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Conserved domains on  [gi|32307144|ref|NP_000293|]
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procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_LH1 cd23004
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ...
 26-254 3.64e-167

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: 479.68  E-value: 3.64e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144  26 DNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGLGEDWNVEKG-TSAGGGQKVRLLKKALEKHADKEDLVILFADSYDV 104
Cdd:cd23004   1 ENLLVLTVATKETDGFRRFRRSAKFFNYKIQVLGLGEEWQGGDDmQPAGGGQKVRLLKSALEPYADKEDLVILFIESYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 105 LFASGPRELLKKFRQARSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQLFYT 184
Cdd:cd23004  81 IFASGPAELLKKFQQAKSKVVFSAENLIYPDRHLEAKYPHVRDGKRFLGSGGFIGYAPNLYKMVSDWSGQDDDSDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 185 KIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLG 254
Cdd:cd23004 161 KIFLDPEKREKINITLDHRCRIFQNLNGALDEVVLKFEDGRVRARNLLYDTLPVIIHGNGPTKLQLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 562-725 5.40e-26

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: 104.78  E-value: 5.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144    562 TEVACDELVEEMEHFGqWSLGNNKDNRIQGgyenvptIDIHMNQ-IGFEREWHK--FLLEYIAPMTEKLYPGYY-TRAQF 637
Cdd:smart00702   1 SPAECQKLLEEAEPLG-WRGEVTRGIGNPN-------ETSQYRQsNGTWLELLErdLVIERIRQRLADFLGLLAgLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144    638 DLAFVVRYKPDeqPSLMPHHDAS-----TFTINIALNRVgvdYEGGGCRFLR---YNCSIRAPRKGWTLMHP-GRLTHYH 708
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDNFlygdrIATFILYLNDV---EEGGELVFPGlrlMVVATVKPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 32307144    709 EGLPTTRGTRYIAVSFV 725
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
 
Name Accession Description Interval E-value
GT_LH1 cd23004
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ...
 26-254 3.64e-167

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: 479.68  E-value: 3.64e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144  26 DNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGLGEDWNVEKG-TSAGGGQKVRLLKKALEKHADKEDLVILFADSYDV 104
Cdd:cd23004   1 ENLLVLTVATKETDGFRRFRRSAKFFNYKIQVLGLGEEWQGGDDmQPAGGGQKVRLLKSALEPYADKEDLVILFIESYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 105 LFASGPRELLKKFRQARSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQLFYT 184
Cdd:cd23004  81 IFASGPAELLKKFQQAKSKVVFSAENLIYPDRHLEAKYPHVRDGKRFLGSGGFIGYAPNLYKMVSDWSGQDDDSDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 185 KIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLG 254
Cdd:cd23004 161 KIFLDPEKREKINITLDHRCRIFQNLNGALDEVVLKFEDGRVRARNLLYDTLPVIIHGNGPTKLQLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 562-725 5.40e-26

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: 104.78  E-value: 5.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144    562 TEVACDELVEEMEHFGqWSLGNNKDNRIQGgyenvptIDIHMNQ-IGFEREWHK--FLLEYIAPMTEKLYPGYY-TRAQF 637
Cdd:smart00702   1 SPAECQKLLEEAEPLG-WRGEVTRGIGNPN-------ETSQYRQsNGTWLELLErdLVIERIRQRLADFLGLLAgLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144    638 DLAFVVRYKPDeqPSLMPHHDAS-----TFTINIALNRVgvdYEGGGCRFLR---YNCSIRAPRKGWTLMHP-GRLTHYH 708
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDNFlygdrIATFILYLNDV---EEGGELVFPGlrlMVVATVKPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 32307144    709 EGLPTTRGTRYIAVSFV 725
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 637-727 3.36e-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: 57.46  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144   637 FDLAFVVRY-KPDEQPS----LMPHHDASTFTINIALNRVGVDYEGGGCrFLRYNCSIRA--PRKG--WTLMHPGRL-TH 706
Cdd:pfam03171   1 PDQCLVLNYyPPHPDPDltlgLGPHTDASILTILLQDDVGGLQVFKDGK-WIDVPPLPGAlvVNIGdqLELLSNGRYkSV 79

                          90       100
                  ....*....|....*....|..
gi 32307144   707 YHEGLPTTRG-TRYIAVSFVDP 727
Cdd:pfam03171  80 LHRVLPVNKGkERISIAFFLRP 101
 
Name Accession Description Interval E-value
GT_LH1 cd23004
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ...
 26-254 3.64e-167

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: 479.68  E-value: 3.64e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144  26 DNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGLGEDWNVEKG-TSAGGGQKVRLLKKALEKHADKEDLVILFADSYDV 104
Cdd:cd23004   1 ENLLVLTVATKETDGFRRFRRSAKFFNYKIQVLGLGEEWQGGDDmQPAGGGQKVRLLKSALEPYADKEDLVILFIESYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 105 LFASGPRELLKKFRQARSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQLFYT 184
Cdd:cd23004  81 IFASGPAELLKKFQQAKSKVVFSAENLIYPDRHLEAKYPHVRDGKRFLGSGGFIGYAPNLYKMVSDWSGQDDDSDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 185 KIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLG 254
Cdd:cd23004 161 KIFLDPEKREKINITLDHRCRIFQNLNGALDEVVLKFEDGRVRARNLLYDTLPVIIHGNGPTKLQLNYLG 230
GT_LH2 cd23003
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar ...
 26-254 2.41e-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: 364.92  E-value: 2.41e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144  26 DNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGLGEDWNV-EKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDV 104
Cdd:cd23003   1 EKLLVLTVATKETDGFHRFMQSAKYFNYTVKVLGMGEEWKGgDVANSIGGGQKVRLLKEEMESLADQEDLVVLFTDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 105 LFASGPRELLKKFRQARSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQLFYT 184
Cdd:cd23003  81 IFAGGPEEVLKKFQQANHKVVFAAEGLIWPDKRLAEKYPVVRSGKRFLNSGGFIGYAPYINRIVQQWNLQDNDDDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 185 KIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLG 254
Cdd:cd23003 161 KIYIDPLQRESINITLDHKCRIFQNLNGAVDEVLLKFENGKARVRNTVYETLPVVIHGNGPTKLLLNYLG 230
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 26-254 1.78e-120

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: 359.89  E-value: 1.78e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144  26 DNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGLGEDWnveKG----TSAGGGQKVRLLKKALEKHADKEDLVILFADS 101
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEW---RGgdvaRTVGGGQKVRWLKKEMEKYADREDMIIMFVDS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 102 YDVLFASGPRELLKKFRQARSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQL 181
Cdd:cd23002  78 YDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVQQWKYKDDDDDQL 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32307144 182 FYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLIHGNGPTKLQLNYLG 254
Cdd:cd23002 158 FYTRLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
GT_LH cd22997
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ...
 30-245 4.20e-56

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: 191.84  E-value: 4.20e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144  30 VLTVATKETEGFRRFKRSAQFFNY-KIQALGLGEDWnveKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFAS 108
Cdd:cd22997   2 VLTPATKPNDGLCRTLLSAALLGYpPPTVLGWGEKW---KGGDGGHGAKIRLLLEYLESLKLPDDDLVLFVDGYDVWFQL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 109 GPRELLKKFRQ-----ARSQVVFSAEELIYPDRRLETKYPVVSD----------------GKRFLGSGGFIGYAPNLSKL 167
Cdd:cd22997  79 PPEELLERFLAlnaaaIRQPIVFSAEKNCWPDDSLAPAYPAVPPsplppdidddldssktRPRYLNSGGIIGRAGDLREL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144 168 VAEW-----EGQDSDSDQLFYTKIFLDPEK-REQINITLDHRCRIFQNLDGALDEVVLKFE-----MGHVRARNLAYDTL 236
Cdd:cd22997 159 LEAAlelieDEKDWDDDQLVFTELYLEQEYwRYEFGIGLDYESELFQTLNGSESDLELLSYddpppLGESRLRNTVTGTV 238


                ....*....
gi 32307144 237 PVLIHGNGP 245
Cdd:cd22997 239 PVVLHFNGP 247
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 562-725 5.40e-26

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: 104.78  E-value: 5.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144    562 TEVACDELVEEMEHFGqWSLGNNKDNRIQGgyenvptIDIHMNQ-IGFEREWHK--FLLEYIAPMTEKLYPGYY-TRAQF 637
Cdd:smart00702   1 SPAECQKLLEEAEPLG-WRGEVTRGIGNPN-------ETSQYRQsNGTWLELLErdLVIERIRQRLADFLGLLAgLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144    638 DLAFVVRYKPDeqPSLMPHHDAS-----TFTINIALNRVgvdYEGGGCRFLR---YNCSIRAPRKGWTLMHP-GRLTHYH 708
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDNFlygdrIATFILYLNDV---EEGGELVFPGlrlMVVATVKPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 32307144    709 EGLPTTRGTRYIAVSFV 725
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 637-727 3.36e-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: 57.46  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144   637 FDLAFVVRY-KPDEQPS----LMPHHDASTFTINIALNRVGVDYEGGGCrFLRYNCSIRA--PRKG--WTLMHPGRL-TH 706
Cdd:pfam03171   1 PDQCLVLNYyPPHPDPDltlgLGPHTDASILTILLQDDVGGLQVFKDGK-WIDVPPLPGAlvVNIGdqLELLSNGRYkSV 79

                          90       100
                  ....*....|....*....|..
gi 32307144   707 YHEGLPTTRG-TRYIAVSFVDP 727
Cdd:pfam03171  80 LHRVLPVNKGkERISIAFFLRP 101
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 640-725 2.35e-03

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: 37.74  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307144   640 AFVVRYKPDEQpsLMPHHDAST---------FTINIALNRvGVDYEGGGCRFLRYNCSIR-APRKGWTLMHPGRLTHYHE 709
Cdd:pfam13640   1 LQLARYGDGGF--YKPHLDFFEgaegggqrrLTVVLYLND-WEEEEGGELVLYDGDGVEDiKPKKGRLVLFPSSELSLHE 77

                          90
                  ....*....|....*.
gi 32307144   710 GLPTTRGTRYIAVSFV 725
Cdd:pfam13640  78 VLPVTGGERWSITGWF 93
 
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.
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