ID U4UDC5_DENPD Unreviewed; 1894 AA.
AC U4UDC5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
GN ORFNames=D910_05981 {ECO:0000313|EMBL:ERL88596.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL88596.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL88596.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least
CC ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the
CC transcription/export (TREX) complex which seems to have a dynamic
CC structure involving ATP-dependent remodeling. Interacts with THOC1,
CC POLDIP3 and ZC3H11A. {ECO:0000256|ARBA:ARBA00025995}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the THOC2 family.
CC {ECO:0000256|ARBA:ARBA00007857}.
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DR EMBL; KB632081; ERL88596.1; -; Genomic_DNA.
DR STRING; 77166.U4UDC5; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0000347; C:THO complex; IEA:InterPro.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR InterPro; IPR040007; Tho2.
DR InterPro; IPR021418; THO_THOC2_C.
DR InterPro; IPR021726; THO_THOC2_N.
DR InterPro; IPR032302; THOC2_N.
DR PANTHER; PTHR21597:SF0; THO COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR21597; THO2 PROTEIN; 1.
DR Pfam; PF11262; Tho2; 1.
DR Pfam; PF11732; Thoc2; 1.
DR Pfam; PF16134; THOC2_N; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT DOMAIN 11..351
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 379..522
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 524..599
FT /note="THO complex subunitTHOC2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11732"
FT DOMAIN 832..1131
FT /note="THO complex subunitTHOC2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11262"
FT REGION 1150..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1623..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 881..915
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1171..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1894 AA; 217112 MW; 750B91D6740D23CA CRC64;
MPTITSYVLQ LIDKGIKGVL KKEAVILALQ ELVSIHADVA SVICDVLNVA DGITSQIDSD
DAKDRANFCS IVKDCEKFLS EKLLKERLEI ETLQEVGILK NRTFYSKFIK IKTKLYYKQR
KFNLFREECE GFAKLQTELN KEFNENTSPA ALIDIVHSLI GCFNLDPNRV LDIILESFEN
KTKDAHIFVP LIELYIKDPS IISEVLSTKL AFLKNTGEDI PASFFLLVAY LLQHSLISLD
HIYSKLSPDE KEIKKHCEKA LKDAAEYVRK LQIISINNKE KEDDKDDAES VEDLFVGNEK
LRLCEALLSI GDWGNARTLI NLLPKHFAIG FQPIALSLCN LLHALIEPVY SLNCALGPNI
NRQPVRPYSN PLAPKAALTF TDLKETVLPM LICLGSSLHY DSVLLSKTIR LFRAVLQEMG
VEAGKAFTPR EDDGLYFEII SILDETILPS LSYLDCNCCI AEEIWNLVKF YPYQIRYCLY
ARWKNDTYSA YPPLMKKRGD AEKQIKNIMK RVSKENVKPV GRLIGKLTHC SPGFLFDYVL
LQIQVYSNLI NPVVDSLKYL TNLSYDVLGY CVIENLCLAD KKRVKHDSTS ISMWLQSLSV
FSGAVYKKYS IELTGLLQYV ANQLKAQKSL DLFILKEVVQ KMAGVEPNED STMEQLYAMS
GGEMLKGEAG YFSQIRNTKR SSLRLKEAMN ENDLAVALCL LMAQQNYCVV YRETQKSHLK
LVGKLSDQCQ DTLVQFGTFL GSTLTVEEYI NKLPTIQCML LNYHIPTEVA FFLARPMFNH
SINQKYDQLR KADPNYKKMS SSIKIQKYYD AVKEVMQPVH SSLLPLHSPK TWEDISPQFL
ATFWSLTMYD LCVPEDIYQQ VINKAKQQSI SAVESLGAKG KKEQERHLSL VEKLMDEKKK
QSEHVEKVLF RLKQEKSSWF LLRAGKSAKT ESITRFLQLC LFPRCTFTQI DAVYCAKFVH
TIHMLKTENF STLLCYDRLF CDVTYSIISC TENEALRYGR FLFAMLETVM KWHKSKETFE
KECSNYPGFM TKYRVSNHTA DSSDNVGFEN YRHVCHKWHY KLAKAVVTCL ESKDYVQIRN
SLIILIKIIP FFPVLIKLAQ FLEKRIEKVR DEEKNNRQDL FTLAISYLGQ LKQRLTSGQM
MKEGDFHIPV EKDKVVKPSP EAPAANGKDL NRHNGEPKEK VFMQQEKKPA RVSSEDGKLQ
RAASSSTDQI AGDKERREDK PTREDQKDKY LKKEEAKRNL IELERDVKRN RIDDRELEDR
NKRSVDPKED RYIEIVSPKE ERYSIERQDR FYEERSSYYH KDISERDNSG SSTTMSKHVS
DPEPERDIKR RKVDVGSAKA AKYGERKVAA GQLLDYPEKI EKKERSASKR REKLSEEDKE
LKKDRKLNRK RWFVAIMKQT SRTGLTASPI KTIYQNKTQK NVQLRAVVKP APFTLKPYAG
LYNPYALGCS LLCNHPMDKD TKELFLKAKE NWANEDKNHS LLAEEMAAIR ANLQPFNCGQ
DGTPPQVESV PEELFRRYTD TDSRPLTPAP TLASAATHAS GSRRCFTPEH RKPQLVLDLR
RSHSHETIPY SGFLNEAPLI RIQHVPARAI SLEDNRDSAG QSPRKVKTAA AFCAINLMGI
KPQRGENQAN REERSETASE EEEVKRRGKR RKKKNSLRGP PAFQLSTDPE TQVAAIGVDS
PDRSARTSIV PINPSQKVEV AGRNSMLASH WSIDVNSFLD AEILMQIRRE LDEETVDSEL
NPNRRQALEE ALKSAARDKP VCQELRDLQK ELKVAKLNSD LWMSLPRTFT RSSARFELPM
SSRSLLTMTP LQYVQEHVNV SSKRKLLFNC VFNRFKIEGT AIGRKLPGHR LQDALDLLMG
RPMRQEEASR FRSLIDWNDQ DCVDFRTFCG IAAL
//
