ASCC3_DICDI
ID ASCC3_DICDI Reviewed; 2195 AA.
AC Q54G57;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE EC=3.6.4.-;
GN Name=ascc3; ORFNames=DDB_G0290389;
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N3C0}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8N3C0}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; AAFI02000163; EAL62210.1; -; Genomic_DNA.
DR RefSeq; XP_635715.1; XM_630623.1.
DR AlphaFoldDB; Q54G57; -.
DR SMR; Q54G57; -.
DR STRING; 44689.DDB0233132; -.
DR PaxDb; Q54G57; -.
DR PRIDE; Q54G57; -.
DR EnsemblProtists; EAL62210; EAL62210; DDB_G0290389.
DR GeneID; 8627633; -.
DR KEGG; ddi:DDB_G0290389; -.
DR dictyBase; DDB_G0290389; ascc3.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; Q54G57; -.
DR OMA; GTHHAGM; -.
DR PhylomeDB; Q54G57; -.
DR PRO; PR:Q54G57; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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; 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; 2.
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; 3.
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; Cytoplasm; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..2195
FT /note="Activating signal cointegrator 1 complex subunit 3"
FT /id="PRO_0000371330"
FT DOMAIN 492..675
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 705..920
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 980..1286
FT /note="SEC63 1"
FT DOMAIN 1336..1511
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1545..1750
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1810..1969
FT /note="SEC63 2"
FT REGION 367..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2032..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..88
FT /evidence="ECO:0000255"
FT MOTIF 617..620
FT /note="DEAH box"
FT MOTIF 1453..1456
FT /note="DEAH box"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1349..1356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2195 AA; 251613 MW; 5E82A963308C0636 CRC64;
MGIFDNQNKF EPTISNTLRS LTNGNTQTFD EQVVARNKEI MKKRNEKKKE KDRIIEKGQL
TWSYFSDSKQ NKEKEKENRQ IFNKFKEIVL EMIGDDEIPS DEIASAVYET FMIVANPHKD
KASKCESLRQ IFHSFFKVAM YNKLSEQVGL LLQIKNPFES DSKASNESVQ TIDSFESMEW
QLPSKYQLQF EDNDEMSIFD EINHFINTKI NNNLDEQKEK EKEKLINTPL SDMVLIHQPG
QIKKSKKLKK LAAAGGSNNL ESNNVVDSTY TIEWLREECS VISIGLGIPS EEIYNTIMSF
LKNKKETIEE DMIGLLGFDH LELIADIIKY RDSILGSVVS GYRASNHSGP LNHFSIQTKD
EKDFDKQLKK DDKKRYKNDQ QQQQQQQYQE EQIKFIDHSQ QSFEQPTIYN QKEFTGGDVC
IDLPYGGKIA LPKGTVRTEK TTHTEVMVPY SLAKPFADNE KLIEIGESIA EISRAAFGSI
KKLNRIQSRV FESAYKSNEN ILISAPTGAG KTNIALLTIL HEIESNINPY GYLDKDNFKI
IYIAPLKALA SEMVEKFSNS LKYLGIVSKE LTGDMQLTQK ELKETQIIVT TPEKWDVITR
KSSDVALTKL VRLIIIDEIH LLHEERGPVL ECIVARTLRQ VETTQEMIRI VGLSATLPNY
KDVARFIRAP ASGTHFFDSS YRPVPLTQNF IGVKDNQGIM VMKNNMNQLC YERLEKSLKE
GHQVMIFVHS RKDTVKSAEI LSDMAKEKHF RFSNEEPSFG AKKEFEKVKS KEIRSLFQHG
ISVHHAGLLR SDRNVVEKYF ANGTIKVLVC TATLAWGVNL PAHTVIIKGT QVYNAKNGGF
MDLGISDVMQ IFGRAGRPQF DTSGEGFLLT SKDKLDHYLS LMSSSMPIES KFITNLEDHL
NAEIVLGTVS NVNEAVNWLS YTYLFIRMLQ NPLVYGIPSS QRSKDPQLEE FKREIIIRAA
KKLEQCKMTR FDEQSENLGM TELGRIASHY YIKHPSIETF NEMLNDQLGQ DQVLNILSNS
SEFENITLRE EESTELDKLA ENQCYYELTV LDSHSKVKCL LQAFFSRANI DGFSLVSDSN
YTVQNSSRIL RGLFEISLKK GWCTVSKTIL DLCKMVDHQL WHFESPLRQA KVLSLDTIRK
IEERDWTPER ICDMEIGELS FVLGNQLIAK TTRKIAQQFP QLDFEIQVQP ITANIIRINM
TLIPMFSWND KMHGDSQPFW IWVQDNESQY IFHSEYFMLT KKIYNQTEPI TLTCIIPLPN
PMPSQFFLHY ISDRWLGSEG IREISFRHLV LPQQDRVVNT ELLDLQPLPK EALKNKDFES
LFKFSHFNPI QTQVFHTLYY TNNNVLLGSP TGSGKTICAE LAMFKVFRDE PHMKVVYIAP
LKALVRERMN DWKVKFQEKL GKKLVELTGD YTPNMIALQN ADIVTTTPEK WDGISRNWKN
RSYVTSVSLL IIDEIHLIGE LRGPILEVIV SRMKLISKQT GVNIRVVGLS TAMANAIDLS
EWMGIDRVGL FNFRPSCRPV PIEVHIQGFQ GKNYCPRMQT MNKPSFAAIA TYSPKKPVLI
FVSSRRQTRL TALDLISYLV VDNDPLQWIQ KGFDIEPTLA RVKDQHLRHT LSFGIGMHHA
GLNDGDRTIV ESLFGENKIQ ILISTSTLAW GVNLPAHLVI IKGTEYFDGK TKRYVDFPLT
DVLQMIGRAG RPQFDKEGKA MVMVHEPKKQ FYKKFLYDPF PVESHLKDFL HDHLNAEIVS
GTIQSKQGAI NYLVNTFFFR RLVVSPSYYG LEDNSVEAVN QYLSDLLDST LADLEQSSCI
EINEYDEIIP MSMGKIASFY YLNYKTVQNF SDNIKRDSDI KTLLRVLSDA AEYSEFPVRH
NEEILNQELN ENLPIKIGNY EDSHTKVHLL LQAHFQRCPL PITDFTTDTK SALDQGIRIL
QAMIDVSFEY GYFATAIQVI RLLQMLVQGR WDYDSSLMTL PHINKDFADF LSSNLILSNG
EQISNLSDML KIPRDKIHLS LTNIGLSDSQ IKETLNVIDH LPKVKIEYFI NTNNNSNNND
DNNNENNNNN NKKNNNNNNN NNKSIVYSGQ EFNIKIKVTR ENKKFSNGHA FAPLYSKDKD
EGWIMVLTDE KEQMIGFKRV PQMISNSVTA NFKIPKAPFQ SSTNYNVKLY SDTYMGLDYF
HTFQVPIVNK KQIRNDDQDG DTIILLEAAT GDMKK
