ID V4B492_LOTGI Unreviewed; 1050 AA.
AC V4B492;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=DNA annealing helicase and endonuclease ZRANB3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LOTGIDRAFT_138707 {ECO:0000313|EMBL:ESP02276.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP02276.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP02276.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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DR EMBL; KB200294; ESP02276.1; -; Genomic_DNA.
DR RefSeq; XP_009046984.1; XM_009048736.1.
DR AlphaFoldDB; V4B492; -.
DR STRING; 225164.V4B492; -.
DR EnsemblMetazoa; LotgiT138707; LotgiP138707; LotgiG138707.
DR GeneID; 20234099; -.
DR KEGG; lgi:LOTGIDRAFT_138707; -.
DR CTD; 20234099; -.
DR HOGENOM; CLU_004251_0_0_1; -.
DR OMA; WRKVVLH; -.
DR OrthoDB; 318617at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18010; DEXHc_HARP_SMARCAL1; 1.
DR CDD; cd00085; HNHc; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.30.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002711; HNH.
DR InterPro; IPR003615; HNH_nuc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR45766:SF7; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3; 1.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01844; HNH; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00507; HNHc; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746}.
FT DOMAIN 29..192
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 308..468
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 505..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 118704 MW; 776116816C55BB30 CRC64;
MKTHIESILE ELPFKLRHKL MQFQKEGIEY AVNNNGRVLL ADEMGLGKTI QAISIAYYYK
EDWPLLIIVP SSLRYCWIEE IEKWLPDIHP HDINLIMMGN DAKNISTAKI SIVTYGLLSK
STSHIVKEAL TNQKFQVIIC DESHYIKNNK TASSKAVVPL VQAAERRILL SGTPALAKPV
ELFPQLDALC PKAFGSWWDF TARYCDAKLE WFGRMKRRKV DGASNLEELQ TKLVKMVMIR
REKKDVLTQL PPKQRQKVLF ELKDSELKKV GITLVDQGQI TSDDKQDTTT LGLISKLLQL
TGEAKVGPVK DYINMLIENE NLKFLVFAYH HVMMNGIQQL LYEKKVKFIR IDGTVPPADR
QMYVTQFQSD PSIKVAILSI LAAGVGLTLT AAKLVVFAEM YWTPGVMVQC EDRAHRIGQT
SCVPVHYLVA KGTMDEWVWS AVCKKTVVTS TTLSGKKQEL EAESGDKYQV ELLSNAEVNY
AVEDENSDMD LSNYFQSQRP NDQKSILDFL TPPTSRNKSA VDTGKRKRNN SEEINLSSSK
KPKTVNQDIV ILDSDSENED FLDSPFISSH SHSSPSNKSD QNGSMKLVKE AMTAPHQKNH
WSCMACTYLN HQQLPYCEMC DTKTPVTPVD SNNRSGCSSR KPLFKQRRSS IEYQTSGDGE
NISQSVNSHH LSPAMTESQE NKTSPIVNNK VLNISIPETV YKIFLYCGSR YTGRIYIFDE
NEEALNINFV PLDIELNNID DLPDLLKYRP HLRLIQNFVR EWNLLTETKR RLLINRGVLF
INPVAAYQQI SSKQTSSTQR HKTKEDISQA AAKLATSING TVRQISKKPT EESNKTNDDS
YGIAQVINPT FSKSAIPCKS KQAHFKASVV NNEGVPLCLN CSQPYSNSLL TTQTITSNNN
AWQTRFCSLN CADSHWTKTD SGYCRDKIYQ IEHGVCQICQ FDAHSFYKQI KDTVDMKVRV
KLISESKFSK LKSKVKEVMA RKPVEGQFWH VDHIKPVFEG GGMCDIDNMR TLCVICHQKV
TSQQASKRAQ VRKLAGAAGS GDITAFFQKI
//
