ID H2AXS8_KAZAF Unreviewed; 719 AA.
AC H2AXS8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=KAFR0G01440 {ECO:0000313|EMBL:CCF59178.1};
GN ORFNames=KAFR_0G01440 {ECO:0000313|EMBL:CCF59178.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59178.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF59178.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
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 -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU000492}.
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DR EMBL; HE650827; CCF59178.1; -; Genomic_DNA.
DR RefSeq; XP_003958313.1; XM_003958264.1.
DR AlphaFoldDB; H2AXS8; -.
DR STRING; 1071382.H2AXS8; -.
DR GeneID; 13887158; -.
DR KEGG; kaf:KAFR_0G01440; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; H2AXS8; -.
DR OrthoDB; 56712at2759; -.
DR Proteomes; UP000005220; Chromosome 7.
DR GO; GO:0030684; C:preribosome; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProt.
DR CDD; cd17946; DEADc_DDX24; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT DOMAIN 135..163
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 166..359
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 413..565
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 83..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..163
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 719 AA; 81323 MW; CC0071B5FB2E46F4 CRC64;
MSKKVQVKPK DLKWKSVQVS DTLDDFGGFY GLEEIDGVDV KIIDGKATFF ATESKNNDVE
QEQRESEDQE LIEFKNLDDI EEGELSALSE SDSDDEDDEI EDEDNLNDDD DELTENVFSA
DLDLQDVVSL VELPEWTKLA KFSMTTLQGL AKLGFTKPTE IQAKTIPLGL GNHDIMGKAS
TGSGKTLAYG IPMLENFVKS FKSKDNNRAI GLIFTPTREL AQQVTQHLTK VSELILKEKN
KYAILSLTGG LSIQKQERLL KYQGSGKIVI ATPGRFLELL EKNNELIERF GKIDTLVLDE
ADRLLQDGHF DEFEKILKLL GNYRKKSSKS HWQTMIFSAT FSTDLFNKLA SNHNHNKNKN
DGENEMETVL KHLMTKIHFK SKPVIVDTNP DEKVSSQIKE SLIECAPMER DLYVYYFLAM
YPGTTLVFCN AIESVKRLNA YLNLLNISSF QIHSSMTQKN RLKNLEKFKQ QAQHNSVLNK
ATVLIASDVA ARGLDIPGIQ HVIHYHLPRT ADVYIHRSGR TARHKNEGVS VMICSPQESM
SSLRKLRKVL SSNEAHLKKG KFRSKQKWQK TVPLLPIEID IVSQLRERSK IASELADHDI
ASKSLSKDDN WLKKAAEDLG IDADSDDENK DTYLAKNKTK KINKTMAKDQ ARYSKAHLNE
LLSIPLRKDM RKKYLTGGLV NLADNLVKKR GHNSIIGQEE IGALALLKNK KNANKRTKK
//
