRIA AFLQLKNYDE ADEDCKHVLV EEIARGDGSL QASLRSMLLD GSLQEVASIL
     SKALYGEPMN GIVAKDLTRL KMLLSEIEAI NRDMAPEYTD DQEEEVQDGW QFRPPPRGVT
     SSEEYTLCKR YLEQGLCRYG AQCTSAHSQE ELMEWQKRYA SRLIRLKQQQ ESKHFTENYM
     ETLIEKWMNS LSPEKVLSDC LEGVIVETSS SLSVTVTTKK SSHSWAFSLL CKPARKLYRI
     ALLYDAHRPH FFITGVSAGE RLQAVPKGCQ EWTPGEDTAL AADNGLDNCL YKVAVSFSTE
     IFGTFRQTVV FDFGSEPVLM QRIMVDAASI EDLEHLMAAR QQLLITAKRW DSSCKTIVEF
     CPNETMAELE RSLLSRYQIP LSADQLFTQS VLDKTLTKDN YQARLHDLLY IEEIAQYKEV
     SKFNIKVNLQ LVTSFMLTGI SVGAKYAQNG QLFARFKLTE TLSEDTLAGR LVMTKVNSVL
     LLPLGREGIN SQPPPGVKER VYEAVIEEKT KEYIFLRICK DCCEELGLQP DREIQVELQF
     QLNRLPLCEM HYALDRIKDN TILFPDVSLV PTIPWSPNRQ WDEQLDPRLN AKQKEAILAI
     TTPISIPLPP ILIIGPYGTG KTFTLAQAVK HILRQDHSRV LICTHSNSAA DLYIKDYLHP
     YVEAGNPHAR PLRVYFRNRW VKTVHPVVQQ YCLISSTQVT FQMPTREDIL RHRVVVVTLS
     TSQYLCQLDL EPGLFTHILL DEAAQAMECE TIMPFALASK TTRIVLAGDH MQLSPFVYSE
     FARERNLHVS LLDRLYEHYP PEFPCRILLC ENYRSHEAII NYTSELFYDG KLMASGKQPS
     HKDFYPLTFF TARGEDVQEK NSTAYYNNAE VFEIVERVEE LRKKWPVAWG KLDEGSIGVV
     SPYADQVFRI RAELRKKRMH EVSVERVLNV QGKQFRVLFL STVRTRHTCK HKQTAIKRKE
     QLVEDSTEDL DYGFLSNYKL LNTAITRAQS LVAVVGDPIA LCSVGRCRKF WEHFISICHE
     NSSLHGITFE QIKAQLEALE LKKTYVLNPL APEFIPRALR PLQGHHSSSQ ALHPHHHPHP
     QHAQPATNKQ GPQQQQQQQQ QQSPPKGKHA NHTEHLPPDG YVQPNPAVLM GNPIRAFTPP
     LGGTAAGMGK SPSPVQRIDP HTGASILYVP AVYGGNMVMS MPLPLPWPGY QNRFAVDPRI
     MSHPAAMAYN FNLLQAQNRG SPIPYSGVGH PSPLGMGQPS PDKELQADPI RNGKLEGCPK
     SEQSRLQTPE RKTADMKEKQ GDLDTGQGRS LDSQTDGLVG FPNALLHRKD PSAAQRPLNY
     HLAPPNPAFP PHPASGRPFP PQYPVSRLPY RVGQPQHPGM AQQSQQQQQQ LSPAYTGGSH
     NASFFSGPIP PHRAVQSPTL DGPESGGLEE MSSSIRTPMG HPGGHHPGLS QHNRVNSFGE
     DGQDGNLGDG LDLQGPLALE ALSQQQQQAA RLGQWGEAAG PFLPGNVAFP LPQQLAHLAQ
     PGMARIPHQL LRAASWGLSA NMEDEAVSSA STGPPYTRYP GLLREIPPQE QPEPREAAEM
     QPPPQSRLLQ YRQSQSRASG DPSSSLATTS NHAGPFPSGP YAHDAGRNLL NDNLLNNPAL
     QQQHPGNPLY NTGSYPHQPP THSASPPPSQ VKYLLQEAQW SHGGAASVSP PQQNHLLGNQ
     GHGLPYGLPI MAHPSRQEQV HLMQLHHQHQ QQQQQQQQQQ QQQQQHYQQQ QQQQQQQHHQ
     HQQSQGPDQE SYHPLSPRTS AATALHNVDE YEPRGPGRPL YQRRISSSYP DEPSPANTHN
     ALSQQSQPCT SDPQDHPHPH IQHHQHPHAH YVYPSHDPWP SNGGGPGPFQ NIPCNGAGTL
     AQHREILASK ALRQTEEQVK AEATAAQQTH PHSLNSLQHL GQFPPLMPNN KQQQQQQQQQ
     QQQQPPPPPP PPPQAPTEPN QGAPNLNKPP TMSYASALRA PPKPRAVRPE QVKKNSDPLS
     LLQELRIGSS NGSNGYYSYF K
//
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