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Conserved domains on  [gi|19112226|ref|NP_595434|]
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chitin synthase-like protein 2 [Schizosaccharomyces pombe]

Protein Classification

chitin synthase( domain architecture ID 10552337)

chitin synthase 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
255-416 1.36e-77

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


:

Pssm-ID: 426363  Cd Length: 163  Bit Score: 249.78  E-value: 1.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226   255 DEDLASFAISLSSIMNNLKHLCSRSKSRVWGNESWEKVLVCVVIDGRNTVHQNVLDLLASIGVYQPHIAKGRVNGKRTLS 334
Cdd:pfam01644   3 NEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPVTA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226   335 HMYEFTSTINVDEKLNLTTATgDGNVPMQMLLCVKDRRLGTYNSHRWFLNGIASLARPKVCLFVRNGARLGPTSIYHAWK 414
Cdd:pfam01644  83 HLFEYTTQLSVDEDLKFKGNE-KGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLWK 161

                  ..
gi 19112226   415 AF 416
Cdd:pfam01644 162 AF 163
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
181-252 1.75e-20

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


:

Pssm-ID: 462467  Cd Length: 70  Bit Score: 85.98  E-value: 1.75e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112226   181 DVPLLCGSLTIDCPTPIDLRGMLGPfmQKNPDEASFLRYSAITCQPEDMNNNGLQLRTWSTGRDIQIAVCLT 252
Cdd:pfam08407   1 KVKLTNGNLVLDCPVPSRLLNALPR--RKGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYGRETELFIVIT 70
 
Name Accession Description Interval E-value
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
255-416 1.36e-77

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


Pssm-ID: 426363  Cd Length: 163  Bit Score: 249.78  E-value: 1.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226   255 DEDLASFAISLSSIMNNLKHLCSRSKSRVWGNESWEKVLVCVVIDGRNTVHQNVLDLLASIGVYQPHIAKGRVNGKRTLS 334
Cdd:pfam01644   3 NEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPVTA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226   335 HMYEFTSTINVDEKLNLTTATgDGNVPMQMLLCVKDRRLGTYNSHRWFLNGIASLARPKVCLFVRNGARLGPTSIYHAWK 414
Cdd:pfam01644  83 HLFEYTTQLSVDEDLKFKGNE-KGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLWK 161

                  ..
gi 19112226   415 AF 416
Cdd:pfam01644 162 AF 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
249-568 2.22e-29

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: 117.41  E-value: 2.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 249 VCLTLSDEDLASFAISLSSIMNNLKHLCSRsksrvwGNESWEKVLVCVVIDGRNTVHQnvldllasigvyqphiakgrvn 328
Cdd:cd04190   1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKKNR---------------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 329 GKRtlshmyeftstinvdeklnlttatgdgnvpmqmllcvkdrrlgtyNSHRWFLNGIASL---ARPKVCLFVRNGARLG 405
Cdd:cd04190  53 GKR---------------------------------------------DSQLWFFNYFCRVlfpDDPEFILLVDADTKFD 87
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 406 PTSIYHAWKAFDVDSTIGGMCGKTSIDTGKFgfrllNPFIASQHFDQMIHNNLRLPYDSCMGYISNALNAIYGFRYVALQ 485
Cdd:cd04190  88 PDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQ-----GPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALK 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 486 DSYPNPGPLADYFEQDqyEIPRRGILQSNAFLAQEQLLFWKVITRKDAKWHLqYVPEACATIEAPNSMAGILESKKSEIN 565
Cdd:cd04190 163 GDNGGKGPLLDYAYLT--NTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWIN 239

                ...
gi 19112226 566 SSF 568
Cdd:cd04190 240 STI 242
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
181-252 1.75e-20

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


Pssm-ID: 462467  Cd Length: 70  Bit Score: 85.98  E-value: 1.75e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112226   181 DVPLLCGSLTIDCPTPIDLRGMLGPfmQKNPDEASFLRYSAITCQPEDMNNNGLQLRTWSTGRDIQIAVCLT 252
Cdd:pfam08407   1 KVKLTNGNLVLDCPVPSRLLNALPR--RKGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYGRETELFIVIT 70
 
Name Accession Description Interval E-value
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
255-416 1.36e-77

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


Pssm-ID: 426363  Cd Length: 163  Bit Score: 249.78  E-value: 1.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226   255 DEDLASFAISLSSIMNNLKHLCSRSKSRVWGNESWEKVLVCVVIDGRNTVHQNVLDLLASIGVYQPHIAKGRVNGKRTLS 334
Cdd:pfam01644   3 NEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPVTA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226   335 HMYEFTSTINVDEKLNLTTATgDGNVPMQMLLCVKDRRLGTYNSHRWFLNGIASLARPKVCLFVRNGARLGPTSIYHAWK 414
Cdd:pfam01644  83 HLFEYTTQLSVDEDLKFKGNE-KGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLWK 161

                  ..
gi 19112226   415 AF 416
Cdd:pfam01644 162 AF 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
249-568 2.22e-29

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: 117.41  E-value: 2.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 249 VCLTLSDEDLASFAISLSSIMNNLKHLCSRsksrvwGNESWEKVLVCVVIDGRNTVHQnvldllasigvyqphiakgrvn 328
Cdd:cd04190   1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKKNR---------------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 329 GKRtlshmyeftstinvdeklnlttatgdgnvpmqmllcvkdrrlgtyNSHRWFLNGIASL---ARPKVCLFVRNGARLG 405
Cdd:cd04190  53 GKR---------------------------------------------DSQLWFFNYFCRVlfpDDPEFILLVDADTKFD 87
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 406 PTSIYHAWKAFDVDSTIGGMCGKTSIDTGKFgfrllNPFIASQHFDQMIHNNLRLPYDSCMGYISNALNAIYGFRYVALQ 485
Cdd:cd04190  88 PDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQ-----GPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALK 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112226 486 DSYPNPGPLADYFEQDqyEIPRRGILQSNAFLAQEQLLFWKVITRKDAKWHLqYVPEACATIEAPNSMAGILESKKSEIN 565
Cdd:cd04190 163 GDNGGKGPLLDYAYLT--NTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWIN 239

                ...
gi 19112226 566 SSF 568
Cdd:cd04190 240 STI 242
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
181-252 1.75e-20

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


Pssm-ID: 462467  Cd Length: 70  Bit Score: 85.98  E-value: 1.75e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112226   181 DVPLLCGSLTIDCPTPIDLRGMLGPfmQKNPDEASFLRYSAITCQPEDMNNNGLQLRTWSTGRDIQIAVCLT 252
Cdd:pfam08407   1 KVKLTNGNLVLDCPVPSRLLNALPR--RKGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYGRETELFIVIT 70
 
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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