ID A0A0V0T9J8_9BILA Unreviewed; 1736 AA.
AC A0A0V0T9J8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
GN Name=THOC2 {ECO:0000313|EMBL:KRX35723.1};
GN ORFNames=T05_7386 {ECO:0000313|EMBL:KRX35723.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX35723.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX35723.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX35723.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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}.
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:KRX35723.1}.
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DR EMBL; JYDJ01000415; KRX35723.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1023..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1090..1114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..362
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 382..524
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 526..601
FT /note="THO complex subunitTHOC2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11732"
FT DOMAIN 837..1156
FT /note="THO complex subunitTHOC2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11262"
FT REGION 1207..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1736 AA; 197014 MW; BFAF0DC574556B12 CRC64;
MSINKQIGEL YVICKSVING ITSVEDGFES LSKVINTHRQ RSCLIDTLAV LDYEQMSKKN
PEIKKRFYEL CAKCSGHLVP EEILKRNVES LNDKSYELRM VRLKTKLFFK QKKCNMLHEQ
PEGFVTLFQL IYNSCNKEEN VERTLADIYG IIGRYCLDPN RVLVVLMTSF QSNLDKHRYF
ASLFKEYISA KDAFSCPVAY ELNCLQNTTD DADSHNAELS EEERLAKVQN FFKMIAYLVH
YGFLDLNMLL TKTSPTSAEM IQEAETALKK AEADQRKLLT LSLRGPKETA EVEDTSEEKP
SYLSNQKLAL AVSFLEIGDW NNAKQVFDHM PEYYAASSLE ANEAFCNLID YKIDRLFVSL
HPIASLARGA EVREPVAQFV DVKCCESLID MCTDVFPIVN YCGPSIAHSP LVLTKLIRLC
CRLVNDKNGQ DEQFSEHLDT LYHLCSSVFL PSLSMLRWNC SLSEDLWLLL SQFPYTLRYR
FYSEWKTVHL KQHPLLLARK GEVVGRARHV MKRLSKDTTK QTGRMIGKLS HSYPVVVFDY
LLSQIQQFEN LIGPVVESLR FVTNLSYDVL AFCIIEHLAR PEKQKLKVSH ATISSWLQSL
ATFVGSVFKK YNIELSGVLQ FVTNQLKRGT SLDLLVLGEI VKNMSGVETA RNLTKDQIET
YAGGDILKSE VGHLSQMRNM RRSVHRLKDS LLQDDLAVTL CILIAQQRKV IVFKDGAKVH
LKLAGQMLDQ CHETFIQFAH FLMANVEIEE YTRRMPLADE LLQLYNLDCS SAMFLTRPAY
NYKIREKFQE LIKAEKAGQQ LEDSKKMQYY ISACEEIYLP LQNKMKELSQ PEMRPELTTK
FFVTFWTLSL YDLFVPTKAY QTAVDGIRKS IEQLESCREL TESKRRKEKE RFLQQESKLL
QEQQTHLEHV SLVKARLMSE SSRWFSSRAP RTALVSQMVQ ACLFPRCVFH EADAFYCVRF
IEMCHLFKTP NFPTLIFWDL SSAVACLSEY EASCYGRFIC ELLELLMSWH SDREKFNQAS
KPFILQCWMK IIIFIIIVML FVFKECANHP GFITRIKAVG GSNNDHSRDF VDYESFRHVL
NKWHYKITRA VLICLTSDSF ILIRNILLIL MKILPYFPLL HNLMLTIEKR VIDVRDREKD
KRQDLHVLAA SYWGHLKLRK DHMFAEEDFH AVNVKERATD CLELFEVSAI IDDEEFFLKV
NDSSSSSNRE VKVEDNNSAT PLLNEAKKPV SSKSSTIKNS GQDTTSAVSK SSNSSSVKSV
ATKTDTDKVS EDAGMSTLKN SSADTEPLPE TMQQHSLQPG PAKVPRLEVA ESGGPVEPAP
LPKNRSSNAA KAAVSASGAS TKESTTVRGA HPHHHQQQQQ QQATTNRLKH KDAVVEQQQS
SSCSTSVGTS ATTRTTTTTT TTTTTSGGRQ GSTRKASLRA PDASSGASST TAETSASSLL
NDSSNLGSNC VTSAEKSNRN DNITSVDSSA TKIDGEQQRQ QNNTASTFED TKSKTDRHLS
SSSTAGHSKN SNIPPLTLES SGRKVTASSS SSTAVSKSSY HQDDRRNGNK EPEHGSAAHK
SRRKGGSVNE SGMPDVLFVC LFVFYIPHLV LHDFLFRQQT AEVGEKNYRG LLRQSTLKRS
PDLKRSSPSS SSSSRRKKNP QRYKEKERTD TYVEFDSAMI DSKKEARKER FAEPVDWRNK
DYRYMSSASV SRMSSFHAGN EPKTMKMVRL SQATSRSVSP RDVYQEKVIH RSSRRR
//
