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Conserved domains on  [gi|1701883108|ref|XP_029749680|]
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hypothetical protein PpBr36_04631 [Pyricularia pennisetigena]

Protein Classification

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. ...
509-671 1.01e-111

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: 345.70  E-value: 1.01e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  509 MYNENEYDFTRTMHAVMKNISHFCRRSKSRTWGENGWQKIVVCIVSDGREKIHPRTLDALAAMGVYQHGIAKNYVNQKAV 588
Cdd:pfam01644    1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  589 QAHVYEYTTQVSLDADLKFKGAEKGIVPCQMLFCLKERNQRKLNSHRWFFNAFGKALNPNVCILLDVGTRPGGNSLYHLW 668
Cdd:pfam01644   81 TAHLFEYTTQLSVDEDLKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                   ...
gi 1701883108  669 KAF 671
Cdd:pfam01644  161 KAF 163
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
438-508 3.42e-31

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


:

Pssm-ID: 462467  Cd Length: 70  Bit Score: 116.80  E-value: 3.42e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1701883108  438 EVQLINGELVLETKIPTILYSFLPRR-DADEFTHMRYTAVTCDPDDFVERGYKLRQNIgvTARETELFVCVT 508
Cdd:pfam08407    1 KVKLTNGNLVLDCPVPSRLLNALPRRkGSREFTHMRYTAVTCDPDDFTKNGYTLRQAL--YGRETELFIVIT 70
Chitin_synth_2 super family cl37687
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
650-839 2.95e-18

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).


The actual alignment was detected with superfamily member pfam03142:

Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 89.82  E-value: 2.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  650 CILLDVGTRPGGNSLYHLWKAFDTDSNVAGACGE--IKAMKGSWginllnpLVASQNFEYKMSNILDKPLESVFGYITVL 727
Cdd:pfam03142  205 VLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIANKRQSW-------VTAIQVFEYYISHHLSKAFESVFGGVTCL 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  728 PGALSAYRYHALQNDANGHGPL-------SQYFKG--ETLHGQHAdvftanMYLAEDRILCwELVAKRDERWVLKYVKGC 798
Cdd:pfam03142  278 PGCFSMYRIKAPKGGDGYWVPIlaspdivEHYSENvvDTLHKKNL------LLLGEDRYLT-TLMLKTFPKRKTVFVPQA 350
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1701883108  799 TGETDVPDTVPEFISQRRRWLNGAFFaAIYSLVHFRQLWAT 839
Cdd:pfam03142  351 VCKTIAPDTFKVLLSQRRRWINSTVH-NLMELVLVRDLCGT 390
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
2-372 2.44e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108    2 DRPLSRGAPPSYSNYDEDPDELRLGP--AGNPAAVRLL--------PASSFDEEIPETRQYVAPLAPHPAVVRKAL---- 67
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRSTPtwSLSTLAPASParegsptpPGPSSPDPPPPTPPPASPPPSPAPDLSEMLrpvg 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108   68 --LPPPLQITKPSYVGGPRKPQPLSTPEHLSKLKQ--QEEARTPQPSAGTARVTFSVTRATP----REKLWEDRGSGTGG 139
Cdd:PHA03307   143 spGPPPAASPPAAGASPAAVASDAASSRQAALPLSspEETARAPSSPPAEPPPSTPPAAASPrpprRSSPISASASSPAP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  140 SPSRRRTVKLQRK-------ITHDTVAQGQTDANLPVIPQGPSPRMMSRSLKKSLSEPGHHPVSKTAHNRQGAPDIDTSF 212
Cdd:PHA03307   223 APGRSAADDAGASssdssssESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  213 SD----VTDHQHSKGRNSESNDTSSrpthrayqpSISSVHSRPSSISNIPSmPPPTESyvsyretGSPTRPWTPSHVGRS 288
Cdd:PHA03307   303 PGsgpaPSSPRASSSSSSSRESSSS---------STSSSSESSRGAAVSPG-PSPSRS-------PSPSRPPPPADPSSP 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  289 SdeyRRPPPSsvhyeRADLNGSPRPGTPSSRYGGSPRRPLPPA----PLFAGPGARNSSFADDATVSIPLSD--VDDPFG 362
Cdd:PHA03307   366 R---KRPRPS-----RAPSSPAASAGRPTRRRARAAVAGRARRrdatGRFPAGRPRPSPLDAGAASGAFYARypLLTPSG 437
                          410
                   ....*....|...
gi 1701883108  363 ---PGSADLGEAR 372
Cdd:PHA03307   438 epwPGSPPPPPGR 450
DUF4271 super family cl40682
Domain of unknown function (DUF4271); This family of integral membrane proteins is ...
851-1013 2.35e-04

Domain of unknown function (DUF4271); This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 221 and 326 amino acids in length.


The actual alignment was detected with superfamily member pfam14093:

Pssm-ID: 454814  Cd Length: 207  Bit Score: 43.76  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  851 IEFVYQLLQVLFTFFSLAnFYLTFYFVAGGLADPLIDPFGNRIGLYIFTILrytLILLICAQFILSLGN---RPQGAKKP 927
Cdd:pfam14093   46 LESRFQLFLLLQTCLLLG-LFLYLYLSYFGPLFGDYLPSSLLLLLIIFLIL---LLYFLLKFLLYRLVGwvfFDKKIIRQ 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  928 YFASMVIY----GIVMVYTTFAAFYIvirqltdpdaklqlgNNVFTNLIVSMASTIGLYFLMSFIYLDPWHMFTSSAQYF 1003
Cdd:pfam14093  122 WIFSYLSYlsllGLLLFPLVLLLVYF---------------PLSSQTALLLILIILLLVKILLYLYKSFRIFFRKKFSLL 186
                          170
                   ....*....|
gi 1701883108 1004 MLLpSYLCTL 1013
Cdd:pfam14093  187 YFI-LYLCAL 195
 
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. ...
509-671 1.01e-111

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: 345.70  E-value: 1.01e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  509 MYNENEYDFTRTMHAVMKNISHFCRRSKSRTWGENGWQKIVVCIVSDGREKIHPRTLDALAAMGVYQHGIAKNYVNQKAV 588
Cdd:pfam01644    1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  589 QAHVYEYTTQVSLDADLKFKGAEKGIVPCQMLFCLKERNQRKLNSHRWFFNAFGKALNPNVCILLDVGTRPGGNSLYHLW 668
Cdd:pfam01644   81 TAHLFEYTTQLSVDEDLKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                   ...
gi 1701883108  669 KAF 671
Cdd:pfam01644  161 KAF 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
505-825 2.56e-96

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: 307.31  E-value: 2.56e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  505 VCVTMYNENEYDFTRTMHAVMKNISHFCRRsksrtwGENGWQKIVVCIVSDGREKIhprtldalaamgvyqhgiaknyvn 584
Cdd:cd04190      1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKK------------------------ 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  585 qkavqahvyeyttqvsldadlkfkgaekgivpcqmlfclkerNQRKLNSHRWFFNAFGKAL---NPNVCILLDVGTRPGG 661
Cdd:cd04190     51 ------------------------------------------NRGKRDSQLWFFNYFCRVLfpdDPEFILLVDADTKFDP 88
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  662 NSLYHLWKAFDTDSNVAGACGEIKAMKGSwginlLNPLVASQNFEYKMSNILDKPLESVFGYITVLPGALSAYRYHALQN 741
Cdd:cd04190     89 DSIVQLYKAMDKDPEIGGVCGEIHPMGKK-----QGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKG 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  742 DANGHGPLSQYFKGETLHGQhaDVFTANMYLAEDRILCWELVAKRDERWVLkYVKGCTGETDVPDTVPEFISQRRRWLNG 821
Cdd:cd04190    164 DNGGKGPLLDYAYLTNTVDS--LHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWINS 240

                   ....
gi 1701883108  822 AFFA 825
Cdd:cd04190    241 TIAN 244
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
438-508 3.42e-31

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


Pssm-ID: 462467  Cd Length: 70  Bit Score: 116.80  E-value: 3.42e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1701883108  438 EVQLINGELVLETKIPTILYSFLPRR-DADEFTHMRYTAVTCDPDDFVERGYKLRQNIgvTARETELFVCVT 508
Cdd:pfam08407    1 KVKLTNGNLVLDCPVPSRLLNALPRRkGSREFTHMRYTAVTCDPDDFTKNGYTLRQAL--YGRETELFIVIT 70
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
650-839 2.95e-18

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: 89.82  E-value: 2.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  650 CILLDVGTRPGGNSLYHLWKAFDTDSNVAGACGE--IKAMKGSWginllnpLVASQNFEYKMSNILDKPLESVFGYITVL 727
Cdd:pfam03142  205 VLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIANKRQSW-------VTAIQVFEYYISHHLSKAFESVFGGVTCL 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  728 PGALSAYRYHALQNDANGHGPL-------SQYFKG--ETLHGQHAdvftanMYLAEDRILCwELVAKRDERWVLKYVKGC 798
Cdd:pfam03142  278 PGCFSMYRIKAPKGGDGYWVPIlaspdivEHYSENvvDTLHKKNL------LLLGEDRYLT-TLMLKTFPKRKTVFVPQA 350
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1701883108  799 TGETDVPDTVPEFISQRRRWLNGAFFaAIYSLVHFRQLWAT 839
Cdd:pfam03142  351 VCKTIAPDTFKVLLSQRRRWINSTVH-NLMELVLVRDLCGT 390
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
727-911 4.71e-08

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: 56.29  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  727 LPGALSAYRYHALQnDANGHGPLSqyfkgetlhgqhadvftanmyLAEDRILCWELVAKRderWVLKYVKGCTGETDVPD 806
Cdd:COG1215    143 ASGANLAFRREALE-EVGGFDEDT---------------------LGEDLDLSLRLLRAG---YRIVYVPDAVVYEEAPE 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  807 TVPEFISQRRRWLNGAFFaaiYSLVHFRQLWATDHTVarkvllhieFVYQLLQVLFTFFSLANFYLTFYFVAGGLADPLI 886
Cdd:COG1215    198 TLRALFRQRRRWARGGLQ---LLLKHRPLLRPRRLLL---------FLLLLLLPLLLLLLLLALLALLLLLLPALLLALL 265
                          170       180
                   ....*....|....*....|....*
gi 1701883108  887 DPFGNRIGLYIFTILRYTLILLICA 911
Cdd:COG1215    266 LALRRRRLLLPLLHLLYGLLLLLAA 290
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2-372 2.44e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108    2 DRPLSRGAPPSYSNYDEDPDELRLGP--AGNPAAVRLL--------PASSFDEEIPETRQYVAPLAPHPAVVRKAL---- 67
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRSTPtwSLSTLAPASParegsptpPGPSSPDPPPPTPPPASPPPSPAPDLSEMLrpvg 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108   68 --LPPPLQITKPSYVGGPRKPQPLSTPEHLSKLKQ--QEEARTPQPSAGTARVTFSVTRATP----REKLWEDRGSGTGG 139
Cdd:PHA03307   143 spGPPPAASPPAAGASPAAVASDAASSRQAALPLSspEETARAPSSPPAEPPPSTPPAAASPrpprRSSPISASASSPAP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  140 SPSRRRTVKLQRK-------ITHDTVAQGQTDANLPVIPQGPSPRMMSRSLKKSLSEPGHHPVSKTAHNRQGAPDIDTSF 212
Cdd:PHA03307   223 APGRSAADDAGASssdssssESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  213 SD----VTDHQHSKGRNSESNDTSSrpthrayqpSISSVHSRPSSISNIPSmPPPTESyvsyretGSPTRPWTPSHVGRS 288
Cdd:PHA03307   303 PGsgpaPSSPRASSSSSSSRESSSS---------STSSSSESSRGAAVSPG-PSPSRS-------PSPSRPPPPADPSSP 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  289 SdeyRRPPPSsvhyeRADLNGSPRPGTPSSRYGGSPRRPLPPA----PLFAGPGARNSSFADDATVSIPLSD--VDDPFG 362
Cdd:PHA03307   366 R---KRPRPS-----RAPSSPAASAGRPTRRRARAAVAGRARRrdatGRFPAGRPRPSPLDAGAASGAFYARypLLTPSG 437
                          410
                   ....*....|...
gi 1701883108  363 ---PGSADLGEAR 372
Cdd:PHA03307   438 epwPGSPPPPPGR 450
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
651-818 8.22e-05

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: 45.32  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  651 ILLDVGTRPGGNSLYHLWKAFDtDSNVAGACGEIKAMK--GSWGINLLNPLVASQNFEYKMSNildkpleSVFGYITVLP 728
Cdd:cd06434     82 VLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRprDSKWSFLAAEYLERRNEEIRAAM-------SYDGGVPCLS 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  729 GALSAYRYHALQndangHGPLSQYFKGETLHGQHADVftanmylAEDRILCWELVAKrdeRWVLKYVKGCTGETDVPDTV 808
Cdd:cd06434    154 GRTAAYRTEILK-----DFLFLEEFTNETFMGRRLNA-------GDDRFLTRYVLSH---GYKTVYQYTSEAYTETPENY 218
                          170
                   ....*....|
gi 1701883108  809 PEFISQRRRW 818
Cdd:cd06434    219 KKFLKQQLRW 228
DUF4271 pfam14093
Domain of unknown function (DUF4271); This family of integral membrane proteins is ...
851-1013 2.35e-04

Domain of unknown function (DUF4271); This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 221 and 326 amino acids in length.


Pssm-ID: 433712  Cd Length: 207  Bit Score: 43.76  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  851 IEFVYQLLQVLFTFFSLAnFYLTFYFVAGGLADPLIDPFGNRIGLYIFTILrytLILLICAQFILSLGN---RPQGAKKP 927
Cdd:pfam14093   46 LESRFQLFLLLQTCLLLG-LFLYLYLSYFGPLFGDYLPSSLLLLLIIFLIL---LLYFLLKFLLYRLVGwvfFDKKIIRQ 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  928 YFASMVIY----GIVMVYTTFAAFYIvirqltdpdaklqlgNNVFTNLIVSMASTIGLYFLMSFIYLDPWHMFTSSAQYF 1003
Cdd:pfam14093  122 WIFSYLSYlsllGLLLFPLVLLLVYF---------------PLSSQTALLLILIILLLVKILLYLYKSFRIFFRKKFSLL 186
                          170
                   ....*....|
gi 1701883108 1004 MLLpSYLCTL 1013
Cdd:pfam14093  187 YFI-LYLCAL 195
 
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. ...
509-671 1.01e-111

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: 345.70  E-value: 1.01e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  509 MYNENEYDFTRTMHAVMKNISHFCRRSKSRTWGENGWQKIVVCIVSDGREKIHPRTLDALAAMGVYQHGIAKNYVNQKAV 588
Cdd:pfam01644    1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  589 QAHVYEYTTQVSLDADLKFKGAEKGIVPCQMLFCLKERNQRKLNSHRWFFNAFGKALNPNVCILLDVGTRPGGNSLYHLW 668
Cdd:pfam01644   81 TAHLFEYTTQLSVDEDLKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                   ...
gi 1701883108  669 KAF 671
Cdd:pfam01644  161 KAF 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
505-825 2.56e-96

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: 307.31  E-value: 2.56e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  505 VCVTMYNENEYDFTRTMHAVMKNISHFCRRsksrtwGENGWQKIVVCIVSDGREKIhprtldalaamgvyqhgiaknyvn 584
Cdd:cd04190      1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKK------------------------ 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  585 qkavqahvyeyttqvsldadlkfkgaekgivpcqmlfclkerNQRKLNSHRWFFNAFGKAL---NPNVCILLDVGTRPGG 661
Cdd:cd04190     51 ------------------------------------------NRGKRDSQLWFFNYFCRVLfpdDPEFILLVDADTKFDP 88
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  662 NSLYHLWKAFDTDSNVAGACGEIKAMKGSwginlLNPLVASQNFEYKMSNILDKPLESVFGYITVLPGALSAYRYHALQN 741
Cdd:cd04190     89 DSIVQLYKAMDKDPEIGGVCGEIHPMGKK-----QGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKG 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  742 DANGHGPLSQYFKGETLHGQhaDVFTANMYLAEDRILCWELVAKRDERWVLkYVKGCTGETDVPDTVPEFISQRRRWLNG 821
Cdd:cd04190    164 DNGGKGPLLDYAYLTNTVDS--LHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWINS 240

                   ....
gi 1701883108  822 AFFA 825
Cdd:cd04190    241 TIAN 244
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
438-508 3.42e-31

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


Pssm-ID: 462467  Cd Length: 70  Bit Score: 116.80  E-value: 3.42e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1701883108  438 EVQLINGELVLETKIPTILYSFLPRR-DADEFTHMRYTAVTCDPDDFVERGYKLRQNIgvTARETELFVCVT 508
Cdd:pfam08407    1 KVKLTNGNLVLDCPVPSRLLNALPRRkGSREFTHMRYTAVTCDPDDFTKNGYTLRQAL--YGRETELFIVIT 70
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
650-839 2.95e-18

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: 89.82  E-value: 2.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  650 CILLDVGTRPGGNSLYHLWKAFDTDSNVAGACGE--IKAMKGSWginllnpLVASQNFEYKMSNILDKPLESVFGYITVL 727
Cdd:pfam03142  205 VLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIANKRQSW-------VTAIQVFEYYISHHLSKAFESVFGGVTCL 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  728 PGALSAYRYHALQNDANGHGPL-------SQYFKG--ETLHGQHAdvftanMYLAEDRILCwELVAKRDERWVLKYVKGC 798
Cdd:pfam03142  278 PGCFSMYRIKAPKGGDGYWVPIlaspdivEHYSENvvDTLHKKNL------LLLGEDRYLT-TLMLKTFPKRKTVFVPQA 350
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1701883108  799 TGETDVPDTVPEFISQRRRWLNGAFFaAIYSLVHFRQLWAT 839
Cdd:pfam03142  351 VCKTIAPDTFKVLLSQRRRWINSTVH-NLMELVLVRDLCGT 390
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
507-739 1.33e-15

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: 76.11  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  507 VTMYNEnEYDFTRTMHAVMKNIshfcrrsksrtwgengWQKIVVCIVSDGRekiHPRTLDALAAMGVYQHGIaknyvnqk 586
Cdd:cd06423      3 VPAYNE-EAVIERTIESLLALD----------------YPKLEVIVVDDGS---TDDTLEILEELAALYIRR-------- 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  587 avqahvyeyttqvsldadlkfkgaekgivpcqMLFCLKERNQRKLNSHRWFFNAfgkaLNPNVCILLDVGTRPGGNSLYH 666
Cdd:cd06423     55 --------------------------------VLVVRDKENGGKAGALNAGLRH----AKGDIVVVLDADTILEPDALKR 98
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701883108  667 LWKAFDTDSNVAGACGEIKAMKGSwginlLNPLVASQNFEYKMSNILDKPLESVFGYITVLPGALSAYRYHAL 739
Cdd:cd06423     99 LVVPFFADPKVGAVQGRVRVRNGS-----ENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAFRREAL 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
727-911 4.71e-08

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: 56.29  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  727 LPGALSAYRYHALQnDANGHGPLSqyfkgetlhgqhadvftanmyLAEDRILCWELVAKRderWVLKYVKGCTGETDVPD 806
Cdd:COG1215    143 ASGANLAFRREALE-EVGGFDEDT---------------------LGEDLDLSLRLLRAG---YRIVYVPDAVVYEEAPE 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  807 TVPEFISQRRRWLNGAFFaaiYSLVHFRQLWATDHTVarkvllhieFVYQLLQVLFTFFSLANFYLTFYFVAGGLADPLI 886
Cdd:COG1215    198 TLRALFRQRRRWARGGLQ---LLLKHRPLLRPRRLLL---------FLLLLLLPLLLLLLLLALLALLLLLLPALLLALL 265
                          170       180
                   ....*....|....*....|....*
gi 1701883108  887 DPFGNRIGLYIFTILRYTLILLICA 911
Cdd:COG1215    266 LALRRRRLLLPLLHLLYGLLLLLAA 290
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2-372 2.44e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108    2 DRPLSRGAPPSYSNYDEDPDELRLGP--AGNPAAVRLL--------PASSFDEEIPETRQYVAPLAPHPAVVRKAL---- 67
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRSTPtwSLSTLAPASParegsptpPGPSSPDPPPPTPPPASPPPSPAPDLSEMLrpvg 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108   68 --LPPPLQITKPSYVGGPRKPQPLSTPEHLSKLKQ--QEEARTPQPSAGTARVTFSVTRATP----REKLWEDRGSGTGG 139
Cdd:PHA03307   143 spGPPPAASPPAAGASPAAVASDAASSRQAALPLSspEETARAPSSPPAEPPPSTPPAAASPrpprRSSPISASASSPAP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  140 SPSRRRTVKLQRK-------ITHDTVAQGQTDANLPVIPQGPSPRMMSRSLKKSLSEPGHHPVSKTAHNRQGAPDIDTSF 212
Cdd:PHA03307   223 APGRSAADDAGASssdssssESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSS 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  213 SD----VTDHQHSKGRNSESNDTSSrpthrayqpSISSVHSRPSSISNIPSmPPPTESyvsyretGSPTRPWTPSHVGRS 288
Cdd:PHA03307   303 PGsgpaPSSPRASSSSSSSRESSSS---------STSSSSESSRGAAVSPG-PSPSRS-------PSPSRPPPPADPSSP 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  289 SdeyRRPPPSsvhyeRADLNGSPRPGTPSSRYGGSPRRPLPPA----PLFAGPGARNSSFADDATVSIPLSD--VDDPFG 362
Cdd:PHA03307   366 R---KRPRPS-----RAPSSPAASAGRPTRRRARAAVAGRARRrdatGRFPAGRPRPSPLDAGAASGAFYARypLLTPSG 437
                          410
                   ....*....|...
gi 1701883108  363 ---PGSADLGEAR 372
Cdd:PHA03307   438 epwPGSPPPPPGR 450
PHA03247 PHA03247
large tegument protein UL36; Provisional
2-317 6.57e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108    2 DRPLSRGAPPSYSNYDEDPDELRLGPAGNPA--AVRLLPASSFDEEIPETRQyvAPLAPHPAVVRKALLP-PPLQITKPS 78
Cdd:PHA03247  2522 DEPVGEPVHPRMLTWIRGLEELASDDAGDPPppLPPAAPPAAPDRSVPPPRP--APRPSEPAVTSRARRPdAPPQSARPR 2599
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108   79 YVGGPRKPQPLSTPEhlSKLKQQEEARTPQPSAGTARVTfsvtratpreklwEDRGSGTGGSPSRRRTvklqrkithdtv 158
Cdd:PHA03247  2600 APVDDRGDPRGPAPP--SPLPPDTHAPDPPPPSPSPAAN-------------EPDPHPPPTVPPPERP------------ 2652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  159 aqgqtdanlpviPQGPSPRMMSRSLKKSlsepghhpvsktahnrqgapdidtsfsdvtdhqhSKGRNSESNDTSSRPTHR 238
Cdd:PHA03247  2653 ------------RDDPAPGRVSRPRRAR----------------------------------RLGRAAQASSPPQRPRRR 2686
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  239 AYQPSISSVhsrpSSISNIPSMPPPTESyvsyreTGSPTRPWTPSHVGRSSDEYRRPPPSSVHYERADLNGS-------- 310
Cdd:PHA03247  2687 AARPTVGSL----TSLADPPPPPPTPEP------APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpggpar 2756

                   ....*...
gi 1701883108  311 -PRPGTPS 317
Cdd:PHA03247  2757 pARPPTTA 2764
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
651-818 8.22e-05

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: 45.32  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  651 ILLDVGTRPGGNSLYHLWKAFDtDSNVAGACGEIKAMK--GSWGINLLNPLVASQNFEYKMSNildkpleSVFGYITVLP 728
Cdd:cd06434     82 VLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRprDSKWSFLAAEYLERRNEEIRAAM-------SYDGGVPCLS 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  729 GALSAYRYHALQndangHGPLSQYFKGETLHGQHADVftanmylAEDRILCWELVAKrdeRWVLKYVKGCTGETDVPDTV 808
Cdd:cd06434    154 GRTAAYRTEILK-----DFLFLEEFTNETFMGRRLNA-------GDDRFLTRYVLSH---GYKTVYQYTSEAYTETPENY 218
                          170
                   ....*....|
gi 1701883108  809 PEFISQRRRW 818
Cdd:cd06434    219 KKFLKQQLRW 228
DUF4271 pfam14093
Domain of unknown function (DUF4271); This family of integral membrane proteins is ...
851-1013 2.35e-04

Domain of unknown function (DUF4271); This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 221 and 326 amino acids in length.


Pssm-ID: 433712  Cd Length: 207  Bit Score: 43.76  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  851 IEFVYQLLQVLFTFFSLAnFYLTFYFVAGGLADPLIDPFGNRIGLYIFTILrytLILLICAQFILSLGN---RPQGAKKP 927
Cdd:pfam14093   46 LESRFQLFLLLQTCLLLG-LFLYLYLSYFGPLFGDYLPSSLLLLLIIFLIL---LLYFLLKFLLYRLVGwvfFDKKIIRQ 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  928 YFASMVIY----GIVMVYTTFAAFYIvirqltdpdaklqlgNNVFTNLIVSMASTIGLYFLMSFIYLDPWHMFTSSAQYF 1003
Cdd:pfam14093  122 WIFSYLSYlsllGLLLFPLVLLLVYF---------------PLSSQTALLLILIILLLVKILLYLYKSFRIFFRKKFSLL 186
                          170
                   ....*....|
gi 1701883108 1004 MLLpSYLCTL 1013
Cdd:pfam14093  187 YFI-LYLCAL 195
PHA02666 PHA02666
hypothetical protein; Provisional
177-306 1.21e-03

hypothetical protein; Provisional


Pssm-ID: 222914 [Multi-domain]  Cd Length: 287  Bit Score: 42.23  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  177 RMMSRSLKKSLSEPGHHPVS--------------KTAHNRQ-----GAPDIDTSFSDVTDHQHSKGRNSESNDTSSRPTH 237
Cdd:PHA02666     9 RCVCNEIWKTMRGDGHHESCfhhrrransmesrrKSRPSRQhrsaeRTPTTASSLTHENNTAPSRHGKQHSCKASSRSSH 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701883108  238 RAYQPSISSVHSRPSSisnipsmPPPTESYVSYRETGSPTRPWTPSHVGRSSDEYRRPPPSSVHYERAD 306
Cdd:PHA02666    89 NRGSTSSSHNHHAHRG-------PHQSAHRRSKHDAVRDTYQPCPQSPETDLYKGRLPGETERHYETPD 150
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
150-437 4.35e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  150 QRKITHDTVAQGQTDANLPVIPQGP--SPRMMSRSLKKSLSEPGHHPVSKTAHNRQ-GAPDIDTSFSDVTDHQHSkgrNS 226
Cdd:PHA03307    47 SAELAAVTVVAGAAACDRFEPPTGPppGPGTEAPANESRSTPTWSLSTLAPASPAReGSPTPPGPSSPDPPPPTP---PP 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  227 ESNDTSSRPTHRAYQPSISSVHSRPSsisniPSMPPPTESyvSYRETGSPTRPWTPSHVGRSSDEYRRPPPSsvhyerad 306
Cdd:PHA03307   124 ASPPPSPAPDLSEMLRPVGSPGPPPA-----ASPPAAGAS--PAAVASDAASSRQAALPLSSPEETARAPSS-------- 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  307 lnGSPRPGTPSSRYGGSprrplppaplfAGPGARNSSFADDATVSIPLSDVDDPFGPGSADLGEARgHQGSYAAQSQVTL 386
Cdd:PHA03307   189 --PPAEPPPSTPPAAAS-----------PRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS-SESSGCGWGPENE 254
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1701883108  387 NEDDDEGSALREGDVGYDDAADEKSAAHYGPAPAEGDQQRRGVRAPQKSRK 437
Cdd:PHA03307   255 CPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
dnaA PRK14086
chromosomal replication initiator protein DnaA;
169-353 4.66e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 40.96  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  169 VIPQGPSPRMMSRSLKKSLSEPGHHPVSKTAHNRqgapdidtsfsdVTDHQHSKGRNSESNDtsSRPTHRAYQPsissvH 248
Cdd:PRK14086    92 AGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPR------------ADDRPPGLPRQDQLPT--ARPAYPAYQQ-----R 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701883108  249 SRPSSISNIP---------SMPPPTESYVSYRETGSPTRPW-TPSHVGRSSDEYRRPPP--SSVHYERADLNGSPRPGTP 316
Cdd:PRK14086   153 PEPGAWPRAAddygwqqqrLGFPPRAPYASPASYAPEQERDrEPYDAGRPEYDQRRRDYdhPRPDWDRPRRDRTDRPEPP 232
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1701883108  317 SS-----RYGGSPRRPLPPAPLFAGPGARNSSFADDATVSIP 353
Cdd:PRK14086   233 PGaghvhRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGP 274
 
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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