ID A0A250XPI4_9CHLO Unreviewed; 923 AA.
AC A0A250XPI4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=CEUSTIGMA_g12389.t1 {ECO:0000313|EMBL:GAX84968.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX84968.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX84968.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX84968.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) 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|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.
CC {ECO:0000256|RuleBase:RU365033}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX84968.1}.
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DR EMBL; BEGY01000143; GAX84968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250XPI4; -.
DR STRING; 1157962.A0A250XPI4; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro.
DR Gene3D; 3.30.70.2330; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR049125; FAN1-like_WH.
DR InterPro; IPR014905; HIRAN.
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; PF08797; HIRAN; 1.
DR SMART; SM00910; HIRAN; 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|RuleBase:RU365033};
KW Manganese {ECO:0000256|RuleBase:RU365033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365033}; Nuclease {ECO:0000256|RuleBase:RU365033};
KW Nucleus {ECO:0000256|RuleBase:RU365033};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT DOMAIN 75..178
FT /note="HIRAN"
FT /evidence="ECO:0000259|SMART:SM00910"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 99280 MW; 49C2451DD541CC6C CRC64;
MRGLGSLQDA VGKTHDFQNK RQSKRLKKSS DPDFSAKVHS ASACTSYLPH EGGRLKSSGT
TTIIACSGNI LSSQPTIIPT YVVGMRHASA QHEGVRNIMS LTLRREPENQ YDRNAILVLT
SDHDGDVSVL GHLPMAVSKH LATLLDRNLV SIQVSVTSSQ KQQEKQHTIP IISAGGTSTF
HSEQGFMEEC SGVCVSQHAA TKQVADYSMY SMTATKQVAD YSMTATKQVA DYSMTATKQV
ADYSMTATKQ VADYSMTATK QVADYSMTTT TGLTMDHAPS EVLSLHGRTS CTNADASSSI
IGKLVTPEVL LSKARSIPIL LIVHPCVNIM HLSDPAQSSA SSIPPVMGSQ NLVEETLQAA
LQAAQSHGAA SGQVLRESFE MIIKEIRELD SHLLCEKEMQ MLKKYEDLPA AAQCLLLRLF
LRKGPWFSVQ DLQYDECPDI PSAVSALLDQ DLVGAPRDDP EVPEWDWSGV LDLLPVAQVR
SVMSRLTVPT MTSSLVSKEE AIRAFRDFRR LASTRQRTNL KPSMTNSQKQ DAGAELSSQL
VDGHAVMEDR NVLLCREAMP KVQPEPEVQL QGTRGGLHGQ EHAAGPRHPD HHPQGLGRSD
ANDAALTALL PSSSYPCTAG CTEDVSDLIY GELKQALGGS AGCIRINPHW QGLMQRMQRI
YFLEEGQDLT RFVASRRGAA PYPKYTVSRS QSAFPERTAL LLYEEALSQA QQLEEAISLE
QWQQAWMVLE DAIAAIKAGQ HGSATSLPPP AATSPAAAAA AAATVLCCVS ASPAANTDLY
PGSACTAAAL DLDHGTSDCA LTAAVGLPAL LEVPSLAEGL EEHPAEATVS SSAQISAGLL
DHSASPPLSS SIHWITCVPT AGGGAASCSS SHQTRHQVVS SSHKGSHGMP CWTRSSYLAR
FSQAWIYTRM CDVAVSMLEK ERR
//
