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Database: UniProt
Entry: U7PP08_SPOS1
LinkDB: U7PP08_SPOS1
Original site: U7PP08_SPOS1 
ID   U7PP08_SPOS1            Unreviewed;      1254 AA.
AC   U7PP08;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA repair and recombination protein RAD26 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1624_06659 {ECO:0000313|EMBL:ERS97327.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS97327.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KI440848; ERS97327.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PP08; -.
DR   STRING; 1391915.U7PP08; -.
DR   eggNOG; KOG0387; Eukaryota.
DR   HOGENOM; CLU_000315_7_0_1; -.
DR   OrthoDB; 5488252at2759; -.
DR   Proteomes; UP000018087; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd22254; CSB_WHD; 1.
DR   CDD; cd18000; DEXHc_ERCC6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   DOMAIN          443..635
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          772..933
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          67..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1037
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1112..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1152..1172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1254 AA;  138829 MW;  3A2F66ABBA061A3F CRC64;
     MSSPSHTPAA PDAVSDNAAM LDEESAIKAL TETVRDQDDL ERDITYQAEL ALIDAEDKRD
     EKRIKRLEAS KTKLEAQRST YQQRLRATST GNPALRRRFE SEIAKLATEI ETADKDLADF
     RRRIDQRHVG DGGRGAAGPS SATDDDKSAG NHRLPNETQR EFLIRTGKIT PFAKVSGARP
     DGIEGDLADV ILEAEDEAIA EELAGSARDE PHSHQNLRLP GFSEGVQAVK LGRADAQRAA
     KQKQETEAQA RPSTAAEASV ESEFSLRPRK KRKTRPVDAA QGSDYSGGDG DEDEWKPAAD
     ASESGTALAS GDESDDDDTT DFTELTRPKA KKQRGRKGRV STLASETEGD SDAKVNLSGV
     DDGNEMVYKQ RLDNWVTRRR NARRLRRQAA GLLADDDDDD DTPEWFKPSP DEPDHVFENG
     LRLPGDIYPS LFAYQKTAVR WLAELYDMRV GGIIGDEMGL GKTVQLISFV AALHYSRRLD
     KPVIVVAPAT VLRQWVNEFH RWWPALRVSI LHSSGSGMLS VKGEDRIEEE ELPWDSRPAK
     RGSSAAAKKI VDRVVKHGHV LVTTYAGLQT YGDVLIPVNW GYAVLDEGHK IRNPNTAITV
     YCKELRTPNR IILSGTPMQN NLTELWSLFD FIYPMRLGTL INFRNQFEIP IRLGGYANAT
     NLQIMTAQKC AETLKDAISP YLLQRLKADV ATDLPKKSEQ VLFCKLTEPQ RLAYELFLKS
     DEMNAILRRA RQSLYGIDIL RKICNHPDLL EPPLKHKEGY YWGNPNKSGK MQVVKTLLQM
     WKRFGHKTLL FSQGTQMLDI LEAFVQRQGD INYLRMDGKT AIKDRQTLVD RFNNNPNIDL
     FLLTTKVGGL GTNLTGANRV IIFDPDWNPS TDVQARERAW RLGQKKEVTI YRLMTAGTIE
     EKIYHRQIFK QFLTNKVLKD PKQRTTFGLH DLHDLFSLGS YEDGVTETSE LFQGSEVTVT
     TGRKQVITPG PDAVPIITDG NKGKATEATA AAAGDGDDAK QLRSMPGVAK LEEFQQADDD
     DANANGETAD TSASAQEDRI MKGIFAQSAL HSAVEHDMIM NGGSSGSGKR TVQADRRILE
     QEARRVASEA AAHLRQAGEE AGRVPIGTVT WTGEVGEAGR PRNVRNERRG RAGPSSSGIL
     ASIADRQGLR MPSSRRSPSG TPDRGYASSA SASASASASA GITVDDFERM IPNFIRRHGG
     KVPSKVLVDH FNQYCTGKQQ AADFKKALEV VARMEKTGSS MRAIWSLKPK FQQA
//
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