ID A0A093JC76_EURHL Unreviewed; 1930 AA.
AC A0A093JC76;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative helicase with zinc finger domain {ECO:0000313|EMBL:KFW12640.1};
GN ORFNames=N326_11215 {ECO:0000313|EMBL:KFW12640.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW12640.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFW12640.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW12640.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK579457; KFW12640.1; -; Genomic_DNA.
DR Proteomes; UP000054232; Unassembled WGS sequence.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR011990; TPR-like_helical_dom_sf.
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; 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 SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:KFW12640.1};
KW Helicase {ECO:0000313|EMBL:KFW12640.1};
KW Hydrolase {ECO:0000313|EMBL:KFW12640.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleotide-binding {ECO:0000313|EMBL:KFW12640.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054232};
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 177..205
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 177..205
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1249..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1930 AA; 218817 MW; A85A151096F74B13 CRC64;
MADRRPEKSC EQACESLKQQ DYEVAVKHCT EALLSLSQYP PAHLPEACQA EFDRIKIETL
LYRIASLLQL KKYGQADEDC RHVLGEGLAK GDGSFRAVLC CMHLKGKLQI VSNVLSKSLM
GESLNGMVTK DLTRLKTLLA ETEAAGKVPS GYHVEDLEEG SRDGWQFRPP PRGVTSSEEY
TLCKRFLEQG ICRYGAQCTS AHSQEELTEW QKRYASRLIR LKQQKENKQC SGSYMETLIE
KWMNSLSPEK VLSESVEGVR VEHNPELSVT VTTKKSHQTW TFALTCKPAR MLYRVALLYD
AHRPHFSIVA ISAGDSTTQV SQEVPENCQE WIGGKMVQNG IDHYIYKVSI AFNTEIFGTF
RQTVVFDFGL EPVLMQRVMI DAASTEDLEY LMHARQQLLT TAKRWDSTSK TIVEFEPNET
TELEKSLLTR YQIPLSADQL FTQSVLDKSL TKTNYQSRLH DLLYIEEIAQ YKEVSKFNIK
VQLQIVASFM LTGVSGGAKY AQNGQLFGRF KLTETLSEDT LAGRLVMTKV NAVYLLPVTK
EKSAQTQGTK EKVYEAAIEE KTKDYIFLRV SRECCEELNL RADCEMQVEL QFQLNRLPLC
EMHYALDRIK DNSILFPDVS MTPTIPWSPN RQWDEQLDPR LNAKQKEAVL AITTPLSIQL
PPVLIIGPYG TGKTFTLAQA VKHILQQQDT SRILICTHSN SAADLYIKDY LHPYVEAGNP
QARPLRVYFR NRWVKTVHPV VHQYCLISST HSTFQMPQKE DILKQRVVVV TLNTSQYLCQ
LDLEPGFFTH ILLDEAAQAM ECETIMPLAL ANKNTRIVLA GDHMQLSPFV YSEFARERNL
HVSLLDRLYE HYPAEFPCRI LLCENYRSHE AIINYTSELF YEGKLMASGK QPAHKDFYPL
TFFTARGEDV QEKNSTAFYN NAEVFEVVER VEELRRKWPV AWGKLDDGSI GVVTPYADQV
FRIRAELRKK RLSDVSVERV LNVQGKQFRV LFLSTVRTRH TCKHKQTPIK RKEQLLEDST
EDLDYGFLSN YKLLNTAITR AQSLVAVVGD PIALCSIGRC RKFWERFIAL CHENESLHGI
TFEQIKAQLE ALELKKTYVL NPLAPEFIPR ALRHQHSANT TKQQQSPPKG KIHLHNQNDH
FAPDGIVQPN PSVLIGNPIR AYTPPPPPLG PHPNLGKSPS PVQRIDPHTG TSILYVPAVY
GGNMVMSVPL PVPWTGYQGR FAVDPRIITH QAAMAYNMNL LQAHGRGSPI PYGLGHHSPV
SIGQQQLQHP DKEQHEQSRN GKSENTAGPE ISKIRTPEKK PVESKQVDLE ANPQNRSPES
RSSVGYPNAK FHRKDTLNPR QLNLHLTPPH SQYAVPSRHF QHVSQIPRQP YPLQQPQNLL
SQQQNHLPEQ QNQMPPQQSQ VVQQHNHLNQ QPPQPSQLSP AYQAGPSQSF FNNPIPHRPH
SPAVDAVISE QHPPPMLQEV SNPLRPIAQH NPVLPTHLNN FIEENRMHGN VALETIRQQQ
QARLQQWNEH NAYLSQGTIP YQHHHHPHLP HLPQQPIGLH QQQQVRANWK LASNTEDETE
ATYSRFQDLL RELSHRDQSE SRDLAEMPPP QSRLLQYRQV QPRSPPALPS PSCNSNHSGP
FPNFTENSRD IEIPNNPAFQ QHLPQIYNPP FSMPSEHITP SPLKYLQPDG SWTYANLQQN
HLMGQGFHYG IPPLPHRSQQ NPFIQIQNHQ HAVGQEPFHP LTSRAVSASS LHSLEEYEPR
GPGRPLYQRR ISSSSVQACS EELSTPQDSL GQCKELQDHS NQSSYNYSSP ELWVNSSSSA
PYPNIPCNGA SRAVPPRELL APPKTVKPPE EHLKAESIQL SNSFNYSVLQ HLGQFPPLMP
NKQIVESNST SQQNAGGSKP VMSYASALRA PPKPKPPPEQ TKKNSDPLSL FQELSLGSSS
GSNGFYSYFK
//
