ZRAB3_BOVIN
ID ZRAB3_BOVIN Reviewed; 1074 AA.
AC E1BB03;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=DNA annealing helicase and endonuclease ZRANB3;
DE AltName: Full=Annealing helicase 2;
DE Short=AH2;
DE AltName: Full=Zinc finger Ran-binding domain-containing protein 3;
DE Includes:
DE RecName: Full=DNA annealing helicase ZRANB3;
DE EC=3.6.4.-;
DE Includes:
DE RecName: Full=Endonuclease ZRANB3;
DE EC=3.1.-.-;
GN Name=ZRANB3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: DNA annealing helicase and endonuclease required to maintain
CC genome stability at stalled or collapsed replication forks by
CC facilitating fork restart and limiting inappropriate recombination that
CC could occur during template switching events. Recruited to the sites of
CC stalled DNA replication by polyubiquitinated PCNA and acts as a
CC structure-specific endonuclease that cleaves the replication fork D-
CC loop intermediate, generating an accessible 3'-OH group in the template
CC of the leading strand, which is amenable to extension by DNA
CC polymerase. In addition to endonuclease activity, also catalyzes the
CC fork regression via annealing helicase activity in order to prevent
CC disintegration of the replication fork and the formation of double-
CC strand breaks. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- SUBUNIT: Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA
CC (when PCNA is polyubiquitinated via 'Lys-63'-linked polyubiquitin).
CC {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FWF4}.
CC Chromosome {ECO:0000250|UniProtKB:Q5FWF4}. Note=Following DNA damage,
CC recruited to sites of DNA damage and stalled replication forks by
CC polyubiquitinated PCNA. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA, while the
CC RanBP2-type zinc finger mediates binding to 'Lys-63'-linked
CC polyubiquitin. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- MISCELLANEOUS: In contrast to classical helicases that unwing DNA,
CC annealing helicases rewind it. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; DAAA02005001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02005002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BB03; -.
DR SMR; E1BB03; -.
DR STRING; 9913.ENSBTAP00000038188; -.
DR PaxDb; E1BB03; -.
DR PRIDE; E1BB03; -.
DR eggNOG; KOG1000; Eukaryota.
DR InParanoid; E1BB03; -.
DR OrthoDB; 1082831at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0036292; P:DNA rewinding; ISS:UniProtKB.
DR GO; GO:0045910; P:negative regulation of DNA recombination; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR CDD; cd00085; HNHc; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
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; SSF52540; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chromosome; DNA damage; DNA repair; Endonuclease; Helicase;
KW Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1074
FT /note="DNA annealing helicase and endonuclease ZRANB3"
FT /id="PRO_0000419489"
FT DOMAIN 46..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 325..481
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1006..1046
FT /note="HNH"
FT ZN_FING 617..647
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 46..481
FT /note="DNA annealing helicase activity"
FT /evidence="ECO:0000250"
FT REGION 659..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1074
FT /note="Endonuclease activity"
FT /evidence="ECO:0000250"
FT MOTIF 157..160
FT /note="DEAH box"
FT MOTIF 519..526
FT /note="PIP-box"
FT MOTIF 1069..1073
FT /note="APIM motif"
FT COMPBIAS 660..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF4"
SQ SEQUENCE 1074 AA; 121768 MW; 28D0ABC8FC9C986F CRC64;
MSRGHNIKKS LTPQISCSTS ESYKQLDFLP DKLRAKLLPF QKDGITFALR RDGRCMVADE
MGLGKTVQAI GIAYFYKEEW PLLIVVPSSL RYPWTEEIEK WIPELSPEEI NVIQNKTDVG
RISTSKVTVL GYGLLTTDAE TLIDALNNQN FKVVIVDESH YMKSRSATRS RILLPIVQKA
KRAILLTGTP ALGRPEELFM QIEALFPQKF GTWTEYAKRY CNAHVRYFGR RSQWDCRGAS
NLNELHQLLS DIMIRRLKTE VLTQLPPKIR QRIPFDLPSA AAKELNSSFE EWEKLMRDPY
SGATETVMGL ITRMFKQTAI AKAGAVKDYI KMMLQNDSLK FLVFAHHLSM LQACTEAVIE
NKTRYIRIDG SVPSSERIHL VNQFQKDPET RVAILSIQAA GQGLTFTAAT HVVFAELYWD
PGHIKQAEDR AHRIGQCSSV NIHYLIANGT LDTLMWGMLN RKAQVTGSTL NGRKEKLQAE
EGDKEKWDFL QFAEAWTPNE RSEELRDEML FTHFEKEKQR DIRSFFLPNA KKRQLETSCD
ESRVSQEKNT IVPADPVKTA TRGDESDLEP EAKKLKSVAI DDPCRPPEEQ PCRPGQAEAL
LTFGICKAKA QATTPAFCGE GWQCAFCTYI NNSVLPYCEM CENPRGGAVP QIDSLNQTQN
KNKNEKDDSQ DTSKKIQTSS DGEKQVLAHS TPEPLAKSKE EISTTESEDR LTPQPGDEQL
KNWPVYDTLM FCASKNTDRI HVYTKDGNQM NCNFIPLDIK LDLWEDLPAS FQLKQNRSLI
LRFVREWSSL TAMKQKIIKK SGQLFRSPVL ALEEIAKQQT KQNSTKRYIT KEDVAAASMD
KVKNDGGHVR LITKGPKPGD PSTKEFLEGG ECVPFLNPCT AQGDLILKAS TSKGYLQAVD
NEGNPLCLRC QQPTCQTKQE RKADAWDSRF CSLKCQEEFW IRSNNSYLRA KVFEIEHGVC
QLCNLNAQEL FLRLRDAPKS QRKSLLDATW TSKLPLEQLN EMIRSPGEGH FWQVDHIKPV
SGGGGQCSLD NLQTLCTVCH RERTAQQAKE RSQVRRQSLA SNHGSDITRF LVKK
