ID   A0A0L7RAQ1_9HYME        Unreviewed;      1415 AA.
AC   A0A0L7RAQ1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
GN   ORFNames=WH47_12322 {ECO:0000313|EMBL:KOC67992.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67992.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC67992.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC67992.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ414618; KOC67992.1; -; Genomic_DNA.
DR   STRING; 597456.A0A0L7RAQ1; -.
DR   EnsemblMetazoa; XM_017944023.1; XP_017799512.1; LOC108580303.
DR   Proteomes; UP000053825; 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:UP000053825}.
FT   DOMAIN          9..378
FT                   /note="THO complex subunit 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16134"
FT   DOMAIN          398..543
FT                   /note="THO complex subunit 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16134"
FT   DOMAIN          545..620
FT                   /note="THO complex subunitTHOC2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11732"
FT   DOMAIN          853..1155
FT                   /note="THO complex subunitTHOC2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11262"
FT   REGION          1169..1392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          876..928
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1177..1200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1201..1277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1415 AA;  163334 MW;  C02E45D363BE133D CRC64;
     MAGKVWNSEI WKAWDKHGKN DFLKLIKHKF KEGNTADWRR GLYELISNGI RGNIKRDNVV
     QTLGELTSVD GAIPSAIVDI FTLIDAEAHN EERNNFYYIV KESEKFLTDR ILKERLEIDT
     LQDVGTLKNK NFQTKFIKVK TKLYYKQRKF NLFREESEGY SKLIVELNQE RPENEVASIL
     EIVKSLIGYF NLDPNRVLDI LLETFENRPQ DDALFIPLIR SYMSDQQVLC EVLGFKYCST
     VNATPFSLQK VTALMLQHGV IELDDILPWL VPDDKTIIKE HEQAMKQAKE YVRKLSVIST
     KDKEEVPEEK ENPLDKYASN QKFGLCEALL EIGAWEVAQN LFNRLPDHSL TDQRPIALSL
     CKMIQSLIEP VYRKHCIISP KLQGRSVPPL ESALAPKSIE NLEEIHDQLL PMLIVLGPNL
     HHDPVLMYKI MRLCHAAIKQ CPLDTNKQPV DKNNNLYYDV LTILDVALLP SLSFMDCNCC
     VAEELWNILK YYPYQNRYCL YARWKNDTPL QHAALLRKRA DAQKKIKSIM KRVSKETIKP
     VGRSIGKLTH SSPGVLFDYV LIQIQLYDNL IGPVVDSLKY LTNISYDVLG YCLVEALAGA
     DRDRFKHDGT SISLWLQSLA SFCGAIFKKY NIELTGLLQY VANQLKAQKS LDLLILKEIV
     QKMAGIEAAE EMTSDQLDAM AGGDLLKNEA GYFSQVRNTK KSSQRLKEAL AEHDLAVALC
     LLMAQQKHCV VYRETDKSHL KLVGKLYDQC QDTLVQFGTF LGSTMTVDEY VERLPSIHSM
     LQDNHIHSDV AFFLARPMFA HAINIKYDAL RKADPNYKKM STAMKQAKYA EAAQAVMAPV
     AQSVRPLHPL KVWEDISPQF LVTFWSLSMY DLYVPVESYQ REINKLKQLA AQSADSKDMN
     VSKGKKEQER YTTLIEKLQD ERRKQEEHVE KVFAYLRQEK DTWFLSRSAK SAKNETITQF
     LQLCLFPRCT FTTVDAMYCA KFVHTIHSLK TANFSTLLCY DRLFCDITYS VTSCTENEAN
     RYGRFLCAML ETVMRWHSEK AIFDKECSNY PGFVTKFRVS NQFSEANDMV GFENYRHVCH
     KWHYKITKAI VVCLDSKDYV QIRNSLIILI KILPHFPVLA KLSQILERKV EKVREEERGQ
     RQDLHVLATS YSGQLKAKTP NMIREADFHH VGDKTGKTQD TPNNDSSEKV GDGISNKEIT
     NGDTRIEKEN KEQREKRSAS NQMHHESSEK IRKKEESKES SEGKDKHLKK EEIKEDDLMD
     KKDRKYYKEE HYYSSGVDNL DRDLSSVSNS SASSGPTQDG SDRDAKRRKV ESVQKEGRRT
     EGSLDKKERS SKGKIRDEQK ELRREKKFAR KRDRADDSAV ATEQKRRKDD EKAKGAHQNG
     DIPEHREKHH YNKVGNSNWN FSLFMYPKYR ALYIY
//