(data stored in ACNUC7421 zone)

EMBL: AM269963.PE14

AM269963.PE14        Location/Qualifiers
FT   CDS             join(36916..37286,37368..37794,37890..38390)
FT                   /locus_tag="An01g04560"
FT                   /EC_number="3.2.1.6"
FT                   /note="Function: mixed-linked glucanases (MLGases) are
FT                   extracellular enzymes able to hydrolyze beta
FT                   1,3-1,4-glucans."
FT                   /note="Similarity: the C-terminal part of the predicted
FT                   protein has similarity to a calcium binding domain found e.
FT                   g. in a penicillin-binding protein of Bacillus subtilis."
FT                   /note="Similarity: the product of MLG1 of C. carbonum has
FT                   no close similarity to any known protein but does contain a
FT                   motif (EIDI) that occurs at the active site of MLGases from
FT                   several prokaryotes; this motif is conserved in the
FT                   predicted protein."
FT                   /note="Title: strong similarity to mixed-linked glucanase
FT                   precursor MLG1 - Cochliobolus carbonum"
FT                   /note="extracellular/secretion proteins"
FT                   /note="See PMID 9464371"
FT                   /db_xref="GOA:A2Q8J5"
FT                   /db_xref="InterPro:IPR000757"
FT                   /db_xref="InterPro:IPR013320"
FT                   /db_xref="UniProtKB/TrEMBL:A2Q8J5"
FT                   /inference="profile:COGS:COG2273"
FT                   /inference="similar to AA sequence:UniProtKB:U81606.1"
FT                   /protein_id="CAK36992.1"
FT                   /translation="MLVAMRRTATLLSALGLTAQLSSAAYTLQDDYSGSGFFDGFSFFT
FT                   DTDPTNGFVDYVDEATAQSNGYISTSGDYVYMGVDHTNVAGSSGRQSVRISSDATYNHG
FT                   LFILDLEHMPGGICGTWPAFWLVGADWPNNGEIDIIEGVNQQSGNDMTLHTSDGCSISS
FT                   SSDFTGSMTTDNCYVYAAGQSSNAGCGITDPDATSYGTAFNANGGGVFATEWTSDAISI
FT                   WFFERGSIPDDIDSGNPDPDSWGSPVARFQGDCDIDSHFDGLQIIFDTTFCGDWAGNVW
FT                   GSGSCASVASSCSSYVANNPGAFVDAYWSINSLKVYQDDGDSTVAGVVDYGDDDDEDED
FT                   DDQDDGDDDSDDDDDDDDDSDSDDDSDDDGDDDDDDDDDDDDDDEDSRPWRGGRNHHGQ
FT                   MLNASTSTSSFPSPSFVKKARWEPRNYMAGMIF"
     MLVAMRRTAT LLSALGLTAQ LSSAAYTLQD DYSGSGFFDG FSFFTDTDPT NGFVDYVDEA        60
     TAQSNGYIST SGDYVYMGVD HTNVAGSSGR QSVRISSDAT YNHGLFILDL EHMPGGICGT       120
     WPAFWLVGAD WPNNGEIDII EGVNQQSGND MTLHTSDGCS ISSSSDFTGS MTTDNCYVYA       180
     AGQSSNAGCG ITDPDATSYG TAFNANGGGV FATEWTSDAI SIWFFERGSI PDDIDSGNPD       240
     PDSWGSPVAR FQGDCDIDSH FDGLQIIFDT TFCGDWAGNV WGSGSCASVA SSCSSYVANN       300
     PGAFVDAYWS INSLKVYQDD GDSTVAGVVD YGDDDDEDED DDQDDGDDDS DDDDDDDDDS       360
     DSDDDSDDDG DDDDDDDDDD DDDDEDSRPW RGGRNHHGQM LNASTSTSSF PSPSFVKKAR       420
     WEPRNYMAGM IF                                                           432
//

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