ID   A0A3M0JBT4_HIRRU        Unreviewed;      1001 AA.
AC   A0A3M0JBT4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
GN   ORFNames=DUI87_25321 {ECO:0000313|EMBL:RMB98415.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB98415.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMB98415.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMB98415.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMB98415.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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}.
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:RMB98415.1}.
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DR   EMBL; QRBI01000153; RMB98415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0JBT4; -.
DR   STRING; 333673.A0A3M0JBT4; -.
DR   Proteomes; UP000269221; 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; 2.
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:UP000269221}.
FT   DOMAIN          8..398
FT                   /note="THO complex subunit 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16134"
FT   DOMAIN          416..550
FT                   /note="THO complex subunit 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16134"
FT   DOMAIN          570..603
FT                   /note="THO complex subunitTHOC2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11732"
FT   DOMAIN          765..899
FT                   /note="THO complex subunitTHOC2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11262"
FT   DOMAIN          898..1000
FT                   /note="THO complex subunitTHOC2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11262"
FT   REGION          317..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          808..835
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1001 AA;  115419 MW;  B118B2F085270B46 CRC64;
     MAALLPAEWI KNWEKGGKSE FVQLCRALSE NKNHDVGFRD IQQALYELAY HVVRGNLKHD
     QASNVLGDVI EFREDMPSIL ADVFCILDIE TSCLEEKNKR DHFTQLVLAC LYLVSDTVLK
     ERLDPETLES LGLIKQSQQF NQKSVKIKTK LFYKQQKFNL LREENEGYAK LIAELGQDLS
     GSITSDLILE NIKSLIGCFN LDPNRVLDII LEVYECRPEY DDFFVPLIES YMYMCEPQTL
     CHILGFKFKF YQDPSGETPS SLYRVAAVLL QHNLIDLEDL YVHLLPGDNA IMEEHKREIV
     EAKQIVRKLT MVVLSSEKTE EKEKEKEKEE EKTEKPPDNQ KLGLLEALLK IGDWQHAQSI
     MDQMPPFYST SHKAIAVALC QLVHVTIEPL YRRVGVPKGA KGSPISSLPN KRAPKQAESF
     EELRKEVFNM LCYLGPHLSH DPILFAKVVR LGKAFMKEFQ SDGSKQEDKE KMETLFSCLL
     SITDQVLLPS LSLMDCNACM SEELWGMFKT FPYQYRYRLY GQWKNETYNS HPLLVKVKAQ
     TIDRAKYIMK CGDSSKESQE SCHVLCRFEC MAILSQIQKY DNLITPVVDS LKYLTSLNYD
     VLACLASFCG AVFRKYPIEL AGLLHFDLLI LKEVVQKMAG IEITEEMTME QLEAMTGGEQ
     LKAECHDTLV QFGGFLASNL STEDYIKRVP SIDVLCNEFH TPHDAAFFLS RPMYAHHISS
     KYDELKKAEK GNKQQHKVHK YITSCELVMA PVHEAVISLH LPKVWDDISP QFYATFWSLT
     MYDLAVPHSS YDREVNKLKV QMKAIDDNQE MDKLLEEEKK QLEHVQRVLQ RLKLEKDNWL
     LAKSTKNETI TKFLQLCIFP RCIFSAIDAV YCAHFVELVH QQKTPNFSTL LCYDRECGNY
     PGFLTILRAT GFDGGNKADQ LDYENFRHVV HKWHYKLTKA SVHCLETGEY THIRNILIVL
     TKILPWYPKV LNLGQALERR VHKICQEEKE KRPDLYALAM G
//