ID F2TYV9_SALR5 Unreviewed; 2166 AA.
AC F2TYV9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=RNA helicase {ECO:0000313|EMBL:EGD78783.1};
GN ORFNames=PTSG_01759 {ECO:0000313|EMBL:EGD78783.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL832957; EGD78783.1; -; Genomic_DNA.
DR RefSeq; XP_004997739.1; XM_004997682.1.
DR STRING; 946362.F2TYV9; -.
DR EnsemblProtists; EGD78783; EGD78783; PTSG_01759.
DR GeneID; 16078334; -.
DR KEGG; sre:PTSG_01759; -.
DR eggNOG; KOG0952; Eukaryota.
DR InParanoid; F2TYV9; -.
DR OMA; MCSATEF; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18022; DEXHc_ASCC3_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EGD78783.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799}.
FT DOMAIN 464..647
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 677..880
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1320..1495
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1525..1723
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 49..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2125..2166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2145..2166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2166 AA; 243774 MW; 7852702CB1B4C9B9 CRC64;
MMTSPQQATA LMETPRLTTA LRTFTSYSED EEFAQGVLSD QELEALIQRK KAKQHADLDE
SEVSDAEDTE SAAASKQQDS SGGQDVVMAE FGVKVAFDKV QSQTLDELLL EAQRYRARER
ARQLQTARRV QAEEQAKATK VLLTSARKPG QRKAKQPQQA AAPKAPSSSS SPPSSSASAQ
QAAASGGPGA HLPRKWLRQK CRQHFDTAAA DNIRAAVFDL LAGPKSTDEL QNDLFDLLGF
ERFELIQELL EKRVDIVAAE ERAVMETAAS ASSSSRKSRN QPQLPMQAGP IGPGVVIMSE
AEKKLMKKHR REERKQARAV AKAKKQLEEE GGDASDIKSI LGFDPEAARL ARERQLARAA
ARSVFASPST AQRVEDRPKY PFVFDSALEN RLKGAYVYGA KVMLPADATR TDSKTHESIV
IPPVQRRAPM TGERRVAVHD LNYVGQLAFQ GYESLNRIQS IVFDTAYTTN HNLLICAPTG
AGKTNIAMLT VLRCIEQHIE QGVVQKDKFK IVYIAPMKAL AAEMTETFGR RLAPLNLAVR
ELTGDMQLTK AEIIRTNMLV TTPEKWDVVT RKGMGDVALT QLVKLLIIDE VHLLHDERGA
VIESLVARTL RQVESSQSMI RIVGLSATLP NYVDVANFLR VNPHKGLFHF DGGFRPVPLQ
QSFVGVKGKN RFAVNDEMDK LCFDVVLENV LRGEQVMVFV HSRNGTLNTA ARLIDLATKE
NQMAAFDCSD SKEFPLAQKA FARCKHKQLK SFLGNGFAVH HAGLLRSDRN VVEKYFAKKL
IKVLVCTATL AWGVNLPAHA VVIKGTELYD ATRGQIVDLG ILDVQQIFGR AGRPQFDTFG
EATLMTTHDK LSHYITRIMN QRPIESNFLS RLPDNLNAEV ALGTVTDVRE AVAWLSYTYL
YVRMLKNPHV YGLTPKEANE DVMLERHREK MIIEAARQLD DRRMLRFQET AGYLSSTDVG
RIASHFYISA ETIEMYNTAF KPHMAEAELI TMVAKSSEFT QIKVRDEELD ELDYLKREYC
VLHPVLGGSE NTYGKVNILL QAYISQAPLR SFSLTSDMNY VAKNAGRLLR GLFEIALRRS
LATLVPKLLT LCLCVDRRLW WHINTPLRQL GNFLPNEMYN KIEGRGMDLF EILDMPEDEL
GHWLRHVRMG DKVKQAAQLI PMIEMDAVIR PVTRTVLKVI LTIEPAFNWR TRFHGKSQSW
WIIVEDPDTE HLYHTELFSL QADKCLARNE SDRLQTLEFT IPIFEPLPTQ YFVRAMSNHW
LGSETVIPLS FRDLILPQLH PPHTPLLDLQ PLPTAALHDK KLEALYPYTH FNPVQTQVFH
TLYHTDHNAL VGAPTGSGKT VAGELAIYRV MREYPGKKAV YIAPLKALVR ERIEDWKVRF
GEKLGKKVVE LTGDVTPDAR AIERADVIVT TPEKWDGISR SWQSRNYVRK VVLLVIDEIH
LLGGDRGPVL EVIVSRTNYI SAHTAHKVRV VGLSTALANA HDLANWLGIT RAGLFNFKPS
VRPVPLTKHI QGFPGKHYCP RMASMNKPAY SAIRTHSPTK PALIFVSSRR QTRLTALDLI
SCCVSDDQPK QWLHMSEVEM ESLLTTIRDA NLRHALSFGI GMHHAGLHER DRKVVEELFL
NQKIQVLVAT ATLAWGVNLP AHLVIVKGTE FFDGKTKRYV DFDITDVLQM TGRAGRPQFD
DHGVAVIFVQ DTKKHFYKKF MHEPFPVESS LAEQLPNHIN AEIVAGTITS KQEAMDYLTW
TYFYRRLVMN PSYYGLTDTS QDDINQFLSE LVEHTVAELE ASRCVVIDDD QMSLEPDVFG
RIASYYYLQH ETMRLFDREI VDHMNIQNIL KVLAHAKEFE ELPVRHNEDQ LNAILAKQCP
IEVPASALDD PHVKTHLLLQ AHFARLQLPI ADYRTDTKSV LDQCMRVLQA MVDAAADAGF
LATALNIMHL AQMVAQGRWF SDSSLLALPF IEPAHVDVFA RMNPSVLVLP QLVHFASEDR
RQAKQLLRRV LDEGRAHKVL SALDGLPRIR VSIAMHGVDA SKLATDSEYT LKVELRRDNP
TRKRAAVAPR FPKPIDESWW LVIGNEATGE LVALKRMGPI LNSATTTITF YTPEEPGAHG
YSFYLMSSTY LGLDQQLSFR FTCTEQHDND NDNDDDDDDD DDESMFDAKT RMRGVAVKEV
SPEVKA
//
