GenomeNet

Database: UniProt
Entry: A6R603
LinkDB: A6R603
Original site: A6R603 
ID   SUB2_AJECN              Reviewed;         442 AA.
AC   A6R603;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   31-JUL-2019, entry version 58.
DE   RecName: Full=ATP-dependent RNA helicase SUB2;
DE            EC=3.6.4.13;
GN   Name=SUB2; ORFNames=HCAG_05061;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=339724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in transcription
CC       elongation and required for the export of mRNA out of the nucleus.
CC       SUB2 plays also a role in pre-mRNA splicing and spliceosome
CC       assembly. May be involved in rDNA and telomeric silencing, and
CC       maintenance of genome integrity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN08562.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH476659; EDN08562.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001539594.1; XM_001539544.1.
DR   SMR; A6R603; -.
DR   PRIDE; A6R603; -.
DR   EnsemblFungi; EDN08562; EDN08562; HCAG_05061.
DR   GeneID; 5446516; -.
DR   KEGG; aje:HCAG_05061; -.
DR   EuPathDB; FungiDB:HCAG_05061; -.
DR   KO; K12812; -.
DR   OrthoDB; 779000at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; mRNA transport; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding; Spliceosome; Transport.
FT   CHAIN         1    442       ATP-dependent RNA helicase SUB2.
FT                                /FTId=PRO_0000310221.
FT   DOMAIN       90    265       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      293    438       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     103    110       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        59     87       Q motif.
FT   MOTIF       212    215       DECD box.
SQ   SEQUENCE   442 AA;  49388 MW;  A3C5AF0A1216F8B3 CRC64;
     MSHEEDLIDY SDEELQATDA AAGTAAAGAN GAAPKKEGDL TVSGARADKK GSYVGIHSTG
     FRDFLLKGEL LRAITDCGFE HPSEVQQVCI PTAILNVDVL CQAKSGLGKT AVFVLTTLHQ
     LEPVPGECSI LVMCHTRELA YQIKNEYARF SKYLPDVKTA VFYGGTPMQK DIELLSSKDT
     YPSIVVGTPG RLNALVRDKK LSLRNIKAFV LDECDKMLDQ IDMRRDVQEI FRATPADKQV
     MMFSATLSQE VRPICKKFMR NPLEVYVDDD TKLTLHGLLQ YYIKLGESEK NRKLNELLDS
     LEFNQVIIFV KSTQRASELD KLLRECNFPS IAVHSGVSQE ERIKRYKEFK EFNKRICVAT
     DVFGRGIDIE RINLAINYDL PADADSYLHR VGRAGRFGTK GLAISFVSSE QDQEVLKDIE
     KRFEVALPEY PQGGVDSSAY MA
//
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