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Database: UniProt
Entry: A0A0V0VUX0_9BILA
LinkDB: A0A0V0VUX0_9BILA
Original site: A0A0V0VUX0_9BILA 
ID   A0A0V0VUX0_9BILA        Unreviewed;      1351 AA.
AC   A0A0V0VUX0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Serine palmitoyltransferase 1 {ECO:0000313|EMBL:KRX67311.1};
DE   Flags: Fragment;
GN   ORFNames=T09_845 {ECO:0000313|EMBL:KRX67311.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX67311.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX67311.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX67311.1};
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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:KRX67311.1}.
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DR   EMBL; JYDN01000006; KRX67311.1; -; Genomic_DNA.
DR   STRING; 181606.A0A0V0VUX0; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd03484; MutL_Trans_hPMS_2_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR   Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR002099; MutL/Mlh/PMS.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR042121; MutL_C_regsub.
DR   InterPro; IPR037198; MutL_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00585; mutl; 1.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Transferase {ECO:0000313|EMBL:KRX67311.1}.
FT   DOMAIN          224..360
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          670..813
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          454..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX67311.1"
SQ   SEQUENCE   1351 AA;  151663 MW;  7A4E50F8926A6491 CRC64;
     LSNDFCQSGS TVKQLNETVV HQISFGQVIS CMTNAIKELV ENALDAGATA IDITLTNSGI
     ERIHVADNGT GIPEKDFQNI CKSHCTSKLS VMDDLSRMKT FGFRGEALCA LCLIGDVIIT
     TRHADSELAY QLHFDRSGQL TKQVACSRQI GTTVEVAEIF HPFPVRRKSL IRSVQKEWPK
     LMHMLQSYAL LPSALRLQVV NKQKGGKQSV AFSALSSENL RENICSVFDV GQLRLLMEFV
     QILPNEETLE QYFVKNFDPA EIDKIKIVGF VSSVQQGRSS GDRQFTYVNN RPCEIRKITQ
     LVNEVYHQFN PVQYPVFVLY INVPTEMLDV NCTPDKRLVY ISRENLLLAI LRHSLTEMYG
     QSSVIMSCSS RWKTLDTPQI EDATVSDVIG NIAASDNNLS VDCSSCSTAG GSSSNKVNLV
     RGVKRLSSRN CRQDHQLVPI RTSDILEAFG FKSKEKKSRR HKEEGQRLHG AEDGGNGWQQ
     GGIDTVDELV GSTSGESGMR ISCCEPLDDE AAVKNFSHGT ADCTRTVQES LPLVVHSITD
     QAAKFKPTAD PRVTIPAATM EVISGQQLST CGKSESAEME VSKSVECVST RGGVCIARRY
     YDLQVNWDDL EIRLLGLIKT FGNNNKCAKT SFNDMNNKKF QIHVDPAKDA QAEEEVKRFL
     TRDMFAEMHV IGQFNCGFIL TRLDDDLFIL DQHASDEKRT FETMRRSTVV QSQLLVHPIC
     SNLTPFDRHV ILENLETFKN LGYTFQFPPE GSDEPVKIVS LPVCHGQIFD QRDFDEMISK
     LSQFPGNLCM PTKIRSILAS RACRKSVMIG TALSMEEMQQ IVERLSSIEH PWNCPHGRPT
     VEFLLIFFFY FNIFQSEKWE IDLSILPYRT FFSISYETLS TQSAPFYHVC VEVALLICIV
     WLVTHKAYVI SDSTDLTVTF FINGNYYQLC ACIFEEKEEL IIEWKPDLLV PLPEQCHLPE
     PHGPMIDSGL GKYVTIDGKE YLNFATQNFL GLATDFKIQD SAIAALHKYG VGACGPRGFY
     GTIDIHLDLE ERLAEFMRCE EAVLYSYGFA TISSAIPAYC KRGDVIFCDA GVNFAIQKGL
     QASRSRVEFF EHNNTRDLER LLKIQRRKDI LACAVHSLCD WNPKKARVTR RFIVVEGIYL
     YYGDICPLVD LVSTMQQRVE HLHPLKLKWK YKVRLFIDES ISFGVLGAGG RGVTEHFGVD
     LDDVDMISST LENAVSSIGG FTCGRSFVVD HQRLSGAGYC FSASMPPLLA AAAIRSLDLM
     QDEPERFQQL RKNSHQLFTA LKSRRPEGQS NFSLTHKAGG EENGILLTKL AFLPAREFMD
     IVPSVKLAIS CEHTEEEIQR LIDLVKSVDN A
//
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