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Conserved domains on  [gi|17554740|ref|NP_499368|]
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Exostosin-2 homolog [Caenorhabditis elegans]

Protein Classification

Glyco_transf_64 domain-containing protein( domain architecture ID 10379573)

Glyco_transf_64 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 561-795 2.76e-94

Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate.


:

Pssm-ID: 430488  Cd Length: 241  Bit Score: 294.97  E-value: 2.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   561 FTVVLLT-YERDAVLTGALERLHQLPYLNKIIVVWNNvNRDPPD--TWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAV 637
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNN-PKPPPElsRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   638 LSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHA------RYGdsmfYNSNHTCQMSMILTGAAFIHKNYLTAYTYE 711
Cdd:pfam09258  80 LSLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFwdlssgRWG----YTSEWTNEYSMVLTGAAFYHRYYLYLYTHS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   712 MPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTE--SLYKEGTHFEKRHECMRLFTKIYGYNPLKF 789
Cdd:pfam09258 156 LPKSLRTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSGkvGLSSRPGHFLQRSKCINKFAAVFGYMPLVY 235


                  ....*.
gi 17554740   790 SQFRAD 795
Cdd:pfam09258 236 SQIRLD 241
RXYLT1-like super family cl20239
ribitol-5-phosphate xylosyltransferase 1, and related proteins; Ribitol-5-phosphate ...
 175-399 3.12e-30

ribitol-5-phosphate xylosyltransferase 1, and related proteins; Ribitol-5-phosphate xylosyltransferase 1 (RXYLT1, also known as transmembrane protein 5, TMEM5) is a transmembrane protein which acts as a UDP-d-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase in the biosynthetic pathway of O-mannosyl glycan. RXYLT1 catalyzes the transfer of UDP-D-xylose to ribitol 5-phosphate (Rbo5P) to form the Xylbeta1-4Rbo5P linkage on O-mannosyl glycan. O-mannosyl glycan is present in a number of glycoproteins, including alpha-dystroglycan. The TMEM5 gene has been associated with alpha-dystroglycanopathies, a diverse group of neuromuscular disorders caused by aberrant O-mannosylation of alpha-dystroglycan.


The actual alignment was detected with superfamily member pfam03016:

Pssm-ID: 473306  Cd Length: 290  Bit Score: 120.99  E-value: 3.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   175 ISSFMPVYV---------DIITSGQSEKEWLNVFQEV--------IPNLVETPDKA-CIKIHISNGIASPNTTFNSI--- 233
Cdd:pfam03016   1 SCKGLKVYVydlpprfneDLLQPCRSLTGWYSAEQFLlesilhsrIECRTSDPDEAdCFFVPFYASLDASRHLLNSAltd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   234 ------------------------LFNVGSPIINFQ--SKSIHVQASKIR--SFDFPVDVNHIAVEKVdlTPLLPFQRE- 284
Cdd:pfam03016  81 lfrelldwlksqypywnrsggrdhFIVSGHPAWSFRrtAPDVDWGRAMLLnlTVLFSEDQFRPGKDVA--LPYPTPFHPd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   285 --NLISLIVDNTELNFSAFSSL---SAEPSRRPIVIVKC----SQENCSLER-------RRQLIGSSTFCFLLPSEMFFQ 348
Cdd:pfam03016 159 igQWQDISPSNRRKTLLFFAGNrrrGYSGKIRPLLLEECkgnpDADICGGLQctpgrdkYMELLRSSRFCLQPPGDTPTS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17554740   349 -DFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSF 399
Cdd:pfam03016 239 pRLFDALLAGCIPVIISDGWELPFADVIDWRKFSVFVPENDIPELKSILRSL 290
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-162 1.33e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740  49 ALKQNIENLDDydascsgysigRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLI---PQKQLELSALEGEIEAA 125
Cdd:COG3206 295 ALRAQIAALRA-----------QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLEREVEVA 363

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17554740 126 QR-------QLEELRETQNVKVFlPFSPLQIPRELEQPSqiSPN 162
Cdd:COG3206 364 RElyesllqRLEEARLAEALTVG-NVRVIDPAVVPLKPV--SPK 404
 
Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 561-795 2.76e-94

Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate.


Pssm-ID: 430488  Cd Length: 241  Bit Score: 294.97  E-value: 2.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   561 FTVVLLT-YERDAVLTGALERLHQLPYLNKIIVVWNNvNRDPPD--TWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAV 637
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNN-PKPPPElsRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   638 LSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHA------RYGdsmfYNSNHTCQMSMILTGAAFIHKNYLTAYTYE 711
Cdd:pfam09258  80 LSLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFwdlssgRWG----YTSEWTNEYSMVLTGAAFYHRYYLYLYTHS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   712 MPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTE--SLYKEGTHFEKRHECMRLFTKIYGYNPLKF 789
Cdd:pfam09258 156 LPKSLRTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSGkvGLSSRPGHFLQRSKCINKFAAVFGYMPLVY 235


                  ....*.
gi 17554740   790 SQFRAD 795
Cdd:pfam09258 236 SQIRLD 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 175-399 3.12e-30

Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.


Pssm-ID: 397245  Cd Length: 290  Bit Score: 120.99  E-value: 3.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   175 ISSFMPVYV---------DIITSGQSEKEWLNVFQEV--------IPNLVETPDKA-CIKIHISNGIASPNTTFNSI--- 233
Cdd:pfam03016   1 SCKGLKVYVydlpprfneDLLQPCRSLTGWYSAEQFLlesilhsrIECRTSDPDEAdCFFVPFYASLDASRHLLNSAltd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   234 ------------------------LFNVGSPIINFQ--SKSIHVQASKIR--SFDFPVDVNHIAVEKVdlTPLLPFQRE- 284
Cdd:pfam03016  81 lfrelldwlksqypywnrsggrdhFIVSGHPAWSFRrtAPDVDWGRAMLLnlTVLFSEDQFRPGKDVA--LPYPTPFHPd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   285 --NLISLIVDNTELNFSAFSSL---SAEPSRRPIVIVKC----SQENCSLER-------RRQLIGSSTFCFLLPSEMFFQ 348
Cdd:pfam03016 159 igQWQDISPSNRRKTLLFFAGNrrrGYSGKIRPLLLEECkgnpDADICGGLQctpgrdkYMELLRSSRFCLQPPGDTPTS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17554740   349 -DFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSF 399
Cdd:pfam03016 239 pRLFDALLAGCIPVIISDGWELPFADVIDWRKFSVFVPENDIPELKSILRSL 290
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-162 1.33e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740  49 ALKQNIENLDDydascsgysigRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLI---PQKQLELSALEGEIEAA 125
Cdd:COG3206 295 ALRAQIAALRA-----------QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLEREVEVA 363

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17554740 126 QR-------QLEELRETQNVKVFlPFSPLQIPRELEQPSqiSPN 162
Cdd:COG3206 364 RElyesllqRLEEARLAEALTVG-NVRVIDPAVVPLKPV--SPK 404
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 73-134 4.36e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 40.65  E-value: 4.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554740    73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSAL----EGEIEAAQRQLEELRE 134
Cdd:pfam18595  52 LEEAKKKLKELRDALEEKEIELRELERREERLQRQLENAQEKLERLreqaEEKREAAQARLEELRE 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-134 7.95e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 7.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740     47 QDALKQNIENLDDYDAscsgysigrILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQ 126
Cdd:TIGR02168  795 KEELKALREALDELRA---------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865


                   ....*...
gi 17554740    127 RQLEELRE 134
Cdd:TIGR02168  866 ELIEELES 873
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
561-644 2.45e-03

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 39.98  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740 561 FTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTW-PSLHIP-VEFIRVAEN----NLNNRFVpwDRIET 634
Cdd:COG1216   5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELlAALAFPrVRVIRNPENlgfaAARNLGL--RAAGG 82

                        90
                ....*....|
gi 17554740 635 EAVLSLDDDI 644
Cdd:COG1216  83 DYLLFLDDDT 92
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-134 6.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   50 LKQNIENLDDYDASCSgySIGRILREQKRILASVRLELTESQVKI----EEIRTVQEELQRL------IPQKQLELSALE 119
Cdd:PRK03918 174 IKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELpelrEELEKLEKEVKELeelkeeIEELEKELESLE 251

                         90
                 ....*....|....*
gi 17554740  120 GEIEAAQRQLEELRE 134
Cdd:PRK03918 252 GSKRKLEEKIRELEE 266
 
Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 561-795 2.76e-94

Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate.


Pssm-ID: 430488  Cd Length: 241  Bit Score: 294.97  E-value: 2.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   561 FTVVLLT-YERDAVLTGALERLHQLPYLNKIIVVWNNvNRDPPD--TWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAV 637
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNN-PKPPPElsRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   638 LSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHA------RYGdsmfYNSNHTCQMSMILTGAAFIHKNYLTAYTYE 711
Cdd:pfam09258  80 LSLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFwdlssgRWG----YTSEWTNEYSMVLTGAAFYHRYYLYLYTHS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   712 MPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTE--SLYKEGTHFEKRHECMRLFTKIYGYNPLKF 789
Cdd:pfam09258 156 LPKSLRTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSGkvGLSSRPGHFLQRSKCINKFAAVFGYMPLVY 235


                  ....*.
gi 17554740   790 SQFRAD 795
Cdd:pfam09258 236 SQIRLD 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 175-399 3.12e-30

Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.


Pssm-ID: 397245  Cd Length: 290  Bit Score: 120.99  E-value: 3.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   175 ISSFMPVYV---------DIITSGQSEKEWLNVFQEV--------IPNLVETPDKA-CIKIHISNGIASPNTTFNSI--- 233
Cdd:pfam03016   1 SCKGLKVYVydlpprfneDLLQPCRSLTGWYSAEQFLlesilhsrIECRTSDPDEAdCFFVPFYASLDASRHLLNSAltd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   234 ------------------------LFNVGSPIINFQ--SKSIHVQASKIR--SFDFPVDVNHIAVEKVdlTPLLPFQRE- 284
Cdd:pfam03016  81 lfrelldwlksqypywnrsggrdhFIVSGHPAWSFRrtAPDVDWGRAMLLnlTVLFSEDQFRPGKDVA--LPYPTPFHPd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   285 --NLISLIVDNTELNFSAFSSL---SAEPSRRPIVIVKC----SQENCSLER-------RRQLIGSSTFCFLLPSEMFFQ 348
Cdd:pfam03016 159 igQWQDISPSNRRKTLLFFAGNrrrGYSGKIRPLLLEECkgnpDADICGGLQctpgrdkYMELLRSSRFCLQPPGDTPTS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17554740   349 -DFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSF 399
Cdd:pfam03016 239 pRLFDALLAGCIPVIISDGWELPFADVIDWRKFSVFVPENDIPELKSILRSL 290
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-162 1.33e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740  49 ALKQNIENLDDydascsgysigRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLI---PQKQLELSALEGEIEAA 125
Cdd:COG3206 295 ALRAQIAALRA-----------QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLEREVEVA 363

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17554740 126 QR-------QLEELRETQNVKVFlPFSPLQIPRELEQPSqiSPN 162
Cdd:COG3206 364 RElyesllqRLEEARLAEALTVG-NVRVIDPAVVPLKPV--SPK 404
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 73-134 4.36e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 40.65  E-value: 4.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554740    73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSAL----EGEIEAAQRQLEELRE 134
Cdd:pfam18595  52 LEEAKKKLKELRDALEEKEIELRELERREERLQRQLENAQEKLERLreqaEEKREAAQARLEELRE 117
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 73-134 6.89e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 6.89e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17554740  73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRE 134
Cdd:COG3883  25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-134 7.95e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 7.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740     47 QDALKQNIENLDDYDAscsgysigrILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQ 126
Cdd:TIGR02168  795 KEELKALREALDELRA---------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865


                   ....*...
gi 17554740    127 RQLEELRE 134
Cdd:TIGR02168  866 ELIEELES 873
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 48-134 1.59e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740  48 DALKQNIENLDdydascsgysigRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQR 127
Cdd:COG4942  30 EQLQQEIAELE------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                ....*..
gi 17554740 128 QLEELRE 134
Cdd:COG4942  98 ELEAQKE 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-134 2.18e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17554740  73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRE 134
Cdd:COG4372  47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
561-644 2.45e-03

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 39.98  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740 561 FTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTW-PSLHIP-VEFIRVAEN----NLNNRFVpwDRIET 634
Cdd:COG1216   5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELlAALAFPrVRVIRNPENlgfaAARNLGL--RAAGG 82

                        90
                ....*....|
gi 17554740 635 EAVLSLDDDI 644
Cdd:COG1216  83 DYLLFLDDDT 92
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 73-137 2.46e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554740  73 LREQKRILASVRLELTESQVKIEEIRTVQEE----LQRLIPQKQLELSALEGEIEAAQRQLEELRETQN 137
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAE 223
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 73-137 3.55e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.55e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554740  73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQN 137
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 68-134 3.66e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 3.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554740     68 SIGRILREQKRILAsvrlELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRE 134
Cdd:TIGR02169  717 KIGEIEKEIEQLEQ----EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 69-137 4.04e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 4.04e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554740  69 IGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQN 137
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
89-132 5.38e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 37.56  E-value: 5.38e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 17554740  89 ESQVKIEEIRTVQEELQRLIPQKQlelsALEGEIEAAQRQLEEL 132
Cdd:COG1382   8 EVQNQLAQLQQLQQQLQAVAAQKQ----QVESELKEAEKALEEL 47
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-137 5.51e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 5.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554740  73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQN 137
Cdd:COG4372  68 LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-134 6.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554740   50 LKQNIENLDDYDASCSgySIGRILREQKRILASVRLELTESQVKI----EEIRTVQEELQRL------IPQKQLELSALE 119
Cdd:PRK03918 174 IKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELpelrEELEKLEKEVKELeelkeeIEELEKELESLE 251

                         90
                 ....*....|....*
gi 17554740  120 GEIEAAQRQLEELRE 134
Cdd:PRK03918 252 GSKRKLEEKIRELEE 266
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-134 7.54e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 7.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17554740     72 ILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRE 134
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 85-137 7.59e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 35.70  E-value: 7.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17554740    85 LELTESQVK--IEEIRTVQEELQRLipqKQlELSALEGEIEAAQRQLEELRETQN 137
Cdd:pfam06005   6 LEQLETKIQaaVDTIALLQMENEEL---KE-ENEELKEEANELEEENQQLKQERN 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-139 8.24e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 8.24e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17554740  71 RILREQKRIL-ASVR-LELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVK 139
Cdd:COG1196 216 RELKEELKELeAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-137 8.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.81e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554740  73 LREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQN 137
Cdd:COG4372  96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
71-137 9.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 9.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554740  71 RILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQN 137
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
 
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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