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HELCL_DICDI
ID   HELCL_DICDI             Reviewed;        2237 AA.
AC   Q55CI8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Activating signal cointegrator 1 complex subunit 3-like;
DE            EC=3.6.4.-;
GN   Name=ascc3l; ORFNames=DDB_G0270042;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72371.1; -; Genomic_DNA.
DR   RefSeq; XP_646493.1; XM_641401.1.
DR   AlphaFoldDB; Q55CI8; -.
DR   SMR; Q55CI8; -.
DR   STRING; 44689.DDB0233131; -.
DR   PaxDb; Q55CI8; -.
DR   PRIDE; Q55CI8; -.
DR   EnsemblProtists; EAL72371; EAL72371; DDB_G0270042.
DR   GeneID; 8617455; -.
DR   KEGG; ddi:DDB_G0270042; -.
DR   dictyBase; DDB_G0270042; ascc3l.
DR   eggNOG; KOG0951; Eukaryota.
DR   HOGENOM; CLU_000335_1_0_1; -.
DR   InParanoid; Q55CI8; -.
DR   OMA; ESFWIIV; -.
DR   PhylomeDB; Q55CI8; -.
DR   Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DDI-72165; mRNA Splicing - Minor Pathway.
DR   PRO; PR:Q55CI8; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:dictyBase.
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; IBA:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; ISS:dictyBase.
DR   GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 2.
DR   Gene3D; 2.60.40.150; -; 2.
DR   Gene3D; 3.40.50.300; -; 4.
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   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF46785; SSF46785; 2.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..2237
FT                   /note="Activating signal cointegrator 1 complex subunit 3-
FT                   like"
FT                   /id="PRO_0000371331"
FT   DOMAIN          561..745
FT                   /note="Helicase ATP-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          755..990
FT                   /note="Helicase C-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1050..1356
FT                   /note="SEC63 1"
FT   DOMAIN          1407..1584
FT                   /note="Helicase ATP-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1657..1832
FT                   /note="Helicase C-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1892..2215
FT                   /note="SEC63 2"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          440..468
FT                   /evidence="ECO:0000255"
FT   MOTIF           687..690
FT                   /note="DEAH box"
FT   MOTIF           1526..1529
FT                   /note="DEAH box"
FT   COMPBIAS        25..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..278
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         574..581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1420..1427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   2237 AA;  256437 MW;  BCA42D336175EA06 CRC64;
     MSEELARSKQ YGYKENSNLV FYSERNRSEL KEPKGEPETL WGRLRGEMGD RVNYSKPLEL
     LEKMQNLKRK TIEKEGGDVN SSNDTYSTTK KVKNQNPLEK KSTNRKSNGN NNNEKPIDIL
     SATESFQGLY KPKTKETRIT YETLLTFIQR YVGDQPTEVV KGALDEILSI LKDDTIRAPE
     KKIEISKLLK GLNDVSFAEL TQLGKQITDF KDSELAKQQQ QQQQQQSMDS LDDEQGVAVI
     IDEEEEEENL SDFEIRDDDD DDDDVDNNEV DDNNNNDSEA QDSEIQTKDE NNNDDDENQK
     IKENNNNNNK SQKPDTKNTK DDKNNNSKLI SPNEIDSFWI QRKISEFERD HDLSKQLAEK
     TLNILRQPNV RRCEQQLVDL FTIDKLDFLK LIINNKQTIL YCTLLAKAEN DQERKKIEDE
     MSSNPVTLSI LNRLKGNEVT AATTEKTIEK TESNKKDVEM KQQQQQQQDE IKKPKKLLNL
     EELSFQQGSH LMTNKEFKFP KGSKREQYKG FEEIHVPARA NPPFNPNERL ISIEELPEWS
     RLPFEESGVK SLNRVQSKLF DCAFKTDNNL LLSAPTSSGK TNVAMLTILH EIGKNRDRDS
     GKIRLDAFKI VYIAPMKSLV QEMVGNFSKR LKSYGIVVNE LTGDQSLTNK QISETQIIVT
     TPEKWDIITR KSGDRAYTQL VKLIIIDEIH LLHDERGPVL ECIVARTLRM IESTQQMVRL
     VGLSATLPNY EDVATFLRVE PDGVFYFDSS YRPIPLEQQY IGISDRGIKQ LQRCNDITFT
     KVSERVGDHQ ILIFVHSRRE TAKTGKDLRD RAVEDQSIDR YIRDPASREI LRATASKQIQ
     NAELKDLLPY GIGIHHAGLS RSDRSLVEDL FGDNRIQVLI STATLAWGVN LPAHTVIIKG
     TQIYNPEKGW CELSPLDVTQ MLGRAGRPPF DKEGEGIIIT SQHELQFYLS LLNTQLSIES
     QFISRIADNL NAEIVLGSIQ TVRDAVNWLG YTYLYICMIR NPPLYEISYD DFEKDPLLEQ
     RRLDLVHSAA TILEKNSLIK YDRKSGKLQS TELGKVASHY YITNSSMSIY QEHLKPSMSD
     IELLRVFSLS SEFKNVVVRE GEKFELEKLL ERVPIPIKEN IEEPSSKINV LLQTYISNLK
     LDGFALVVDM FYIAQSASRI TRALFEIVLK KGWAQLAKKI LNLAKMIDSK MWSSQSPLRQ
     FHKISPKVLN QLERRGIPIE DLYEYNSQQL GNAIQNPSEG KQLFDLIHNF PKLDLTAHVQ
     PILHGLLRVE LSITPDFQYD ERYHNNSIGW WIIVEDVDGE RILYFEYFSL KKKMVNGEDQ
     LVSFTVPLSQ PLPPQYYVRV ISDHWIGAEY SLPISFQHLI LPEKYPPCRP LLDLQPLPIQ
     VLKDPKAESI FKPTFSIFNA IQTQVFNCMY QSNDNAFISA PTNSGKTVCA EIALIRCFKQ
     NPKAKVVYLA PMQDLASVRL KDWSNKFGVK SPFGLVVSDL TGDAVTDNKI LDRSNIIVTN
     CEKWDILSRK WKQRKALQSI NLLIVDELHL IGGEYGPTME IVVSRMRYIS TQTGNALRVI
     ALSSSIANAR DLVLWIGATP QTCYNFHPNV RPIPVEYQIQ GFEFPHFNAR MLAMTKPTVY
     EVAKNKNQQS IVFVPTRKLS RSLAADIIAN VSSFEDTLTK PYLVCEEHVL TPYLEDVDSF
     ALKQSLQMGV AFYHDGLTER ERRVVEILFR SGSIRVLIAT HSVAWLLDNV FAQLVVIMGT
     QLYQGKDIRY IDYPINDILQ MIGRAGKQEG GGVISNKVAK VLLLCHAPKK EYYKMFLNEP
     LPVESHLDHC LHDQFNSEIV TKTITKKQDA LDYLTWTFLY RRLNQNPNYY NLSGVSHLHL
     SEHLSELVEN TLVELEQSNC ITIQDDQDKV SPLNLGIIAS YYYLKYQTIE LFGSSLKSTT
     RRRGIMDIIS NAPEFNSLPI RHREDQILMK LASHLPQKID KPNYQEISTK VNVLLQCHFS
     RESISADLYQ DQKFILENAT RLLQAIVDVI SSNSWLQPAI AAMELSQMIT QAMWDSDSVF
     KQLPHMNKRR IDAITSQGIE SVFDLMSLDD NSRIQLLDLS QQESNDLVQS FMKYPDIDIS
     YQVQDEDDLH ADSIMTVEMV IERDLGDDEE NPIEINDSIN VVSAPYYPKE KICGWWALIG
     DSKNNHLLAI KRITFLKKTK VKFEFPTPAV GKHQLSLYLF SDSYNGCDQE HELNINILPA
     EIEDEDEDEE EDNEMDE
 
 
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