ID A0A1U8JYR8_GOSHI Unreviewed; 951 AA.
AC A0A1U8JYR8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-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 Name=LOC107910178 {ECO:0000313|RefSeq:XP_016693444.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016693444.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016693444.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016693444.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_016693444.1; XM_016837955.1.
DR AlphaFoldDB; A0A1U8JYR8; -.
DR STRING; 3635.A0A1U8JYR8; -.
DR PaxDb; 3635-A0A1U8JYR8; -.
DR GeneID; 107910178; -.
DR KEGG; ghi:107910178; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000189702; Chromosome 20.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; 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; IBA:GO_Central.
DR CDD; cd22326; FAN1-like; 1.
DR Gene3D; 3.30.70.2330; -; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 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; IPR014905; HIRAN.
DR InterPro; IPR006642; Rad18_UBZ4.
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; PF08797; HIRAN; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00990; VRR_NUC; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
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:UP000189702};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01256}.
FT DOMAIN 61..90
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT REGION 144..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 107760 MW; F627153178A2A43E CRC64;
MLTGRESLSR LIGKRRRFLP NLQSILSLPI RSSLNLLSDK NGGLTETESS KGKVEISSSD
LVTCPVCGSK VRGEDYTINS HLDRCLSRRT NRKLTQRTLL ELNFGCSQSK LQISSDESEQ
LLSSDLSKNC SDYEENVTRC FSKIDPREEK SHDQGRQFPH TESVKQIDVA GSAENPISDG
RANTMVDFSA LSTDNEESRN HMDGTADSIS GMAIDTFIVG RKFSDEKEVN LGANIYLLRD
PDNIKDSNAI KVLSASSACC KVLGYLPLEL AQYLSPLIEK YCLSFEGYVI SVPKRSLDAV
PIQIVCQNSI FNGKKGCDEF EALHLWQKAL QVVEFAKNRP PNTTKYQQNF CLLLKEVLTS
SPHLFTKDKK KFIESFTSLS EDSQRLFVRL YTRKGPWFRL STIMYPEICN PQQAVKELSA
TGYLYLFEDT TKLHDDEMKD LLSLLTVSEL RDILCTLRKK CNQGSRKQNL IASLLSCYKG
GSCPVLQRLI LERTEICIRT SPEAESLFWR AERLFFLNGE QDLSAFLLVD LGIVKYPTYN
CIILEQIFSN ESDLLAYEEA IEVAQVIDQS LDENNFELVL RCIMIADSRI SCCPEKLIDS
TSPDLMAIFR SCFSASWVYS KVILLGISFL ECERRYKDAI HLLRRLLDCF TCDTRRGYWT
VRLAVDLEHI GCPNESLSVA EAGLLDPWVR AGSRMALQRR VLRLAKPPRR WKTPSFSVSL
KRKIVEVHIQ GRPLNCEAGR KSRFYGEDGE QCGVEQLALQ YYAREGGWQG VHTESGIWMT
IFGLLMWDIL LSDVPNVFRT RFQTAPLDME TDHFYLARKS LIEPQLQKIH DGLAEEILIT
SWELHMGTAC RGVNWDQHSL SDLRAAVSCI RGPCLASLCR HLAQDYSSWS SGMPDLLLWR
FHGDYKGEAK LVEVKGPRDQ LSEQQRAWLL LLMDCGFNAE VCKVSTTGTS P
//
