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Database: UniProt
Entry: G9P1P4_HYPAI
LinkDB: G9P1P4_HYPAI
Original site: G9P1P4_HYPAI 
ID   G9P1P4_HYPAI            Unreviewed;      1982 AA.
AC   G9P1P4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Activating signal cointegrator 1 complex subunit 3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIATDRAFT_34398 {ECO:0000313|EMBL:EHK43376.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK43376.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK43376.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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:EHK43376.1}.
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DR   EMBL; ABDG02000026; EHK43376.1; -; Genomic_DNA.
DR   RefSeq; XP_013940651.1; XM_014085176.1.
DR   STRING; 452589.G9P1P4; -.
DR   GeneID; 25783930; -.
DR   eggNOG; KOG0952; Eukaryota.
DR   HOGENOM; CLU_000335_2_0_1; -.
DR   OMA; MCSATEF; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000005426; 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:0010467; P:gene expression; IEA:UniProt.
DR   GO; GO:0090304; P:nucleic acid metabolic process; 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; 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; 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; 1.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426}.
FT   DOMAIN          284..477
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          508..711
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1143..1318
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1348..1558
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1958..1982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1982 AA;  222712 MW;  05713D65A065D439 CRC64;
     MASTDLINAE SEWRQQFEAM QAALAKLKLP QHDAKADADL DDDDFGGYSS TTSGHDVWDF
     IEDDDEYGYY SSDFADEGPG AATGGFGVEW LAIKCASIAD KNGMAPDVFQ TQLLNVLSSG
     QPEDELQQHL TDLVGFDDLD FIIELLSHKD EVVASAADFH DAPETKGRRL LTKAERDEAL
     RTRDYQHKNA ALAPSFAKEP QYPHVYRAYN AGNTLSSSGK KYGLPVGSER LQFEKYEEYS
     VPAGKKGVPG PGEKLVKISD LDGLCRNTFK GYKSLNRMQS LVYPVGYKTS ENMLICAPTG
     AGKTDAAMLT ILHTIGQHVE PNPIENPEAT EFAVNTDDFK IVYVAPMKAL AAEVTEKLGK
     RLAWLGIKCR EYTGDMQLTK AEIVQTQIIV TTPEKWDVVT RKGTGDTELV QKVRLLIIDE
     VHMLHDERGA VLESLVARTE RQVESTQSLI RIVGLSATLP NYVDVADFLK VNKYAGLFYF
     DASFRPVPLE QHFIGVKGKA GSKQSKENLD NVAFDKVKEM LQRDHQVMVF VHSRRDTMVT
     ARMLHQKAIE QFCVDLFDPT GHPHFGQASR DMNQSKSKDI RDLLSKGIGV HHAGMARADR
     NLMERLFADG VLKVLCCTAT LAWGVNLPAA AVVIKGTQVY SAQEGKFIDL SILDVLQIFG
     RAGRPQFEDT GIGMICTTHD KLPHYLSAIT EQQPIESKFS TKLVDNLNAE IALGTVTSIP
     EAVQWIGYSY LFVRMQRSPM TYGIEWAEIR DDPNLVQRRR QLAIQAARTL QQSQMIIFNE
     NTEELRSKDI GRIASQYYIL HTSIQVFNTM MHPQATEADV LKMISMSGEF DNIQSRDNEA
     KELTQFKDIV PCDVDKGIDT PQAKTNILLQ SYISKIQPDD FALSNDMNYV AQQSGRICRA
     LFMLALNRRW GHQCLVLLTL SKSIEKRIWP FQHPLHQFEL TKPVLNQLDS KENLTIDTMK
     EMEPAELGSL VHNQGAGKNI AKILNNFPLV HVEAEIAPLN RDVLRIKLYV IPDFLWKDHV
     HGTSESFYIW VENSETSEIY HHEYFILNRR KLHDEHELNF TIPLSDPLPT QIYVRAISDR
     WLGSETVTPV SFQHLIRPDT ESVYTDLLNL QPLPITALKN PGLEELYAKR FSFFNPMQTQ
     IFHTLYHTSA NVLLGSPTGS GKTVAAELAM WWAFRERPKS KVVYIAPMKA LVRERVVDWG
     NRLAKPLGLK LVELTGDNTP DTRTIKDADI IITTPEKWDG ISRSWQTRGY VRQVSLVIID
     EIHLLAGDRG PILEIIVSRM NYISSSLKNK VRLLGMSTAC ANATDLANWL GVKEGLFNFR
     HSVRPVPLEL YIDGFPEIRG FCPLMQSMNR PTFLAIKNHS PEKPVIVFVA SRRQTRLTAK
     DLINYCGMED NPRRFLRMDE EDLQLNLSRV KDDALKEAIN FGIGLHHAGL VESDRQIAEE
     LFLNNKIQIL VATSTLAWGV NLPAHLVVVK GTQFYDAKTS GYKDMDLTDV LQMLGRAGRP
     QFDNSGVARI FTQDAKKDFY KHFLHTGFPV ESSLHKVLDN HICAEISAET IMNKQDALDY
     LTWTFFFRRL HKNPSYYGLE ISAEEHSTIA AQMQANEYMI EMVEKSLGEL EDSKCVESFP
     NGDVDPTPLG KIMSYYYLSH KTIRHLVHNI KPNASFLNVL SWMCHATEYD ELPVRHNEDL
     VNDVLSQNLP FPGNSFNLPM WDPHVKSFLL LQAFMSRIEL PVTDYVGDQT SVLDQAIRII
     QASIDVITEM GYLSSCLQMM KLMQSIKCAR WPTDSPASIL PGVEPESTKD ETSLAKISTY
     SQDQVNAFAK KLRIPSNLQP RFKRAVSMLP NISVSVDDIT TISLTVNIKR LNPLVDREAR
     IWAPKFHKPQ TEGWFVIIAD SAKDEVIAVK RVGWAGLSTS GNGTGGKKAL GQGSRPTART
     VLKLPEPKAR EARKLDVFVV SDGYVGMEHR VMGVDIPAPP VADDDLDKKN QGKTVVAGGS
     SA
//
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