ID A0A166A447_EXIGL Unreviewed; 860 AA.
AC A0A166A447;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=EXIGLDRAFT_651295 {ECO:0000313|EMBL:KZV88299.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88299.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV88299.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88299.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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}.
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DR EMBL; KV426103; KZV88299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166A447; -.
DR STRING; 1314781.A0A166A447; -.
DR InParanoid; A0A166A447; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000077266; 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:UP000077266}.
FT DOMAIN 671..787
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 789..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..825
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 97563 MW; C9ACA0E211B7AF6F CRC64;
MHHRASLLTD AALFRVDDVL DPFDIVQHVT DGAGDVEGQS KDFRESMYVL ILKEILNTVF
PAEAYLFSED ELEAFNRFGQ LSYEAKYLLL RLSLRKEGKW HSLSGLDASY HADLGPRLRG
AMQELSGILP SPPEEEKKPR IIKTSQPKVI DLTLDDEDDE PDVPVQPSTL PLPTSDASTA
VAVAVAGPLF AHGESSAELA DLLQCLNKDQ LKAVAIQLKI ANVNKKNRDE LVESLLDHAS
SQSTLQGRGP LKQLTLNFHM GKKKSQSDLL RQRVMKILVH AIKLEAEVLA LLRRLQIVFF
RATMYAADLF LPSILARAKR RNYASYKYER TLNIFPSREQ FLDYEKALKM ESEMDMLLDG
YGTMYKPKSK SAQAHAKSIS ATPRQDAAAR AKDLASEAWL RWDELLISAE EQGLTKADTY
IARFHPGHVY TRILHNGCRA LAILKDYQSE ITALKALLEQ MIWRKSKRGA WYERLALLYH
QYGHRVTLDE EDAAKFVDLE DQHLHLARET VLKGLEDEHT HLVWRIALEN RLSRLEKRLK
LSKEERYEIT PRLKNPRTVC FQGKRIWEKE DSPAGDANAS WTGKSLWFGA NGEKVSVEDL
SVQWYAKKGF KAVHSEGRIV TSIFALLFWD VLFAPVQGAF ETKFQNAPLD MFHDTFFQAR
KELIESRLAE LEANKARTLL ETVDDRERPR KTVCIGLRWD MFSKEDLCEV VDCLGGRALA
VMCRILCEDY AGRTSGVPDL LAWNPRTGKA KFVEVKGPGD QLRDGQRLWI HCLLSAGVDV
ELCKVEEKEE RDRAKSRSKS ARADSDEDTA EESGAEEDEQ LEDEDEEPAS RPKGKKRPSD
SAEATSESKR KKPRSQSIEL
//
