ID B6Q3Q4_TALMQ Unreviewed; 1573 AA.
AC B6Q3Q4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PMAA_029620 {ECO:0000313|EMBL:EEA28143.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28143.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; DS995899; EEA28143.1; -; Genomic_DNA.
DR RefSeq; XP_002144658.1; XM_002144622.1.
DR STRING; 441960.B6Q3Q4; -.
DR VEuPathDB; FungiDB:PMAA_029620; -.
DR HOGENOM; CLU_001103_16_3_1; -.
DR OrthoDB; 5474026at2759; -.
DR PhylomeDB; B6Q3Q4; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
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:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEA28143.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 714..895
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 923..1069
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1323..1406
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 112..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1573 AA; 174598 MW; 588CD9FBEC511FAB CRC64;
MTKNNLKQHL RWLVDRGQPD FAALDVLLTR SGVDASNVQV SAQPHSDIPQ PTRTEESTIT
TNANLLAILK GNEDVELKVD SDGDCLLQDA NMARLNLIPS SVSKPRMLSI AAGNRSDDAR
PLTPGSDARK DNAPDNSRIG DTTYRSAPAT IISSPSRSNR NAPSTKLGPI LSSDYKSQFD
DIESIDLTGD VEPTTSSGTV EAFGDSQTLW REDYAMRPEP VARKGKKRKS DEYQSDLRSP
RRNSPRVKAS HILDDDDALV VDITPTISSD PPCYDHISSQ ELAQQSPVRS AVSKKPTTTT
KPGDKSRNKR ISQDEDVDRL FSWDSDEDAF EPLPNKETRP IEERLNPRDS DRVTEHSNVG
ATSEDELIPA QVKPVSPKKA SPKKTSPKKR QTIVETVTST PLSQTLQNPK VDQFLSLDPT
VVDAAIEKLN KDLVANANIV VQHAIEGELP PPELVAEGKA ARTKVEALGK VKTERVRYDE
KKLRKQQLKD MMVKAVADGE DLNGLAAEIK ESQDIAKELQ AIDAQLGDLL SVIDMDLSTF
LPPPQFANLR TTVLPATPQT LVRPLAQPAP QRFQTDTPSI LPSNGSNTSL NTTYRRDLST
FQEGNSYSTG IPSNSAGAFI TSDDFDFDEE DFLEADNAMS TAHYEPPATF SDSRRVFGET
SGNASRQPQL QPTQKPTVPD SNSMLSFAWS KDVKTVLRDR FHLKGFRPHQ LEAINATLGG
KDAFVLMPTG GGKSLCYQLP SVIHSGRTKG VTIVVSPLLS LMEDQVDHLQ KLGIKAYFIN
GDVSSEHKRW VMSALASPYA DREIELLYVT PEMINKNVTL CDILKTLHDN RKFARLVIDE
AHCVSQWGHD FRPDYKELGA FRSKFSGLPV MALTATATEN VKIDVINNLR MKDCEVLSQS
FNRPNLTYDV LPKKGSAPDI ISQIADIIET SYRRKAGIVY CLSRKDCEKV AQELSQGYNI
KATHYHAGMP SEERTSVQRD WQAGRYDVIV ATIAFGMGID KPDVRFVIHH TIPKSLEGYY
QETGRAGRDG KRSGCYLFYS YRDTAAQKRF IEQSEGDWQQ KNRQRQMLRH VVQFCENQSD
CRRVQILAYF NESFSVSDCH RTCDNCKTDE AFQTIDFSTY AKKAIQLVKF FHERGEDVTI
LHCIDIFAGS NKKMKGDHAQ VPQYGAGTEL ELGDVERLFF KLVGEDVLEE WSKTTSRFTH
RYVKPGPKAA QFLASRSPFT MQIRASSKSA KRASDASRRT TSTGVSGVSD YHPQSTNVPS
PVQGSRRKAA PKAKSKRGVP QAVDGDEDSD GFEPVREAGK SSRRKKADVG PPIVEDGRLA
ELDNNQQIVV EDFVANAKEL CQQIMMEKHL RNQPFSDAIL REMAIHLPED TNAMNAIPGI
NKDKVRIYGS RFLKLIRNAK KLLSDIRSNN EVIHDPNHTN VINLDSDDEY GNDDDFMLSL
SQMDTNDPSN TSQYFDTSAS QTRVPSTQFT ALDAPSTSSR KTTSKASSAS RSRPRGSTQR
TSSGSSSKRR KTPWNPESYR YAGKGSNRGY NNPGRGSSSS GYSNYRRSTS TSTNTKRKTS
TKPSGPAIDL MPT
//
