GenomeNet

Database: UniProt
Entry: A0A093XCY4_TALMA
LinkDB: A0A093XCY4_TALMA
Original site: A0A093XCY4_TALMA 
ID   A0A093XCY4_TALMA        Unreviewed;       875 AA.
AC   A0A093XCY4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Helicase POLQ-like {ECO:0000313|EMBL:KFX43063.1};
GN   ORFNames=GQ26_0380350 {ECO:0000313|EMBL:KFX43063.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX43063.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX43063.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX43063.1,
RC   ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT   of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX43063.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPOX01000038; KFX43063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093XCY4; -.
DR   HOGENOM; CLU_006553_2_0_1; -.
DR   Proteomes; UP000029285; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18026; DEXHc_POLQ-like; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.20; -; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR046931; HTH_61.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR048960; POLQ-like_helical.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF6; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF20470; HTH_61; 1.
DR   Pfam; PF21099; POLQ_helical; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KFX43063.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          164..353
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          365..536
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   875 AA;  96022 MW;  CFEC40CDC6587385 CRC64;
     MSGPPLQSHG FQTSVDTAHQ QTTAIAGLKR PHQNVVSKEP VTAVTTSMTA AATNATTVRQ
     SNNSKRRPVD LIRASAATHE TRIAASPIRS VLSGSTANNS GSAIPPLAPP PPAPSQSMLS
     SSTSNPLLSL QHPKYGLPPA LVANFQAVGI HSIYPWQASC LLGRGHLTAE KNLLYTAPTG
     GGKSLVADVL MLRRVIDNPH RKAILVLPYV ALVQEKLKWL RRIVQGVEKN IDTSASMKQP
     WKQPSKEIRV TGFFGGSKSR ATWADTDIAI CTIEKANALV NTAIEECNID DLAVVVVDEI
     HMLDDDSRGY LLELMVTKLL LLQQDIQIIG MSATLSSGPV QDAVPPCRKI DPSPFKPLSL
     PTANAMVSLA IETATAGFGA EAMPSPSTLD AELLERRLDL VAELGSLPCG LDPVFQNTII
     KGVAFHHAGL TTEERELVAE AYDRGTIKVI VATCSLAAGV NLPARRVIMQ GARMGRDIVG
     PALLRQMRGR AGRKGKDTVG ETYLICQQAD LEVISEIWDA ETPAIDSCLA QDNKGVKRAL
     LEGIATRLVS GREAIDEFMR CTLLCKTREE AEIEKLIETS LQELVNTDLI RLRDDDSYES
     TKLGAAIVAS SFSPDDGIFV YEELKRALQA FVMDGEMHIF YMFTPLSVAM NTNIDWLIFR
     DQLDQLDESG IRALLFVGVQ PGFVNNMVQT GRNFKEDDPK QLQLSRIYRR AYAAFQLRDL
     SNEVPLSTIA SRYNVPRGVV QTLAQTCHGF AAGMVKFCQR MGWGMLAVVL EHMRDRLQAG
     ARDDLLEMAQ VTHVKSWTAR LLWENGFRSV RALASTDAKD IIPVLIMARS RKSQSHPNSE
     REAERYTEKM TRKAEMIIAS ANKIYERQMQ VEIEE
//
DBGET integrated database retrieval system