ID A0A195BPW9_9HYME Unreviewed; 943 AA.
AC A0A195BPW9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=ALC53_03439 {ECO:0000313|EMBL:KYM87539.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM87539.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM87539.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM87539.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM87539.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-2015) 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; KQ976432; KYM87539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195BPW9; -.
DR STRING; 520822.A0A195BPW9; -.
DR Proteomes; UP000078540; 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:UP000078540}.
FT DOMAIN 829..926
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 108312 MW; 1A89AEC9BF7E5475 CRC64;
MAQTRIDQYY KVTSSNKKSE SVKRNIKKSS NARSRSPIIG RTKDRQVSGN SRTPVRKKQS
PYKIKQNGMY SNVSFGNGAS PFKTNMNNSP IKITEMTIMS STIEHNSPDI IYVGSQQHTI
SHSGIKSTST PKTFPTKNAR DKSPPAKIPR RKLFMDKAKY SPIKLFKDRI ENSSTNIIEN
KIMLPTTEHF SPDIIYVGSQ QCTASCSGTK FTPKTSSPIK NKSSSPIIAR KKLFNDRIEE
LTSATISNLN LAKEGAIGNN DIDLEKVYSS KRFDYKYNPI DTTISTKYEI NDVVVPTDKN
SLLFFLAIVT VFSKPINCGY FDQDELDFIF SMITLRRNAQ ALLIRMLKRK HMWHRISNIK
YDEISNDLKP IFDELVSRSI FKNNMDKEDI FILLNLLHAD EVSKICRELK INVRGKRLSI
ESILAFCKTK SLFPGMATPA TKLRASINKV LGDCILLNDK VKELADRIIT LLIPNRNPDE
TFADVFQMLW NVEADELEFP EVIISDLPIF ISKRHLLDYI EAKNALTNIL TAIEKKQWNT
VQNLGTLAAQ RLPLFLEVES ESFQDSSLPH HIRHFMPGYI WLKVLSKSID AFKKSKETLS
QAIKFLLILI EQNCHMKHRK GQWYSELIKI EMFHRKNFEA SFMFLSKAML CENLTEVDEF
NLLDRAKKIY KRKSGIEEKT KNSVKIMLNT VFSRIQLTHQ NSKTIEGTVC GNTLQGKSTW
CISRGIDQVY GSVESLALYH YKNEGYIKGV HCEGAFPITL FAILFWNEIY NINVPGTWVS
SYQDAPLDLY TSEFYENRKK EIDEKLQNIR SYDSEKMSKH LQNEFESYSK YKSISQSNIF
DDSNSFKEIA FCLGVKGVVG ICERLIHNFS LWKAGFPDII VWNINTKQYK IIEVKGPNDT
LSTKQTLWLN YLNRIGLNTE VCYCESNTSY SRGHKRKHEE AVI
//
