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Conserved domains on  [gi|1120121432|ref|WP_072991863|]
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amylo-alpha-1,6-glucosidase [Pseudozobellia thermophila]

Protein Classification

amylo-alpha-1,6-glucosidase( domain architecture ID 11465557)

amylo-alpha-1,6-glucosidase catalyzes the hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin and with 4-alpha-D-glucanotransferase, constitute a glycogen debranching enzyme

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
261-648 3.00e-156

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


:

Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 456.26  E-value: 3.00e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 261 HWIHRSKADLVSlmADTPTGKYPYAGVPWYNTAFGRDGIITALQTLWVAPRLSKDVLLFLADQQAtslnesidaEPGKIL 340
Cdd:COG3408     2 RALRRAADQLRT--NTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQE---------EPGKIP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 341 HEIRGGEMAamaelpfkkYYGTVDATPLFVMLAGEYHKRTGDLKTIKRIWKPIEKALDWIDRyGDIDQDGYVEYQAKskn 420
Cdd:COG3408    71 HEVRDGEEP---------YYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 421 GLTNQGWKDS-HDSIFhangqlaGGSIALCEVQGYVYSAKRHGARLAKLFGYDEKSARWEADAIRLKERFNRDFWDDTLN 499
Cdd:COG3408   138 GLDNQTWMDSkVDSVT-------PRSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 500 SYVLALDGNKEACKVKSSNA--GQVLFTGIADPEKADKLVKTLLQPDMFSGWGLRTLSSDEIRYNPMSYHNGSVWPHDVA 577
Cdd:COG3408   211 YLADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNG 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120121432 578 LVADGMGKYGYQEQALRLMTGLFDASLFTPLQRMPELFCGFgkrtgegpTAYPVACSPQAWSVAAVFLLLK 648
Cdd:COG3408   291 LYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGF--------DGYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
20-215 2.70e-56

N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the N-terminal of some glycogen debranching enzymes and is usually followed by the GDE_C (PF06202) and in this sense it is analogous (but probably not homologous) to the GDE_N (PF12439). Its exact function is unknown


:

Pssm-ID: 434175  Cd Length: 193  Bit Score: 190.11  E-value: 2.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432  20 LNHRDTFGIMNRSGDILPLGKEVHGIYHKDTRFVNQLRLRINQQLPVLLSSNIKEANEILSVDLTNPGHPlPDGRQMEQG 99
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPPGGGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDLTNPDLE-DDGGGLPDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 100 SIHIHRSQLVrNGNFHEKIELKNYQNETLPINLSLHFDGDFKDIFEIRGTRRDHRGSdRGHERIDDHTVVFSNQGLDGAI 179
Cdd:pfam14742  80 TLHIRRERFL-GGGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGRRARRGR-LLPPVVEGDELRLAYRGLDGVL 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1120121432 180 RKCKIVFNQPfSDFQTPGKVCFDLPLAPKELKCIEY 215
Cdd:pfam14742 158 RETRIRFDPA-PDELDGGRATFRVELAPGESWTLTL 192
 
Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
261-648 3.00e-156

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 456.26  E-value: 3.00e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 261 HWIHRSKADLVSlmADTPTGKYPYAGVPWYNTAFGRDGIITALQTLWVAPRLSKDVLLFLADQQAtslnesidaEPGKIL 340
Cdd:COG3408     2 RALRRAADQLRT--NTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQE---------EPGKIP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 341 HEIRGGEMAamaelpfkkYYGTVDATPLFVMLAGEYHKRTGDLKTIKRIWKPIEKALDWIDRyGDIDQDGYVEYQAKskn 420
Cdd:COG3408    71 HEVRDGEEP---------YYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 421 GLTNQGWKDS-HDSIFhangqlaGGSIALCEVQGYVYSAKRHGARLAKLFGYDEKSARWEADAIRLKERFNRDFWDDTLN 499
Cdd:COG3408   138 GLDNQTWMDSkVDSVT-------PRSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 500 SYVLALDGNKEACKVKSSNA--GQVLFTGIADPEKADKLVKTLLQPDMFSGWGLRTLSSDEIRYNPMSYHNGSVWPHDVA 577
Cdd:COG3408   211 YLADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNG 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120121432 578 LVADGMGKYGYQEQALRLMTGLFDASLFTPLQRMPELFCGFgkrtgegpTAYPVACSPQAWSVAAVFLLLK 648
Cdd:COG3408   291 LYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGF--------DGYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
20-215 2.70e-56

N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the N-terminal of some glycogen debranching enzymes and is usually followed by the GDE_C (PF06202) and in this sense it is analogous (but probably not homologous) to the GDE_N (PF12439). Its exact function is unknown


Pssm-ID: 434175  Cd Length: 193  Bit Score: 190.11  E-value: 2.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432  20 LNHRDTFGIMNRSGDILPLGKEVHGIYHKDTRFVNQLRLRINQQLPVLLSSNIKEANEILSVDLTNPGHPlPDGRQMEQG 99
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPPGGGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDLTNPDLE-DDGGGLPDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 100 SIHIHRSQLVrNGNFHEKIELKNYQNETLPINLSLHFDGDFKDIFEIRGTRRDHRGSdRGHERIDDHTVVFSNQGLDGAI 179
Cdd:pfam14742  80 TLHIRRERFL-GGGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGRRARRGR-LLPPVVEGDELRLAYRGLDGVL 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1120121432 180 RKCKIVFNQPfSDFQTPGKVCFDLPLAPKELKCIEY 215
Cdd:pfam14742 158 RETRIRFDPA-PDELDGGRATFRVELAPGESWTLTL 192
GDE_C pfam06202
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
275-643 6.16e-21

Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog Swiss:O93808 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).


Pssm-ID: 428822  Cd Length: 370  Bit Score: 95.09  E-value: 6.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 275 ADTPTGKYPYAGVPWYNTaFGRDGIItALQTLWVAPR---LSKDVLLFLADQqatslnesidaepgkilheIRGGEMAAM 351
Cdd:pfam06202  13 ASGKQGPSIIAGYHWFSD-WGRDTFI-ALPGLLLVTGrfeEARDIILTFAGY-------------------LRHGLIPNL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 352 AELPFKKYYGTVDATPLFVMLAGEYHKRTGDLKTIKRIWKPIEKALDW----IDRYGDIDQDGYVEYQAKSKNGLTnqgW 427
Cdd:pfam06202  72 FPAGGEPRYNTVDASLWFIYAVQKYLEYAPDAEFLRRIFPTIQEILGAyfkgTDFNIGLDPEDGLIHGGSRGNQLT---W 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 428 KDShdsifHANGQLAGGSI-ALCEVQGYVYSAKRHGARLAKLFGYDEKSaRWEADAIRLKERFNRDFWDDTLNsYVLALD 506
Cdd:pfam06202 149 MDA-----KVGGWPVTPRDgKAVEINALWYNALRFASRLANKILGEDKS-SYKELAEKIKDNFEKKFWNNKRG-ILYDVI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 507 GNKEACKVK-SSNAGQVLFTG--IADPEKADKLV----KTLLQPdmfsgWGLRTLSSDEIRYNP----------MSYHNG 569
Cdd:pfam06202 222 DPSLPKDYQlRPNFLIALSLAptLLSPEKAKKALdlaeEELLTP-----YGLRTLDPDDPDYLGtyrgdqdsrdMAYHQG 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1120121432 570 SVWPHDVALVADGMGKYGY-QEQALRLMTGLFDAS---LFT-PLQRMPELFCGFGKRTGEGptaypvaCSPQAWSVAAV 643
Cdd:pfam06202 297 TVWPWLIGYFLRAKLKFGDdSKLALDLVAPLLEGHykhLQEaGWGGIPELFDGDGPYCPRG-------CIAQAWSVAEI 368
PRK10137 PRK10137
alpha-glucosidase; Provisional
394-601 1.28e-13

alpha-glucosidase; Provisional


Pssm-ID: 236653  Cd Length: 786  Bit Score: 74.42  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 394 EKALDWIDRYGDIDQDgyvEYQAKSKNGLTNQGWK----DSHDsifhANGQLAGGSIALCEVQ--GYVYSAKRHGARLAK 467
Cdd:PRK10137  524 ESGRDDAAVFGFIDKE---QLDKYVANGGKRSDWTvkfaENRS----QDGTLLGYSLLQESVDqaSYMYSDNHYLAEMAT 596
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 468 LFGYDEKSARWEADAIRLKERFNRDFWDDTLNSY-----VLALDGNKEACKV-----KSSNAGQVLFTGIADPEKADKLV 537
Cdd:PRK10137  597 ILGKPEEAKRYRQLAQQLADYINTCMFDETTGFYydvriEDKPLANGCAGKPivergKGPEGWSPLFNGAATQANADAVV 676
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1120121432 538 KTLLQPDMFSGW-GLRTLSSDEIRYNPMSYHNGSVWPHDVALVADGMGKYGYQEQALRLMTGLFD 601
Cdd:PRK10137  677 KVMLDPKEFNTFvPLGTAALTNPAFGADIYWRGRVWVDQFYFGLKGMERYGYRDDALKLADTFFR 741
 
Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
261-648 3.00e-156

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 456.26  E-value: 3.00e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 261 HWIHRSKADLVSlmADTPTGKYPYAGVPWYNTAFGRDGIITALQTLWVAPRLSKDVLLFLADQQAtslnesidaEPGKIL 340
Cdd:COG3408     2 RALRRAADQLRT--NTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQE---------EPGKIP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 341 HEIRGGEMAamaelpfkkYYGTVDATPLFVMLAGEYHKRTGDLKTIKRIWKPIEKALDWIDRyGDIDQDGYVEYQAKskn 420
Cdd:COG3408    71 HEVRDGEEP---------YYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 421 GLTNQGWKDS-HDSIFhangqlaGGSIALCEVQGYVYSAKRHGARLAKLFGYDEKSARWEADAIRLKERFNRDFWDDTLN 499
Cdd:COG3408   138 GLDNQTWMDSkVDSVT-------PRSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 500 SYVLALDGNKEACKVKSSNA--GQVLFTGIADPEKADKLVKTLLQPDMFSGWGLRTLSSDEIRYNPMSYHNGSVWPHDVA 577
Cdd:COG3408   211 YLADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNG 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120121432 578 LVADGMGKYGYQEQALRLMTGLFDASLFTPLQRMPELFCGFgkrtgegpTAYPVACSPQAWSVAAVFLLLK 648
Cdd:COG3408   291 LYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGF--------DGYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
20-215 2.70e-56

N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the N-terminal of some glycogen debranching enzymes and is usually followed by the GDE_C (PF06202) and in this sense it is analogous (but probably not homologous) to the GDE_N (PF12439). Its exact function is unknown


Pssm-ID: 434175  Cd Length: 193  Bit Score: 190.11  E-value: 2.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432  20 LNHRDTFGIMNRSGDILPLGKEVHGIYHKDTRFVNQLRLRINQQLPVLLSSNIKEANEILSVDLTNPGHPlPDGRQMEQG 99
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPPGGGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDLTNPDLE-DDGGGLPDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 100 SIHIHRSQLVrNGNFHEKIELKNYQNETLPINLSLHFDGDFKDIFEIRGTRRDHRGSdRGHERIDDHTVVFSNQGLDGAI 179
Cdd:pfam14742  80 TLHIRRERFL-GGGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGRRARRGR-LLPPVVEGDELRLAYRGLDGVL 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1120121432 180 RKCKIVFNQPfSDFQTPGKVCFDLPLAPKELKCIEY 215
Cdd:pfam14742 158 RETRIRFDPA-PDELDGGRATFRVELAPGESWTLTL 192
GDE_C pfam06202
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
275-643 6.16e-21

Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog Swiss:O93808 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).


Pssm-ID: 428822  Cd Length: 370  Bit Score: 95.09  E-value: 6.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 275 ADTPTGKYPYAGVPWYNTaFGRDGIItALQTLWVAPR---LSKDVLLFLADQqatslnesidaepgkilheIRGGEMAAM 351
Cdd:pfam06202  13 ASGKQGPSIIAGYHWFSD-WGRDTFI-ALPGLLLVTGrfeEARDIILTFAGY-------------------LRHGLIPNL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 352 AELPFKKYYGTVDATPLFVMLAGEYHKRTGDLKTIKRIWKPIEKALDW----IDRYGDIDQDGYVEYQAKSKNGLTnqgW 427
Cdd:pfam06202  72 FPAGGEPRYNTVDASLWFIYAVQKYLEYAPDAEFLRRIFPTIQEILGAyfkgTDFNIGLDPEDGLIHGGSRGNQLT---W 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 428 KDShdsifHANGQLAGGSI-ALCEVQGYVYSAKRHGARLAKLFGYDEKSaRWEADAIRLKERFNRDFWDDTLNsYVLALD 506
Cdd:pfam06202 149 MDA-----KVGGWPVTPRDgKAVEINALWYNALRFASRLANKILGEDKS-SYKELAEKIKDNFEKKFWNNKRG-ILYDVI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 507 GNKEACKVK-SSNAGQVLFTG--IADPEKADKLV----KTLLQPdmfsgWGLRTLSSDEIRYNP----------MSYHNG 569
Cdd:pfam06202 222 DPSLPKDYQlRPNFLIALSLAptLLSPEKAKKALdlaeEELLTP-----YGLRTLDPDDPDYLGtyrgdqdsrdMAYHQG 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1120121432 570 SVWPHDVALVADGMGKYGY-QEQALRLMTGLFDAS---LFT-PLQRMPELFCGFGKRTGEGptaypvaCSPQAWSVAAV 643
Cdd:pfam06202 297 TVWPWLIGYFLRAKLKFGDdSKLALDLVAPLLEGHykhLQEaGWGGIPELFDGDGPYCPRG-------CIAQAWSVAEI 368
Bac_rhamnosid6H pfam17389
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial ...
337-505 9.06e-14

Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.


Pssm-ID: 407469  Cd Length: 340  Bit Score: 73.12  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 337 GKILHEIR-----GGEMAAMAELPFKKYYGTVDATPLFVMLAGEYHKRTGDLKTIKRIWKPIEKALDWIDRYGDIDQDGY 411
Cdd:pfam17389  66 AKWLRDLAdeqreNGAVPDVAPNVRGPGSPGPEWGDAIVIVPWALYRNYGDTRILQDQYPSMKRWLDYLLQRSDDGLWGL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 412 veyqakSKNGLTNQGWKDSHDSIFHANGQLaggsIALCevqgYVYSAKRHGARLAKLFGYDEKSARWEADAIRLKERFNR 491
Cdd:pfam17389 146 ------SGWGLGDWLDPDGRPGDAPTPGDL----VATA----YYYRSLGLMAKMAELLGKDEDAKRYAALAEELKAAFNK 211
                         170       180
                  ....*....|....*....|..
gi 1120121432 492 DFWD--------DTLNSYVLAL 505
Cdd:pfam17389 212 KYLDtetgsyanDTQTANALPL 233
PRK10137 PRK10137
alpha-glucosidase; Provisional
394-601 1.28e-13

alpha-glucosidase; Provisional


Pssm-ID: 236653  Cd Length: 786  Bit Score: 74.42  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 394 EKALDWIDRYGDIDQDgyvEYQAKSKNGLTNQGWK----DSHDsifhANGQLAGGSIALCEVQ--GYVYSAKRHGARLAK 467
Cdd:PRK10137  524 ESGRDDAAVFGFIDKE---QLDKYVANGGKRSDWTvkfaENRS----QDGTLLGYSLLQESVDqaSYMYSDNHYLAEMAT 596
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 468 LFGYDEKSARWEADAIRLKERFNRDFWDDTLNSY-----VLALDGNKEACKV-----KSSNAGQVLFTGIADPEKADKLV 537
Cdd:PRK10137  597 ILGKPEEAKRYRQLAQQLADYINTCMFDETTGFYydvriEDKPLANGCAGKPivergKGPEGWSPLFNGAATQANADAVV 676
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1120121432 538 KTLLQPDMFSGW-GLRTLSSDEIRYNPMSYHNGSVWPHDVALVADGMGKYGYQEQALRLMTGLFD 601
Cdd:PRK10137  677 KVMLDPKEFNTFvPLGTAALTNPAFGADIYWRGRVWVDQFYFGLKGMERYGYRDDALKLADTFFR 741
TreA COG1626
Neutral trehalase [Carbohydrate transport and metabolism];
463-597 1.97e-06

Neutral trehalase [Carbohydrate transport and metabolism];


Pssm-ID: 441233  Cd Length: 438  Bit Score: 51.00  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 463 ARLAKLFGYDEKSARWEADAIRLKERFNRDFWDDTLNSYvlaLDGN-KEACKVKSSNAGQV--LFTGIADPEKADKLVKT 539
Cdd:COG1626   252 AKAYALAGDPAKAAEYRARAERRKEAINRYLWDEERGFY---FDYDfVTGKQTAVLSAAAFypLFAGIATPEQAARVAET 328
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1120121432 540 ----LLQPdmfsGwGLRTLSSDeirynpmS-----YHNGsvW-PHDVaLVADGMGKYGYQEQALRLMT 597
Cdd:COG1626   329 lepqLLKP----G-GLVTTLVN-------SgqqwdAPNG--WaPLQW-MAVKGLRNYGYDDLAREIAR 381
Trehalase pfam01204
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
367-595 1.32e-03

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: 41.93  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 367 PLFVMLAGEYHKRTGDLKTIKRIWKPIEKALD-WID--RYGDI--DQDGY--------------------VEYQAK-SKN 420
Cdd:pfam01204 181 PFLTDMVLLVYEKTEDDALLRRYLAALKKEYAfWMAnpRLDPVtgLSDGYllnrygvppetprpesyledVEYAEKlPKE 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 421 GLTNQ-----------GWkDSHDSIF---HANGQLAGG---SIALCEVQGYVYSAKRHGARLAKLFGYDEKSARWEADAI 483
Cdd:pfam01204 261 RPKAYnyrdlkagaesGW-DFSSRWVregHDTGYLAEIrttSLVPVDLNALLYKYEKDIAFFCDVLGDSETSAIWEERAE 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120121432 484 RLKERFNRDFWDDTLNSYvlaLDGN---KEACKVKSSNAGQVLFTGIADPEKADKLVKTLLQPDMFSG----WGLRTLSS 556
Cdd:pfam01204 340 QRRLAIDKYLWNEEAGVW---FDYDlkkRKQTNYFSATNFWPLWAGLASPDQAKMVAKVLPKLEESGLlvfpGGRPTSLL 416
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1120121432 557 DEIRynPMSYHNGsvWPHDVALVADGMGKYGYQEQALRL 595
Cdd:pfam01204 417 DSGQ--QWDYPNG--WAPLQWLAVEGLQRYGYDELAERL 451
SGA1 COG3387
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and ...
462-508 2.74e-03

Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism];


Pssm-ID: 442614 [Multi-domain]  Cd Length: 585  Bit Score: 40.92  E-value: 2.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1120121432 462 GARLAKLFGYDEKSARWEADAIRLKERFNRDFWDDTLNSYVLALDGN 508
Cdd:COG3387   411 AARLAELLGLPAPAERWRALADEIRAEILERGWDEERGAFVQAYGSD 457
 
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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