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Conserved domains on  [gi|24651430|ref|NP_733378|]
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prolyl-4-hydroxylase-alpha NE2 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 342-513 9.96e-41

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


:

Pssm-ID: 214780  Cd Length: 165  Bit Score: 144.84  E-value: 9.96e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    342 SQKESTLIRTSSKEHMLPSATTDPDASDDETqvDTYRTSKSVWYS-SDFNDTTKKITERLGDATGL---DMNSTEFYQVI 417
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNET--SQYRQSNGTWLElLERDLVIERIRQRLADFLGLlagLPLSAEDAQVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    418 NYGLGGFFETHLDMLLseknrfngTSDRIATTLFYLNEVRQGGGTYFPRLNL----TVFPQPGSALFWYNLDTKgndhmg 493
Cdd:smart00702  79 RYGPGGHYGPHVDNFL--------YGDRIATFILYLNDVEEGGELVFPGLRLmvvaTVKPKKGDLLFFPSGHGR------ 144

                          170       180
                   ....*....|....*....|
gi 24651430    494 SLHTGCPVIVGSKWVMSKWI 513
Cdd:smart00702 145 SLHGVCPVTRGSRWAITGWI 164
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 33-163 1.32e-29

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


:

Pssm-ID: 462433  Cd Length: 135  Bit Score: 113.14  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    33 SVVNMDDMLNLEDDLVSNVEKLAEALARKAKTIKWGVFKMMKRRQEYKSSME-IFANPIDTFSLIRHMQSNWLMWLLYLE 111
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEeYLSNPLNAFSLIKRLHQDWPKWEKLMK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24651430   112 TPVGQEELFFVD---SRMPLLPKYFDFIDAAEGIRKMQATYQMFSSDIAKGLLDG 163
Cdd:pfam08336  81 TNQAVGFLEQLTemrSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 217-260 3.25e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 43.84  E-value: 3.25e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24651430 217 PKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPEIYEEY 260
Cdd:COG4235  14 PNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 176-254 5.70e-03

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


:

Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 35.77  E-value: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24651430   176 LAIGLHLMNNSRWYAAEQWISASIEAYDqkssqtdmellRGPKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDP 254
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFP-----------ESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 342-513 9.96e-41

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 144.84  E-value: 9.96e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    342 SQKESTLIRTSSKEHMLPSATTDPDASDDETqvDTYRTSKSVWYS-SDFNDTTKKITERLGDATGL---DMNSTEFYQVI 417
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNET--SQYRQSNGTWLElLERDLVIERIRQRLADFLGLlagLPLSAEDAQVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    418 NYGLGGFFETHLDMLLseknrfngTSDRIATTLFYLNEVRQGGGTYFPRLNL----TVFPQPGSALFWYNLDTKgndhmg 493
Cdd:smart00702  79 RYGPGGHYGPHVDNFL--------YGDRIATFILYLNDVEEGGELVFPGLRLmvvaTVKPKKGDLLFFPSGHGR------ 144

                          170       180
                   ....*....|....*....|
gi 24651430    494 SLHTGCPVIVGSKWVMSKWI 513
Cdd:smart00702 145 SLHGVCPVTRGSRWAITGWI 164
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 33-163 1.32e-29

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 113.14  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    33 SVVNMDDMLNLEDDLVSNVEKLAEALARKAKTIKWGVFKMMKRRQEYKSSME-IFANPIDTFSLIRHMQSNWLMWLLYLE 111
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEeYLSNPLNAFSLIKRLHQDWPKWEKLMK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24651430   112 TPVGQEELFFVD---SRMPLLPKYFDFIDAAEGIRKMQATYQMFSSDIAKGLLDG 163
Cdd:pfam08336  81 TNQAVGFLEQLTemrSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 414-513 9.98e-17

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 75.49  E-value: 9.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430   414 YQVINYGLGGFFETHLDMLLSEKnrfnGTSDRIATTLFYLNEVR--QGGGT--YFPRLNLTVFPQPGSALFWYNldtkgn 489
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE----GGGQRRLTVVLYLNDWEeeEGGELvlYDGDGVEDIKPKKGRLVLFPS------ 70

                          90       100
                  ....*....|....*....|....
gi 24651430   490 dHMGSLHTGCPVIVGSKWVMSKWI 513
Cdd:pfam13640  71 -SELSLHEVLPVTGGERWSITGWF 93
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 324-528 4.88e-16

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 78.94  E-value: 4.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430  324 KTEILSIDPFVVLLHDMISQKESTLIRTSSKEHMLPSATTDPDASddETQVDTYRTSKSVWYSSDFNDTTKKITERLGDA 403
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSG--KSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAW 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430  404 TGLDMNSTEFYQVINYGLGGFFETHLDMLLSEKNRFNGtSDRIATTLFYLNEVRQGGGTYFPRLN--------------- 468
Cdd:PLN00052 124 TFLPEENAENIQILRYEHGQKYEPHFDYFHDKINQALG-GHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfseca 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430  469 ---LTVFPQPGSALFWYNLDTKGNDHMGSLHTGCPVIVGSKWVMSKWINDMGQE-------FTRPCVESS 528
Cdd:PLN00052 203 hkgLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYEhppvvpkDTEGCADKS 272
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 217-260 3.25e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 43.84  E-value: 3.25e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24651430 217 PKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPEIYEEY 260
Cdd:COG4235  14 PNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 220-252 9.77e-04

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 36.73  E-value: 9.77e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 24651430   220 ADLCRILGQVQMKQRNHEGALQAYQVALKLSPH 252
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 176-254 5.70e-03

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 35.77  E-value: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24651430   176 LAIGLHLMNNSRWYAAEQWISASIEAYDqkssqtdmellRGPKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDP 254
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFP-----------ESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 342-513 9.96e-41

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 144.84  E-value: 9.96e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    342 SQKESTLIRTSSKEHMLPSATTDPDASDDETqvDTYRTSKSVWYS-SDFNDTTKKITERLGDATGL---DMNSTEFYQVI 417
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNET--SQYRQSNGTWLElLERDLVIERIRQRLADFLGLlagLPLSAEDAQVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    418 NYGLGGFFETHLDMLLseknrfngTSDRIATTLFYLNEVRQGGGTYFPRLNL----TVFPQPGSALFWYNLDTKgndhmg 493
Cdd:smart00702  79 RYGPGGHYGPHVDNFL--------YGDRIATFILYLNDVEEGGELVFPGLRLmvvaTVKPKKGDLLFFPSGHGR------ 144

                          170       180
                   ....*....|....*....|
gi 24651430    494 SLHTGCPVIVGSKWVMSKWI 513
Cdd:smart00702 145 SLHGVCPVTRGSRWAITGWI 164
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 33-163 1.32e-29

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 113.14  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430    33 SVVNMDDMLNLEDDLVSNVEKLAEALARKAKTIKWGVFKMMKRRQEYKSSME-IFANPIDTFSLIRHMQSNWLMWLLYLE 111
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEeYLSNPLNAFSLIKRLHQDWPKWEKLMK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24651430   112 TPVGQEELFFVD---SRMPLLPKYFDFIDAAEGIRKMQATYQMFSSDIAKGLLDG 163
Cdd:pfam08336  81 TNQAVGFLEQLTemrSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 414-513 9.98e-17

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 75.49  E-value: 9.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430   414 YQVINYGLGGFFETHLDMLLSEKnrfnGTSDRIATTLFYLNEVR--QGGGT--YFPRLNLTVFPQPGSALFWYNldtkgn 489
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE----GGGQRRLTVVLYLNDWEeeEGGELvlYDGDGVEDIKPKKGRLVLFPS------ 70

                          90       100
                  ....*....|....*....|....
gi 24651430   490 dHMGSLHTGCPVIVGSKWVMSKWI 513
Cdd:pfam13640  71 -SELSLHEVLPVTGGERWSITGWF 93
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 324-528 4.88e-16

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 78.94  E-value: 4.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430  324 KTEILSIDPFVVLLHDMISQKESTLIRTSSKEHMLPSATTDPDASddETQVDTYRTSKSVWYSSDFNDTTKKITERLGDA 403
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSG--KSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAW 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430  404 TGLDMNSTEFYQVINYGLGGFFETHLDMLLSEKNRFNGtSDRIATTLFYLNEVRQGGGTYFPRLN--------------- 468
Cdd:PLN00052 124 TFLPEENAENIQILRYEHGQKYEPHFDYFHDKINQALG-GHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfseca 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430  469 ---LTVFPQPGSALFWYNLDTKGNDHMGSLHTGCPVIVGSKWVMSKWINDMGQE-------FTRPCVESS 528
Cdd:PLN00052 203 hkgLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYEhppvvpkDTEGCADKS 272
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 217-260 3.25e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 43.84  E-value: 3.25e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24651430 217 PKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPEIYEEY 260
Cdd:COG4235  14 PNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 213-257 5.12e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 5.12e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24651430 213 LLRGPKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPEIY 257
Cdd:COG3914 139 LALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEAL 183
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 220-252 9.77e-04

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 36.73  E-value: 9.77e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 24651430   220 ADLCRILGQVQMKQRNHEGALQAYQVALKLSPH 252
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 217-266 2.03e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.63  E-value: 2.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24651430 217 PKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPEIYEEYRILEKR 266
Cdd:COG4783  69 PDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA 118
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 226-257 2.91e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 2.91e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 24651430 226 LGQVQMKQRNHEGALQAYQVALKLSPHDPEIY 257
Cdd:COG5010  94 LALLYSRSGDKDEAKEYYEKALALSPDNPNAY 125
TPR_11 pfam13414
TPR repeat;
227-257 3.44e-03

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 35.53  E-value: 3.44e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 24651430   227 GQVQMKQRNHEGALQAYQVALKLSPHDPEIY 257
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAY 31
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 176-260 4.92e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 37.48  E-value: 4.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24651430 176 LAIGLHLMNNSRWYAAEQWISASIEAYdqkssqtdmellrgPKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPE 255
Cdd:COG4783   8 YALAQALLLAGDYDEAEALLEKALELD--------------PDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE 73


                ....*
gi 24651430 256 IYEEY 260
Cdd:COG4783  74 ARLNL 78
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 176-254 5.70e-03

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 35.77  E-value: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24651430   176 LAIGLHLMNNSRWYAAEQWISASIEAYDqkssqtdmellRGPKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDP 254
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFP-----------ESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
217-257 7.07e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.45  E-value: 7.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24651430 217 PKLADLCRILGQVQMKQRNHEGALQAYQVALKLSPHDPEIY 257
Cdd:COG0457  39 PDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEAL 79
TPR_1 pfam00515
Tetratricopeptide repeat;
220-253 7.81e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 34.32  E-value: 7.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 24651430   220 ADLCRILGQVQMKQRNHEGALQAYQVALKLSPHD 253
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
 
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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