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Conserved domains on  [gi|1622940812|ref|XP_001101549|]
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beta-mannosidase isoform X2 [Macaca mulatta]

Protein Classification

beta-mannosidase( domain architecture ID 14312054)

beta-mannosidase, a glycoside hydrolase family 2 protein, is an exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
46-661 9.16e-68

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


:

Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 237.35  E-value: 9.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  46 WTYSKEFKIPfEISKWQKVNLILEGVDTISKILFNEVTIGETDNMFNRYSFDITNVVRD-VNSIELRFQSAVLYAAQQSk 124
Cdd:COG3250    54 GWYRRTFTVP-ASWKGKRVFLHFEGVDTAAEVWVNGKKVGYHEGGFTPFEFDITDYLKPgENVLAVRVDNPSDGSYLEG- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 125 ahtrypvppdcpplvqkgechvnfvrkeqcsfsWDWgpsFPTQGIWKDVRIEAYNICHLNDFTFSPiyDKSAQAWNLEIE 204
Cdd:COG3250   132 ---------------------------------QDW---WRTSGIYRDVWLEATPKVHIEDVFVTP--DLDDGSATLTVE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 205 ATFDVVSSKPVggQVIVAIP----KLQTQQMYNLELQPGK-RIVELFLNISKnitVETWWPHghgNQTGYNMTILFELDG 279
Cdd:COG3250   174 VELENESDAGV--TVEVTLLdadgKVVATATAKVTLAAGEeNTVTLTLTVPN---PKLWSPE---DPNLYTLVVTLKDDG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 280 GLNIEKSAKVYFRTVELIEEpikgspglsFYFKINGFPVFLKGSNWI---PADSfqDRVTSELLRLLLQSVVDANMNTLR 356
Cdd:COG3250   246 KVVDTVSTRFGFRTIEIDGD---------GGFLLNGKPVFLKGVNRHedwPDDG--RAVTDEAMRRDLELMKEAGFNAVR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 357 VWGGgiYEQDEFYELCDELGIMVWQDFMFACALYPT-DQGFLDSVRAEVAYQIKRLKSHPSIIIWSGNNENEEAlmmnWY 435
Cdd:COG3250   315 TSHY--PEDPEFYDLCDELGLLVWDEAPFEWHGMLGdDPEFLEAVEAELREMVRRDRNHPSIILWSGGNESGGG----PN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 436 HISITDrpiYIKDYvtlyvknirelvlagDKSRPFitssptngaetvaegwvsqnpnsnyfgdvhfydyisdcwnwkvfp 515
Cdd:COG3250   389 FAALYE---WVKEL---------------DPTRPV--------------------------------------------- 405
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 516 raRFASEYGYQSWPSFstlekvsstedwsfsskfslhRQHHEGGNKQMLYQAGLHFklpestdplrtfkdtiyltqvmqa 595
Cdd:COG3250   406 --RFLSEYGHAMPNSL---------------------GGGYHQPSDFEEYQALQAL------------------------ 438
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622940812 596 qcvKTETEFYRRgrseivdqQGHTMGALYWQLNDIWQAP--------SWASLEY-GGKWKMLHYFAQNFFAPLLP 661
Cdd:COG3250   439 ---EEYWEAFRR--------RPRLAGGFIWQLNDYWPEPrdndgnfcSWGLVDYyDRTPKPAYYEVKSAWQPVLV 502
Ig_mannosidase pfam17753
Ig-fold domain; This Ig-like fold domain is found in mannosidase enzymes.
769-845 6.69e-25

Ig-fold domain; This Ig-like fold domain is found in mannosidase enzymes.


:

Pssm-ID: 465483  Cd Length: 78  Bit Score: 98.87  E-value: 6.69e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622940812 769 KAQITAIISQQGDIFVFDLETSAVAPFVWLDVGSIPGRFSDNGFLMTE-KTRTILFYPWEPTSKSELEQSFHVTSLTD 845
Cdd:pfam17753   1 DPEITATVTETDGGFEITLTADALALFVWLELAGVDGRFSDNYFDLLPgEPKTVTFTPGEDTTLEELKKSLTVRSLYD 78
Mannosidase_ig pfam17786
Mannosidase Ig/CBM-like domain; This domain corresponds to domain 4 in the structure of ...
668-763 1.88e-10

Mannosidase Ig/CBM-like domain; This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.


:

Pssm-ID: 465505  Cd Length: 90  Bit Score: 57.97  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 668 NTFYIYGVSDLHSDYSMTLTVRVHTWSSLEPVCScvTEHLVMKGGEAVRLYEEPVSELLrrcGNCTRESCVVSFYLSADH 747
Cdd:pfam17786   1 GKLEVWVVNDTLEPVKGTLELRLIDFDGKVLYER--TVDVTVPANSSTEVASLDFAELL---GGADPRSVVLVARLLADG 75
                          90
                  ....*....|....*.
gi 1622940812 748 ELLSpTNYHFLSSLKE 763
Cdd:pfam17786  76 EVLA-RNVYYFVPPKD 90
LRRC37AB_C super family cl20801
LRRC37A/B like protein 1 C-terminal domain; This family represents the C-terminal domain of ...
1-27 2.57e-05

LRRC37A/B like protein 1 C-terminal domain; This family represents the C-terminal domain of the putative Leucine Rich Repeat Containing protein 37A or protein 37B (LRRC37A/B) found in eukaryotes. The Leucine Rich Repeats (LRR) lies in the central region. The gene that encodes this protein is found in the chromosomal position 17q11.2, and its microdeletion results in the disease, neurofibromatosis type-1 (NF1). The function of the protein, LRRC37B is unknown, however experimental data shows expression in the aorta, heart, skeletal muscle, liver and brain during gestation.


The actual alignment was detected with superfamily member pfam14914:

Pssm-ID: 464370  Cd Length: 147  Bit Score: 45.10  E-value: 2.57e-05
                          10        20
                  ....*....|....*....|....*..
gi 1622940812   1 MDQWKTESCINESTEAQSKQKEQKSSE 27
Cdd:pfam14914  76 TDQWKNENYINESTEAQSKQKKQSSRE 102
 
Name Accession Description Interval E-value
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
46-661 9.16e-68

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 237.35  E-value: 9.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  46 WTYSKEFKIPfEISKWQKVNLILEGVDTISKILFNEVTIGETDNMFNRYSFDITNVVRD-VNSIELRFQSAVLYAAQQSk 124
Cdd:COG3250    54 GWYRRTFTVP-ASWKGKRVFLHFEGVDTAAEVWVNGKKVGYHEGGFTPFEFDITDYLKPgENVLAVRVDNPSDGSYLEG- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 125 ahtrypvppdcpplvqkgechvnfvrkeqcsfsWDWgpsFPTQGIWKDVRIEAYNICHLNDFTFSPiyDKSAQAWNLEIE 204
Cdd:COG3250   132 ---------------------------------QDW---WRTSGIYRDVWLEATPKVHIEDVFVTP--DLDDGSATLTVE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 205 ATFDVVSSKPVggQVIVAIP----KLQTQQMYNLELQPGK-RIVELFLNISKnitVETWWPHghgNQTGYNMTILFELDG 279
Cdd:COG3250   174 VELENESDAGV--TVEVTLLdadgKVVATATAKVTLAAGEeNTVTLTLTVPN---PKLWSPE---DPNLYTLVVTLKDDG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 280 GLNIEKSAKVYFRTVELIEEpikgspglsFYFKINGFPVFLKGSNWI---PADSfqDRVTSELLRLLLQSVVDANMNTLR 356
Cdd:COG3250   246 KVVDTVSTRFGFRTIEIDGD---------GGFLLNGKPVFLKGVNRHedwPDDG--RAVTDEAMRRDLELMKEAGFNAVR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 357 VWGGgiYEQDEFYELCDELGIMVWQDFMFACALYPT-DQGFLDSVRAEVAYQIKRLKSHPSIIIWSGNNENEEAlmmnWY 435
Cdd:COG3250   315 TSHY--PEDPEFYDLCDELGLLVWDEAPFEWHGMLGdDPEFLEAVEAELREMVRRDRNHPSIILWSGGNESGGG----PN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 436 HISITDrpiYIKDYvtlyvknirelvlagDKSRPFitssptngaetvaegwvsqnpnsnyfgdvhfydyisdcwnwkvfp 515
Cdd:COG3250   389 FAALYE---WVKEL---------------DPTRPV--------------------------------------------- 405
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 516 raRFASEYGYQSWPSFstlekvsstedwsfsskfslhRQHHEGGNKQMLYQAGLHFklpestdplrtfkdtiyltqvmqa 595
Cdd:COG3250   406 --RFLSEYGHAMPNSL---------------------GGGYHQPSDFEEYQALQAL------------------------ 438
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622940812 596 qcvKTETEFYRRgrseivdqQGHTMGALYWQLNDIWQAP--------SWASLEY-GGKWKMLHYFAQNFFAPLLP 661
Cdd:COG3250   439 ---EEYWEAFRR--------RPRLAGGFIWQLNDYWPEPrdndgnfcSWGLVDYyDRTPKPAYYEVKSAWQPVLV 502
Ig_mannosidase pfam17753
Ig-fold domain; This Ig-like fold domain is found in mannosidase enzymes.
769-845 6.69e-25

Ig-fold domain; This Ig-like fold domain is found in mannosidase enzymes.


Pssm-ID: 465483  Cd Length: 78  Bit Score: 98.87  E-value: 6.69e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622940812 769 KAQITAIISQQGDIFVFDLETSAVAPFVWLDVGSIPGRFSDNGFLMTE-KTRTILFYPWEPTSKSELEQSFHVTSLTD 845
Cdd:pfam17753   1 DPEITATVTETDGGFEITLTADALALFVWLELAGVDGRFSDNYFDLLPgEPKTVTFTPGEDTTLEELKKSLTVRSLYD 78
ebgA PRK10340
cryptic beta-D-galactosidase subunit alpha; Reviewed
166-425 7.16e-11

cryptic beta-D-galactosidase subunit alpha; Reviewed


Pssm-ID: 236673 [Multi-domain]  Cd Length: 1021  Bit Score: 66.24  E-value: 7.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  166 TQGIWKDVRIEAYNICHLNDFTFSPIYDKSAQAWNLEIEATFDVVSSKPVGGQVIVAipkLQTQQMYNLELQPGKRIVEL 245
Cdd:PRK10340   194 LAGIFRDVYLVGKPLTHINDFTVRTDFDEDYCDATLSCEVVLENLAASPVVTTLEYT---LFDGERVVHSSAIDHLAIEK 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  246 FLNISKNITVE--TWW----PHGhgnqtgYNMTI-LFELDGGLNIEKSAKVYFRTVElieepIKGspGLsfyFKINGFPV 318
Cdd:PRK10340   271 LTSASFAFTVEqpQQWsaesPYL------YHLVMtLKDANGNVLEVVPQRVGFRDIK-----VRD--GL---FWINNRYV 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  319 FLKGSNWIPADSFQDRVTSEL-----LRLLLQSvvdaNMNTLRVwggGIYEQDE-FYELCDELGIMVWQDfmfacalypT 392
Cdd:PRK10340   335 KLHGVNRHDNDHRKGRAVGMDrvekdIQLMKQH----NINSVRT---AHYPNDPrFYELCDIYGLFVMAE---------T 398
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622940812  393 D---QGF---------LDSVRAEVAY------QIKRLKSHPSIIIWSGNNE 425
Cdd:PRK10340   399 DvesHGFanvgdisriTDDPQWEKVYvdrivrHIHAQKNHPSIIIWSLGNE 449
Mannosidase_ig pfam17786
Mannosidase Ig/CBM-like domain; This domain corresponds to domain 4 in the structure of ...
668-763 1.88e-10

Mannosidase Ig/CBM-like domain; This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.


Pssm-ID: 465505  Cd Length: 90  Bit Score: 57.97  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 668 NTFYIYGVSDLHSDYSMTLTVRVHTWSSLEPVCScvTEHLVMKGGEAVRLYEEPVSELLrrcGNCTRESCVVSFYLSADH 747
Cdd:pfam17786   1 GKLEVWVVNDTLEPVKGTLELRLIDFDGKVLYER--TVDVTVPANSSTEVASLDFAELL---GGADPRSVVLVARLLADG 75
                          90
                  ....*....|....*.
gi 1622940812 748 ELLSpTNYHFLSSLKE 763
Cdd:pfam17786  76 EVLA-RNVYYFVPPKD 90
Glyco_hydro_2_C pfam02836
Glycosyl hydrolases family 2, TIM barrel domain; This family contains beta-galactosidase, ...
311-425 1.98e-06

Glycosyl hydrolases family 2, TIM barrel domain; This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.


Pssm-ID: 397119 [Multi-domain]  Cd Length: 302  Bit Score: 50.52  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 311 FKINGFPVFLKGSN---WipADSFQDRVTSELLRLLLQSVVDANMNTLRVwggGIY-EQDEFYELCDELGIMV------- 379
Cdd:pfam02836   8 FLINGKPFYFRGVNrheD--HDRRGRGFDMDLMVKDIQLMKQNNINAVRT---SHYpNHPEWYQLCDEYGIYVideanle 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622940812 380 ----WQDFMFACALY--PTDQGFLDSVRAEVAYQ-IKRLKSHPSIIIWSGNNE 425
Cdd:pfam02836  83 thglWQKFGEIEPSYseLTDNPEWLPAHLERAEElVQRDKNHPSVIIWSLGNE 135
LRRC37AB_C pfam14914
LRRC37A/B like protein 1 C-terminal domain; This family represents the C-terminal domain of ...
1-27 2.57e-05

LRRC37A/B like protein 1 C-terminal domain; This family represents the C-terminal domain of the putative Leucine Rich Repeat Containing protein 37A or protein 37B (LRRC37A/B) found in eukaryotes. The Leucine Rich Repeats (LRR) lies in the central region. The gene that encodes this protein is found in the chromosomal position 17q11.2, and its microdeletion results in the disease, neurofibromatosis type-1 (NF1). The function of the protein, LRRC37B is unknown, however experimental data shows expression in the aorta, heart, skeletal muscle, liver and brain during gestation.


Pssm-ID: 464370  Cd Length: 147  Bit Score: 45.10  E-value: 2.57e-05
                          10        20
                  ....*....|....*....|....*..
gi 1622940812   1 MDQWKTESCINESTEAQSKQKEQKSSE 27
Cdd:pfam14914  76 TDQWKNENYINESTEAQSKQKKQSSRE 102
 
Name Accession Description Interval E-value
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
46-661 9.16e-68

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 237.35  E-value: 9.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  46 WTYSKEFKIPfEISKWQKVNLILEGVDTISKILFNEVTIGETDNMFNRYSFDITNVVRD-VNSIELRFQSAVLYAAQQSk 124
Cdd:COG3250    54 GWYRRTFTVP-ASWKGKRVFLHFEGVDTAAEVWVNGKKVGYHEGGFTPFEFDITDYLKPgENVLAVRVDNPSDGSYLEG- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 125 ahtrypvppdcpplvqkgechvnfvrkeqcsfsWDWgpsFPTQGIWKDVRIEAYNICHLNDFTFSPiyDKSAQAWNLEIE 204
Cdd:COG3250   132 ---------------------------------QDW---WRTSGIYRDVWLEATPKVHIEDVFVTP--DLDDGSATLTVE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 205 ATFDVVSSKPVggQVIVAIP----KLQTQQMYNLELQPGK-RIVELFLNISKnitVETWWPHghgNQTGYNMTILFELDG 279
Cdd:COG3250   174 VELENESDAGV--TVEVTLLdadgKVVATATAKVTLAAGEeNTVTLTLTVPN---PKLWSPE---DPNLYTLVVTLKDDG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 280 GLNIEKSAKVYFRTVELIEEpikgspglsFYFKINGFPVFLKGSNWI---PADSfqDRVTSELLRLLLQSVVDANMNTLR 356
Cdd:COG3250   246 KVVDTVSTRFGFRTIEIDGD---------GGFLLNGKPVFLKGVNRHedwPDDG--RAVTDEAMRRDLELMKEAGFNAVR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 357 VWGGgiYEQDEFYELCDELGIMVWQDFMFACALYPT-DQGFLDSVRAEVAYQIKRLKSHPSIIIWSGNNENEEAlmmnWY 435
Cdd:COG3250   315 TSHY--PEDPEFYDLCDELGLLVWDEAPFEWHGMLGdDPEFLEAVEAELREMVRRDRNHPSIILWSGGNESGGG----PN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 436 HISITDrpiYIKDYvtlyvknirelvlagDKSRPFitssptngaetvaegwvsqnpnsnyfgdvhfydyisdcwnwkvfp 515
Cdd:COG3250   389 FAALYE---WVKEL---------------DPTRPV--------------------------------------------- 405
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 516 raRFASEYGYQSWPSFstlekvsstedwsfsskfslhRQHHEGGNKQMLYQAGLHFklpestdplrtfkdtiyltqvmqa 595
Cdd:COG3250   406 --RFLSEYGHAMPNSL---------------------GGGYHQPSDFEEYQALQAL------------------------ 438
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622940812 596 qcvKTETEFYRRgrseivdqQGHTMGALYWQLNDIWQAP--------SWASLEY-GGKWKMLHYFAQNFFAPLLP 661
Cdd:COG3250   439 ---EEYWEAFRR--------RPRLAGGFIWQLNDYWPEPrdndgnfcSWGLVDYyDRTPKPAYYEVKSAWQPVLV 502
Ig_mannosidase pfam17753
Ig-fold domain; This Ig-like fold domain is found in mannosidase enzymes.
769-845 6.69e-25

Ig-fold domain; This Ig-like fold domain is found in mannosidase enzymes.


Pssm-ID: 465483  Cd Length: 78  Bit Score: 98.87  E-value: 6.69e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622940812 769 KAQITAIISQQGDIFVFDLETSAVAPFVWLDVGSIPGRFSDNGFLMTE-KTRTILFYPWEPTSKSELEQSFHVTSLTD 845
Cdd:pfam17753   1 DPEITATVTETDGGFEITLTADALALFVWLELAGVDGRFSDNYFDLLPgEPKTVTFTPGEDTTLEELKKSLTVRSLYD 78
ebgA PRK10340
cryptic beta-D-galactosidase subunit alpha; Reviewed
166-425 7.16e-11

cryptic beta-D-galactosidase subunit alpha; Reviewed


Pssm-ID: 236673 [Multi-domain]  Cd Length: 1021  Bit Score: 66.24  E-value: 7.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  166 TQGIWKDVRIEAYNICHLNDFTFSPIYDKSAQAWNLEIEATFDVVSSKPVGGQVIVAipkLQTQQMYNLELQPGKRIVEL 245
Cdd:PRK10340   194 LAGIFRDVYLVGKPLTHINDFTVRTDFDEDYCDATLSCEVVLENLAASPVVTTLEYT---LFDGERVVHSSAIDHLAIEK 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  246 FLNISKNITVE--TWW----PHGhgnqtgYNMTI-LFELDGGLNIEKSAKVYFRTVElieepIKGspGLsfyFKINGFPV 318
Cdd:PRK10340   271 LTSASFAFTVEqpQQWsaesPYL------YHLVMtLKDANGNVLEVVPQRVGFRDIK-----VRD--GL---FWINNRYV 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812  319 FLKGSNWIPADSFQDRVTSEL-----LRLLLQSvvdaNMNTLRVwggGIYEQDE-FYELCDELGIMVWQDfmfacalypT 392
Cdd:PRK10340   335 KLHGVNRHDNDHRKGRAVGMDrvekdIQLMKQH----NINSVRT---AHYPNDPrFYELCDIYGLFVMAE---------T 398
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622940812  393 D---QGF---------LDSVRAEVAY------QIKRLKSHPSIIIWSGNNE 425
Cdd:PRK10340   399 DvesHGFanvgdisriTDDPQWEKVYvdrivrHIHAQKNHPSIIIWSLGNE 449
Mannosidase_ig pfam17786
Mannosidase Ig/CBM-like domain; This domain corresponds to domain 4 in the structure of ...
668-763 1.88e-10

Mannosidase Ig/CBM-like domain; This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.


Pssm-ID: 465505  Cd Length: 90  Bit Score: 57.97  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 668 NTFYIYGVSDLHSDYSMTLTVRVHTWSSLEPVCScvTEHLVMKGGEAVRLYEEPVSELLrrcGNCTRESCVVSFYLSADH 747
Cdd:pfam17786   1 GKLEVWVVNDTLEPVKGTLELRLIDFDGKVLYER--TVDVTVPANSSTEVASLDFAELL---GGADPRSVVLVARLLADG 75
                          90
                  ....*....|....*.
gi 1622940812 748 ELLSpTNYHFLSSLKE 763
Cdd:pfam17786  76 EVLA-RNVYYFVPPKD 90
Glyco_hydro_2_C pfam02836
Glycosyl hydrolases family 2, TIM barrel domain; This family contains beta-galactosidase, ...
311-425 1.98e-06

Glycosyl hydrolases family 2, TIM barrel domain; This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.


Pssm-ID: 397119 [Multi-domain]  Cd Length: 302  Bit Score: 50.52  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940812 311 FKINGFPVFLKGSN---WipADSFQDRVTSELLRLLLQSVVDANMNTLRVwggGIY-EQDEFYELCDELGIMV------- 379
Cdd:pfam02836   8 FLINGKPFYFRGVNrheD--HDRRGRGFDMDLMVKDIQLMKQNNINAVRT---SHYpNHPEWYQLCDEYGIYVideanle 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622940812 380 ----WQDFMFACALY--PTDQGFLDSVRAEVAYQ-IKRLKSHPSIIIWSGNNE 425
Cdd:pfam02836  83 thglWQKFGEIEPSYseLTDNPEWLPAHLERAEElVQRDKNHPSVIIWSLGNE 135
LRRC37AB_C pfam14914
LRRC37A/B like protein 1 C-terminal domain; This family represents the C-terminal domain of ...
1-27 2.57e-05

LRRC37A/B like protein 1 C-terminal domain; This family represents the C-terminal domain of the putative Leucine Rich Repeat Containing protein 37A or protein 37B (LRRC37A/B) found in eukaryotes. The Leucine Rich Repeats (LRR) lies in the central region. The gene that encodes this protein is found in the chromosomal position 17q11.2, and its microdeletion results in the disease, neurofibromatosis type-1 (NF1). The function of the protein, LRRC37B is unknown, however experimental data shows expression in the aorta, heart, skeletal muscle, liver and brain during gestation.


Pssm-ID: 464370  Cd Length: 147  Bit Score: 45.10  E-value: 2.57e-05
                          10        20
                  ....*....|....*....|....*..
gi 1622940812   1 MDQWKTESCINESTEAQSKQKEQKSSE 27
Cdd:pfam14914  76 TDQWKNENYINESTEAQSKQKKQSSRE 102
 
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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