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Database: UniProt
Entry: A0A084Q8H7_STAC4
LinkDB: A0A084Q8H7_STAC4
Original site: A0A084Q8H7_STAC4 
ID   A0A084Q8H7_STAC4        Unreviewed;       805 AA.
AC   A0A084Q8H7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=DNA repair protein rhp54 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=S40285_08044 {ECO:0000313|EMBL:KFA60262.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60262.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA60262.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60262.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KL660940; KFA60262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084Q8H7; -.
DR   STRING; 1283841.A0A084Q8H7; -.
DR   HOGENOM; CLU_000315_10_2_1; -.
DR   InParanoid; A0A084Q8H7; -.
DR   OMA; YTEHERM; -.
DR   OrthoDB; 5480555at2759; -.
DR   Proteomes; UP000028524; 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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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; IPR013967; Rad54_N.
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; PF08658; Rad54_N; 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:UP000028524}.
FT   DOMAIN          233..411
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          566..719
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  90675 MW;  880788147F1CA056 CRC64;
     MSRSALVSTP LASKANRGAR PTPSTDSASK LVRPFKCPGS ANRRQVDDRP ARKRRKVDYK
     GADGDADEDK PYSNDDRLAL ATRDANRFPV FQAKDKTTVF RKAFSVPLKD KNTGAYNPNR
     PPPTLGLRQG AIFTPRPLHD PSGEFAIVLY DPTIDDKAAV LPDEQSTEKK LEPPPAKIDA
     PLMHKSLAEI LGIKKKVEND HPRVPVVIDP RLAKVLRPHQ VEGVKFMYKC VTGMIDSKAN
     GCIMADEMGL GKTLQCITLL WTLLKQSPDA GKPTCQKAIV VCPASLVKNW ANELVKWLGA
     NAINPFAIDG KASKEELTRQ LRQWAMASGR AVTRPVIIVS YETLRLNVEE LKHTKIGLLF
     CDEGHRLKNG DSNTFNALNN LNVSRRVILT GTPIQNDLTE YFSLTSFANP DLLGSRLEFR
     KRFELPILRG RDAAASEADR ERGDQCTAEL LGIVNKFLIR RTNDLLSKYL PVKYEHVVFC
     NLAPFQLDLY NYFITSPDIK ALLRGKGSQP LKAINILKKL CNHPDLLTLS EDLPGSEKCF
     PEDYVPKEAR GRDREVKPWY SGKMQVLDRM LARIRQDTND KIVLISNYTS TLDLFERLCR
     SRQYGCLRLD GTMNVSKRQK LVDRFNDPEG EEFVFLLSSK AGGCGINLIG ANRLVLFDPD
     WNPAADQQAL ARVWRDGQKK DCFVYRFIAT GTIEEKIFQR QSHKQSLSSC VVDSAEDVER
     HFSLDSLREL FQYRPGTTSD THDTFKCKRC KPDGKQYLKS PAMLYGDTST WNHFVNSGLK
     PIQDLLLRQE AEETEVSAVF QYISH
//
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