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Database: UniProt
Entry: A0A0V1LC16_9BILA
LinkDB: A0A0V1LC16_9BILA
Original site: A0A0V1LC16_9BILA 
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
//
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