ID A0A0V1BJ13_TRISP Unreviewed; 1366 AA.
AC A0A0V1BJ13;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Splicing factor YJU2 {ECO:0000256|HAMAP-Rule:MF_03226};
GN Name=Slc26a5 {ECO:0000313|EMBL:KRY36882.1};
GN ORFNames=T01_13928 {ECO:0000313|EMBL:KRY36882.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY36882.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY36882.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY36882.1};
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 -!- FUNCTION: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA. Plays a role in stabilizing the structure of the
CC spliceosome catalytic core and docking of the branch helix into the
CC active site, producing 5'-exon and lariat intron-3'-intermediates.
CC {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SUBUNIT: Component of the spliceosome. Present in the activated B
CC complex, the catalytically activated B* complex which catalyzes the
CC branching, the catalytic step 1 C complex catalyzing the exon ligation,
CC and the postcatalytic P complex containing the ligated exons (mRNA) and
CC the excised lariat intron. {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03226}.
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:KRY36882.1}.
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DR EMBL; JYDH01000038; KRY36882.1; -; Genomic_DNA.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IEA:UniProtKB-UniRule.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 6.10.280.30; -; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR11814:SF105; STAS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00836; Stathmin; 1.
DR Pfam; PF00916; Sulfate_transp; 2.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR SUPFAM; SSF101494; Stathmin; 1.
DR PROSITE; PS50801; STAS; 1.
DR PROSITE; PS51663; STATHMIN_3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03226};
KW mRNA processing {ECO:0000256|HAMAP-Rule:MF_03226};
KW mRNA splicing {ECO:0000256|HAMAP-Rule:MF_03226};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03226};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Spliceosome {ECO:0000256|HAMAP-Rule:MF_03226};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|HAMAP-Rule:MF_03226}.
FT TRANSMEM 870..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1104..1123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1135..1166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1189..1358
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 1243..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..503
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1249..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
SQ SEQUENCE 1366 AA; 154529 MW; A618EA5B50F68AEB CRC64;
MYVFAFSVVK STPPQTSVET LNDVEFLSQK STCPYVSVKI EKVVYMRFCD VGKGNNEIEG
KSCMSLILTV MEYCSLYCFF KAAMTGTERK ALNKYYPPDF DPRKLPKVSI PRNRQYVIRV
MAPFNMKCNT CGEYIYKGKK FNARRETVED EDYIGLSIFR FYIRCPQCLA EITFKTDLKN
CDYAEEHGAT RLFEAEKMLI NQLSVMEEEA EKEKGNAMLM LEKRTKMSRF EMEALERLED
LKELNKRQAT VDYDALIEQA KEEELAEILH QKEEEDRYVQ SVFENTIDKS GPSSSSLLIK
RLPDLSDEET DKKLETSTFV VEKKPRISKQ KLFLRGVVKK KDTSVVEKKK TFSQLGNDST
APDTGSLGLL GTYGGGICKL ILKSFYACCG FFRLAGSQMK ISLLSMNPES ESSLVMNTSS
SGNLSFELIL RPPTKHAPAN LSSPCNLKTT LQEIEGKLKA AEERRLNVEA EKVEKAKIEE
RLLEAAERRK ALLQKFQEET EKEIQNRAKV TSLNREKLFE ERIEKIKDHE KHVEEVRRSR
GKLSPNTKSE MEADLAYVKS LEKMTIAELE EKLTEKDKLI DEIQTAMKGE IESGQFDATF
RLAEAKAYRR IISGIIKENL LIFFVWITVI LRWTFQIVQL FGSVCHVLCI TFELQITIIK
YPYCRCAQCV KNSSVFSVEK SQHQVVIHRK VYNLEEFDEE FDKRYVDLTL IGRAKKTLLN
IWNEGFSFFQ RLLSARFPCI KWLLQYNVKK DLPTDVLSGI TVGVFNIPQG MAYGMLAGTS
AANGLYTSFY PPLIYSIFGS SNQISIGTFS VISLMTAGVI AKFSHFTCKD FGSYFSHNAT
VSTPENWFCG SSSSRCTPDV NEVTEIAMSL AFLVGVFQIL LGLMNMGFLS VYLSDQLVEG
LTTGSAVLVF TSQIRHVFGI KGLPDTGNPL DIIKFYGCFF IKIDYFNWLA LVISAICILS
IIVVKQFLDP PFKRYFKFSL PFELFLVIAT TAISYGLNLN EAYSIDIVGK VPKGLVYPRL
PRWDLFPELA SDAIAISVVI YSICISLAKL NGSPLEWSTW DLRFSLANAP ALHLVELAGV
FAAAVVMIVL LFLAGLLTHL PKCVLASVII VALKGMFFQM RSLPKLWRCS KPDFLIWVVS
FCSVVLLDIT YGLLVSVAFA LLTIVFKSQP DSICLGRIPK TELYRGLNAY AKAEEIPGVK
IYRFDSPLFF ANVENFRQRL YECTGIDPID QKVADDLSKK HKNYGSMESR STEKQPNVNS
SEWPVTESKT DASSIVACPS CSANLHTIII DCSSFPFVDL MGVESMKQIY LEYKKIGIAV
KFAYCKVSLR QILERTDFFQ TVPKARLYPS IEDAVAVATC CSCTSF
//