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Conserved domains on  [gi|221460681|ref|NP_733394|]
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uncharacterized protein Dmel_CG31013 [Drosophila melanogaster]

Protein Classification

prolyl 4-hydroxylase subunit alpha( domain architecture ID 10551047)

prolyl 4-hydroxylase catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins

CATH:  2.60.120.620
EC:  1.14.11.2
Gene Ontology:  GO:0004656|GO:0031418|GO:0005506
PubMed:  20199358|23489300

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 31-162 6.38e-47

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: 160.13  E-value: 6.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   31 SLVTMVPLLELEKKLIDNLENYTNALEQKLEIIRSQLLVIRAENEKGRRNAISYLSNPLNGFSIIRRLHQDWINWRKYME 110
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221460681  111 --QPVG-IWQLKAFYSWKDELPTERDLWDACEGIARIQSTYDLKVGDFINGNING 162
Cdd:pfam08336  81 tnQAVGfLEQLTEMRSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 336-513 9.32e-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: 144.45  E-value: 9.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   336 SAREISMLIGKAAQNMKNTKIhkERAVPKKNRG---RTAKGFWLKK-ESNELTKRITRRIMDMTGF---DLADSEGFQVI 408
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEV--TRGIGNPNETsqyRQSNGTWLELlERDLVIERIRQRLADFLGLlagLPLSAEDAQVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   409 NYGIGGHYFLHMDYFDFassnhtdtrsrysidlGDRIATVLFYLTDVEQGGATVFGDVGYY----VSPQAGTAIFWYNld 484
Cdd:smart00702  79 RYGPGGHYGPHVDNFLY----------------GDRIATFILYLNDVEEGGELVFPGLRLMvvatVKPKKGDLLFFPS-- 140

                          170       180
                   ....*....|....*....|....*....
gi 221460681   485 tdgnGDPRTRHAACPVIVGSKWVMTEWIR 513
Cdd:smart00702 141 ----GHGRSLHGVCPVTRGSRWAITGWIR 165
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 181-256 5.42e-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: 43.07  E-value: 5.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460681 181 LFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG4235   61 LLAAGDTEEAEELLERA-------LALDPDN-----PEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLL 124
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 31-162 6.38e-47

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: 160.13  E-value: 6.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   31 SLVTMVPLLELEKKLIDNLENYTNALEQKLEIIRSQLLVIRAENEKGRRNAISYLSNPLNGFSIIRRLHQDWINWRKYME 110
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221460681  111 --QPVG-IWQLKAFYSWKDELPTERDLWDACEGIARIQSTYDLKVGDFINGNING 162
Cdd:pfam08336  81 tnQAVGfLEQLTEMRSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 336-513 9.32e-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: 144.45  E-value: 9.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   336 SAREISMLIGKAAQNMKNTKIhkERAVPKKNRG---RTAKGFWLKK-ESNELTKRITRRIMDMTGF---DLADSEGFQVI 408
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEV--TRGIGNPNETsqyRQSNGTWLELlERDLVIERIRQRLADFLGLlagLPLSAEDAQVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   409 NYGIGGHYFLHMDYFDFassnhtdtrsrysidlGDRIATVLFYLTDVEQGGATVFGDVGYY----VSPQAGTAIFWYNld 484
Cdd:smart00702  79 RYGPGGHYGPHVDNFLY----------------GDRIATFILYLNDVEEGGELVFPGLRLMvvatVKPKKGDLLFFPS-- 140

                          170       180
                   ....*....|....*....|....*....
gi 221460681   485 tdgnGDPRTRHAACPVIVGSKWVMTEWIR 513
Cdd:smart00702 141 ----GHGRSLHGVCPVTRGSRWAITGWIR 165
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 318-534 4.27e-24

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 102.82  E-value: 4.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681 318 KTEQIGLDPYVVLYHEVLSAREISMLIGKAAQNMKNTKIHKERAVPK-KNRGRTAKGFWLKKESNELTKRITRRIMDMTG 396
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSGKSvMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681 397 FDLADSEGFQVINYGIGGHYFLHMDYFdfassnHTDTRSRYSidlGDRIATVLFYLTDVEQGGATVFGDV---------- 466
Cdd:PLN00052 126 LPEENAENIQILRYEHGQKYEPHFDYF------HDKINQALG---GHRYATVLMYLSTVDKGGETVFPNAegwenqpkdd 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460681 467 --------GYYVSPQAGTAIFWYNLDTDGNGDPRTRHAACPVIVGSKWVMTEWIReKRQIFIRPCLPK-AKGTSTKS 534
Cdd:PLN00052 197 tfsecahkGLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIH-IRSYEHPPVVPKdTEGCADKS 272
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 405-513 1.60e-19

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: 83.19  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681  405 FQVINYGIGGHYFLHMDYFDFASSNhtdtrsrysidlGDRIATVLFYLTDV--EQGGATVFGDVGYY--VSPQAGTAIFW 480
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGG------------GQRRLTVVLYLNDWeeEEGGELVLYDGDGVedIKPKKGRLVLF 68

                          90       100       110
                  ....*....|....*....|....*....|...
gi 221460681  481 YNldtdgngDPRTRHAACPVIVGSKWVMTEWIR 513
Cdd:pfam13640  69 PS-------SELSLHEVLPVTGGERWSITGWFR 94
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 181-256 5.42e-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: 43.07  E-value: 5.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460681 181 LFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG4235   61 LLAAGDTEEAEELLERA-------LALDPDN-----PEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLL 124
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 31-162 6.38e-47

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: 160.13  E-value: 6.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   31 SLVTMVPLLELEKKLIDNLENYTNALEQKLEIIRSQLLVIRAENEKGRRNAISYLSNPLNGFSIIRRLHQDWINWRKYME 110
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221460681  111 --QPVG-IWQLKAFYSWKDELPTERDLWDACEGIARIQSTYDLKVGDFINGNING 162
Cdd:pfam08336  81 tnQAVGfLEQLTEMRSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 336-513 9.32e-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: 144.45  E-value: 9.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   336 SAREISMLIGKAAQNMKNTKIhkERAVPKKNRG---RTAKGFWLKK-ESNELTKRITRRIMDMTGF---DLADSEGFQVI 408
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEV--TRGIGNPNETsqyRQSNGTWLELlERDLVIERIRQRLADFLGLlagLPLSAEDAQVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681   409 NYGIGGHYFLHMDYFDFassnhtdtrsrysidlGDRIATVLFYLTDVEQGGATVFGDVGYY----VSPQAGTAIFWYNld 484
Cdd:smart00702  79 RYGPGGHYGPHVDNFLY----------------GDRIATFILYLNDVEEGGELVFPGLRLMvvatVKPKKGDLLFFPS-- 140

                          170       180
                   ....*....|....*....|....*....
gi 221460681   485 tdgnGDPRTRHAACPVIVGSKWVMTEWIR 513
Cdd:smart00702 141 ----GHGRSLHGVCPVTRGSRWAITGWIR 165
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 318-534 4.27e-24

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 102.82  E-value: 4.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681 318 KTEQIGLDPYVVLYHEVLSAREISMLIGKAAQNMKNTKIHKERAVPK-KNRGRTAKGFWLKKESNELTKRITRRIMDMTG 396
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSGKSvMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681 397 FDLADSEGFQVINYGIGGHYFLHMDYFdfassnHTDTRSRYSidlGDRIATVLFYLTDVEQGGATVFGDV---------- 466
Cdd:PLN00052 126 LPEENAENIQILRYEHGQKYEPHFDYF------HDKINQALG---GHRYATVLMYLSTVDKGGETVFPNAegwenqpkdd 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460681 467 --------GYYVSPQAGTAIFWYNLDTDGNGDPRTRHAACPVIVGSKWVMTEWIReKRQIFIRPCLPK-AKGTSTKS 534
Cdd:PLN00052 197 tfsecahkGLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIH-IRSYEHPPVVPKdTEGCADKS 272
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 405-513 1.60e-19

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: 83.19  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681  405 FQVINYGIGGHYFLHMDYFDFASSNhtdtrsrysidlGDRIATVLFYLTDV--EQGGATVFGDVGYY--VSPQAGTAIFW 480
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGG------------GQRRLTVVLYLNDWeeEEGGELVLYDGDGVedIKPKKGRLVLF 68

                          90       100       110
                  ....*....|....*....|....*....|...
gi 221460681  481 YNldtdgngDPRTRHAACPVIVGSKWVMTEWIR 513
Cdd:pfam13640  69 PS-------SELSLHEVLPVTGGERWSITGWFR 94
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 181-256 5.42e-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: 43.07  E-value: 5.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221460681 181 LFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG4235   61 LLAAGDTEEAEELLERA-------LALDPDN-----PEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLL 124
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 402-514 3.11e-04

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


Pssm-ID: 397334 [Multi-domain]  Cd Length: 101  Bit Score: 40.13  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681  402 SEGFQVINYgigghYFLHMDYF-DFASSNHTDtrsrysidlgdriATVLFYLTDVEQGGATVFGDVGYYVSPQAGTAI-- 478
Cdd:pfam03171   1 PDQCLVLNY-----YPPHPDPDlTLGLGPHTD-------------ASILTILLQDDVGGLQVFKDGKWIDVPPLPGALvv 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 221460681  479 -------FWYNldtdgNGDPRTRHAACPVIVG-SKWVMTEWIRE 514
Cdd:pfam03171  63 nigdqleLLSN-----GRYKSVLHRVLPVNKGkERISIAFFLRP 101
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 178-256 7.24e-04

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: 39.79  E-value: 7.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPrhlpiKEVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG4783   45 GEILLQLGDLDEAIVLLHEA-------LELDP-----DEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLR 111
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 178-256 1.04e-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: 39.40  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG4783   11 AQALLLAGDYDEAEALLEKA-------LELDPDN-----PEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLN 77
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 178-256 1.66e-03

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: 38.83  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKA-------LRLDPDN-----ADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL 90
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 178-256 1.77e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG2956  151 AELYLEQGDYDEAIEALEKA-------LKLDPDC-----ARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPR 217
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 178-256 4.66e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 4.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRL 256
Cdd:COG3914  119 GNLLLALGRLEEALAALRRA-------LALNPDF-----AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 194-260 7.57e-03

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 38.74  E-value: 7.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221460681 194 LQEVPQRlqEELLIQ-PRHLPIKEVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRLWKKT 260
Cdd:COG3071   63 LGDYERR--DEYLAQaLELAPEAELAVLLTRAELLLDQGQAEQALATLEALRAGAPRHPQVLRLLLQA 128
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
178-254 9.24e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.06  E-value: 9.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVL 254
Cdd:COG0457   15 GLAYRRLGRYEEAIEDYEKA-------LELDPDD-----AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEAL 79
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 178-257 9.36e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.82  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221460681 178 GAYLFMKNRPSDAIQWLQEVpqrlqeeLLIQPRHlpikeVDALRLLAEAQIKDQNYSEALPLLHNCLKLQPHDARVLRLW 257
Cdd:COG3914  153 GEALRRLGRLEEAIAALRRA-------LELDPDN-----AEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
 
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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