SLX4_NEOFI
ID SLX4_NEOFI Reviewed; 812 AA.
AC A1CZ18;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=slx4; ORFNames=NFIA_035560;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Regulatory subunit of the slx1-slx4 structure-specific
CC endonuclease that resolves DNA secondary structures generated during
CC DNA repair and recombination. Has endonuclease activity towards
CC branched DNA substrates, introducing single-strand cuts in duplex DNA
CC close to junctions with ss-DNA. {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- SUBUNIT: Forms a heterodimer with slx1. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- PTM: Phosphorylated in response to DNA damage. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
CC -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
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DR EMBL; DS027686; EAW23988.1; -; Genomic_DNA.
DR RefSeq; XP_001265885.1; XM_001265884.1.
DR AlphaFoldDB; A1CZ18; -.
DR SMR; A1CZ18; -.
DR STRING; 331117.A1CZ18; -.
DR PRIDE; A1CZ18; -.
DR EnsemblFungi; EAW23988; EAW23988; NFIA_035560.
DR GeneID; 4592818; -.
DR KEGG; nfi:NFIA_035560; -.
DR VEuPathDB; FungiDB:NFIA_035560; -.
DR eggNOG; ENOG502S832; Eukaryota.
DR HOGENOM; CLU_016773_0_0_1; -.
DR OMA; TWHEKIL; -.
DR OrthoDB; 231792at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR HAMAP; MF_03110; Endonuc_su_Slx4; 1.
DR InterPro; IPR027784; Slx4_ascomycetes.
DR InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR Pfam; PF09494; Slx4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..812
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000388033"
FT REGION 36..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 89111 MW; 9DF5A78FF8061FF2 CRC64;
MYTATDVVVL SSSPDQIPSL TLAKPKCDAE KAFVLSPVSS SPSALPSASE LFQPPTRSRF
FKTGDGNEGS SRTAREESET GTKQNDLAAS RRKRAARGGR QKRTKEQPTN ESQTLFDHPE
PPIPKHVGCT SKKGTGSKKK RTDAANKCTK SENKTITGKV TKPGITETTK SEDKTKELVT
ADVSTGKSPA NKLELEKDGL QLEVAMKRRL DWTPTKDTGK QAVALDDTGD NKTRFGELLS
EYGFLKAATD SQGDSKLSDG APTKRRRLEL VDTRTPSTSK RTSPDADSDR SNVRSTRSSK
APAAEGKPKK RSRKITTLTG RVTALYTNDC TDHLDAANTM ISPSDDVSSK LFSKSLDIDS
CVLPPEDAVD YLKDQDLIFG TCSQLEREDS PTMLRDMQKA IRASENSMIE NRKPSSTTRA
GSGLYSHTAV SRFQTPRDLW SVAARDMDGS LAEIEVLDMV DITDISELPP KPNGELPDRS
EKNDKDTVSQ GESFRPVEIT DEVEVEVDVR TENLATSETN PGETACGASE LRPRPRFADW
KDSDLLKQVR LYGFKPMKSR RKMIEVLERC WKAQHVSTRT GVQDVPGKPD DGSAGKAGTI
KSQTNKQASK MDAAEKTRKA SACLKEEAKS STALEDKPSH AADGSSQVLT KSSFADVEEI
EDSEDEVIPS PSRLQSRYKR HISESRSSQP LSVSATPSTP SSPTRTNADS GTKPSPFGLA
AESRLPDLAS QITKAVRLQP RSFSVDCKRP SWHEKILMYD PIILEDFATW LNIEGLGLVH
EDREVSAEFV RQWCESNGIC CGFRKNSRQS ER
