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Database: UniProt
Entry: A0A150GRQ7_GONPE
LinkDB: A0A150GRQ7_GONPE
Original site: A0A150GRQ7_GONPE 
ID   A0A150GRQ7_GONPE        Unreviewed;      1182 AA.
AC   A0A150GRQ7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE            EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN   ORFNames=GPECTOR_9g569 {ECO:0000313|EMBL:KXZ52525.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ52525.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC       links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of
CC       DNA and cleaves DNA successively at every third nucleotide, allowing to
CC       excise an ICL from one strand through flanking incisions.
CC       {ECO:0000256|RuleBase:RU365033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC         3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC         EC=3.1.4.1; Evidence={ECO:0000256|ARBA:ARBA00000983,
CC         ECO:0000256|RuleBase:RU365033};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365033};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU365033};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365033}.
CC   -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000256|ARBA:ARBA00005533,
CC       ECO:0000256|RuleBase:RU365033}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXZ52525.1}.
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DR   EMBL; LSYV01000010; KXZ52525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150GRQ7; -.
DR   STRING; 33097.A0A150GRQ7; -.
DR   OrthoDB; 38749at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR   GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro.
DR   CDD; cd22326; FAN1-like; 1.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   InterPro; IPR033315; Fan1-like.
DR   InterPro; IPR049132; FAN1-like_euk.
DR   InterPro; IPR049126; FAN1-like_TPR.
DR   InterPro; IPR049125; FAN1-like_WH.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   InterPro; IPR014883; VRR_NUC.
DR   PANTHER; PTHR15749; FANCONI-ASSOCIATED NUCLEASE 1; 1.
DR   PANTHER; PTHR15749:SF4; FANCONI-ASSOCIATED NUCLEASE 1; 1.
DR   Pfam; PF21315; FAN1_HTH; 1.
DR   Pfam; PF21170; FAN1_TPR; 1.
DR   Pfam; PF08774; VRR_NUC; 1.
DR   SMART; SM00990; VRR_NUC; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU365033};
KW   DNA repair {ECO:0000256|RuleBase:RU365033};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365033};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU365033};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU365033};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365033};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU365033};
KW   Nucleus {ECO:0000256|RuleBase:RU365033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT   DOMAIN          1051..1165
FT                   /note="VRR-NUC"
FT                   /evidence="ECO:0000259|SMART:SM00990"
FT   REGION          226..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..477
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1182 AA;  120153 MW;  3E2AB31BB6FDE76E CRC64;
     MAEATTATAV KEAAVLMASV TGREGVIAAL AAAAAAAASA SLGGGATGGP AGPAAAAGEV
     LRANLAVIAE DVRRHDGHLL SGEEAALLDR LLGLPPGPAC LFLRLALRKG PWFALAAIAY
     TECGDAAEAA EVLLAAGLAE RPQPEDWPQV AALLPVAEVR SLAKGAPPLP PLPRAASAPS
     ASAAVAPGRS SILSYTRRLT AAASVPIVAA ADGLAKAPQM VLTAPASPST TADALGRPSQ
     TCSGVAAGDA KRVVKGADEG AGSAPRRQNG RAASGSGNAA AGGGNAAAAA GGKGVSGGRG
     PGSGKAAVIE SLRQRHGDGS ACMSQKVAAR VGPCIRLAPA ATELLGRLQR LYFLGEGPAA
     DMGRFLATDR GVIRYPRYTI RRSGSAFGSR QQLLEYEQAL QHAARLEECL EAGDEDGAAA
     ALAPALAAVA SGAAQAVRWA GDATVPVRAV PGPWPWEDHP PAQPLPPLPP TAAARLPLPP
     HPRDAKGGCD ELGPADGRAV CGAEGRQRGC GCSASAPAVA AVAAAAAVKG RTAARGTGAS
     RRDSVDLTLS SDSDSGAGEE EGQEGEGSGP STGQDGHSHG GSGGFRGCCV GAARPGAADS
     GVTGSTGDQE AGLPPDSDGV DGTGGYWAGL GVAPGAAGCR GSQMRESGSR APGGGGYPLE
     AERAGFPPRR PDRCEPQRRD GGDRAADEGA TLYGADGCMP CDDGSHVYGD DDVVYGDELE
     DGPGGAASPP GAACEDAPGA AQGRGAAGPG QGTVRDEAVL GGEEQPPLPQ QLHARLGQGQ
     EGQPHGQSPA HPFLARFCAA WVYASMGTVG VSLLERQRRY PEAVALLRSL LRGRCCPGRR
     GEWWTRMSLD LQHLGREEEA LQVAEAALTD PWVRHGDRLS LQRRVLRLGR PPRRWRRPAW
     AEAALAEPRE VVVSATMLRG ATGFKSRFIV PHAAKARPPS DGDLPGGATA ADGPGAHGAG
     GPDAAAGGDG TVGVEELALL HYRSPAGGGW RGVHSEGGVW GTLWGLLMWD VLFADVPEVF
     RSPFQTAPLD LDTDAFLPSR RELVDARLQA IAGGAAPELL RGAWSAHEGT WARGVNWERQ
     PLEELLEIAR CVGGLGLSVV CRLLCEDCAG WRGGMPDLLL WRPERGDAMV SEVKGPRDRL
     SDQQRAWMAA LAAAEVRAEV LRVVEAAPGE AEGGGGGHSP LH
//
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