NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034633909|ref|XP_016862114|]
View 

procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GT_LH super family cl45890
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ...
 1-174 2.84e-122

catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The lysyl hydroxylase (LH) family includes LH1-3. LH1 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 or PLOD1) and LH2 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 or PLOD2) form hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. LH3 (EC 1.14.11.4/EC 2.4.1.50/EC 2.4.1.66), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3), or multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, is a multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. It converts collagen lysines into 1,2-glucosylgalactosyl-5-hydroxylysines through three consecutive reactions: hydroxylation of collagen lysines (LH activity), N-linked conjugation of galactose to hydroxylysines (GT activity), and conjugation of glucose to galactosyl-5-hydroxylysines (GGT activity). LH3 monomer encompasses three domains; the first two N-terminal domains (catalytic glycosyltransferase domain and accessory domain) show Rossmann-fold architectures reminiscent of glycosyltransferases, whereas the C-terminal domain is characterized by a double-stranded beta-helix (DSBH) fold, highly conserved among the 2-oxoglutarate, Fe2+-dependent dioxygenases. This model corresponds to the N-terminal catalytic glycosyltransferase (GT) domain, which is solely responsible for glycosyltransferase activities (both GT and GGT).


The actual alignment was detected with superfamily member cd23003:

Pssm-ID: 459235  Cd Length: 230  Bit Score: 362.61  E-value: 2.84e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909   1 MKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGY 80
Cdd:cd23003    57 LKEEMESLADQEDLVVLFTDSYDVIFAGGPEEVLKKFQQANHKVVFAAEGLIWPDKRLAEKYPVVRSGKRFLNSGGFIGY 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  81 APYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAI 160
Cdd:cd23003   137 APYINRIVQQWNLQDNDDDQLFYTKIYIDPLQRESINITLDHKCRIFQNLNGAVDEVLLKFENGKARVRNTVYETLPVVI 216

                         170
                  ....*....|....
gi 1034633909 161 NGNGPTKILLNYFG 174
Cdd:cd23003   217 HGNGPTKLLLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 501-664 2.57e-20

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: 88.21  E-value: 2.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  501 SEKACDELVEEMEHYGKwsggkhhDSRISGGYENVPTDDI--HMKQVDLENVWLHFIREFIAPVTLKVFAGYY-TKGFAL 577
Cdd:smart00702   1 SPAECQKLLEEAEPLGW-------RGEVTRGIGNPNETSQyrQSNGTWLELLERDLVIERIRQRLADFLGLLAgLPLSAE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  578 LNFVVKYspERQRSLRPHHDAS-----TFTINIALNNVgedFQGGGCKFLRYNCSIES---PRKGWSFMHP-GRLTHLHE 648
Cdd:smart00702  74 DAQVARY--GPGGHYGPHVDNFlygdrIATFILYLNDV---EEGGELVFPGLRLMVVAtvkPKKGDLLFFPsGHGRSLHG 148

                          170
                   ....*....|....*.
gi 1034633909  649 GLPVKNGTRYIAVSFI 664
Cdd:smart00702 149 VCPVTRGSRWAITGWI 164
 
Name Accession Description Interval E-value
GT_LH2 cd23003
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar ...
 1-174 2.84e-122

catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar proteins; Lysyl hydroxylase 2 (LH2; EC 1.14.11.4), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2), forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. The model corresponds to the N-terminal conserved domain of LH2, which shows high sequence similarity with catalytic glycosyltransferase (GT) domain of LH3.


Pssm-ID: 438559  Cd Length: 230  Bit Score: 362.61  E-value: 2.84e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909   1 MKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGY 80
Cdd:cd23003    57 LKEEMESLADQEDLVVLFTDSYDVIFAGGPEEVLKKFQQANHKVVFAAEGLIWPDKRLAEKYPVVRSGKRFLNSGGFIGY 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  81 APYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAI 160
Cdd:cd23003   137 APYINRIVQQWNLQDNDDDQLFYTKIYIDPLQRESINITLDHKCRIFQNLNGAVDEVLLKFENGKARVRNTVYETLPVVI 216

                         170
                  ....*....|....
gi 1034633909 161 NGNGPTKILLNYFG 174
Cdd:cd23003   217 HGNGPTKLLLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 501-664 2.57e-20

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: 88.21  E-value: 2.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  501 SEKACDELVEEMEHYGKwsggkhhDSRISGGYENVPTDDI--HMKQVDLENVWLHFIREFIAPVTLKVFAGYY-TKGFAL 577
Cdd:smart00702   1 SPAECQKLLEEAEPLGW-------RGEVTRGIGNPNETSQyrQSNGTWLELLERDLVIERIRQRLADFLGLLAgLPLSAE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  578 LNFVVKYspERQRSLRPHHDAS-----TFTINIALNNVgedFQGGGCKFLRYNCSIES---PRKGWSFMHP-GRLTHLHE 648
Cdd:smart00702  74 DAQVARY--GPGGHYGPHVDNFlygdrIATFILYLNDV---EEGGELVFPGLRLMVVAtvkPKKGDLLFFPsGHGRSLHG 148

                          170
                   ....*....|....*.
gi 1034633909  649 GLPVKNGTRYIAVSFI 664
Cdd:smart00702 149 VCPVTRGSRWAITGWI 164
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 586-666 8.92e-10

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: 56.31  E-value: 8.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909 586 PERQRSLRPHHDASTFTINIALNNVGEDFQGGGCkFLRYNCSIES--PRKG--WSFMHPGRL-THLHEGLPV-KNGTRYI 659
Cdd:pfam03171  16 PDLTLGLGPHTDASILTILLQDDVGGLQVFKDGK-WIDVPPLPGAlvVNIGdqLELLSNGRYkSVLHRVLPVnKGKERIS 94


                  ....*..
gi 1034633909 660 AVSFIDP 666
Cdd:pfam03171  95 IAFFLRP 101
 
Name Accession Description Interval E-value
GT_LH2 cd23003
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar ...
 1-174 2.84e-122

catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar proteins; Lysyl hydroxylase 2 (LH2; EC 1.14.11.4), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2), forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. The model corresponds to the N-terminal conserved domain of LH2, which shows high sequence similarity with catalytic glycosyltransferase (GT) domain of LH3.


Pssm-ID: 438559  Cd Length: 230  Bit Score: 362.61  E-value: 2.84e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909   1 MKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGY 80
Cdd:cd23003    57 LKEEMESLADQEDLVVLFTDSYDVIFAGGPEEVLKKFQQANHKVVFAAEGLIWPDKRLAEKYPVVRSGKRFLNSGGFIGY 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  81 APYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAI 160
Cdd:cd23003   137 APYINRIVQQWNLQDNDDDQLFYTKIYIDPLQRESINITLDHKCRIFQNLNGAVDEVLLKFENGKARVRNTVYETLPVVI 216

                         170
                  ....*....|....
gi 1034633909 161 NGNGPTKILLNYFG 174
Cdd:cd23003   217 HGNGPTKLLLNYLG 230
GT_LH1 cd23004
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ...
 1-174 4.31e-93

catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar proteins; LH1 (EC 1.14.11.4), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (PLOD1), forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. This model corresponds to the N-terminal conserved domain of LH1, which shows high sequence similarity with catalytic glycosyltransferase (GT) domain of LH3.


Pssm-ID: 438560  Cd Length: 230  Bit Score: 287.46  E-value: 4.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909   1 MKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGY 80
Cdd:cd23004    57 LKSALEPYADKEDLVILFIESYDVIFASGPAELLKKFQQAKSKVVFSAENLIYPDRHLEAKYPHVRDGKRFLGSGGFIGY 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  81 APYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAI 160
Cdd:cd23004   137 APNLYKMVSDWSGQDDDSDQLFYTKIFLDPEKREKINITLDHRCRIFQNLNGALDEVVLKFEDGRVRARNLLYDTLPVII 216

                         170
                  ....*....|....
gi 1034633909 161 NGNGPTKILLNYFG 174
Cdd:cd23004   217 HGNGPTKLQLNYLG 230
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 1-174 5.51e-90

catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar proteins; Lysyl hydroxylase 3 (LH3; EC 1.14.11.4/EC 2.4.1.50/EC 2.4.1.66), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3), or multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, is a multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. It converts collagen lysines into 1,2-glucosylgalactosyl-5-hydroxylysines through three consecutive reactions: hydroxylation of collagen lysines (LH activity), N-linked conjugation of galactose to hydroxylysines (GT activity), and conjugation of glucose to galactosyl-5-hydroxylysines (GGT activity). LH3 monomer encompasses three domains; the first two N-terminal domains (catalytic glycosyltransferase domain and accessory domain) show Rossmann-fold architectures reminiscent of glycosyltransferases, whereas the C-terminal domain is characterized by a double-stranded beta-helix (DSBH) fold, highly conserved among the 2-oxoglutarate, Fe2+-dependent dioxygenases. This model corresponds to the N-terminal catalytic glycosyltransferase (GT) domain, which is solely responsible for glycosyltransferase activities (both GT and GGT).


Pssm-ID: 438558  Cd Length: 230  Bit Score: 279.39  E-value: 5.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909   1 MKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGY 80
Cdd:cd23002    57 LKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGF 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  81 APYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAI 160
Cdd:cd23002   137 ATTIHQIVQQWKYKDDDDDQLFYTRLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVV 216

                         170
                  ....*....|....
gi 1034633909 161 NGNGPTKILLNYFG 174
Cdd:cd23002   217 HGNGPTKLQLNYLG 230
GT_LH cd22997
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ...
 1-165 9.58e-42

catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The lysyl hydroxylase (LH) family includes LH1-3. LH1 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 or PLOD1) and LH2 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 or PLOD2) form hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. LH3 (EC 1.14.11.4/EC 2.4.1.50/EC 2.4.1.66), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3), or multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, is a multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. It converts collagen lysines into 1,2-glucosylgalactosyl-5-hydroxylysines through three consecutive reactions: hydroxylation of collagen lysines (LH activity), N-linked conjugation of galactose to hydroxylysines (GT activity), and conjugation of glucose to galactosyl-5-hydroxylysines (GGT activity). LH3 monomer encompasses three domains; the first two N-terminal domains (catalytic glycosyltransferase domain and accessory domain) show Rossmann-fold architectures reminiscent of glycosyltransferases, whereas the C-terminal domain is characterized by a double-stranded beta-helix (DSBH) fold, highly conserved among the 2-oxoglutarate, Fe2+-dependent dioxygenases. This model corresponds to the N-terminal catalytic glycosyltransferase (GT) domain, which is solely responsible for glycosyltransferase activities (both GT and GGT).


Pssm-ID: 438557  Cd Length: 247  Bit Score: 151.78  E-value: 9.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909   1 MKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKAN-----HKVVFAADGILWPDKRLADKYPVV---------- 65
Cdd:cd22997    51 LLEYLESLKLPDDDLVLFVDGYDVWFQLPPEELLERFLALNaaairQPIVFSAEKNCWPDDSLAPAYPAVppsplppdid 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  66 ------HIGKRYLNSGGFIGYAPYVNRIVQQW-----NLQDNDDDQLFYTKVYID-PLKREAINITLDHKCKIFQTLNGA 133
Cdd:cd22997   131 ddldssKTRPRYLNSGGIIGRAGDLRELLEAAlelieDEKDWDDDQLVFTELYLEqEYWRYEFGIGLDYESELFQTLNGS 210

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034633909 134 VDEVVLKFEN-----GKARAKNTFYETLPVAINGNGP 165
Cdd:cd22997   211 ESDLELLSYDdppplGESRLRNTVTGTVPVVLHFNGP 247
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 501-664 2.57e-20

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: 88.21  E-value: 2.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  501 SEKACDELVEEMEHYGKwsggkhhDSRISGGYENVPTDDI--HMKQVDLENVWLHFIREFIAPVTLKVFAGYY-TKGFAL 577
Cdd:smart00702   1 SPAECQKLLEEAEPLGW-------RGEVTRGIGNPNETSQyrQSNGTWLELLERDLVIERIRQRLADFLGLLAgLPLSAE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909  578 LNFVVKYspERQRSLRPHHDAS-----TFTINIALNNVgedFQGGGCKFLRYNCSIES---PRKGWSFMHP-GRLTHLHE 648
Cdd:smart00702  74 DAQVARY--GPGGHYGPHVDNFlygdrIATFILYLNDV---EEGGELVFPGLRLMVVAtvkPKKGDLLFFPsGHGRSLHG 148

                          170
                   ....*....|....*.
gi 1034633909  649 GLPVKNGTRYIAVSFI 664
Cdd:smart00702 149 VCPVTRGSRWAITGWI 164
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 586-666 8.92e-10

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: 56.31  E-value: 8.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633909 586 PERQRSLRPHHDASTFTINIALNNVGEDFQGGGCkFLRYNCSIES--PRKG--WSFMHPGRL-THLHEGLPV-KNGTRYI 659
Cdd:pfam03171  16 PDLTLGLGPHTDASILTILLQDDVGGLQVFKDGK-WIDVPPLPGAlvVNIGdqLELLSNGRYkSVLHRVLPVnKGKERIS 94


                  ....*..
gi 1034633909 660 AVSFIDP 666
Cdd:pfam03171  95 IAFFLRP 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH