Species | UMGS1994 sp900556975 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; UMGS1994; UMGS1994 sp900556975 | |||||||||||
CAZyme ID | MGYG000002811_00149 | |||||||||||
CAZy Family | GT39 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 10368; End: 12092 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT39 | 161 | 362 | 2.4e-48 | 0.9237668161434978 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam16192 | PMT_4TMC | 1.91e-24 | 393 | 565 | 1 | 198 | C-terminal four TMM region of protein-O-mannosyltransferase. PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes. |
COG1928 | PMT1 | 5.89e-19 | 164 | 570 | 46 | 696 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]. |
pfam13231 | PMT_2 | 3.13e-18 | 191 | 351 | 2 | 154 | Dolichyl-phosphate-mannose-protein mannosyltransferase. This family contains members that are not captured by pfam02366. |
pfam02366 | PMT | 4.42e-16 | 160 | 358 | 15 | 235 | Dolichyl-phosphate-mannose-protein mannosyltransferase. This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families. |
COG1807 | ArnT | 1.71e-14 | 191 | 353 | 64 | 219 | 4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEH68061.1 | 1.44e-115 | 14 | 565 | 22 | 551 |
ADZ82369.1 | 1.86e-115 | 14 | 565 | 19 | 548 |
QUI22495.1 | 8.96e-89 | 9 | 567 | 408 | 967 |
QGQ95333.1 | 3.14e-88 | 18 | 569 | 394 | 988 |
QGQ95357.1 | 6.19e-85 | 18 | 569 | 704 | 1279 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6P25_A | 9.25e-06 | 371 | 570 | 508 | 730 | Structureof S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_A Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
L8F4Z2 | 5.29e-28 | 168 | 567 | 67 | 515 | Probable dolichyl-phosphate-mannose--protein mannosyltransferase OS=Mycolicibacterium smegmatis (strain MKD8) OX=1214915 GN=pmt PE=3 SV=1 |
Q8NRZ6 | 2.52e-14 | 191 | 567 | 99 | 519 | Probable dolichyl-phosphate-mannose--protein mannosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=pmt PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.855368 | 0.117393 | 0.022928 | 0.000736 | 0.000376 | 0.003192 |
start | end |
---|---|
7 | 24 |
210 | 232 |
266 | 285 |
305 | 327 |
340 | 362 |
450 | 469 |
476 | 493 |
497 | 519 |
526 | 548 |
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