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Conserved domains on  [gi|2257820060|ref|XP_001625539|]
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exostosin-3 [Nematostella vectensis]

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 ...
 625-862 6.89e-134

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: 399.36  E-value: 6.89e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 625 FTVVMLT-YERELVLMEAIQRLVGLSYLNKVVIVWNSPLAPSLSLHWPDIGVPVHVVRTTKNSLNNRFLPYDVIETDAIL 703
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNNPKPPPELSRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 704 SIDDDVELRHDEILLAFRVWRENRDRIVGFPGRYHAWDSVRNRWTYVSNHSCELSLILTGAAFIHRYYTYLFTHWMQQSI 783
Cdd:pfam09258  81 SLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFWDLSSGRWGYTSEWTNEYSMVLTGAAFYHRYYLYLYTHSLPKSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 784 REKIDEFMNCEDIAMNFLVSHITRKPPIKVTSRWTFVCSSCP--VSLWSDKSHFEERHQCINYFEKVYGYMPLLRTQYRA 861
Cdd:pfam09258 161 RTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSgkVGLSSRPGHFLQRSKCINKFAAVFGYMPLVYSQIRL 240


                  .
gi 2257820060 862 D 862
Cdd:pfam09258 241 D 241
RXYLT1-like super family cl20239
ribitol-5-phosphate xylosyltransferase 1, and related proteins; Ribitol-5-phosphate ...
 192-471 1.10e-23

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: 102.12  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 192 AGFSIYVYN-PEKYTIGERTDLV-----FEIYGILQKT------AYYTEREEDACSFIV------------LIGSLGSSS 247
Cdd:pfam03016   3 KGLKVYVYDlPPRFNEDLLQPCRsltgwYSAEQFLLESilhsriECRTSDPDEADCFFVpfyasldasrhlLNSALTDLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 248 SHFIREQLQSLPHWGK-NGSNHILLKLSDRYTQSLLLLEANMGLSILATSTYLPDV-QYRIGFDVIVpPLLGPTSGEVWA 325
Cdd:pfam03016  83 RELLDWLKSQYPYWNRsGGRDHFIVSGHPAWSFRRTAPDVDWGRAMLLNLTVLFSEdQFRPGKDVAL-PYPTPFHPDIGQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 326 QAGQQLPTLRKYFLTFEGsfhlsNEGAEEvskddlvflsKESSDLFIAVECvtydkiSNSAGWNLCGSHKNRTVR----- 400
Cdd:pfam03016 162 WQDISPSNRRKTLLFFAG-----NRRRGY----------SGKIRPLLLEEC------KGNPDADICGGLQCTPGRdkyme 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257820060 401 -LKKSTFSLVPVGNSgfVTHVRLIEALQTGAIPVILGTTNMLPLAEFIDWRSVSITLTPARIMELNTILRTV 471
Cdd:pfam03016 221 lLRSSRFCLQPPGDT--PTSPRLFDALLAGCIPVIISDGWELPFADVIDWRKFSVFVPENDIPELKSILRSL 290
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
63-144 9.62e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREvqiYGSKIERSKtETSRLQVKANRAKRDLEILQMERKRL 142
Cdd:COG2433   416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE---ERREIRKDR-EISRLDREIERLERELEEERERIEEL 491


                  ..
gi 2257820060 143 NK 144
Cdd:COG2433   492 KR 493
 
Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 625-862 6.89e-134

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: 399.36  E-value: 6.89e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 625 FTVVMLT-YERELVLMEAIQRLVGLSYLNKVVIVWNSPLAPSLSLHWPDIGVPVHVVRTTKNSLNNRFLPYDVIETDAIL 703
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNNPKPPPELSRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 704 SIDDDVELRHDEILLAFRVWRENRDRIVGFPGRYHAWDSVRNRWTYVSNHSCELSLILTGAAFIHRYYTYLFTHWMQQSI 783
Cdd:pfam09258  81 SLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFWDLSSGRWGYTSEWTNEYSMVLTGAAFYHRYYLYLYTHSLPKSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 784 REKIDEFMNCEDIAMNFLVSHITRKPPIKVTSRWTFVCSSCP--VSLWSDKSHFEERHQCINYFEKVYGYMPLLRTQYRA 861
Cdd:pfam09258 161 RTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSgkVGLSSRPGHFLQRSKCINKFAAVFGYMPLVYSQIRL 240


                  .
gi 2257820060 862 D 862
Cdd:pfam09258 241 D 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 192-471 1.10e-23

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: 102.12  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 192 AGFSIYVYN-PEKYTIGERTDLV-----FEIYGILQKT------AYYTEREEDACSFIV------------LIGSLGSSS 247
Cdd:pfam03016   3 KGLKVYVYDlPPRFNEDLLQPCRsltgwYSAEQFLLESilhsriECRTSDPDEADCFFVpfyasldasrhlLNSALTDLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 248 SHFIREQLQSLPHWGK-NGSNHILLKLSDRYTQSLLLLEANMGLSILATSTYLPDV-QYRIGFDVIVpPLLGPTSGEVWA 325
Cdd:pfam03016  83 RELLDWLKSQYPYWNRsGGRDHFIVSGHPAWSFRRTAPDVDWGRAMLLNLTVLFSEdQFRPGKDVAL-PYPTPFHPDIGQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 326 QAGQQLPTLRKYFLTFEGsfhlsNEGAEEvskddlvflsKESSDLFIAVECvtydkiSNSAGWNLCGSHKNRTVR----- 400
Cdd:pfam03016 162 WQDISPSNRRKTLLFFAG-----NRRRGY----------SGKIRPLLLEEC------KGNPDADICGGLQCTPGRdkyme 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257820060 401 -LKKSTFSLVPVGNSgfVTHVRLIEALQTGAIPVILGTTNMLPLAEFIDWRSVSITLTPARIMELNTILRTV 471
Cdd:pfam03016 221 lLRSSRFCLQPPGDT--PTSPRLFDALLAGCIPVIISDGWELPFADVIDWRKFSVFVPENDIPELKSILRSL 290
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
63-144 9.62e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREvqiYGSKIERSKtETSRLQVKANRAKRDLEILQMERKRL 142
Cdd:COG2433   416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE---ERREIRKDR-EISRLDREIERLERELEEERERIEEL 491


                  ..
gi 2257820060 143 NK 144
Cdd:COG2433   492 KR 493
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 63-143 9.64e-05

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 43.05  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRhriqreVQIYgskiERSKTEtsrlqvkanrakrdLEILQMERKRL 142
Cdd:pfam10473  83 ENLTKELQKKQERVSELESLNSSLENLLEEKEQEK------VQMK----EESKTA--------------VEMLQTQLKEL 138


                  .
gi 2257820060 143 N 143
Cdd:pfam10473 139 N 139
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
625-740 8.82e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 41.52  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 625 FTVVMLTYERELVLMEAIQRLVGLSYLN-KVVIVWNSPLAPSL----SLHWPDigvpVHVVRTTKN----SLNNRFLpyD 695
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPfEVIVVDNGSTDGTAellaALAFPR----VRVIRNPENlgfaAARNLGL--R 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257820060 696 VIETDAILSIDDDVELRHD--EILLAFR---VWRENRDRIVGFPGRYHAW 740
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDwlERLLAAAcllIRREVFEEVGGFDERFFLY 128
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 67-116 9.54e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.51  E-value: 9.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257820060  67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKT 116
Cdd:PRK03992    1 ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKS 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-144 1.22e-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: 42.74  E-value: 1.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060   67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 52-128 8.03e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060   52 RTKLDKTFGK-DEFLMERVEELRGQISELEKIKLSLSNELR-----DLEAKRHRIQREVQIYGSKIERSKTE-TSRLQVK 124
Cdd:smart00935  20 QKQLEKEFKKrQAELEKLEKELQKLKEKLQKDAATLSEAARekkekELQKKVQEFQRKQQKLQQDLQKRQQEeLQKILDK 99


                   ....
gi 2257820060  125 ANRA 128
Cdd:smart00935 100 INKA 103
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 63-118 9.50e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 37.13  E-value: 9.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREV----QIYGSKIERSKTET 118
Cdd:cd20482     3 ESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEInetfQFYRSMLEERKDEL 62
 
Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 625-862 6.89e-134

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: 399.36  E-value: 6.89e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 625 FTVVMLT-YERELVLMEAIQRLVGLSYLNKVVIVWNSPLAPSLSLHWPDIGVPVHVVRTTKNSLNNRFLPYDVIETDAIL 703
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNNPKPPPELSRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 704 SIDDDVELRHDEILLAFRVWRENRDRIVGFPGRYHAWDSVRNRWTYVSNHSCELSLILTGAAFIHRYYTYLFTHWMQQSI 783
Cdd:pfam09258  81 SLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFWDLSSGRWGYTSEWTNEYSMVLTGAAFYHRYYLYLYTHSLPKSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 784 REKIDEFMNCEDIAMNFLVSHITRKPPIKVTSRWTFVCSSCP--VSLWSDKSHFEERHQCINYFEKVYGYMPLLRTQYRA 861
Cdd:pfam09258 161 RTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSgkVGLSSRPGHFLQRSKCINKFAAVFGYMPLVYSQIRL 240


                  .
gi 2257820060 862 D 862
Cdd:pfam09258 241 D 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 192-471 1.10e-23

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: 102.12  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 192 AGFSIYVYN-PEKYTIGERTDLV-----FEIYGILQKT------AYYTEREEDACSFIV------------LIGSLGSSS 247
Cdd:pfam03016   3 KGLKVYVYDlPPRFNEDLLQPCRsltgwYSAEQFLLESilhsriECRTSDPDEADCFFVpfyasldasrhlLNSALTDLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 248 SHFIREQLQSLPHWGK-NGSNHILLKLSDRYTQSLLLLEANMGLSILATSTYLPDV-QYRIGFDVIVpPLLGPTSGEVWA 325
Cdd:pfam03016  83 RELLDWLKSQYPYWNRsGGRDHFIVSGHPAWSFRRTAPDVDWGRAMLLNLTVLFSEdQFRPGKDVAL-PYPTPFHPDIGQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 326 QAGQQLPTLRKYFLTFEGsfhlsNEGAEEvskddlvflsKESSDLFIAVECvtydkiSNSAGWNLCGSHKNRTVR----- 400
Cdd:pfam03016 162 WQDISPSNRRKTLLFFAG-----NRRRGY----------SGKIRPLLLEEC------KGNPDADICGGLQCTPGRdkyme 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257820060 401 -LKKSTFSLVPVGNSgfVTHVRLIEALQTGAIPVILGTTNMLPLAEFIDWRSVSITLTPARIMELNTILRTV 471
Cdd:pfam03016 221 lLRSSRFCLQPPGDT--PTSPRLFDALLAGCIPVIISDGWELPFADVIDWRKFSVFVPENDIPELKSILRSL 290
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
63-144 9.62e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREvqiYGSKIERSKtETSRLQVKANRAKRDLEILQMERKRL 142
Cdd:COG2433   416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE---ERREIRKDR-EISRLDREIERLERELEEERERIEEL 491


                  ..
gi 2257820060 143 NK 144
Cdd:COG2433   492 KR 493
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 63-143 9.64e-05

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 43.05  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRhriqreVQIYgskiERSKTEtsrlqvkanrakrdLEILQMERKRL 142
Cdd:pfam10473  83 ENLTKELQKKQERVSELESLNSSLENLLEEKEQEK------VQMK----EESKTA--------------VEMLQTQLKEL 138


                  .
gi 2257820060 143 N 143
Cdd:pfam10473 139 N 139
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 63-144 2.27e-04

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: 44.37  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRL 142
Cdd:COG4942   146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225


                  ..
gi 2257820060 143 NK 144
Cdd:COG4942   226 EA 227
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 65-144 3.09e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  65 LMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKtetSRL-QVKANR----AKRDLEILQMER 139
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLgNVRNNKeyeaLQKEIESLKRRI 105


                  ....*
gi 2257820060 140 KRLNK 144
Cdd:COG1579   106 SDLED 110
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
65-142 3.10e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  65 LMERVEELRGQISELEKIKLSLSNELRDL---EAKRHRIQREVQIYgskiersKTETSRLQVKANRAKRDLEILQMERKR 141
Cdd:COG2433   425 LEAEVEELEAELEEKDERIERLERELSEArseERREIRKDREISRL-------DREIERLERELEEERERIEELKRKLER 497


                  .
gi 2257820060 142 L 142
Cdd:COG2433   498 L 498
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
65-144 3.41e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  65 LMERVEELRGQIS----ELEKIKLSLS---NELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQM 137
Cdd:COG4372    43 LQEELEQLREELEqareELEQLEEELEqarSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122


                  ....*..
gi 2257820060 138 ERKRLNK 144
Cdd:COG4372   123 ERQDLEQ 129
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
625-740 8.82e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 41.52  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060 625 FTVVMLTYERELVLMEAIQRLVGLSYLN-KVVIVWNSPLAPSL----SLHWPDigvpVHVVRTTKN----SLNNRFLpyD 695
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPfEVIVVDNGSTDGTAellaALAFPR----VRVIRNPENlgfaAARNLGL--R 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257820060 696 VIETDAILSIDDDVELRHD--EILLAFR---VWRENRDRIVGFPGRYHAW 740
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDwlERLLAAAcllIRREVFEEVGGFDERFFLY 128
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 67-116 9.54e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.51  E-value: 9.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257820060  67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKT 116
Cdd:PRK03992    1 ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKS 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-144 1.22e-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: 42.74  E-value: 1.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060   67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-144 1.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060  67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
65-144 1.55e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  65 LMERVEELRGQISELEKIKLSLSNELRDLEAKRhriqREvqiygskiERSKTETSRLQVKANRAKRD--LEILQM---ER 139
Cdd:COG1340    13 LEEKIEELREEIEELKEKRDELNEELKELAEKR----DE--------LNAQVKELREEAQELREKRDelNEKVKElkeER 80


                  ....*
gi 2257820060 140 KRLNK 144
Cdd:COG1340    81 DELNE 85
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 50-142 1.58e-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: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  50 QTRTKLDKtfgkdefLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAK 129
Cdd:COG4942    24 EAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90
                  ....*....|...
gi 2257820060 130 RDLEILQMERKRL 142
Cdd:COG4942    97 AELEAQKEELAEL 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
50-144 1.75e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  50 QTRTKLDKTFGKDEFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVK----- 124
Cdd:COG4372   112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDellke 191

                          90       100
                  ....*....|....*....|
gi 2257820060 125 ANRAKRDLEILQMERKRLNK 144
Cdd:COG4372   192 ANRNAEKEEELAEAEKLIES 211
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
67-144 2.06e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060  67 ERVEELRGQISELEKiklslsnELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:COG4372   108 EEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 61-142 2.07e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 38.70  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  61 KDEFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQRevqiygsKIERSKTETSRLQVKANRAKRDLEILQMERK 140
Cdd:pfam13863  25 LEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALK-------KAEEETKLKKEKEKEIKKLTAQIEELKSEIS 97


                  ..
gi 2257820060 141 RL 142
Cdd:pfam13863  98 KL 99
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-144 2.47e-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: 41.58  E-value: 2.47e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060   67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-142 3.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  54 KLDKTFGKDEFLMERVEELRGQIS----------ELEKIKLSLSNELRDLEAKRHRIQREVQIYG-SKIERSKTETSRLQ 122
Cdd:PRK03918  519 ELEKKAEEYEKLKEKLIKLKGEIKslkkelekleELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598

                          90       100
                  ....*....|....*....|....*.
gi 2257820060 123 ------VKANRAKRDLEILQMERKRL 142
Cdd:PRK03918  599 pfyneyLELKDAEKELEREEKELKKL 624
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
51-142 3.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  51 TRTKLDKTFGKDEFLMERVEELRGQISELEKI------------KLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTET 118
Cdd:PRK03918  624 LEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelreeYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703

                          90       100
                  ....*....|....*....|....
gi 2257820060 119 SRLQvkanRAKRDLEILQMERKRL 142
Cdd:PRK03918  704 EERE----KAKKELEKLEKALERV 723
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 67-152 3.23e-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: 41.21  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060   67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLE-----ILQMERKR 141
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEeleedLSSLEQEI 753

                           90
                   ....*....|.
gi 2257820060  142 LNKCPQLPHLR 152
Cdd:TIGR02169  754 ENVKSELKELE 764
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 50-144 3.44e-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: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  50 QTRTKLDKTfgkDEFLmERVE----ELRGQISELEKIK------LSLSNELRDLEA-----KRHRIQREVQIYGSKIERS 114
Cdd:COG1196   176 EAERKLEAT---EENL-ERLEdilgELERQLEPLERQAekaeryRELKEELKELEAellllKLRELEAELEELEAELEEL 251

                          90       100       110
                  ....*....|....*....|....*....|
gi 2257820060 115 KTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELEL 281
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 65-142 3.56e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 39.14  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  65 LMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQ-IYGSKIERSKTETSRLQVKANRAKRDLE---ILQMERK 140
Cdd:PRK14473   37 LNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAkIVAQAQERARAQEAEIIAQARREAEKIKeeaRAQAEQE 116


                  ..
gi 2257820060 141 RL 142
Cdd:PRK14473  117 RQ 118
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-144 4.64e-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: 40.13  E-value: 4.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060  67 ERVEELRGQISELEKiklslsnELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:COG4942    27 AELEQLQQEIAELEK-------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-144 5.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  50 QTRTKLDKTfgkdEFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQrevqiygSKIERSKTETSRLQVKANRAK 129
Cdd:PRK03918  218 ELREELEKL----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-------ERIEELKKEIEELEEKVKELK 286

                          90
                  ....*....|....*
gi 2257820060 130 rDLEILQMERKRLNK 144
Cdd:PRK03918  287 -ELKEKAEEYIKLSE 300
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 67-143 5.47e-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: 40.44  E-value: 5.47e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257820060   67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREvqiygskIERSKTETSRLQVKANRAKRDLEILQMERKRLN 143
Cdd:TIGR02169  854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------RDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-144 6.77e-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: 40.43  E-value: 6.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257820060   67 ERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREVQIYGSKIERSKTETSRLQVKANRAKRDLEILQMERKRLNK 144
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 52-128 8.03e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060   52 RTKLDKTFGK-DEFLMERVEELRGQISELEKIKLSLSNELR-----DLEAKRHRIQREVQIYGSKIERSKTE-TSRLQVK 124
Cdd:smart00935  20 QKQLEKEFKKrQAELEKLEKELQKLKEKLQKDAATLSEAARekkekELQKKVQEFQRKQQKLQQDLQKRQQEeLQKILDK 99


                   ....
gi 2257820060  125 ANRA 128
Cdd:smart00935 100 INKA 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
65-144 9.45e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  65 LMERVEELRGQI---SELEKIKLSLSNELRDLEAKRHRIQREVQIYGSK-IERSKTETSRLQVKANRAKRDLEILQMERK 140
Cdd:COG4717   144 LPERLEELEERLeelRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELE 223


                  ....
gi 2257820060 141 RLNK 144
Cdd:COG4717   224 ELEE 227
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 63-118 9.50e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 37.13  E-value: 9.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257820060  63 EFLMERVEELRGQISELEKIKLSLSNELRDLEAKRHRIQREV----QIYGSKIERSKTET 118
Cdd:cd20482     3 ESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEInetfQFYRSMLEERKDEL 62
 
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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