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Conserved domains on  [gi|4505891|ref|NP_001075|]
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multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 37-266 9.29e-177

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: 504.34  E-value: 9.29e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891   37 EKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 116
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  117 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYT 196
Cdd:cd23002  81 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVQQWKYKDDDDDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  197 RLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 266
Cdd:cd23002 161 RLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 573-736 9.29e-23

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: 95.53  E-value: 9.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891     573 SEQMCDELVAEMEHYGqWSGGRHEDSRLAGgyenvptVDIHMKQVG---YEDQWLQLLRTYVGPMTESLFPG-YHTKARA 648
Cdd:smart00702   1 SPAECQKLLEEAEPLG-WRGEVTRGIGNPN-------ETSQYRQSNgtwLELLERDLVIERIRQRLADFLGLlAGLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891     649 VMNFVVRYRPDeqPSLRPHHD-----SSTFTLNVALNHkglDYEGGGCRFLRYDCVISS---PRKGWALLHP-GRLTHYH 719
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDnflygDRIATFILYLND---VEEGGELVFPGLRLMVVAtvkPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 4505891     720 EGLPTTWGTRYIMVSFV 736
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
 
Name Accession Description Interval E-value
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 37-266 9.29e-177

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: 504.34  E-value: 9.29e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891   37 EKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 116
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  117 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYT 196
Cdd:cd23002  81 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVQQWKYKDDDDDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  197 RLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 266
Cdd:cd23002 161 RLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 573-736 9.29e-23

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: 95.53  E-value: 9.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891     573 SEQMCDELVAEMEHYGqWSGGRHEDSRLAGgyenvptVDIHMKQVG---YEDQWLQLLRTYVGPMTESLFPG-YHTKARA 648
Cdd:smart00702   1 SPAECQKLLEEAEPLG-WRGEVTRGIGNPN-------ETSQYRQSNgtwLELLERDLVIERIRQRLADFLGLlAGLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891     649 VMNFVVRYRPDeqPSLRPHHD-----SSTFTLNVALNHkglDYEGGGCRFLRYDCVISS---PRKGWALLHP-GRLTHYH 719
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDnflygDRIATFILYLND---VEEGGELVFPGLRLMVVAtvkPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 4505891     720 EGLPTTWGTRYIMVSFV 736
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 653-736 1.62e-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: 38.13  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891    653 VVRYRPDEQpsLRPHHDSST---------FTLNVALNhKGLDYEGGGCRFLRYDCVIS-SPRKGWALLHPGRLTHYHEGL 722
Cdd:pfam13640   3 LARYGDGGF--YKPHLDFFEgaegggqrrLTVVLYLN-DWEEEEGGELVLYDGDGVEDiKPKKGRLVLFPSSELSLHEVL 79

                          90
                  ....*....|....
gi 4505891    723 PTTWGTRYIMVSFV 736
Cdd:pfam13640  80 PVTGGERWSITGWF 93
 
Name Accession Description Interval E-value
GT_LH3 cd23002
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ...
 37-266 9.29e-177

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: 504.34  E-value: 9.29e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891   37 EKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 116
Cdd:cd23002   1 EKLLVITVATAETEGYLRFLRTAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  117 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYT 196
Cdd:cd23002  81 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVQQWKYKDDDDDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  197 RLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 266
Cdd:cd23002 161 RLYLDPGLREKFSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 230
GT_LH1 cd23004
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ...
 37-266 5.56e-128

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: 379.53  E-value: 5.56e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891   37 EKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 116
Cdd:cd23004   1 ENLLVLTVATKETDGFRRFRRSAKFFNYKIQVLGLGEEWQGGDDMQPAGGGQKVRLLKSALEPYADKEDLVILFIESYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  117 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYT 196
Cdd:cd23004  81 IFASGPAELLKKFQQAKSKVVFSAENLIYPDRHLEAKYPHVRDGKRFLGSGGFIGYAPNLYKMVSDWSGQDDDSDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  197 RLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 266
Cdd:cd23004 161 KIFLDPEKREKINITLDHRCRIFQNLNGALDEVVLKFEDGRVRARNLLYDTLPVIIHGNGPTKLQLNYLG 230
GT_LH2 cd23003
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar ...
 37-266 1.91e-124

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: 370.70  E-value: 1.91e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891   37 EKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDV 116
Cdd:cd23003   1 EKLLVLTVATKETDGFHRFMQSAKYFNYTVKVLGMGEEWKGGDVANSIGGGQKVRLLKEEMESLADQEDLVVLFTDSYDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  117 ILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYT 196
Cdd:cd23003  81 IFAGGPEEVLKKFQQANHKVVFAAEGLIWPDKRLAEKYPVVRSGKRFLNSGGFIGYAPYINRIVQQWNLQDNDDDQLFYT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  197 RLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLG 266
Cdd:cd23003 161 KIYIDPLQRESINITLDHKCRIFQNLNGAVDEVLLKFENGKARVRNTVYETLPVVIHGNGPTKLLLNYLG 230
GT_LH cd22997
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ...
 41-257 7.14e-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: 204.94  E-value: 7.14e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891   41 VITVATAETEGYLRFLRSAEFFNY-TVRTLGLGEEWRGGDVartvGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILA 119
Cdd:cd22997   2 VLTPATKPNDGLCRTLLSAALLGYpPPTVLGWGEKWKGGDG----GHGAKIRLLLEYLESLKLPDDDLVLFVDGYDVWFQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  120 GSPTELLKKFVQSG-----SRLLFSAESFCWPEWGLAEQYPEV----------------GTGKRFLNSGGFIGFATTIHQ 178
Cdd:cd22997  78 LPPEELLERFLALNaaairQPIVFSAEKNCWPDDSLAPAYPAVppsplppdidddldssKTRPRYLNSGGIIGRAGDLRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891  179 IVRQW-----KYKDDDDDQLFYTRLYLD-PGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRV-----RIRNVAYDT 247
Cdd:cd22997 158 LLEAAlelieDEKDWDDDQLVFTELYLEqEYWRYEFGIGLDYESELFQTLNGSESDLELLSYDDPPplgesRLRNTVTGT 237

                       250
                ....*....|
gi 4505891  248 LPIVVHGNGP 257
Cdd:cd22997 238 VPVVLHFNGP 247
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 573-736 9.29e-23

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: 95.53  E-value: 9.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891     573 SEQMCDELVAEMEHYGqWSGGRHEDSRLAGgyenvptVDIHMKQVG---YEDQWLQLLRTYVGPMTESLFPG-YHTKARA 648
Cdd:smart00702   1 SPAECQKLLEEAEPLG-WRGEVTRGIGNPN-------ETSQYRQSNgtwLELLERDLVIERIRQRLADFLGLlAGLPLSA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891     649 VMNFVVRYRPDeqPSLRPHHD-----SSTFTLNVALNHkglDYEGGGCRFLRYDCVISS---PRKGWALLHP-GRLTHYH 719
Cdd:smart00702  73 EDAQVARYGPG--GHYGPHVDnflygDRIATFILYLND---VEEGGELVFPGLRLMVVAtvkPKKGDLLFFPsGHGRSLH 147

                          170
                   ....*....|....*..
gi 4505891     720 EGLPTTWGTRYIMVSFV 736
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 653-736 1.62e-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: 38.13  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505891    653 VVRYRPDEQpsLRPHHDSST---------FTLNVALNhKGLDYEGGGCRFLRYDCVIS-SPRKGWALLHPGRLTHYHEGL 722
Cdd:pfam13640   3 LARYGDGGF--YKPHLDFFEgaegggqrrLTVVLYLN-DWEEEEGGELVLYDGDGVEDiKPKKGRLVLFPSSELSLHEVL 79

                          90
                  ....*....|....
gi 4505891    723 PTTWGTRYIMVSFV 736
Cdd:pfam13640  80 PVTGGERWSITGWF 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.
  • 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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