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Database: UniProt
Entry: A0A0F9XJW6_TRIHA
LinkDB: A0A0F9XJW6_TRIHA
Original site: A0A0F9XJW6_TRIHA 
ID   A0A0F9XJW6_TRIHA        Unreviewed;      1644 AA.
AC   A0A0F9XJW6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Bloom syndrome protein {ECO:0000313|EMBL:KKP00743.1};
GN   ORFNames=THAR02_07169 {ECO:0000313|EMBL:KKP00743.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP00743.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(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   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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:KKP00743.1}.
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DR   EMBL; JOKZ01000233; KKP00743.1; -; Genomic_DNA.
DR   OMA; MAINWTT; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000034112; 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; 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; 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; 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; 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.
PE   3: Inferred from homology;
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:UP000034112}.
FT   DOMAIN          775..956
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          987..1130
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          21..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1280..1405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1552..1644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          495..560
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        22..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1349..1368
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1552..1572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1592..1620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1644 AA;  182821 MW;  08A40B53166C3EDF CRC64;
     MTRNNLPDNI AWLLKNAALS KPTAPQFPQT SDTASFRFTQ SQSTNGRTAD LSQETTVSAG
     SDRRTNQAQG SWSSNGPPKR EEASQNTEVV VLEDDSMGRL SLSTKSRKPV LLSQNVQREA
     PSSADGRSKQ VLNESLKPNA IPKSEKQTQN GISPGKQAPS RHNQSPGLDA DFADFDVDDL
     EYMDLTRTTG ISDESDEFGE DVKVWAEKDA SWEAPLPKSK KRKSADDAAA DSQFPDVYQL
     LGTDPPVPTP SRRTAKKTAQ NASSKMPLPG SSSPLGRVAS RKAPSPVRQT PERDYVISSS
     ERRKKVKIAG HRSVSPDSRN IDEDIQQPEQ NQADEFFIPD SDDEFVTPPS RTTTSKKQPM
     EPLIDPQEED AFIMDIEDLH VSPQPRRKRS QPPPQRIQAK NLEPSHHNLS ETQSTATADN
     VSEINNPQQS FTPSSQTPKL LSLILRNSQL LTKRCEYLNS QIQKNERNFM QAINDRLPKD
     KRNEIKAEKE RFIQQQKATQ DLNGLVERYK TLSEQREAVA QQVARSYSNG QDTDEDEARL
     DELTERIEAT ERELFQMMNT AGLDEASLLE PLEVPAPSRR DDHIVVLGTQ AGHGGMVNMS
     RSSRDVPLPM GGTQVVHQTQ LPEPRPPMNR DLGAEEDLFS DIDDMEMHLL PKPVKKTTQL
     DTRKTPQRNR AQRAGNEFSD FSDDADMLAF AQDYEVRQTA GEPSLDPRRA FSETSGNAGP
     APKQKQTSKR QPPPDSSQTR IPPELMRHSW SAEVQKTLKD RFRMKGFRQN QLEAINATLA
     GDDAFVLMPT GGGKSLCYQL PAVVKSGKTR GVTIVVSPLL SLMQDQVDHM KALGIQAVAF
     NSECSPEYKR QVMSAFNERN PEHFIELLYV TPEMASKSPQ FMNALQSLYR SRKFARIVID
     EAHCVSQWGH DFRPDYKTLG QLRSKFPQVP VMALTATATQ NVIVDIKHNL GMNNCQVFSQ
     SFNRPNLYYE VRPKSSNPVA TQAIAALINS KYPNVTGIVY TISRKQAEDV AQKLSENGIT
     ARHYHAAITP AEKVEVQTAW QKGQVKVVVA TIAFGMGIDK PDVRFVMHHG IPKSLEGYYQ
     ETGRAGRDGK HSDCILFYGK ADIRVLKRLI IDGEGSKDQK ERQMAMLNRV TAFCDNKADC
     RRTEVLRYFG EDFTPSQCHK TCDNCQAGLV FEQQDFSEYA IAAIRIVQQQ QRLTANQCAD
     ILIGRKYPDN QEENSYEYHG MAKGMKKHEM VRVIDRLSAE KGFHEENIVG NHGVAIQYLQ
     IGPAANQFLS GRRKLMLTVQ VSDSGDSNQT KIKKPRANKK QKEPANNVQS TYVSSPINTR
     RKRAAVIDSD DESNLPTTSN GYVNDGFVVS DEEFEDEAEE EMDEDEEAFE PLPQHRPAKP
     TTSKPSSKKA LRPEPIPSKR RLQDLPDIHQ DVVDAFVQAA RQLEERIRNG LGLRRPMFTD
     THLQEMAINW TTSIERMSRI PGIDVDRVRE VGPKLIQMLN VYHKSYREIA GTGAGEASAS
     TSNLDQEIVD LISSDLDIDE DEEEAMGDGE SSHYFVSKPS ADVQAFNDRL QSLNDQPSQS
     RGRSSSYSRG GGNRKFSGKR WSKRGGSGGG SQRRGGGSSR RGGGSSSAAG SSSRSGGAGS
     SSGGFKRDGR IVKKSGGGIG LMPL
//
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