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Database: UniProt
Entry: C6HA30_AJECH
LinkDB: C6HA30_AJECH
Original site: C6HA30_AJECH 
ID   C6HA30_AJECH            Unreviewed;       820 AA.
AC   C6HA30;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE            EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN   ORFNames=HCDG_03061 {ECO:0000313|EMBL:EER43163.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER43163.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) 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; GG692421; EER43163.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HA30; -.
DR   STRING; 544712.C6HA30; -.
DR   VEuPathDB; FungiDB:HCDG_03061; -.
DR   HOGENOM; CLU_005116_1_0_1; -.
DR   OMA; ECRVESM; -.
DR   Proteomes; UP000002624; 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:UP000002624}.
FT   DOMAIN          702..810
FT                   /note="VRR-NUC"
FT                   /evidence="ECO:0000259|SMART:SM00990"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  94720 MW;  F3A87C59AC85441F CRC64;
     MDDIDPPPKR LRRTGSPGDL FSNAESESEV FPLENYIPPS KTEAGSNDDD GINNTSGVED
     YPPSTQTDLE SSLPPIKTDY EASKAQELTT ENGAANLHHC YEERGWVKGN SSIYVDAFNV
     ALESVLVDET HLFDETEMAV FDHWRRLSYE AQYLYVRLFL RKTSAWHRVN RLGYYQDIAD
     MPAAVKELRH SRKLPSSSTL LQPPYIPALK SPENVVLGEN FQFAEGLEEI NTLEEASSLL
     LLDELKSFSK EAKVQGKNKK ELLKGLRESS TTQSGLSWLP RCKPDDEVPS DSSLNRMSNS
     LSRGNTRDLH FTKKILDHTG DCIRLSSAPR RLFERVHLLF YRSTEWTEKS LTTIILAKIS
     RRNYPNYIVS RSNSIFPSRF ALLEFEAALR VQFDIDNTLE SPDLPIMEKL AFIKSLSESV
     YERWKALIAE EQHKEHVYET GEGAYLRRFS PAWVYTRIIH KGLYALGRFK NYKREHELLT
     ELLDQRLFHA ARRGAWYQRK ALLEEHYMWS LTPFENRSEE IQKRVWKRTA LRTCEEGLED
     PDCHLVYHYD LQKRITKLEK SLKVTKREQH DFGHVMLVKP EERIVEGIRI EKDIPIKSGS
     KETANSVSRR GRPTVWVDER EGGGECRVEN MCLSWYRDKG WKGFHCESGI VRTLFGYLFY
     DILYAYVPNV FQTPFQTCPL DLHTDSFYPT RASEINHRLA QIANGDAEKL IHEVHDREAE
     RETCVIGIDW SFELSDLVEI VQCFRGEALA TEYQQRGGGI PDLFLWSMER KEVMFVEVKS
     ENDRLSDTQR LWIHVLTGAG VRVELCNAVA REVRVETSVA
//
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