ID A0A0P1BRV0_9BASI Unreviewed; 964 AA.
AC A0A0P1BRV0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH19173.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH19173.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CCYA01000277; CEH19173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BRV0; -.
DR STRING; 401625.A0A0P1BRV0; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000054845; 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; 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; 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:UP000054845}.
FT DOMAIN 837..951
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 22..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 107419 MW; B76BAA5236EBC447 CRC64;
MEQVISDSSS FCLVDDQRPI KRSANDLQQP QLGELSKMAA GSASLFGDSK RMRTNTSDRS
SPRGVGNDSK EPCRNVSDVA DGDGGASQPA SPPKPDLDRS ASDLSSSSTS SSASSRRTGE
SMYPAILGEM IDAVLEKEEY LFSPLEVVML REYQQLPSDP RYVFARLVQR RDVWQRPDRL
RFEERDCGDL AGAIRKLCEP VFLQASQVSH SSAQPASQSN DSEKMGHYCL GVQEMDPDDV
HASLELLTLE ELKRLAKMMG SKRSSDTNTR AIAIATLLES RTQCTFSFGP SPKSGSATHS
NKAAPIKGQT KLNFSPTKPV SATDSHMPAK RSSQMDVLKW HMSSIIGDCV RLAPLARSLI
ARLALVYYRA TVQSEGSALT TAVLARSRRR VYPVYQHQRT APLFASRQHL ISMEKALKLE
VTIDELIEWD GSKEAFAKGL NIFESVWQEW RECVEDAQRQ NPDGVDRMTY HKMRCHPGWP
LTRIVYKGAH LLGRFKLYER EEEVLRALLA QRAFRRGRRG DWYDRLALIL AQYPADGDAK
RGKMRALEVA VQGIEDSDTH LIYHDTLQRR ITRLENQLNI PFSQKHDFSY AKLATCRDRV
FEGTRLDAMA SMEPKRGIFG SVMPSQRRTS GSAGGGKSFP KRSASNESLL SSHGDSLSGF
QERAPLRKVI QVERAHVARK ADTSGSPVGV NRKGIKRDAS TSSPVDAEGT KKAERDESDV
QDVSFASSRS SVGEVSSAGS TTSIERKSMS SIWRGLDSEP CRVEDLVLQH YSMQGYSGYH
CEGSIISMLF TLLMWDVIFL PTPGAFETAY QSAPLDIGED SFIVARAPQV RQRLHLIEER
GGLDLMEEVH KRESQRKTWA IGCKWDTYPL EDLLQIAQCV GGKGLAVICQ MMCEEYMTAG
MPDLVVWNWK EKKVRFCEVK GPGDRLREKQ KVWIDVLLRA GLDVEVSIVK EGITSNFSAG
AKVQ
//
