ID A0A094EJ70_9PEZI Unreviewed; 951 AA.
AC A0A094EJ70;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=V494_00106 {ECO:0000313|EMBL:KFY47197.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY47197.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY47197.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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}.
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:KFY47197.1}.
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DR EMBL; JPJW01000020; KFY47197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EJ70; -.
DR STRING; 1420907.A0A094EJ70; -.
DR HOGENOM; CLU_005116_1_0_1; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000029288; 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:UP000029288}.
FT DOMAIN 734..849
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 107767 MW; 3C880B34ABDD1E01 CRC64;
MAATDERDGY PVKRRKTGEQ AETLKPATPS AASDGFDDSS LSWDIDTSGS DTDAVESKPD
TSDPTALEST LSHLDQGKSA IIDYEAMQPF EKALNIPTDP EDNLNAPELP GGRRSIYVDA
FNLALETVLD EESHLFDKNE ERVFIEWRGL SYEAQYLYVR LFLRKTSAWH RISKLGYHSD
ISDMPTAIES LQYPRPLPQV SDAVPVTGVK IEDADSHFTG DSFAFADALA KDTTTLEEVS
SLLSLDELKS IGKEAKVRGR NKTELLGALQ RMSRAQSGLG SVGLVILKSK SDPEMVSSEP
SILNIPHISA EDCGVVQLDG SANRLNGNAK LPDHAFGDNN RDKHFILKIL NNIGPCIRLS
SSTLKLFERV HMVYYRSTRW TEKSLTTIIL ARIQMRNFPS YLICRSTNIF PSREMLLEFE
ASIRLQHHVD SILDNGIQDK QVQEEMLSIF EEVYPKWQAL VADEQRKEER VYESGEGAYL
RLFSPCSVYT RIIFKATLVF GRLKMYEREH SVLTKLLQQR LFIYRRGGIY QRKALLEEHY
LAEAGAGSTE TAGMSQDQQK RHWKRLSLKT AEEGLQDRDC HVIYHYDLQK RIVKLEKAIK
IPKREQHDFG HTRFITPIET NVEGIQIRVM PGDVGRAGAE ERRGLKTVWV DEKDGGECSV
EAMCLSWYRS QGWKGYHAEG GILQTLFAYL FYDILFAYIP NVFQTEFQTC PLDLYTEAFF
PSRASEIYHR LAELSNGGAG RLIREVNERE RDRRTCVVGL NWDFALDDLL EIATCFDGSA
LASICMVMAQ DYRQRGGGVP DLFLWNPETS QVMFSEVKSE NDRLSDTQRL WIHVLMGAGV
RVELCNAVAR ERLKNRRQLA WTYLEDEGGL ELNLDPAPVR VEGREGRAKV KHSLNRRAPT
YLEDEFPQNI VMSAVYSSLP RVDDIHRTPM TFSGAAHNRQ TCPISVPYAS S
//
