(data stored in ACNUC7421 zone)

HOGENOMDNA: ASHGO_3.PE420

ASHGO_3.PE420        Location/Qualifiers
FT   CDS             complement(726871..728280)
FT                   /codon_start=1
FT                   /gene_family="HOG000239405" [ FAMILY / ALN / TREE ]
FT                   /evidence="3: Inferred from homology "
FT                   /gene_id="IGI20622470"
FT                   /gene_name="SHM2"
FT                   /locus_tag="ACR215C"
FT                   /product="Serine hydroxymethyltransferase, cytosolic "
FT                   /EC_number="2.1.2.1"
FT                   /function="glycine hydroxymethyltransferase activity "
FT                   /function="pyridoxal phosphate binding"
FT                   /biological_process="L-serine metabolic process "
FT                   /biological_process="glycine metabolic process "
FT                   /biological_process="one-carbon metabolic process "
FT                   /cellular_component="cytoplasm"
FT                   /protein_id="AAS51441.2"
FT                   /db_xref="EMBL:CAD27656.1"
FT                   /db_xref="GO:0004372"
FT                   /db_xref="GO:0005737"
FT                   /db_xref="GO:0006544"
FT                   /db_xref="GO:0006563"
FT                   /db_xref="GO:0006730"
FT                   /db_xref="GO:0030170"
FT                   /db_xref="HOGENOM:HBG301263"
FT                   /db_xref="HOGENOM:HBG420026"
FT                   /db_xref="InterPro:IPR001085"
FT                   /db_xref="InterPro:IPR015421"
FT                   /db_xref="InterPro:IPR015422"
FT                   /db_xref="InterPro:IPR015424"
FT                   /db_xref="InterPro:IPR019798"
FT                   /db_xref="UniParc:UPI00004B2543"
FT                   /db_xref="UniProtKB/Swiss-Prot:Q75BQ6"
FT                   /transl_table=1
FT                   /translation="MPYHLSESHKKLISSHLSESDPEVDAIIKDEIDRQKHSIVLIASE
FT                   NLTSTAVFDALGTPMCNKYSEGYPGARYYGGNQHIDRMELLCQRRALEAFHVTPDRWGV
FT                   NVQSLSGSPANLQVYQALMKPHERLMGLHLPDGGHLSHGYQTETRKISAVSTYFESFPY
FT                   RVDPETGIIDYDTLEKNAVLYRPKILVAGTSAYCRLIDYKRMREIADKVGAYLMVDMAH
FT                   ISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFFRRGVRSVHPKTGEEVMYDLEG
FT                   PINFSVFPGHQGGPHNHTISALATALKQATTPEFREYQELVLKNAKVLETEFKKLNYRL
FT                   VSDGTDSHMVLVSLREKGVDGARVEHVCEKINIALNKNSIPGDKSALVPGGVRIGAPAM
FT                   TTRGMGEEDFARIVGYINRAVEIARSIQQSLPKEANRLKDFKAKVEDGTDEIAQLAQEI
FT                   YSWTEEYPLPV"
     MPYHLSESHK KLISSHLSES DPEVDAIIKD EIDRQKHSIV LIASENLTST AVFDALGTPM        60
     CNKYSEGYPG ARYYGGNQHI DRMELLCQRR ALEAFHVTPD RWGVNVQSLS GSPANLQVYQ       120
     ALMKPHERLM GLHLPDGGHL SHGYQTETRK ISAVSTYFES FPYRVDPETG IIDYDTLEKN       180
     AVLYRPKILV AGTSAYCRLI DYKRMREIAD KVGAYLMVDM AHISGLVAAG VIPSPFEYAD       240
     IVTTTTHKSL RGPRGAMIFF RRGVRSVHPK TGEEVMYDLE GPINFSVFPG HQGGPHNHTI       300
     SALATALKQA TTPEFREYQE LVLKNAKVLE TEFKKLNYRL VSDGTDSHMV LVSLREKGVD       360
     GARVEHVCEK INIALNKNSI PGDKSALVPG GVRIGAPAMT TRGMGEEDFA RIVGYINRAV       420
     EIARSIQQSL PKEANRLKDF KAKVEDGTDE IAQLAQEIYS WTEEYPLPV                   469
//

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