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Database: UniProt
Entry: A0A0V0TUK9_9BILA
LinkDB: A0A0V0TUK9_9BILA
Original site: A0A0V0TUK9_9BILA 
ID   A0A0V0TUK9_9BILA        Unreviewed;       918 AA.
AC   A0A0V0TUK9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00015825};
GN   Name=AMT {ECO:0000313|EMBL:KRX42681.1};
GN   ORFNames=T05_16055 {ECO:0000313|EMBL:KRX42681.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42681.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX42681.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX42681.1};
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   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|ARBA:ARBA00011690}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
CC   -!- SIMILARITY: Belongs to the Hyccin family.
CC       {ECO:0000256|ARBA:ARBA00034482}.
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:KRX42681.1}.
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DR   EMBL; JYDJ01000138; KRX42681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TUK9; -.
DR   STRING; 144512.A0A0V0TUK9; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR018619; Hyccin.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF15; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01571; GCV_T; 2.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   Pfam; PF09790; Hyccin; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methyltransferase {ECO:0000313|EMBL:KRX42681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Transferase {ECO:0000313|EMBL:KRX42681.1}.
FT   DOMAIN          32..89
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          114..314
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          345..404
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   REGION          826..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..854
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  102681 MW;  B387A8F9CC29D141 CRC64;
     MRPLTISLQS RALLKNSFRR NASQGLPKKT CLFDFHKAHQ AKMVEFGGWL MPVSYADQSV
     GESHLHTRNH CSIFDVSHML QTRIFGEDRH GRRILFKFNF NFDQNCLFLF LRIAFIEKLT
     VADVQGLKEH RSVLTVFTND NGGIKDDLII TKDDDHLFLV SNAACSDKDI AHMKLELENF
     KKDGRDVTVE HLNNRALIAV QGLMDGPEMI KVVQAGVKYD MRCLIFMSSV VTSVFDIPNC
     RLSRCGYTGE DGVEISIDSD RAVELCEKIL NSTHAPVKLA GLGARDSLRL EAAMCLYGTD
     MDETTTPVEA GLSWLIARRR REMADFPGAD IIMKQLKSKE KNISKKRVGM ISTSGRPPRG
     NYDILIPNGD VVIGKVTSGC PSPVLKENVA MGYVKSEYTK VGTHGEDAVC STSILRPLIQ
     RSVCLDLSSV CPFLCKLHYT GSGVRFLAEN WHIKNNASER DELIHADGSD MKNNELFTLL
     EDYKEKLRDA ETKPSSVQLQ ERIINLLRNF QDHANEETIS ICSELLDFYH KGQMWRDFCF
     EFLPSLIECY LLSRCSGSSN VSLAVGTLLI TIYNCELQNA DGSLKKEVIR LAPATQSSVF
     NRDPSNVMTL EGMTEKNVFS LNTEGIHHCQ IGPHLAYSSI NASNRFLLLT NLLKTYNSLM
     DKFSLMSIES YCAMCYSICR SGFQFETLDV LKSFVGPGLR RQEQHLHHFM EERPNAPRIL
     LSSYFLVEAI NGLQHAMFGN ACVSALLAIE SIHLRAKYEL YTDVLLVTNA ILNSLETYKN
     AGMTLDNLIG IYTACSPAVQ VHIQRSPGLI TKASFKLRKF SSKLMPHALS NSSSPSGSPR
     SPRKHEHETT ACLVEEEDDG QLPTTSISSL KNIDSLAESP NKSFIGDEAD EDSNTLTILL
     TANGDDKRHQ SVEEELGR
//
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