ID G7XGT7_ASPKW Unreviewed; 850 AA.
AC G7XGT7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=AKAW_04260 {ECO:0000313|EMBL:GAA86146.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA86146.1};
RN [1] {ECO:0000313|EMBL:GAA86146.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA86146.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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; DF126455; GAA86146.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XGT7; -.
DR STRING; 1033177.G7XGT7; -.
DR VEuPathDB; FungiDB:AKAW_04260; -.
DR eggNOG; KOG2143; Eukaryota.
DR InParanoid; G7XGT7; -.
DR Proteomes; UP000006812; 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 709..844
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 97645 MW; 6BB1135B85B77761 CRC64;
MSLLHYWDTL RPSAKRRKTT KEETDTGDEK DTPDSSDSPL IKSSETALPE RLDYNPIPVE
AGFGAAGDDS EVPPNSQTEL ESSLPAIQAD NRAIEEYEAS RAADDENEPD LRQRLRDGTW
RKGRSSIYVD AFNLALETVL DEEAHLFDKA EMEVFRQWRE LDYESQYLYV RLFLRKTSAW
HRVNRLGYYS DIADMSRVVA ELRRARNLPS TSEDGNSTDG TVPVDTSSVL GQDGEFKFAE
EMDQITTLEE ASSLLLLDEL KTLARDAKVT GKSKKELVNA LQRSSQKQTG LDWNSKSNGN
NRHDHFIQKI LDYTGDCIRL ASGPRALFER VHLVFYRSTE WTEKSLTTII LAKISRRNFP
EYVVCRTNSI FPSREILLEF ESALRTQYQI DNLLEFNGTP TVELLTQVKD LAYKVYPRWK
TLLHQEQQKE DTIYDYNEGA YLRRFSPAWV YTRIIHKGLH PLGRFKEHEE EHRLLSELLA
QRLFHAARRG AWYQRKALLE EHYLWALKPS EGRTEEAQRK HWRRVALQTC ETGLQDPDCH
LIYHYDLQKR ITKLERALKV VKREQHDFGH VRLAKPAERT IEGIQIERDE PTQTQPSTPA
DTTTTTTTTP TITTSSKRGR PTIWLDPRDG GECRVESMCL SWYRDRGWKG YHSEGGIIRT
LFTYLFYDIL YTYVPNVFQT PFQTSPLDLH TDAFYPTRLS QINHRLVEIT NGESERLIRA
VYADQSPRQT CAIGLDWSFE LDDLVQIVRC FPGEALAAVC KVVAQEYQAR GGGVPDLLVW
RVYDGEEGRS DGDGDGNGKG KEGYGEVMFV EVKSANDRLS DSQRLWIHVL ASAGVRVEVC
NVVAKEVIRS
//
