ID I2GVW0_TETBL Unreviewed; 1043 AA.
AC I2GVW0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ATP-dependent helicase FUN30 {ECO:0008006|Google:ProtNLM};
GN Name=TBLA0A04680 {ECO:0000313|EMBL:CCH58262.1};
GN ORFNames=TBLA_0A04680 {ECO:0000313|EMBL:CCH58262.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH58262.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH58262.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; HE806316; CCH58262.1; -; Genomic_DNA.
DR RefSeq; XP_004177781.1; XM_004177733.1.
DR AlphaFoldDB; I2GVW0; -.
DR STRING; 1071380.I2GVW0; -.
DR GeneID; 14493672; -.
DR KEGG; tbl:TBLA_0A04680; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_2_1; -.
DR InParanoid; I2GVW0; -.
DR OMA; ELQAYND; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
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; cd17998; DEXHc_SMARCAD1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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:UP000002866}.
FT DOMAIN 502..670
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 871..1027
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 119833 MW; 021E396D5F289A27 CRC64;
MDHDDNEIQV PGTSSPVKYN YRLDSSSPLK PEVENQKFKA QVLRDKFSFV PNANNTPGAT
DPVKTDLELK QLEEEFKDFS PGLVHAVFRS NSWNVDLTRG RLNGIRKKRT GWSWNASFKR
ENESIKKPKK SGRLPSIKND VFKADPSSKI TVDKQKTSIF DRYSSVMSQN NRKIPSKIYS
EDDDEDDLPV IRKKRKLVRA DVLSNKQPTR LDKAKNKILN MRTERLLNQD GDAAENDDDD
ELSADDDISG EEYEERVVEL NIDDQVLTFI NTALAADLAN LSDAPIEKAN VIISMRPFSS
LDEFSKKEFL TEKEKAAKAK NPKKKGGRGS SKKNESERYI EKITQSIRGY NAIDSLIKKC
SSYGDTLASQ MKRWGVNFSD ANNGADLDFM CVDSDAAIVE EFDESDVNSA SSTPAPTLLP
KPTVEKKIKT LGSDEEDFED FEDSEEDEEY GVTVNRRRNI QLNRRASPQR KALIKFFKGK
PRLLAPEISL KDYQQTGINW LNLLYQNQMS CILADDMGLG KTCQVISFFA YLKQINQAGP
HLVVVPSSTL ENWLREFQKF APSLKIEPYY GSQQERAELR GILEQNEGQY DVIVTTYNLA
AGNKYDVSFL RSRNFNVIVY DEGHMLKNSM TDRFAKLMKI AGNFRLLLTG TPLQNNLREL
MSLLEFIMPS IFESKKESLA SVFKQRARTS DNNKDYNPLL AEEAITRAKT MMRPFILRRR
KDQVLKHLPK KHKKIEFCDM TDLQKDIYHK QISSVIEHKR MIKEDLLPEN KKERAKILAS
GSNNLIMSLR KASNHPLLFR HIYDDKKITK MSDAILDEPE YMENGNREYI KEDMSVMSDF
ELHLLCCNFP NTLKKFTIKN DEWMNYWESY IINKIIEKII IGRQEKVLIF SQFTQVLDIL
EKVLSTLNYK FLRLDGSTQV NDRQSLIDKF YEDKEIPIFI LSTKAGGFGI NLVCANNVII
FDQSFNPHDD RQAADRAHRV GQTKEVNVSI LITKNSIDEK IYELAQNKLA LDQHISEDDP
KNLEAMNSKV SDMLEDIIYE ENK
//
