ID A8NYF9_COPC7 Unreviewed; 992 AA.
AC A8NYF9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=CC1G_01329 {ECO:0000313|EMBL:EAU84333.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU84333.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU84333.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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:EAU84333.2}.
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DR EMBL; AACS02000005; EAU84333.2; -; Genomic_DNA.
DR RefSeq; XP_001837417.2; XM_001837365.2.
DR AlphaFoldDB; A8NYF9; -.
DR STRING; 240176.A8NYF9; -.
DR GeneID; 6013973; -.
DR KEGG; cci:CC1G_01329; -.
DR VEuPathDB; FungiDB:CC1G_01329; -.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_005116_0_0_1; -.
DR InParanoid; A8NYF9; -.
DR OMA; ECRVESM; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000001861; 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; 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; 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:UP000001861}.
FT DOMAIN 788..904
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 152..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 113214 MW; 11D03C6A6433C1F8 CRC64;
MSETAKTNRF IQINIFGDKL YNAVNSDDDE ISEIEDNDMK RTWDADGTRR PSGYITVFEE
MVNDVLEHDR HLLSESELDA LDAFSRLCCK FGYFLNEDPS RYCLVRMLLL KPGRWNPMCK
FEKWKTEVGP DGLLPSIEPL CQPIKDLLAL PSQPSSQVRV GQDTQPPRPE IIDLTESDDE
DANSNVPGPS AIPQKPPSDD PIDRIINRSS ESDDITLAYF CESDEKMSLY ELLQSLTVEQ
LKGLAKSNKC QPGPKSTKQD FVHALLDNAT SQGVLGFAMK DNKGKGKASV PLKQTQLTSF
IIGKSKACPR QSQEKRLRAQ ILKILGRCFR VNHDFFRLVR RIHVIAFRCT EHPPKLMLPA
LLTRFKKRTY AEYKHERDVD IWPSRIELVH YEEALELEMH LDQLLESKPE EQPRGKTVDP
KARETPATPG PKRVTMKTPR ASKTTAPSTP REGEYIDFGP DGWDIDEEEE EETPEPDDPK
IKKAKQIVKH LDEWILQRWT LWLEWKHHRN AGRTPALQRF EPGYIYSRMM RKVLKSLAQL
KEYQRELDVI QAMLGQRLFL RGKRAKLYER RAILQTRYLH KTPEGKVDLN VLRQALEGVK
EALLDDDTVL VARPSLVRRL RKLEARLKLP PGDRTVCEGE LREAQTVNIV AKRIFKPDST
GKPTNKENIA SYMKNNSTPN VKQPQRRDSV PNPAQRKHPG KSIWVGRNSA EVSVEQVALE
YYEDLGFKGF HAETSIMTTI FGLLFWDIIF ADIRGAFETK FQSAPLDIVD DSFYYARKDM
IDARLEELRQ GKGVEILQRH YAAHSETKTC CIGVRWDICT EQDLVEILEC LGGKQLASIC
KLFCEDYTGR CSGAPDLIAW NAQHRICKFI EVKGPGDTPQ ENQKLWFDSL LAANIDVEIC
RVADVNDVKT HTTAKKKGRS SAAPSTRKRK RSTTKHSGSD SDVEEQNYDK LDPHCDDELP
QVSSSRKRRR ATDPGEPLCL QSLGAPPRRS GQ
//
