ID A0A0V0VVN9_9BILA Unreviewed; 1328 AA.
AC A0A0V0VVN9;
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:KRX67309.1};
DE Flags: Fragment;
GN ORFNames=T09_845 {ECO:0000313|EMBL:KRX67309.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX67309.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX67309.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX67309.1};
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:KRX67309.1}.
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DR EMBL; JYDN01000006; KRX67309.1; -; Genomic_DNA.
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; 3.40.640.10; 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; 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:KRX67309.1}.
FT DOMAIN 224..360
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 670..790
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:KRX67309.1"
SQ SEQUENCE 1328 AA; 149128 MW; A7761D28F291E363 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 LGYTFQFPPD FDEMISKLSQ FPGNLCMPTK IRSILASRAC
RKSVMIGTAL SMEEMQQIVE RLSSIEHPWN CPHGRPTVEF LLIFFFYFNI FQSEKWEIDL
SILPYRTFFS ISYETLSTQS APFYHVCVEV ALLICIVWLV THKAYVISDS TDLTVTFFIN
GNYYQLCACI FEEKEELIIE WKPDLLVPLP EQCHLPEPHG PMIDSGLGKY VTIDGKEYLN
FATQNFLGLA TDFKIQDSAI AALHKYGVGA CGPRGFYGTI DIHLDLEERL AEFMRCEEAV
LYSYGFATIS SAIPAYCKRG DVIFCDAGVN FAIQKGLQAS RSRVEFFEHN NTRDLERLLK
IQRRKDILAC AVHSLCDWNP KKARVTRRFI VVEGIYLYYG DICPLVDLVS TMQQRVEHLH
PLKLKWKYKV RLFIDESISF GVLGAGGRGV TEHFGVDLDD VDMISSTLEN AVSSIGGFTC
GRSFVVDHQR LSGAGYCFSA SMPPLLAAAA IRSLDLMQDE PERFQQLRKN SHQLFTALKS
RRPEGQSNFS LTHKAGGEEN GILLTKLAFL PAREFMDIVP SVKLAISCEH TEEEIQRLID
LVKSVDNA
//
