ID C1GSU4_PARBA Unreviewed; 2012 AA.
AC C1GSU4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Activating signal cointegrator 1 complex subunit 3 {ECO:0000313|EMBL:EEH39127.1};
GN ORFNames=PAAG_01589 {ECO:0000313|EMBL:EEH39127.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH39127.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH39127.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN293994; EEH39127.1; -; Genomic_DNA.
DR RefSeq; XP_002796581.1; XM_002796535.1.
DR AlphaFoldDB; C1GSU4; -.
DR STRING; 502779.C1GSU4; -.
DR GeneID; 9099877; -.
DR KEGG; pbl:PAAG_01589; -.
DR VEuPathDB; FungiDB:PAAG_01589; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_2_0_1; -.
DR OMA; MCSATEF; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000002059; Partially assembled 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; 2.
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:UP000002059}.
FT DOMAIN 289..482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 521..732
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1150..1325
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1355..1565
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1959..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2012 AA; 226752 MW; 53A5C633F2A0E2BC CRC64;
MSPEIQLAES QWLSQLAVMR QAMADLKLPK SEDSILYEND LFFDEDDIAS APESVEDLWD
IISEDEDAVD DSDEMVDDRA NGQEISEPKG FYNHQWLFHK CQSIAEQNSS LNASELQQQL
LSVLGASAPP DELQISLTEI VGFDDLDFVI DLIAHRDELT SMKDSEGNDI FSRLQTKGQR
EEALRQQDYE HKHAKLAQKQ NREGPIYPHV YKAYQAGNTL SVNGRKYGLP VGSTHAEEPR
YTEYTIPATK VGTLGADQKL VSISSMDGLC KGTFRGYKSL NRMQSLLYPV AYGTNENMLI
CAPTGAGKTD AAVLTILNVI AKNIIPNSLE SHDATEFAVM TDEFKIVYVA PMKALAAEVT
EKLGKRLAWL GIQVRELTGD IQLTKKEIVQ TQIIVTTPEK WDVVTRKGTG DTELVQKVRL
LIIDEVHMLH DERGAVIESL VARTQRQVES TQSLIRIVGL SATLPNYIDV ADFLKVNRMA
GLFYFDASFR PVPLEQHFIG VKGDVGTKKS RENLDIVCFE KVREMLERGH QVMVFVHSRK
ETLNAARLLH RMAVDNQCAD LFSPVEHRNY SQALRDIKTS RGREIRELVP YGLGTHHAGM
ARSDRNLMER LFSEGVLKVL CCTATLAWGV NLPAAAVIIK GTQLYSAQEG KFIDLGILDV
LQIFGRAGRP QFQDTGIGFL CTSHNKLQHY LSAVTSQEPI ESRFSRKLVD NLNAEIALGT
VTSVPEAVQW LGYSYLFVRM RRNPHSYGID WTEIRDDPQL VLRRRDLIIK AARTLQQSQM
IIFNERTEEL RAKDVGRIAS QYYVLQTSVE IFNAMMKPMA NDADVMKMIS MSGEFDNIQS
RENEFKELDR LRLEAIKTEV EGSNDNAHAK TNILLQSYIS RARIEDFALV SDSAYVAQNA
ARICRALFMV ALNRRWGYQC QVLLSTCKSI EKQIWPFQHP FHQFDLPQPV LKNLDEKFPV
SSIESLRDME PAEIGQLVHN NRMGNTISKL LDNFPTLAVE AEIAPLNRDV LRIRLYLYPE
FRWNDRHHGT SESYWIWVEN SETSEIYHHE YFILSRKKLN DDHELNFTIP LSDPLPSQIY
VRAISDRWLG AETVTPVSFQ HLIRPDTESV YTDLLNLQPL PISALKNPIL EEIYGQRFQF
FNPMQTQIFH TLYHTPTNVL LGSPTGSGKT VAAELAMWWA FRERPGSKVV YIAPMKALVR
ERVHDWKRRL TVPMGLKLVE LTGDNTPDTR TIRDADIIIT TPEKWDGISR SWQTRGYVRQ
VSLVIIDEIH LLGSDRGPIL EIIVSRMNYI ASQSKGAVRL LGMSTACANA TDLGNWLGVK
EGLFNFRHSV RPVPLEIYID GFPEQRGFCP LMQSMNRPTF LAIKNHSPEK PVIVFVASRR
QTRLTAKDLI NFCGMEDNPR RFLHMSEEDL QLNLSRVKDE ALKEALGFGI ALHHAGLVES
DRQLSEELFA NNKIQILVAT STLAWGVNLP AHLVVVKGTQ FFDAKIEGYK DMDLTDVLQM
LGRAGRPQFD TSGIARIFTQ GSKKAFYKHF LHTGFPVEST LHKVLHDHLG AEVSAGTITT
KQDALDYLTW TFFFRRLHKN PSYYGLEISA EEHNTMAAQQ IVSDFIVELV DQCLSELAES
SCVLFDSATG FVDPTPFGKI MSYYYLSHKT VRFVMSHAKP NPTFSDVLSW MCFATEFDEL
PVRHNEDLIN AELAQNLPLP ITAMGTSLPL WDPHIKAFLL LQAFMSRIDL PITDYVGDQI
SVLDQGIRII QACIDILAEL GYPNACTTMM TLLQCIKSAR WPDDHPISIL PGIAPAANES
PNPTQLPASL PSLLALPQST LTSLLHTLNL STQLSSQFYQ ALFLLPVVSI SIFDPSPAGL
TVSLTRKHPL PSHPRRRTTT QGDDQSFRVY APHFPKPQTE GWFVVVTSNP RATGVDSGGV
RENILALKRV SWSSSTSTSR PGDRGNVVAR AKIRFPEGWN NDDSHELEVG GADEKGKGKT
KHKDHEDAGE ILNVTVRVIS DAYIGMEWSV VC
//