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Conserved domains on  [gi|24662595|ref|NP_729687|]
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procollagen lysyl hydroxylase, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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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 ...
 27-257 2.46e-76

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 cd23002:

Pssm-ID: 459235  Cd Length: 230  Bit Score: 245.10  E-value: 2.46e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595  27 DKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGDMQKP-GGGFKLNLLREAIAPYKNEPETIILFTDSYDV 105
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEWRGGDVARTvGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 106 IITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEVeGKASRFLNSGAFIGYAPQVFALLVD-PIEDTADDQLYF 184
Cdd:cd23002  81 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEV-GTGKRFLNSGGFIGFATTIHQIVQQwKYKDDDDDQLFY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24662595 185 TKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKvdLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYG 257
Cdd:cd23002 160 TRLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLK--FDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 555-719 1.35e-29

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: 115.18  E-value: 1.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595    555 SDAFCDDLVAIMEaHNGWSDGSNNDNRLEGgyeavptRDIHMKQVG---LERLYLKFLQMFVRPLQERAFTGYFHNPPRA 631
Cdd:smart00702   1 SPAECQKLLEEAE-PLGWRGEVTRGIGNPN-------ETSQYRQSNgtwLELLERDLVIERIRQRLADFLGLLAGLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595    632 LMNFMVRYRPDeqPSLRPHHD-----SSTYTINIAMNragIDYQGGGCRF---IRYNCSVTDTKKGWMLMHP-GRLTHYH 702
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDnflygDRIATFILYLN---DVEEGGELVFpglRLMVVATVKPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 24662595    703 EGLLVTNGTRYIMISFI 719
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 303-395 5.80e-04

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06439:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 251  Bit Score: 42.18  E-value: 5.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 303 LEGIESLNYPKEKLHLLIYSnvafhD------DDIksfvnkhAKEYATAKFALstDELDERQGRQLALDKA-RLHQSDYI 375
Cdd:cd06439  48 LENLLALDYPRDRLEIIVVS-----DgstdgtAEI-------AREYADKGVKL--LRFPERRGKAAALNRAlALATGEIV 113

                        90       100
                ....*....|....*....|
gi 24662595 376 FFVDADAHIDDgEVLRELLR 395
Cdd:cd06439 114 VFTDANALLDP-DALRLLVR 132
 
Name Accession Description Interval E-value
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 27-257 2.46e-76

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: 245.10  E-value: 2.46e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595  27 DKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGDMQKP-GGGFKLNLLREAIAPYKNEPETIILFTDSYDV 105
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEWRGGDVARTvGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 106 IITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEVeGKASRFLNSGAFIGYAPQVFALLVD-PIEDTADDQLYF 184
Cdd:cd23002  81 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEV-GTGKRFLNSGGFIGFATTIHQIVQQwKYKDDDDDQLFY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24662595 185 TKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKvdLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYG 257
Cdd:cd23002 160 TRLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLK--FDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 555-719 1.35e-29

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: 115.18  E-value: 1.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595    555 SDAFCDDLVAIMEaHNGWSDGSNNDNRLEGgyeavptRDIHMKQVG---LERLYLKFLQMFVRPLQERAFTGYFHNPPRA 631
Cdd:smart00702   1 SPAECQKLLEEAE-PLGWRGEVTRGIGNPN-------ETSQYRQSNgtwLELLERDLVIERIRQRLADFLGLLAGLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595    632 LMNFMVRYRPDeqPSLRPHHD-----SSTYTINIAMNragIDYQGGGCRF---IRYNCSVTDTKKGWMLMHP-GRLTHYH 702
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDnflygDRIATFILYLN---DVEEGGELVFpglRLMVVATVKPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 24662595    703 EGLLVTNGTRYIMISFI 719
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 303-395 5.80e-04

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 42.18  E-value: 5.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 303 LEGIESLNYPKEKLHLLIYSnvafhD------DDIksfvnkhAKEYATAKFALstDELDERQGRQLALDKA-RLHQSDYI 375
Cdd:cd06439  48 LENLLALDYPRDRLEIIVVS-----DgstdgtAEI-------AREYADKGVKL--LRFPERRGKAAALNRAlALATGEIV 113

                        90       100
                ....*....|....*....|
gi 24662595 376 FFVDADAHIDDgEVLRELLR 395
Cdd:cd06439 114 VFTDANALLDP-DALRLLVR 132
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 303-395 7.81e-04

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 42.04  E-value: 7.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 303 LEGIESLNYPKEKLHLLIYSNVAfhDDDIKSFVNKHAKEYATAKFalstDELDERQGRQLALDKA-RLHQSDYIFFVDAD 381
Cdd:COG1215  48 LRSLLAQDYPKEKLEVIVVDDGS--TDETAEIARELAAEYPRVRV----IERPENGGKAAALNAGlKAARGDIVVFLDAD 121

                        90
                ....*....|....
gi 24662595 382 AHIDDGeVLRELLR 395
Cdd:COG1215 122 TVLDPD-WLRRLVA 134
 
Name Accession Description Interval E-value
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 27-257 2.46e-76

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: 245.10  E-value: 2.46e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595  27 DKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGDMQKP-GGGFKLNLLREAIAPYKNEPETIILFTDSYDV 105
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEWRGGDVARTvGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 106 IITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEVeGKASRFLNSGAFIGYAPQVFALLVD-PIEDTADDQLYF 184
Cdd:cd23002  81 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEV-GTGKRFLNSGGFIGFATTIHQIVQQwKYKDDDDDQLFY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24662595 185 TKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKvdLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYG 257
Cdd:cd23002 160 TRLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLK--FDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
GT_LH1 cd23004
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ...
 27-257 9.95e-73

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: 235.46  E-value: 9.95e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595  27 DKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGD-MQKPGGGFKLNLLREAIAPYKNEPETIILFTDSYDV 105
Cdd:cd23004   1 ENLLVLTVATKETDGFRRFRRSAKFFNYKIQVLGLGEEWQGGDdMQPAGGGQKVRLLKSALEPYADKEDLVILFIESYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 106 IITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEV-EGKasRFLNSGAFIGYAPQVFALLVD-PIEDTADDQLY 183
Cdd:cd23004  81 IFASGPAELLKKFQQAKSKVVFSAENLIYPDRHLEAKYPHVrDGK--RFLGSGGFIGYAPNLYKMVSDwSGQDDDSDQLF 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24662595 184 FTKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKvdLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYG 257
Cdd:cd23004 159 YTKIFLDPEKREKINITLDHRCRIFQNLNGALDEVVLK--FEDGRVRARNLLYDTLPVIIHGNGPTKLQLNYLG 230
GT_LH2 cd23003
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar ...
 27-257 5.00e-66

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: 217.77  E-value: 5.00e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595  27 DKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGDMQKP-GGGFKLNLLREAIAPYKNEPETIILFTDSYDV 105
Cdd:cd23003   1 EKLLVLTVATKETDGFHRFMQSAKYFNYTVKVLGMGEEWKGGDVANSiGGGQKVRLLKEEMESLADQEDLVVLFTDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 106 IITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEVE-GKasRFLNSGAFIGYAPQVFALLVD-PIEDTADDQLY 183
Cdd:cd23003  81 IFAGGPEEVLKKFQQANHKVVFAAEGLIWPDKRLAEKYPVVRsGK--RFLNSGGFIGYAPYINRIVQQwNLQDNDDDQLF 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24662595 184 FTKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKvdLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYG 257
Cdd:cd23003 159 YTKIYIDPLQRESINITLDHKCRIFQNLNGAVDEVLLK--FENGKARVRNTVYETLPVVIHGNGPTKLLLNYLG 230
GT_LH cd22997
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ...
 30-247 4.12e-61

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: 205.32  E-value: 4.12e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595  30 KVFTVATEPTDGYTRYIRSARVYD-IEVTTLGLGEEWKGGDmqkPGGGFKLNLLREAIAPYKNEPETIILFTDSYDVIIT 108
Cdd:cd22997   1 HVLTPATKPNDGLCRTLLSAALLGyPPPTVLGWGEKWKGGD---GGHGAKIRLLLEYLESLKLPDDDLVLFVDGYDVWFQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 109 TTLDEIFEKFKESGA-----KILFSAEKYCWPDKSLANDYPEVEGKAS---------------RFLNSGAFIGYAPQVFA 168
Cdd:cd22997  78 LPPEELLERFLALNAaairqPIVFSAEKNCWPDDSLAPAYPAVPPSPLppdidddldssktrpRYLNSGGIIGRAGDLRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 169 LL------VDPIEDTADDQLYFTKIFLD-ETKRAKLGLKLDVQSRLFQNLHGAKNDVKLK---VDLESNQGVLQNVDFMT 238
Cdd:cd22997 158 LLeaalelIEDEKDWDDDQLVFTELYLEqEYWRYEFGIGLDYESELFQTLNGSESDLELLsydDPPPLGESRLRNTVTGT 237


                ....*....
gi 24662595 239 TPSIIHGNG 247
Cdd:cd22997 238 VPVVLHFNG 246
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 555-719 1.35e-29

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: 115.18  E-value: 1.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595    555 SDAFCDDLVAIMEaHNGWSDGSNNDNRLEGgyeavptRDIHMKQVG---LERLYLKFLQMFVRPLQERAFTGYFHNPPRA 631
Cdd:smart00702   1 SPAECQKLLEEAE-PLGWRGEVTRGIGNPN-------ETSQYRQSNgtwLELLERDLVIERIRQRLADFLGLLAGLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595    632 LMNFMVRYRPDeqPSLRPHHD-----SSTYTINIAMNragIDYQGGGCRF---IRYNCSVTDTKKGWMLMHP-GRLTHYH 702
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDnflygDRIATFILYLN---DVEEGGELVFpglRLMVVATVKPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 24662595    703 EGLLVTNGTRYIMISFI 719
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 303-395 5.80e-04

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 42.18  E-value: 5.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 303 LEGIESLNYPKEKLHLLIYSnvafhD------DDIksfvnkhAKEYATAKFALstDELDERQGRQLALDKA-RLHQSDYI 375
Cdd:cd06439  48 LENLLALDYPRDRLEIIVVS-----DgstdgtAEI-------AREYADKGVKL--LRFPERRGKAAALNRAlALATGEIV 113

                        90       100
                ....*....|....*....|
gi 24662595 376 FFVDADAHIDDgEVLRELLR 395
Cdd:cd06439 114 VFTDANALLDP-DALRLLVR 132
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 303-395 7.81e-04

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 42.04  E-value: 7.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662595 303 LEGIESLNYPKEKLHLLIYSNVAfhDDDIKSFVNKHAKEYATAKFalstDELDERQGRQLALDKA-RLHQSDYIFFVDAD 381
Cdd:COG1215  48 LRSLLAQDYPKEKLEVIVVDDGS--TDETAEIARELAAEYPRVRV----IERPENGGKAAALNAGlKAARGDIVVFLDAD 121

                        90
                ....*....|....
gi 24662595 382 AHIDDGeVLRELLR 395
Cdd:COG1215 122 TVLDPD-WLRRLVA 134
 
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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