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Conserved domains on  [gi|916891202|ref|WP_051498258|]
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MULTISPECIES: trehalase family glycosidase [unclassified Pseudoalteromonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TreA super family cl34326
Neutral trehalase [Carbohydrate transport and metabolism];
4-125 4.47e-62

Neutral trehalase [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG1626:

Pssm-ID: 441233  Cd Length: 438  Bit Score: 195.84  E-value: 4.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   4 PEQRFFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAV 83
Cdd:COG1626  285 EERGFYFDYDFVTGKQTAVLSAAAFYPLFAGIATPEQAARVAETLEPQLLKPGGLVTTLVNSGQQWDAPNGWAPLQWMAV 364
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 916891202  84 KGLRNYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNVCTP 125
Cdd:COG1626  365 KGLRNYGYDDLAREIARRWLALVERVYERTGKLVEKYNVVDP 406
 
Name Accession Description Interval E-value
TreA COG1626
Neutral trehalase [Carbohydrate transport and metabolism];
4-125 4.47e-62

Neutral trehalase [Carbohydrate transport and metabolism];


Pssm-ID: 441233  Cd Length: 438  Bit Score: 195.84  E-value: 4.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   4 PEQRFFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAV 83
Cdd:COG1626  285 EERGFYFDYDFVTGKQTAVLSAAAFYPLFAGIATPEQAARVAETLEPQLLKPGGLVTTLVNSGQQWDAPNGWAPLQWMAV 364
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 916891202  84 KGLRNYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNVCTP 125
Cdd:COG1626  365 KGLRNYGYDDLAREIARRWLALVERVYERTGKLVEKYNVVDP 406
Trehalase pfam01204
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
5-122 1.27e-35

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


Pssm-ID: 395961 [Multi-domain]  Cd Length: 509  Bit Score: 127.83  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202    5 EQRFFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVL--SEQF---LKVGGIVTTVVDTPQQWDSPNGWAPLQ 79
Cdd:pfam01204 353 EAGVWFDYDLKKRKQTNYFSATNFWPLWAGLASPDQAKMVAKVLpkLEESgllVFPGGRPTSLLDSGQQWDYPNGWAPLQ 432
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 916891202   80 WFAVKGLRNYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNV 122
Cdd:pfam01204 433 WLAVEGLQRYGYDELAERLAYRWLFTNTKAFVDEGKMVEKYDV 475
treF PRK13270
alpha,alpha-trehalase TreF;
9-122 2.10e-35

alpha,alpha-trehalase TreF;


Pssm-ID: 183934  Cd Length: 549  Bit Score: 127.61  E-value: 2.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   9 FVDYNHKVSKpSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAVKGLRN 88
Cdd:PRK13270 401 YRDYDWRREQ-LALFSAAAIVPLYVGMANHEQADRLANAVRSRLLTPGGILASEYETGEQWDKPNGWAPLQWMAIQGFKM 479
                         90       100       110
                 ....*....|....*....|....*....|....
gi 916891202  89 YGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNV 122
Cdd:PRK13270 480 YGDDLLGDEIARSWLKTVNQFYQEHHKLIEKYHI 513
 
Name Accession Description Interval E-value
TreA COG1626
Neutral trehalase [Carbohydrate transport and metabolism];
4-125 4.47e-62

Neutral trehalase [Carbohydrate transport and metabolism];


Pssm-ID: 441233  Cd Length: 438  Bit Score: 195.84  E-value: 4.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   4 PEQRFFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAV 83
Cdd:COG1626  285 EERGFYFDYDFVTGKQTAVLSAAAFYPLFAGIATPEQAARVAETLEPQLLKPGGLVTTLVNSGQQWDAPNGWAPLQWMAV 364
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 916891202  84 KGLRNYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNVCTP 125
Cdd:COG1626  365 KGLRNYGYDDLAREIARRWLALVERVYERTGKLVEKYNVVDP 406
Trehalase pfam01204
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
5-122 1.27e-35

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


Pssm-ID: 395961 [Multi-domain]  Cd Length: 509  Bit Score: 127.83  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202    5 EQRFFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVL--SEQF---LKVGGIVTTVVDTPQQWDSPNGWAPLQ 79
Cdd:pfam01204 353 EAGVWFDYDLKKRKQTNYFSATNFWPLWAGLASPDQAKMVAKVLpkLEESgllVFPGGRPTSLLDSGQQWDYPNGWAPLQ 432
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 916891202   80 WFAVKGLRNYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNV 122
Cdd:pfam01204 433 WLAVEGLQRYGYDELAERLAYRWLFTNTKAFVDEGKMVEKYDV 475
treF PRK13270
alpha,alpha-trehalase TreF;
9-122 2.10e-35

alpha,alpha-trehalase TreF;


Pssm-ID: 183934  Cd Length: 549  Bit Score: 127.61  E-value: 2.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   9 FVDYNHKVSKpSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAVKGLRN 88
Cdd:PRK13270 401 YRDYDWRREQ-LALFSAAAIVPLYVGMANHEQADRLANAVRSRLLTPGGILASEYETGEQWDKPNGWAPLQWMAIQGFKM 479
                         90       100       110
                 ....*....|....*....|....*....|....
gi 916891202  89 YGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNV 122
Cdd:PRK13270 480 YGDDLLGDEIARSWLKTVNQFYQEHHKLIEKYHI 513
treA PRK13272
alpha,alpha-trehalase TreA;
8-122 2.26e-33

alpha,alpha-trehalase TreA;


Pssm-ID: 183936  Cd Length: 542  Bit Score: 121.94  E-value: 2.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   8 FFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAVKGLR 87
Cdd:PRK13272 390 YYADYDWQTRTLSEQVTAAALYPLFAGLASDDRAKRTADSVRAQLLRPGGLATTALKTGQQWDEPNGWAPLQWVAVDGLR 469
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 916891202  88 NYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNV 122
Cdd:PRK13272 470 RYGEDALARTIGERFLAQVQALFAREHKLVEKYGL 504
treA PRK13271
alpha,alpha-trehalase TreA;
5-124 2.70e-32

alpha,alpha-trehalase TreA;


Pssm-ID: 237326  Cd Length: 569  Bit Score: 119.26  E-value: 2.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202   5 EQRFFVDYNHKVSKPSAILSAAASTPLFVNLASQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAVK 84
Cdd:PRK13271 387 KEGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKVAAATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATE 466
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 916891202  85 GLRNYGIDQLATRIMKNWLTMVEQDFIENKCLLEKYNVCT 124
Cdd:PRK13271 467 GLQNYGQKEVAMDVTWRFLTNVQHTYDREKKLVEKYDVSS 506
PLN02567 PLN02567
alpha,alpha-trehalase
29-122 1.37e-13

alpha,alpha-trehalase


Pssm-ID: 215307  Cd Length: 554  Bit Score: 66.21  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916891202  29 TPLFVNLA---SQQQAELVANVLSEQFLKVGGIVTTVVDTPQQWDSPNGWAPLQWFAVKGLRNYGID---QLATRIMKNW 102
Cdd:PLN02567 413 VPLWCGVVppgDAKVEKVVESLKSSGLVLPAGIATSLRNTGQQWDFPNAWAPLQHMIVEGLAASGSKegkALAEDIARRW 492
                         90       100
                 ....*....|....*....|
gi 916891202 103 LTMVEQDFIENKCLLEKYNV 122
Cdd:PLN02567 493 LRSNYVAYKKTGAMHEKYDA 512
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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