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Database: UniProt
Entry: A0A0V1H7C7_9BILA
LinkDB: A0A0V1H7C7_9BILA
Original site: A0A0V1H7C7_9BILA 
ID   A0A0V1H7C7_9BILA        Unreviewed;      1196 AA.
AC   A0A0V1H7C7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000313|EMBL:KRZ06323.1};
DE   Flags: Fragment;
GN   Name=SART3 {ECO:0000313|EMBL:KRZ06323.1};
GN   ORFNames=T11_4477 {ECO:0000313|EMBL:KRZ06323.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ06323.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ06323.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ06323.1};
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   -!- 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:KRZ06323.1}.
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DR   EMBL; JYDP01000121; KRZ06323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1H7C7; -.
DR   STRING; 268475.A0A0V1H7C7; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IEA:UniProt.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd12391; RRM1_SART3; 1.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034217; SART3_RRM1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR12001:SF69; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SMART; SM00386; HAT; 5.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   4: Predicted;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT   DOMAIN          667..743
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          767..844
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          523..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ06323.1"
SQ   SEQUENCE   1196 AA;  136638 MW;  676DA3918CAA8C51 CRC64;
     LKRKLPYFEI FSENTNIIMN QSAEDMEELG EELNDMDFDS HLDDELEVQL TNLRQMVTDN
     PTSFSVYNDL VQALKCAGEL IELRETRSEM SRRFVLLPNV WLEWIGDELE LGTPTADILS
     MFEQGLKDFP ASLHLWMEYL NLYCTASQPD EMRSRIEQAV TAVGLNVAEA STIWQMYRDF
     EMAMTPLQQP NGSSSSPSDE KAQYLSVFRR QLSVPHIGLR EAYEEYKDLL NGAEVDKATE
     FAYRGALKEL EMLENFEKQL ESYSGPRSSK FSAYIDFEMK QKCPARLQVL FERAILHCYT
     DETLWLRYLN WLNENMNLPD VTLPVYGRAV RSCPRSMKIR QMYLLACERF KCDWSTISKV
     MTDALENSYS QLETVELLLT HIYQRKRFIS TEGGQYSEVI KGFKDGAEIL KDRFHGAWDA
     DFWYRQSWAR FAADDCKDMN AARLLWKEIM HEAGGTNPTL WLDYVWLERQ HGDFQHVCSI
     YQQAANSLAE HHGALFAEWQ QYVNEKGTLD DVLSTMHRIE RHRMRLKESQ NKGKLQRKKQ
     QQISKKRAEQ EEAAPAPAPA PPAAPAAESL NSAMQRDGVS VKPYVSVGEK ASSLPSKDYF
     KKDSIVTNEI YPAAVVRETT VQVDADGFLI PPVPKKTKTE SQAKHAEIVE QPTLETTTND
     TSAKHANTVF VSNLDFTLSK ERLKDTMAEA GEVVDVRMIM LRPNRSKGYA YVDYKDEASV
     KKALKMDRRC IDGRPMYVSI CRGDVEGGQQ MEKQNSGFQY SVGLEKNKLF VKNIPTFATE
     SDLESLFRQY GDLRSVRLVL HKSGKSKGLA YVEFDNEEAA ERGRLAQNGA HFFGKRLSVE
     FSNPPPRQDR SSSTFTRRSQ NPFSGGGPSR STDVPRSAPR LRLVPRALST SQKLMDKSNS
     MMLSLTAPAS KEEEELIAPF KYICSIPGKQ IRVKLGFNLW LNVDNEIVNS ISEIVEMLHN
     ASLMIDDIED SSELRRGMPV THRIYGLPTT LNTANYIYFV ALSKTVQLHH TDAVKVFTES
     LLDLHRGQGM EIFWRDAVIC PTEAKYLDMV IKKTGGLFRL GVNMLQLFSS NKMNYNQLLN
     DMATYFQIRD DYMNLVAGEL KGFAEDLTEG KFSFPIIHAL QSHPENDQIL KILRQRTNSV
     ELKKHCINML SSLGSLDYTK QRLNELSKKI LSDIEKFGGN AHLQELMDML KQLHGC
//
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