ID C4JZP8_UNCRE Unreviewed; 1123 AA.
AC C4JZP8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=SNF2 family helicase/ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UREG_07649 {ECO:0000313|EMBL:EEP82784.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP82784.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH476619; EEP82784.1; -; Genomic_DNA.
DR RefSeq; XP_002582876.1; XM_002582830.1.
DR AlphaFoldDB; C4JZP8; -.
DR STRING; 336963.C4JZP8; -.
DR GeneID; 8440596; -.
DR KEGG; ure:UREG_07649; -.
DR VEuPathDB; FungiDB:UREG_07649; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_2_1; -.
DR InParanoid; C4JZP8; -.
DR OMA; ELQAYND; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002058; 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; 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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT DOMAIN 586..753
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 939..1089
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 124168 MW; B0E0056800780721 CRC64;
MIDCIPDTPI RKKTAAEELI PSASDSSEDE TVATVPLYQS LHSTATQAST IPTQALYTQK
MTQPTQIIER PTPPKSSPLR NPPVVQVATS SPLAPTTFSR YPAARAGVLS SSMAPSGTRF
RAPAMAAPVK RTPVIDLEDD GPTYRGGSSD EEDLRRGTTD IKPSTFIKAS KSPEKERVAE
SPVAATKFKE ITAAAFYNPT SAFKGPGKRQ ADTTRDPSAK RPRSNLTSPV SEPLALADIE
DYNIKTKVER MRNVFPNKSV QACLDALLAK KGNYEDAVDY IGQLDDAPVE NAMSDDELSL
DHKSAGPSAP VNTAKQQIKA RTRIQDKWAT GQRIGQRAGS PQARRRLIRG SKSRRVSPIP
ISSPVTGGIT KKPGRLVRGR KARSRSRSES PVLSYVESDD SDSAPEASED DGSLQVKVLK
FFNTCSADDL ADIAELAPDV VTHFMSKRPF TSLAQVREIS IEPVQPKGAK ARKAKKPLGD
KVVDKCLDMW TGYEAVDALV KKCEDLGKPI AEEMKRWGVD IFGSKTAGEL ELVSLEKSSS
SHDSGVGTPS SVSSESTGNK FIGQPAIMSE DIKMKDYQIV GINWLSLLFE QKLSCILADD
MGLGKTCQVI AFLAHLFEKG VSGPHLVVVP SSTLENWLRE FSVFCPKLNV MPYYAGQKER
AIIREQIEDD RENINVVITT YTIAKAKMDA AFLSTMDFCA CVFDEGHMLK SSKSQLYNKL
IRIPAQFRLL LTGTPLQNNL QELASLLGFI LPQVFKERKD DLEYIFSAKA KTIDTHSALL
SAQRIARAKS MLTPFVLRRK KHQVIDLPAK ITRVEYCTLN EAQKSIYENE IETVRRTLAD
RAAGKKIGNK STNILMKLRQ AAIHPLFYRR HYDDQTLSRI AKACLKDPKW AMSDPDAIYE
ELVAYNDFEC HTLCSNSPDA LGKFALKNDE WMNSGKVEKL CELLKKFTEN GDRVLVFSQF
TMVMDILEHV LETLQIRFFR LDGTTSVEDR QSILDAFYEQ VDIPVFMLST KAGGAGINLA
CANKVIIFDS SFNPQDDIQA ENRAHRVGQT REVEVVRLVT KDTIEEQIYA LGQTKLVLDQ
RVAGEEEGGK KGEEAGIKAV EEMVLAKLED EQSERKDAGE QQG
//