ID A0A078B4I6_STYLE Unreviewed; 1248 AA.
AC A0A078B4I6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN Name=Contig11848.g12666 {ECO:0000313|EMBL:CDW88137.1};
GN ORFNames=STYLEM_17254 {ECO:0000313|EMBL:CDW88137.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW88137.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW88137.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW88137.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) 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; CCKQ01016265; CDW88137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078B4I6; -.
DR EnsemblProtists; CDW88137; CDW88137; STYLEM_17254.
DR InParanoid; A0A078B4I6; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000039865; 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 Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
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:UP000039865}.
FT DOMAIN 1134..1240
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 870..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 147093 MW; E5D621C266013ABA CRC64;
MSSALTNSSS GSSVSTLDKH QKSLENFYNI KTPHPKKESS ATDSEYFEYY QFPMVFRQKI
LYRKQYEQNH KPDKNLLKCN HAIKVVASRT TRQEDRTDLI EEFDLGYLAV DFSFNMSIIL
NENREYFKID CKFTNSPKTD MIDIAVGFLD HILKDQKIKD SAISDQVESG CSSYSVKDFW
GMPKILQKAF KQIDIHNINK EVGFEFYAKS NNDQNDLILE QAQLKEEAGH FDYFKEYVPP
ESLCLSQSEA STEILSSIKE EIINSQTSSL SQKTYQESLQ NYKQPIDEDN RNFDLVLQTV
LKYENLFTED EKSLIYLFMA QENQVKTLYA RMFFRRRYWF NNHILSKYTS NSEQIETSVQ
RLYKNGFVRN DQDVVYDNDF ERISELIENG INISGIKILE SEIKKIIRGQ SRDDLPHEFD
LIHVNNFYQL KHTFEGPLAE TCIKASQKIS LWIRQISEEN IQSGKKVLFF RDNQMSDKLK
MTNRIMSRIM NTLGEKNDNS FGSSKINATT AASSLLSFMK LSNEISKKLS KGDNQLKERI
LDAFYKANDN SRTYYLEEKS RSLFYRCLRL FFFYQKKDAY ETLLGHDYGF YRYEKFQNYL
SDKDRNPDNH NLKPIFQNRD DFITFDESSQ IIGATFDFLS INLKRRDLEC KLATKIIKRT
LRILGVEYRK DNREFLLFDN LRALHQDSEV GTKVSDDKHQ FIDRYRSEWS YLRILDALFP
ILEKDKQYQI SAITLIFLLQ NKIFYTQRGK WWHRLAVNLK HMKNKNDALK TCDLALRDEF
VKGDKKNMIL KIRLNLFVEI NRQQGKLLLK NSKAKAKLKG KKDKLQIKKK KSSKTDNIHM
MEQLNKSFAQ SQGIIRDMKR KLNRITMLNS FLDDDNPGGQ GGISNVHILD DYSDEEDNDK
QVGKKRKKKS KKQLYSDEDE DDEKYSTDGD VQNETSDIDE ETHTNNIMIF GNDKSSSNIC
SQTSDLQITE IRSLDTSKEL NLSLNPDVLI EKEKKSTYDQ LQRSCESKIN KEYFKEVFLN
ARRNFNGEHL KSVYLDKKSN KFFNVENLAL HYYGQKQKWN GAHVENSLMK YMYGIMMWDE
IFNDDIPYVF QTTYQFQPLD FDYPEFYTHR KKLIDDKLQR IINMPRMEIK KYLTSEYEKH
KNYHNPIVNW DNIKLTKERM ASIAYCMGGP LIAMFFEKLA QDFKNWGYGM PDLVLWREDK
AAIKFVEVKS ENDNVSEQQK CWIYNITECG IDVEVCWITD KVEGVDVF
//
