ID G3WVC9_SARHA Unreviewed; 1111 AA.
AC G3WVC9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Zinc finger RANBP2-type containing 3 {ECO:0000313|Ensembl:ENSSHAP00000019384.2};
GN Name=ZRANB3 {ECO:0000313|Ensembl:ENSSHAP00000019384.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000019384.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000019384.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000019384.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3WVC9; -.
DR STRING; 9305.ENSSHAP00000019384; -.
DR Ensembl; ENSSHAT00000019541.2; ENSSHAP00000019384.2; ENSSHAG00000016465.2.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000158559; -.
DR HOGENOM; CLU_004251_0_0_1; -.
DR InParanoid; G3WVC9; -.
DR TreeFam; TF354227; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; IEA:Ensembl.
DR GO; GO:0004520; F:DNA endonuclease activity; IEA:Ensembl.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0036292; P:DNA rewinding; IEA:Ensembl.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IEA:Ensembl.
DR GO; GO:0071932; P:replication fork reversal; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
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; 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:UP000007648}.
FT DOMAIN 70..232
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 355..515
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 126917 MW; D97C4CE660B6990F CRC64;
MGVPMLPNPW RDPELQNSSP TRLNMNNISS TQGSLTPKNS SLKSEHEDEL LFLPEKLRAR
LLPFQKDGIT FALKRDGRCM VADEMGLGKT IQAIAIAYFY KNEWPLLIVV PSSLRYPWTE
EIEKWIPELG PHEIIIIQNK TDVGRISTSK VTVLGYGLLT TDAKLLIDTL YKQNFKVVII
DESHYMKSRN ASRSKILLPV VQNSRRAILL TGTPALGRPE ELFMQIDALF PKQFGTWTEY
AKRYCNAHIR YFGKRAQWDC RGASNLNELH QLLSNIMIRR LKTEVLTQLP PKIRQRIPFD
LPSVAAKELN TSFEEWEKLI RAPHSGSTET GSHFFQAMGL MTRMFKQTAI AKAGAVKDYI
KMMLQNDSLK FLVFAHHLSM LQACTEAAIE SKARYIRIDG SVPSSERVYL VNQFQKDPET
RVAILSIQAA GQGLTFTAAN HVIFAELYWD PGHIKQAEDR AHRIGQSSSI NVHYLIANGT
LDSLMWGMLN RKAIVTGSTL NGRKEKLEAE EGDKEKWDFL KFAEVWTPNE SFEEIKNEVL
FTHFEKEKQH DIRAFFLPKH NKKRHTMASC DESCVLQERD TEKALDCRNI AARDAIDCGC
DFEPAAKRWK SVTTQNNSSQ KEKRPSCSSP ANTEFIKETI QKTKSNSINI SLPRKTWQCG
LCTYVNSSLL PYCEMCETPQ GSAENLSKQQ IDLICIQDGK GNQVNESPKN SILQVETSPS
CMQQVIEQST TEQFVERQEE KAKNENEGEL KSQKEQMENS DPLPVYDVLM FCASKNTERI
HLYTKDGEQM NCNFIPLDVK LDLWEDLPAC FQVKQNRSLI LKFVREWNSL TAMKQRIIRR
SGHIFCSPIL ALDEITKQQT KQNSIKRYIT KEDVAAATMN KVQNDGGSIR VITKKSRFSS
KNQTSSDIET WETTINPVQN DLITQPSTSK GFLQAMDIKG NPLCLHCQQP TCKSDQQYNM
SAWDSRFCSQ KCQEEFWIRS NNSYLRAKVF EIEHGVCQLC NLNAQELFLS VRDAPKNQRK
NLLQTTWISK LSIEQLNEMM INPVEGHFWQ VDHIRPVYSG GGQCSLENLQ TLCTVCHKEK
TAKQAKERSQ AKRKSSASKH GSDITRFFIK K
//
