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Conserved domains on  [gi|599350344|ref|XP_007391081|]
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glycosyltransferase family 2 protein [Phanerochaete carnosa HHB-10118-sp]

Protein Classification

chitin synthase( domain architecture ID 12042369)

chitin synthase converts UDP-N-acetyl-D-glucosamine into chitin and UDP; chitin is a structural polymer of the cell wall and septum

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
644-1170 0e+00

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


:

Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 994.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   644 PCPFPLHNVVPQPPPDYEPFNYPLAHTICLVTAYSESVEGLRTTLDSLATTDYPNSHKLILVIADGMVKGAGNTMTTPEI 723
Cdd:pfam03142    1 VSTIIHKFIAAQPLGTKRPFGFPLKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   724 CLSMMKDFVINPSEVEPHSYVAIADGHKRHNMAQVYAGFYAYD-DATVERSKQQKVPIVLVAKCGNPLEKNDPKPGNRGK 802
Cdd:pfam03142   81 VLDMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDgDSHIPEEKQQRVPMIVVVKCGTPSEASEKKPGNRGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   803 RDSQIVLMAFMQKVMFDERMTTFEYEFFNSIWRVTGVSPDHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETK 882
Cdd:pfam03142  161 RDSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   883 IANKAETWVTMMQVFEYYISHHMTKAFEAMFGGVTCLPGCFSMYRIKAPKGENGYWVPILANPDIVQHYSENVVDTLHKK 962
Cdd:pfam03142  241 IANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKGGDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   963 NLLLLGEDRYLTTLMLKTFPKRKNVFCPQAVCKTVVPDTFRILLSQRRRWINSTVHNLAELLLVRDLCGTFCFSMQFVVG 1042
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  1043 MELAGTLVLPAAISFTLYLIIISIIPGGTNTTIPLILLAIVLGLPGVLIVITSRKIAYVGWMIVYLLSLPIWNGILPAYA 1122
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILTPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 599350344  1123 FWHFDDFSWGQTRQVAGEKGAgDNHGDKEGEFDSSHIVMKRWAEFERE 1170
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGK-KVHGTDEGEFDPSKIPMKRWEEFERE 527
 
Name Accession Description Interval E-value
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
644-1170 0e+00

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 994.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   644 PCPFPLHNVVPQPPPDYEPFNYPLAHTICLVTAYSESVEGLRTTLDSLATTDYPNSHKLILVIADGMVKGAGNTMTTPEI 723
Cdd:pfam03142    1 VSTIIHKFIAAQPLGTKRPFGFPLKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   724 CLSMMKDFVINPSEVEPHSYVAIADGHKRHNMAQVYAGFYAYD-DATVERSKQQKVPIVLVAKCGNPLEKNDPKPGNRGK 802
Cdd:pfam03142   81 VLDMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDgDSHIPEEKQQRVPMIVVVKCGTPSEASEKKPGNRGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   803 RDSQIVLMAFMQKVMFDERMTTFEYEFFNSIWRVTGVSPDHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETK 882
Cdd:pfam03142  161 RDSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   883 IANKAETWVTMMQVFEYYISHHMTKAFEAMFGGVTCLPGCFSMYRIKAPKGENGYWVPILANPDIVQHYSENVVDTLHKK 962
Cdd:pfam03142  241 IANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKGGDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   963 NLLLLGEDRYLTTLMLKTFPKRKNVFCPQAVCKTVVPDTFRILLSQRRRWINSTVHNLAELLLVRDLCGTFCFSMQFVVG 1042
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  1043 MELAGTLVLPAAISFTLYLIIISIIPGGTNTTIPLILLAIVLGLPGVLIVITSRKIAYVGWMIVYLLSLPIWNGILPAYA 1122
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILTPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 599350344  1123 FWHFDDFSWGQTRQVAGEKGAgDNHGDKEGEFDSSHIVMKRWAEFERE 1170
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGK-KVHGTDEGEFDPSKIPMKRWEEFERE 527
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
672-1019 4.57e-98

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 314.25  E-value: 4.57e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  672 CLVTAYSESVEGLRTTLDSLATTDYP--------NSHKLILVIADGMVKGagntmttpeiclsmmkdfvinpsevephsy 743
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPfcarggdsWKKIVVCVIFDGAIKK------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  744 vaiadghkrhnmaqvyagfyayddatverskqqkvpivlvakcgnplekndpkpgNRGKRDSQIVLMAFMQKVMFdermt 823
Cdd:cd04190    51 -------------------------------------------------------NRGKRDSQLWFFNYFCRVLF----- 70
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  824 tfeyeffnsiwrvtgvsPDHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETKIANKAETWVTMMQVFEYYISH 903
Cdd:cd04190    71 -----------------PDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISH 133
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  904 HMTKAFEAMFGGVTCLPGCFSMYRIKAPKGENGYWVPILANpdivqHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTFPK 983
Cdd:cd04190   134 WLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDY-----AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGPK 208
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 599350344  984 RKNVFCPQAVCKTVVPDTFRILLSQRRRWINSTVHN 1019
Cdd:cd04190   209 RKYLYVPGAVAETDVPETFVELLSQRRRWINSTIAN 244
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
673-1102 4.77e-11

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: 65.53  E-value: 4.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  673 LVTAYSESvEGLRTTLDSLATTDYPNSHKLILVIADGmvkgagNTMTTPEIclsmmkdfvinpsevephsyvaiadghkr 752
Cdd:COG1215    34 IIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDG------STDETAEI----------------------------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  753 hnmaqvyagfyayddatVERSKQQKVPIVLVAKcgnplekndpkPGNRGKRDSqivLMAFMQKVmfdermttfeyeffns 832
Cdd:COG1215    78 -----------------ARELAAEYPRVRVIER-----------PENGGKAAA---LNAGLKAA---------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  833 iwrvtgvspdHYELVLCVDADTKVFPDSLSRMVSCMVNDyeimglcgetkiankaetwvtmmqvfeyyishhmtkafeam 912
Cdd:COG1215   111 ----------RGDIVVFLDADTVLDPDWLRRLVAAFADP----------------------------------------- 139
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  913 fgGVTClPGCFSMYRIKAPKgENGYWVPILanpdivqhysenvvdtlhkknlllLGEDRYLTTLMLKTfpKRKNVFCPQA 992
Cdd:COG1215   140 --GVGA-SGANLAFRREALE-EVGGFDEDT------------------------LGEDLDLSLRLLRA--GYRIVYVPDA 189
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  993 VCKTVVPDTFRILLSQRRRWINSTVHNLAELLLVRDLCGTFCFSMQFVVG-MELAGTLVLPAAISFTLYLIIISIIPGGT 1071
Cdd:COG1215   190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPlLLLLLLLALLALLLLLLPALLLALLLALR 269
                         410       420       430
                  ....*....|....*....|....*....|.
gi 599350344 1072 NTTIPLILLAIVLGLPGVLIVITSRKIAYVG 1102
Cdd:COG1215   270 RRRLLLPLLHLLYGLLLLLAALRGKKVVWKK 300
 
Name Accession Description Interval E-value
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
644-1170 0e+00

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 994.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   644 PCPFPLHNVVPQPPPDYEPFNYPLAHTICLVTAYSESVEGLRTTLDSLATTDYPNSHKLILVIADGMVKGAGNTMTTPEI 723
Cdd:pfam03142    1 VSTIIHKFIAAQPLGTKRPFGFPLKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   724 CLSMMKDFVINPSEVEPHSYVAIADGHKRHNMAQVYAGFYAYD-DATVERSKQQKVPIVLVAKCGNPLEKNDPKPGNRGK 802
Cdd:pfam03142   81 VLDMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDgDSHIPEEKQQRVPMIVVVKCGTPSEASEKKPGNRGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   803 RDSQIVLMAFMQKVMFDERMTTFEYEFFNSIWRVTGVSPDHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETK 882
Cdd:pfam03142  161 RDSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   883 IANKAETWVTMMQVFEYYISHHMTKAFEAMFGGVTCLPGCFSMYRIKAPKGENGYWVPILANPDIVQHYSENVVDTLHKK 962
Cdd:pfam03142  241 IANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKGGDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   963 NLLLLGEDRYLTTLMLKTFPKRKNVFCPQAVCKTVVPDTFRILLSQRRRWINSTVHNLAELLLVRDLCGTFCFSMQFVVG 1042
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  1043 MELAGTLVLPAAISFTLYLIIISIIPGGTNTTIPLILLAIVLGLPGVLIVITSRKIAYVGWMIVYLLSLPIWNGILPAYA 1122
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILTPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 599350344  1123 FWHFDDFSWGQTRQVAGEKGAgDNHGDKEGEFDSSHIVMKRWAEFERE 1170
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGK-KVHGTDEGEFDPSKIPMKRWEEFERE 527
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
672-1019 4.57e-98

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 314.25  E-value: 4.57e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  672 CLVTAYSESVEGLRTTLDSLATTDYP--------NSHKLILVIADGMVKGagntmttpeiclsmmkdfvinpsevephsy 743
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPfcarggdsWKKIVVCVIFDGAIKK------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  744 vaiadghkrhnmaqvyagfyayddatverskqqkvpivlvakcgnplekndpkpgNRGKRDSQIVLMAFMQKVMFdermt 823
Cdd:cd04190    51 -------------------------------------------------------NRGKRDSQLWFFNYFCRVLF----- 70
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  824 tfeyeffnsiwrvtgvsPDHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETKIANKAETWVTMMQVFEYYISH 903
Cdd:cd04190    71 -----------------PDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISH 133
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  904 HMTKAFEAMFGGVTCLPGCFSMYRIKAPKGENGYWVPILANpdivqHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTFPK 983
Cdd:cd04190   134 WLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDY-----AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGPK 208
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 599350344  984 RKNVFCPQAVCKTVVPDTFRILLSQRRRWINSTVHN 1019
Cdd:cd04190   209 RKYLYVPGAVAETDVPETFVELLSQRRRWINSTIAN 244
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
673-940 5.30e-21

CESA_like is the cellulose synthase superfamily; The cellulose synthase (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 include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 91.91  E-value: 5.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  673 LVTAYSESvEGLRTTLDSLATTDYPNshKLILVIADGMVKGagntmtTPEIClsmmkdfvinpsevephsyvaiadghkr 752
Cdd:cd06423     2 IVPAYNEE-AVIERTIESLLALDYPK--LEVIVVDDGSTDD------TLEIL---------------------------- 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  753 hnmaqvyagfyayddatVERSKQQKVPIVLVakcgnplekndPKPGNRGKRDSQivlmafmqkvmfdermttfeyeffNS 832
Cdd:cd06423    45 -----------------EELAALYIRRVLVV-----------RDKENGGKAGAL------------------------NA 72
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  833 IWRVTgvspdHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETKIANKAETWVTMMQVFEYYISHHMTKAFEAM 912
Cdd:cd06423    73 GLRHA-----KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSA 147
                         250       260
                  ....*....|....*....|....*...
gi 599350344  913 FGGVTCLPGCFSMYRIKAPKgENGYWVP 940
Cdd:cd06423   148 LGGVLVLSGAFGAFRREALR-EVGGWDE 174
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
845-1016 1.10e-12

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 69.21  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  845 ELVLCVDADTKVFPDSLSRMVSCMVnDYEIMGLCGETKIANKAETWVTMMQVFEYYISHHMTKAFEAMFGGVTCLPGCFS 924
Cdd:cd06434    79 DIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTA 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  925 MYRIKapkgengywvpILANPDivqhYSENVVDTLHKKNLLLLGEDRYLTTLMLKTFPKRKNVFCPqaVCKTVVPDTFRI 1004
Cdd:cd06434   158 AYRTE-----------ILKDFL----FLEEFTNETFMGRRLNAGDDRFLTRYVLSHGYKTVYQYTS--EAYTETPENYKK 220
                         170
                  ....*....|..
gi 599350344 1005 LLSQRRRWINST 1016
Cdd:cd06434   221 FLKQQLRWSRSN 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
673-1102 4.77e-11

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: 65.53  E-value: 4.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  673 LVTAYSESvEGLRTTLDSLATTDYPNSHKLILVIADGmvkgagNTMTTPEIclsmmkdfvinpsevephsyvaiadghkr 752
Cdd:COG1215    34 IIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDG------STDETAEI----------------------------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  753 hnmaqvyagfyayddatVERSKQQKVPIVLVAKcgnplekndpkPGNRGKRDSqivLMAFMQKVmfdermttfeyeffns 832
Cdd:COG1215    78 -----------------ARELAAEYPRVRVIER-----------PENGGKAAA---LNAGLKAA---------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  833 iwrvtgvspdHYELVLCVDADTKVFPDSLSRMVSCMVNDyeimglcgetkiankaetwvtmmqvfeyyishhmtkafeam 912
Cdd:COG1215   111 ----------RGDIVVFLDADTVLDPDWLRRLVAAFADP----------------------------------------- 139
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  913 fgGVTClPGCFSMYRIKAPKgENGYWVPILanpdivqhysenvvdtlhkknlllLGEDRYLTTLMLKTfpKRKNVFCPQA 992
Cdd:COG1215   140 --GVGA-SGANLAFRREALE-EVGGFDEDT------------------------LGEDLDLSLRLLRA--GYRIVYVPDA 189
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  993 VCKTVVPDTFRILLSQRRRWINSTVHNLAELLLVRDLCGTFCFSMQFVVG-MELAGTLVLPAAISFTLYLIIISIIPGGT 1071
Cdd:COG1215   190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPlLLLLLLLALLALLLLLLPALLLALLLALR 269
                         410       420       430
                  ....*....|....*....|....*....|.
gi 599350344 1072 NTTIPLILLAIVLGLPGVLIVITSRKIAYVG 1102
Cdd:COG1215   270 RRRLLLPLLHLLYGLLLLLAALRGKKVVWKK 300
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
846-1092 8.55e-08

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 53.88  E-value: 8.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   846 LVLCVDADTKVFPDSLSRMVSCM-VNDYEIMGLCGetkIANKAETWVTMMQVFEYYISHHMTKAFEAMFGGVTCLPGCFS 924
Cdd:pfam13632    1 WILLLDADTVLPPDCLLGIANEMaSPEVAIIQGPI---LPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344   925 MYRIKAPKgENGYWvpilaNPDIVqhysenvvdtlhkknllllGEDrylTTLMLKTFPKRKNV-FCPQAVCKTVVPDTFR 1003
Cdd:pfam13632   78 FLRRSALQ-EVGGW-----DDGSV-------------------SED---FDFGLRLQRAGYRVrFAPYSAVYEKSPLTFR 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  1004 ILLSQRRRWINstvhnlaelllvrdlcgtFCFSMQFVVGMELAGTLVLpAAISFTLYLIIISIIpggtnttIPLILLAIV 1083
Cdd:pfam13632  130 DFLRQRRRWAY------------------GCLLILLIRLLGYLGTLLW-SGLPLALLLLLLFSI-------SSLALVLLL 183

                   ....*....
gi 599350344  1084 LGLPGVLIV 1092
Cdd:pfam13632  184 LALLAGLLL 192
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
825-917 4.56e-03

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 40.06  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  825 FEYEFFNSIWRVTGVSPDHyELVLCVDADTKVFPDSLSRMVSCMvNDYEIMGLCGETKIANKAETWVTMMQVFEYYISHH 904
Cdd:cd06436    72 AAYDQIRQILIEEGADPER-VIIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIA 149
                          90
                  ....*....|...
gi 599350344  905 MTKAFEAMFGGVT 917
Cdd:cd06436   150 ATQSLRALTGTVG 162
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
825-905 8.82e-03

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 38.74  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599350344  825 FEYEF-FNSIWRVtgvsPDHYELVLCVDADTKVFPDSLSRMVSCMVNDYEIMGLCGETKiaNKAETWVTMMQVFEYYISH 903
Cdd:cd06438    66 YALDFgFRHLLNL----ADDPDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNSK--NPDDSWITRLYAFAFLVFN 139

                  ..
gi 599350344  904 HM 905
Cdd:cd06438   140 RL 141
 
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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