ID   A0A158PT13_9BILA        Unreviewed;      1376 AA.
AC   A0A158PT13;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Activating signal cointegrator 1 complex subunit 3 {ECO:0000313|WBParaSite:BTMF_0000825401-mRNA-1};
GN   ORFNames=BTMF_LOCUS6321 {ECO:0000313|EMBL:VDO21444.1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000825401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0000825401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO21444.1, ECO:0000313|Proteomes:UP000280834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UZAG01015558; VDO21444.1; -; Genomic_DNA.
DR   STRING; 42155.A0A158PT13; -.
DR   WBParaSite; BTMF_0000825401-mRNA-1; BTMF_0000825401-mRNA-1; BTMF_0000825401.
DR   Proteomes; UP000050602; Unplaced.
DR   Proteomes; UP000280834; 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:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd18020; DEXHc_ASCC3_1; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
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; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; 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; PF02889; Sec63; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000280834}.
FT   DOMAIN          329..511
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1164..1340
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          181..228
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1376 AA;  157224 MW;  FAB4BA8D9302275B CRC64;
     MNMKEFVEKY STGTINPPAD EYGPRTTRHV YWRKRFVEQA LHSSTAQSDD TVITIPSTTI
     NNAPSSSKEI MTSGDIISAI NGIYDDPESV SRHLFDLLRS PNEDDDIQGE LIDLLGFEQF
     DLVSKILSSR EELLNSYNSV RQDIAQTTKL ERILQQSQKQ REQPLYCQQV IVQSNADVNM
     RKMAKREQKR AAKQLNKITQ NLSESEKLEL KQVQNEMLKE RFQELEAERW LETLHENRRT
     IPRERFPYVY DALTESEHIF ITVDGSKRCL PANSSRVIRD TYEEVYVPAM DRSQVTAVQQ
     INIEDFDELG KKCFIGFEKL NVIQSLVFTQ AYKSQENLLI CAPTGAGKTN IALLAILNTI
     HAYMDNGVIH KNDFKIVYIA PMKALATEMT MNFAKRLAPL NLHVRELTGD TTLSRKQIAE
     TQMLVLTPEK WDVVTRKAID LPLSKMVRLL IIDEIHLLHD DRGPVIETIV ARTLRQVEMS
     QQCVRIIGLS ATLPNYIDVA RFLRVNPHKG MFFFDGRFRP VPLSQTFIGV RNPRNMGPDI
     MREMDEVCYD KVHQFVSKGH QVLVFVTARN ATTKLATTFR DEAAKRGELS HFLPTNNGSV
     QYINAMKSIQ NYRNGMLAEF FRLGFGIHHA GLPRRERLMT EKFFANGHIT GTEIFNVQKG
     GFSDIGVLDV QQIFGRAGRP QYESSGHGVI ITWKKSMLQY LNMLLRQAPI ESQFMSRIYD
     NLNAEISLGT VSSIPEAVEW LKYTYFFIRA KLNPLAYGIP RSQLEHDPDL YEYLTQMMTE
     AAEKLDKNQM IRNGYVASTD LGRIASNYYM KYETIEVFMN GVGEIKLQAF MSDDMILSLI
     ASATEFDQIK VVREEEMMEL EELVQTSCPL RLKRGALATV PGKINCLIQA HISRAFIGSY
     SLVSESMFIQ QNCDRLCRAM FEITLRKGWA QAANATLAMA KCFDKQVWSF QTPLRQLSDF
     IRADWIPKIE RRKLSHYQLY EMSAKELGTM LSCDGQKMYE AVRMLPVMNL EASVKPVTNT
     IIQVTVILTP DFIWNEHFLG STGVQVFWIF VEDINENIII HHDQIVVNKN KVRNSEPQNL
     IFTVPIRDQQ LTHNYQVRVA SDRYVVDDSV VPISMHNCVL PSSHCPHTDL LDLDPLPLTA
     LKNETFQSIY SFEFFNPVQT QVFYCLYNTD QNALIGAPTG SGKTLCAELA MYRIFREYPA
     KKCVYIAPLK ALVRERVSDW DDKFRKLNIR TVELTGDHSP DIRSLSSAKI VITTPEKWDG
     ITRSWEIRQY VKDVALVIVD EIHLLGVERG AVLEAIITRL KLMARKEGSR NPVRVVGLST
     ALANAGDVAE WLGVDDAGLF NFRPNVRPVP IEVHIAGFPG QHYCPRMALM NRPAFK
//