ID A0A177D9X6_ALTAL Unreviewed; 855 AA.
AC A0A177D9X6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=CC77DRAFT_1043752 {ECO:0000313|EMBL:OAG16081.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG16081.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG16081.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG16081.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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; KV441491; OAG16081.1; -; Genomic_DNA.
DR RefSeq; XP_018381502.1; XM_018527328.1.
DR AlphaFoldDB; A0A177D9X6; -.
DR STRING; 5599.A0A177D9X6; -.
DR GeneID; 29112922; -.
DR KEGG; aalt:CC77DRAFT_1043752; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1043752; -.
DR OMA; ECRVESM; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000077248; 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:UP000077248}.
FT DOMAIN 730..849
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 98821 MW; EA2D2AC24A337D97 CRC64;
MALNPRSPSV HNQMITRFIK HPKSTNFDGE QDRPAKRQKT GNSPKKPPPT PRKTTKREML
DSEDECESIV IKKEEREHKT DLETALPQVD TSDDAIRAYE AYKAEEESKT ERADERLEKR
AWIRGKSSLY VDAFNLALDT VLDEESHLFD EAETEVFRIW REIGYEAQYL YVRLFLRKTS
VWHRIKNLGY HSDISDLEAA AETLQRTYNL PPSSSEVESH PGELKAPAGT TLGTSFTFAD
RSEEEISTLE EASSLLKLDE LKVLAKDAKV KGKNKGELLK ALRRTSQKQA GLGYVGLKRS
DSEISRGSSA SRSRPETPEV ELEPEGDLSD DANRDAHFTR RIMQETGPCI RLSLDTLKLF
ERVHLVFYRS TEWTEKSLTT IILAKIARWN FPEYIVSRSA NIFASRSLLL EYEASIRTQY
RIDSILEFNG RPTEKGYQEI IDTFNEVYPR WQVLVQEEQQ KENSIYQSGE GSYLRRLSPA
WIYTRIIHKA LDVLRRRKEH VREHELLTEL LQQRLFHHSR RGAWYQRKAL LEEHYMAALT
DSEKRSADKQ KRHWKLIALQ TCEDGLQDNL VHIIYHYDLQ KRITKLELSL NFAKRMQHDF
SHVRLTKPVE VSMEGTRIER ERPSLSRRNS SPHSKFGRRG GKTIWIDPRE DGECSVEAMC
LSHYRNRGWK GYHSEGGIVR TLFAYLFFDV LFTYVPNVFQ TPYQTCPLDL HTDAFYASRI
SEINARLNEI SNGDAPAIIQ RIYDDHHERR TCVVGLDWTY DVLDLLEIAH CFDGEALATV
CKVMAQEYGQ RGGGVPDLFL WRISEEGKKG EVKFAEVKSE NDRLSDTQRL WIHVLSGAGV
RVELCAAVAK EVKVI
//
