ID A0A1B8FFV7_9PEZI Unreviewed; 860 AA.
AC A0A1B8FFV7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=VE02_08934 {ECO:0000313|EMBL:OBT82469.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT82469.1};
RN [1] {ECO:0000313|EMBL:OBT82469.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT82469.1};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) 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; KV459575; OBT82469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8FFV7; -.
DR Proteomes; UP000091872; 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}.
FT DOMAIN 737..852
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 97621 MW; 7EEB05BAC31BC12C CRC64;
MATNDDSDNG YPVKRRKTGE QVETLKPATH SAASNGFEDA NLALDLDTFS PDTDTGEPKP
DTDGPTELES ALPYLDQGKD AIVDYEAIQP SEKDLNISKD PENNLSPQKL PGDRRSIYVD
AFNLALETVL DEESHLFDEK EGKVFDEWRG LSYGAQYLYV RLFLRKTSAW HRTSRLGYHS
DISDIDASIE SLQSPRPLPQ VSEAVPVTSI KIEDSDSHLE GNSFAFADAL TKDTTTLEEV
SSLLSLDELK SIGKEAKVRG KNKTELLSAL RRMSRAQSGL GSVGLRILKA KSDPEIVSSE
IRISDIPHIS VENGDGGGFH QDENATRSNG TVKFSDQTFG ENNRDKHFVL RILGNIGSCI
RLSSSTLKLF ERVHMVYYRS TKWTDKSLTT IILARIQKRN FPNYLICRSA NIFPSRAMLV
EFEASIRLQH QVDTILENGL QDKQVQEEML SIFEEVYPKW QALVEDEQRK EDRVYESGEG
AYLRLFSPCS VYTRIIFKAT LVFGRLKMYE REHSVLTKLL EQRLFIYRRG GIYQRKALLE
EHYLADAGAS STETAGMSQD QLKRYWKRSS LKTAEEGLQD RDCHVIYHYD LEKRIVKLEK
AIKIPKREQH DFGHTRLIAP IERNVEGIQV RVIPADVGRA GAEERRSLKT IWIDEKDGGE
CSVEAMCLSW YRSQGWKGYH AEGGILQTLF AYLFYDILFA YIPNVFQTEF QTCPLDLYTE
AFFPSRASEI HHRLAELSNG GAGRLIREVD ERERERRTCV VGLNWDFAVE DLLEIAACFD
GSALASICIV MAQDYRQRGG GVPDLFLWNP ETSQVMFSEV KSENDRLSDT QRLWIHALMG
SGVKVELCNA VAREVRTREE
//
