ID A0A0V0SB11_9BILA Unreviewed; 1991 AA.
AC A0A0V0SB11;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=abs {ECO:0000313|EMBL:KRX23901.1};
GN ORFNames=T07_721 {ECO:0000313|EMBL:KRX23901.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX23901.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX23901.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX23901.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX41 subfamily.
CC {ECO:0000256|ARBA:ARBA00023594}.
CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00011010}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX23901.1}.
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DR EMBL; JYDL01000021; KRX23901.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17951; DEADc_DDX41; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044113; DEADc_DDX41.
DR InterPro; IPR022157; Dynactin.
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 InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF103; ATP-DEPENDENT RNA HELICASE DDX41-RELATED; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF12455; Dynactin; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRX23901.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 35..77
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 1536..1564
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 1567..1751
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1776..1936
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1951..1966
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 93..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..588
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 987..1014
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1047..1099
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1443..1470
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 1536..1564
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 152..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1991 AA; 226789 MW; 268F846F27EC1603 CRC64;
MSSSQLLDNS NSNLRVGDRV CLSDKRLFGI VAYVGTTQFS PGKWIGVILD EPKGKNNGLV
QGKEYFRCEA NHGIFVRPAQ VKLIENESVG VENSKTLNPS TTSGLPRPKG DPKFVKKEIA
RPVSSSGSKQ TSAREPQLKP RPFVKQSASL EKVAPTEGSG SDTQRMCQSD VVALDDRKQE
VEDVEVSRTT EEEKDLSCSG NAVSAELVDS KRTEVANLND GHHHHTMNEE GKQRLSVSKQ
VALLEREINA AEKQSVSLSM AEGVELEYLK SEVKDLSEKL ETLRAKRHED KQKLIDYERC
KIQLQQLTEY KNRMVEVHSE LQRQLQQAKK EAREAIESRE AYSEEMAGVS EAIEMATLDK
EMAEERAEML CQELDVVKDR VRELEVELEI LKNELNANGA PNSETPTPYQ IKQLEQQNDR
MKEALVKVRD LSVQERATNE RLNKELGVLK ADMAELQKKY DRLKIAEEDF ENQITELKDQ
VDAAVGAEEM VEHLTAKNLS LEEELRTLME TIEDFEQMRV VDEELQESSR ETEKELRLEL
DRMHGQITEL KQQLQLANSR MADRESTIAK FRQQTASLLE QIQNYKDQLS ILTEPKKNIS
NENDDSTNDR SLSATSRQMS EIVDSQLCKI ELDDSRRENQ FLRIFFSDDF TNTGGDSDCI
SVNLVFTRLI EKAKLLIKHV NGIFPRVPQG VQREHLFLSH KGEQWSYSLK FIYHLHCLIA
VLRKCENALS RCSVERLNKV AQLRSEITAQ ERLLSYYFNL LKENNLDENS SLRNMEKLLA
FFKQFCETNY TAEQFDSNAV LIDMLLSLLS VVSWLQFELQ RAKLYLTDTS GSEKLLELFN
KMSNSVHDME QFLVLAKTKV PKGDDLVVDH TSSDVGLLDS MSENVYAVEN VAKILNQCCA
KAASQASMLP DVHGIDASMM EEFLNDSYLE IMRPEKNEST ESFFEFHLKN VVQYCEQLCN
TFDVNLKKKS AEEKQQFPPI LERAHIRKEN IAECERLRKE IEKKDRDIME IKRALKLKAE
EISEMHVRKE IAEKRLADSG KEGDERVVRL QNKLAEVQHD YKNKERHYEQ TMDSLQQELD
SLEKENASLK ERIVVLSKKQ LLIGVTKPLA AVSNSPLSTS ASVQDQHEGG FMIDQMKHFQ
YVMQHWKSAQ ASEVGKRMQN AMESMKPLNI PKKHSGRSSI FCGIESDQLS HKRHDEINQL
LREVDRFHKE LRKFLSENMI VSIRNTATSP DIVWSKYYRQ LNRWNSLINW KNHLKSKIQQ
CIVAQGYPAE AAGDLSSFAF FEASCEESVN SISFFANCNF LQNERKKPFC SVTVPCSDSN
GKVLPIAATN VEIRNFFSHL AANAFTDWYI MDETGKELKS YRRKTESESD SLLATDDEDY
VPYVPLKKRR EQQLVKIGLL NRNSGTEGVG STAKMVESES SAVDSAKKYG RTIEFERSAV
TLLEQHTELK KQTESHKEDA IEKKLKEEEQ LLESFAGRTA LMAAAEIAKD VKYVEAIRTG
WQPPRYVENL TYEQIVRFRK LHGILAEGEN IPAPLRSFRE MKFPKSILSA LTKKNITVPT
PIQMQGLPIA LKGRDMIGIA YTGSGKTLVF VLPLIMFCME QQIRLPFIDN EGPYGLIVVP
SRELAKQIYD IVCYYCEALY ADNLPKLRVC LCIGGVSLSE QLSTARRGVH IVVATPGRFI
EILSKKVLTL DSCRYLCMDE ADRMIDLGFE EDVRTIFSFF KGQRQTLLFS ATMPRKIQNF
AKSALVQPIV VNVGRAGAAN LNVLQDVVDF VLLNDRVDQI VEYVRNEDKL MQILSALEKT
PPPVLIFAEK KDDVDRILEY LLLKGLQAVA IHGGKDQQER LTALTSFQFG AKDILVATDV
ASKGLDFPQI QHVINYDLPD DIENYVHRIG RTGRHHQKGR ATTFVNRSCD ISVLLDLKHL
LLEAKQEVPL FLSSFEAESE KLLEIGDERG CTFCGGLGHR ISDCPKLESL QNKRAQSLNK
RDFLAYNTAD W
//
