ID A0A0V1LC16_9BILA Unreviewed; 1323 AA.
AC A0A0V1LC16;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Splicing factor YJU2 {ECO:0000256|HAMAP-Rule:MF_03226};
GN Name=Slc26a5 {ECO:0000313|EMBL:KRZ57053.1};
GN ORFNames=T02_3330 {ECO:0000313|EMBL:KRZ57053.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ57053.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ57053.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ57053.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ57053.1}.
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DR EMBL; JYDW01000082; KRZ57053.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1LC16; -.
DR Proteomes; UP000054721; 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:UP000054721};
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 769..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1036..1063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1069..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1100..1131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1154..1323
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 1208..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..487
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1214..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
SQ SEQUENCE 1323 AA; 149708 MW; 4C85C48819BE3DF1 CRC64;
MINDFSVLIW LHLGHRKVYT WFSDVGKGNN KIEGKSCMSL ILTVMEYCSL VISRFCRFCC
FFKVAMTGTE RKALNKYYPP DFDPRKLPKV SIPRNRQYVI RVMAPFNMKC NTCGEYIYKG
KKFNARRETV EDEDYIGLSI FRFYIRCPQC LAEITFKTDL KNCDYAEEHG ATRLFEAEKM
LINQLSVMEA EAEKEKGNAM LMLEKRTKMS RFEMEALERL EDLKELNKRQ ATVDYDALIE
QAKEEELAEI LHQKEEEDRY VQSVFENTID KSGPSSSSLL IKRLPDLSDE ETDKKLETST
FVVEKKPRIS KQKLFLRGVV KKKDTSVEKK KTFSQLGNDS TTPDTGSLGL LGTYGGGICK
LMLKLAGSQM KIVMLSLQLL DLASQSLLSM NPESESSLIM NTSSSGNLSF ELILRPPTKH
APANLSSPCN LKTTLQEIEG KLKAAEERRL NVEAEKVEKA KIEERLLEVA ERRKALLQKF
QEETEKEIQN RAKVTSLNRE KLFEERIEKI KDHEKHVEEV RRSRGKLSPN TKSEMEADLA
YVKSLEKMTI AELEEKLTEK DKLIDEIQTA MKGEIESGQF AATFRLAEAK AYRRIISGII
KANTVILRWT FQIVQLFGSV CHVLCITFEL QITIVKNSSV FSVEKSQHQV VIHRKVYNLE
EFDEEFDKRY VDLTLIGRAK KTLLNIWNEG FSFFQRLLSA RFPCIKWLLQ YNVKKDLPTD
VLSGITVGVF NIPQGMAYGM LAGTSAANGL YTSFYPPLIY SIFGSSNQIS IGTFSVISLM
TAGVIAKFSH FTCKDFGGYF SHNATVSTPE NWFCGSSSSR CTPDVNEVTE IAMSLAFLVG
VFQILLGLMN MGFLSVYLSD QLVEGLTTGS AVLVFTSQIR HVFGIKGLPD TGNPLDIIKF
YGCFFIKIDN FNWLALVISA ICILSIIVVK QFLDPPFKRY FKFSLPFELF LVIATTAISY
GLNLNEAYSI DIVGKVPKGL VYPRLPRWDL FPELASDAIA ISVVIYSICI SLAKLNGSPL
EWSTWDLRFS LANAPALHLV ELAGVFAAAV VMIVLLFLAG LLTHLPKCVL ASVIIVALKG
MFFQMRNLPK LWRCSKPDFL IWVVSFCSVV LLDITYGLLV SVAFALLTIV FKSQPDSICL
GRIPKTELYR GLNAYAKAEE IPGVKIYRFD SPLFFANVEN FRQRLYECTG IDPIDQKVAD
DLSKKHKNYG SMESRSTEKQ PNVNSSEWPV TESKTDASSI VACPSCSANL HTIIIDCSSF
PFVDLMGVES MKQIYLEYKK IGIAVKFAYC KVSLRQILER TDFFQTVPKA RLYPSIEDAV
AHW
//