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Conserved domains on  [gi|818897332|gb|KKW31676|]
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Chromosome partition protein Smc, partial [Candidatus Uhrbacteria bacterium GW2011_GWA2_52_8d]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-170 1.66e-89

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 280.67  E-value: 1.66e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGR 80
Cdd:COG1196    1 MRLKRLELAGFKSFADPTTIPFEPG------ITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 AGFAQVSLSLNNEDGSMPIDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTP 160
Cdd:COG1196   75 LGRAEVSLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKP 154

                        170
                 ....*....|
gi 818897332 161 EERKSFFDDA 170
Cdd:COG1196  155 EERRAIIEEA 164
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-170 1.66e-89

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 280.67  E-value: 1.66e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGR 80
Cdd:COG1196    1 MRLKRLELAGFKSFADPTTIPFEPG------ITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 AGFAQVSLSLNNEDGSMPIDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTP 160
Cdd:COG1196   75 LGRAEVSLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKP 154

                        170
                 ....*....|
gi 818897332 161 EERKSFFDDA 170
Cdd:COG1196  155 EERRAIIEEA 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-170 2.94e-75

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: 243.81  E-value: 2.94e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332     3 LTKLELQGFKTFAKKTELSFlPPSsqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGRAG 82
Cdd:TIGR02168    2 LKKLELAGFKSFADPTTINF-DKG-----ITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    83 FAQVSLSLNNEDGSMP-IDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTPE 161
Cdd:TIGR02168   76 LAEVELVFDNSDGLLPgADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPE 155


                   ....*....
gi 818897332   162 ERKSFFDDA 170
Cdd:TIGR02168  156 ERRAIFEEA 164
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2-170 4.02e-54

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 184.02  E-value: 4.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332     2 HLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSegKGRA 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPG------FTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKS--GAFV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    82 GFAQVSLSLNNEDGSMPIDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTPE 161
Cdd:pfam02463   73 NSAEVEITFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKP 152


                   ....*....
gi 818897332   162 ERKSFFDDA 170
Cdd:pfam02463  153 ERRLEIEEE 161
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 3-156 4.26e-45

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 146.84  E-value: 4.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGRAG 82
Cdd:cd03278    1 LKKLELKGFKSFADKTTIPFPPG------LTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPAN 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818897332  83 FAQVSLSLNNEDGsmpidythvtitrrlyrdgtseyllnespvrladiqlllaqanvgqrSYSVVGQGMIDHIL 156
Cdd:cd03278   75 FAEVTLTFDNSDG-----------------------------------------------RYSIISQGDVSEII 101
recF PRK00064
recombination protein F; Reviewed
 1-168 9.57e-08

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 50.16  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKkTELSFLPPssqrcpITAVVGPNGSGKSNLADAIrWVLGeqSLKLLRGKESQDVIFSGSEGkgr 80
Cdd:PRK00064   1 MYLTRLSLTDFRNYEE-LDLELSPG------VNVLVGENGQGKTNLLEAI-YLLA--PGRSHRTARDKELIRFGAEA--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 agfAQVSLSLNNEDGSMPIDYTHVTITRRLYRdgtseylLNESPV-RLAD-IQLLlaqanvgqrsySVVgqgMI----DH 154
Cdd:PRK00064  68 ---AVIHGRVEKGGRELPLGLEIDKKGGRKVR-------INGEPQrKLAElAGLL-----------NVV---LFtpedLR 123

                        170
                 ....*....|....
gi 818897332 155 ILVSTPEERKSFFD 168
Cdd:PRK00064 124 LVKGGPSERRRFLD 137
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
32-54 1.73e-03

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 37.21  E-value: 1.73e-03
                         10        20
                 ....*....|....*....|...
gi 818897332  32 ITAVVGPNGSGKSNLADAIRWVL 54
Cdd:NF040873  20 LTAVVGPNGSGKSTLLKVLAGVL 42
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-170 1.66e-89

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 280.67  E-value: 1.66e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGR 80
Cdd:COG1196    1 MRLKRLELAGFKSFADPTTIPFEPG------ITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 AGFAQVSLSLNNEDGSMPIDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTP 160
Cdd:COG1196   75 LGRAEVSLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKP 154

                        170
                 ....*....|
gi 818897332 161 EERKSFFDDA 170
Cdd:COG1196  155 EERRAIIEEA 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-170 2.94e-75

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: 243.81  E-value: 2.94e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332     3 LTKLELQGFKTFAKKTELSFlPPSsqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGRAG 82
Cdd:TIGR02168    2 LKKLELAGFKSFADPTTINF-DKG-----ITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    83 FAQVSLSLNNEDGSMP-IDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTPE 161
Cdd:TIGR02168   76 LAEVELVFDNSDGLLPgADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPE 155


                   ....*....
gi 818897332   162 ERKSFFDDA 170
Cdd:TIGR02168  156 ERRAIFEEA 164
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2-170 4.02e-54

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 184.02  E-value: 4.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332     2 HLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSegKGRA 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPG------FTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKS--GAFV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    82 GFAQVSLSLNNEDGSMPIDYTHVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTPE 161
Cdd:pfam02463   73 NSAEVEITFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKP 152


                   ....*....
gi 818897332   162 ERKSFFDDA 170
Cdd:pfam02463  153 ERRLEIEEE 161
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 3-156 4.26e-45

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 146.84  E-value: 4.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGRAG 82
Cdd:cd03278    1 LKKLELKGFKSFADKTTIPFPPG------LTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPAN 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818897332  83 FAQVSLSLNNEDGsmpidythvtitrrlyrdgtseyllnespvrladiqlllaqanvgqrSYSVVGQGMIDHIL 156
Cdd:cd03278   75 FAEVTLTFDNSDG-----------------------------------------------RYSIISQGDVSEII 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-169 8.75e-38

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: 137.12  E-value: 8.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332     2 HLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGrA 81
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIPFSKG------FTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQS-G 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    82 GFAQVSLSLNNEDGSMPIDYThVTITRRLYRDG-TSEYLLNESPVRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTP 160
Cdd:TIGR02169   74 NEAYVTVTFKNDDGKFPDELE-VVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSP 152


                   ....*....
gi 818897332   161 EERKSFFDD 169
Cdd:TIGR02169  153 VERRKIIDE 161
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1-156 1.43e-23

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 92.75  E-value: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKKTELSFLPPSsqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGsegkGR 80
Cdd:cd03273    1 MHIKEIILDGFKSYATRTVISGFDPQ-----FNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKR----GQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 AGF--AQVSLSLNNED-GSMPIDYTH---VTITRRLYRDGTSEYLLNESPVRLADIQLLL--AQANVGQRSYsVVGQGMI 152
Cdd:cd03273   72 AGItkASVTIVFDNSDkSQSPIGFENypeITVTRQIVLGGTNKYLINGHRAQQQRVQDLFqsVQLNVNNPHF-LIMQGRI 150


                 ....
gi 818897332 153 DHIL 156
Cdd:cd03273  151 TKVL 154
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 3-139 2.37e-17

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 76.46  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSlKLLRGKESQDVIFSGSEGKGRAG 82
Cdd:cd03275    1 LKRLELENFKSYKGRHVIGPFDR------FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYRARVGKPDSN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 818897332  83 FAQVSLSLNNEDGSmpidythVTITRRLYRDGTSEYLLNESPVRLADIQLLLAQANV 139
Cdd:cd03275   74 SAYVTAVYEDDDGE-------EKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINI 123
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 3-92 7.26e-17

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 73.50  E-value: 7.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFAKKTelsFLPPSSqrcPITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVifsGSEGKGRAG 82
Cdd:cd03239    1 IKQITLKNFKSYRDET---VVGGSN---SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLA---GGGVKAGIN 71

                         90
                 ....*....|
gi 818897332  83 FAQVSLSLNN 92
Cdd:cd03239   72 SASVEITFDK 81
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 5-155 1.50e-15

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 71.52  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   5 KLELQGFKTFAKKTELSFLPPSsqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKlLRGKESQDVIFsgsEGKGRAGF- 83
Cdd:cd03272    3 QVIIQGFKSYKDQTVIEPFSPK-----HNVVVGRNGSGKSNFFAAIRFVLSDEYTH-LREEQRQALLH---EGSGPSVMs 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818897332  84 AQVSLSLNNEDGSMPIDYTHVTITRR--LYRDgtsEYLLNESPVRLADIQLLLAQANVgQRS--YSVVGQGMIDHI 155
Cdd:cd03272   74 AYVEIIFDNSDNRFPIDKEEVRLRRTigLKKD---EYFLDKKNVTKNDVMNLLESAGF-SRSnpYYIVPQGKINSL 145
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 3-110 5.99e-14

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 66.48  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVL-GEQSLKLLRGKESQDVIFSGSEGkgra 81
Cdd:cd03240    1 IDKLSIRNIRSFHERSEIEFFSP------LTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEVR---- 70

                         90       100
                 ....*....|....*....|....*....
gi 818897332  82 gfAQVSLSLNNEDGsmpidyTHVTITRRL 110
Cdd:cd03240   71 --AQVKLAFENANG------KKYTITRSL 91
AAA_23 pfam13476
AAA domain;
6-170 2.14e-13

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 64.82  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    6 LELQGFKTFaKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKGRAGFAQ 85
Cdd:pfam13476   1 LTIENFRSF-RDQTIDFSKG------LTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   86 VSLSLNNEDGsmpIDYTHVTITRRLYRDGTSEYllnespvRLADIQLLLAQANVGQRSYSVVGQGMIDHILVSTPEERKS 165
Cdd:pfam13476  74 VEITFENNDG---RYTYAIERSRELSKKKGKTK-------KKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREE 143


                  ....*
gi 818897332  166 FFDDA 170
Cdd:pfam13476 144 EFERK 148
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-130 1.59e-12

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 62.72  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   2 HLTKLELQGFKTFAKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKllRGKESQDVIFSGSEGkgra 81
Cdd:COG0419    1 KLLRLRLENFRSYRDTETIDFDDG------LNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSEE---- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818897332  82 gfAQVSLSLNNEDgsmpidyTHVTITRrlyRDGTSEYLLNESPVRLADI 130
Cdd:COG0419   69 --ASVELEFEHGG-------KRYRIER---RQGEFAEFLEAKPSERKEA 105
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
2-169 1.96e-11

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 60.94  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   2 HLTKLELQGFKTFAKkTELSFLPPssqrcpITAVVGPNGSGKSNLADAIrWVLGeqSLKLLRGKESQDVIFSGSEgkgra 81
Cdd:COG1195    1 RLKRLSLTNFRNYES-LELEFSPG------INVLVGPNGQGKTNLLEAI-YLLA--TGRSFRTARDAELIRFGAD----- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  82 gFAQVSLSLNNEDGSMPIDYthvtitrRLYRDGTSEYLLNESPV-RLADIqlllaqanVGQrsYSVVgqgMI---DHILV 157
Cdd:COG1195   66 -GFRVRAEVERDGREVRLGL-------GLSRGGKKRVRINGKPVrRLSDL--------AGL--LPVV---LFspeDLRLV 124

                        170
                 ....*....|...
gi 818897332 158 S-TPEERKSFFDD 169
Cdd:COG1195  125 KgGPSERRRFLDR 137
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 1-60 4.58e-11

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 60.02  E-value: 4.58e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFaKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLK 60
Cdd:COG3593    1 MKLEKIKIKNFRSI-KDLSIELSDD------LTVLVGENNSGKSSILEALRLLLGPSSSR 53
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 5-76 9.43e-11

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 56.98  E-value: 9.43e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818897332   5 KLELQGFKTFAKKTELSFLPPSsqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSE 76
Cdd:cd03227    1 KIVLGRFPSYFVPNDVTFGEGS-----LTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAV 67
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-79 2.88e-10

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 57.32  E-value: 2.88e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818897332   1 MHLTKLELQGFKTFaKKTELSFLPPSsqrcPITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEGKG 79
Cdd:COG3950    1 MRIKSLTIENFRGF-EDLEIDFDNPP----RLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDS 74
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 3-76 9.22e-10

ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 55.38  E-value: 9.22e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818897332   3 LTKLELQGFKTFAKKTELSFLPPSsqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESqDVIFSGSE 76
Cdd:cd03274    3 ITKLVLENFKSYAGEQVIGPFHKS-----FSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLS-DLIHNSAG 70
COG4637 COG4637
Predicted ATPase [General function prediction only];
3-53 2.12e-09

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 54.94  E-value: 2.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 818897332   3 LTKLELQGFKTFaKKTELSFlppssqrCPITAVVGPNGSGKSNLADAIRWV 53
Cdd:COG4637    2 ITRIRIKNFKSL-RDLELPL-------GPLTVLIGANGSGKSNLLDALRFL 44
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
2-54 8.10e-09

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 53.51  E-value: 8.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 818897332   2 HLTKLELQGFKTFAKKTELSFLPpSSQRC-PITAVVGPNGSGKSNLADAIRWVL 54
Cdd:COG1106    1 MLISFSIENFRSFKDELTLSMVA-SGLRLlRVNLIYGANASGKSNLLEALYFLR 53
recF PRK00064
recombination protein F; Reviewed
 1-168 9.57e-08

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 50.16  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKkTELSFLPPssqrcpITAVVGPNGSGKSNLADAIrWVLGeqSLKLLRGKESQDVIFSGSEGkgr 80
Cdd:PRK00064   1 MYLTRLSLTDFRNYEE-LDLELSPG------VNVLVGENGQGKTNLLEAI-YLLA--PGRSHRTARDKELIRFGAEA--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 agfAQVSLSLNNEDGSMPIDYTHVTITRRLYRdgtseylLNESPV-RLAD-IQLLlaqanvgqrsySVVgqgMI----DH 154
Cdd:PRK00064  68 ---AVIHGRVEKGGRELPLGLEIDKKGGRKVR-------INGEPQrKLAElAGLL-----------NVV---LFtpedLR 123

                        170
                 ....*....|....
gi 818897332 155 ILVSTPEERKSFFD 168
Cdd:PRK00064 124 LVKGGPSERRRFLD 137
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1-164 1.64e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.97  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332     1 MHLTKLELQGFKTFaKKTELSFLPPSSqrcPITAVVGPNGSGKSNLADAIRWVLGEqslKLLRGKESQDVIFSGSEGKGR 80
Cdd:TIGR00618    1 MKPLRLTLKNFGSY-KGTHTIDFTALG---PIFLICGKTGAGKTTLLDAITYALYG---KLPRRSEVIRSLNSLYAAPSE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332    81 AGFAQVSLSLNNEdgsmpIDYTHVTITRRLYRDGTSEyllnESPVRL----ADIQLLLAQANVGQ--------------- 141
Cdd:TIGR00618   74 AAFAELEFSLGTK-----IYRVHRTLRCTRSHRKTEQ----PEQLYLeqkkGRGRILAAKKSETEevihdllkldyktft 144

                          170       180
                   ....*....|....*....|...
gi 818897332   142 RSySVVGQGMIDHILVSTPEERK 164
Cdd:TIGR00618  145 RV-VLLPQGEFAQFLKAKSKEKK 166
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 1-54 8.00e-07

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 47.59  E-value: 8.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 818897332    1 MHLTKLELQGFKTFaKKTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVL 54
Cdd:pfam13175   1 MKIKSIIIKNFRCL-KDTEIDLDED------LTVLIGKNNSGKSSILEALDIFL 47
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 1-54 2.15e-06

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 45.72  E-value: 2.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 818897332   1 MHLTKLELQGFKTFAKKTELSFLPPSSQrcPITAVVGPNGSGKSNLADAIRWVL 54
Cdd:cd03279    1 MKPLKLELKNFGPFREEQVIDFTGLDNN--GLFLICGPTGAGKSTILDAITYAL 52
COG4938 COG4938
Predicted ATPase [General function prediction only];
3-97 1.01e-05

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 44.19  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFaKKTELSFLPpssqrcpITAVVGPNGSGKSNLAdairwvlgeQSLKLLRgkeSQDVIFSGSEgkgRAG 82
Cdd:COG4938    1 IKSISIKNFGPF-KEAELELKP-------LTLLIGPNGSGKSTLI---------QALLLLL---QSNFIYLPAE---RSG 57

                         90
                 ....*....|....*
gi 818897332  83 FAQVSLSLNNEDGSM 97
Cdd:COG4938   58 PARLYPSLVRELSDL 72
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 32-101 1.53e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 43.92  E-value: 1.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   32 ITAVVGPNGSGKSNLADAIRWVLGEQSlkllrgkesqDVIFSGSEGKGRAGFAQVSLSLNNEDGSMPIDY 101
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDA----------LVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEF 60
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
19-62 1.82e-04

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 40.38  E-value: 1.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 818897332  19 ELSFLPPSSQrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLL 62
Cdd:PRK11231  20 DLSLSLPTGK---ITALIGPNGCGKSTLLKCFARLLTPQSGTVF 60
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-72 4.10e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818897332   1 MHLTKLELQGFKTFAKKTeLSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVL----GEQSLKLLRGKESQDVIF 72
Cdd:COG4717    1 MKIKELEIYGFGKFRDRT-IEFSPG------LNVIYGPNEAGKSTLLAFIRAMLlerlEKEADELFKPQGRKPELN 69
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
 3-169 4.16e-04

ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213209 [Multi-domain]  Cd Length: 270  Bit Score: 39.59  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLELQGFKTFAKkTELSFLPPssqrcpITAVVGPNGSGKSNLADAIRWVLgeqSLKLLRGKESQDVIFSGsegkgrAG 82
Cdd:cd03242    1 LKSLELRNFRNYAE-LELEFEPG------VTVLVGENAQGKTNLLEAISLLA---TGKSHRTSRDKELIRWG------AE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  83 FAQVSLSLNNEDGSMPIDYTHVTITRRLYRdgtseylLNESPVR-LADiqlLLAQANVGQRSYSvvgqgmiDHILV-STP 160
Cdd:cd03242   65 EAKISAVLERQGGELALELTIRSGGGRKAR-------LNGIKVRrLSD---LLGVLNAVWFAPE-------DLELVkGSP 127


                 ....*....
gi 818897332 161 EERKSFFDD 169
Cdd:cd03242  128 ADRRRFLDR 136
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 32-50 7.83e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.99  E-value: 7.83e-04
                         10
                 ....*....|....*....
gi 818897332  32 ITAVVGPNGSGKSNLADAI 50
Cdd:cd00267   27 IVALVGPNGSGKSTLLRAI 45
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
 1-55 1.36e-03

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 38.10  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 818897332    1 MHLTKLELQGFKTFAKkTELSFLPPssqrcpITAVVGPNGSGKSNLADAIrWVLG 55
Cdd:TIGR00611   1 MYLSRLELTDFRNYDA-VDLELSPG------VNVIVGPNGQGKTNLLEAI-YYLA 47
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
32-54 1.73e-03

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 37.21  E-value: 1.73e-03
                         10        20
                 ....*....|....*....|...
gi 818897332  32 ITAVVGPNGSGKSNLADAIRWVL 54
Cdd:NF040873  20 LTAVVGPNGSGKSTLLKVLAGVL 42
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 32-65 1.87e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 37.51  E-value: 1.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 818897332  32 ITAVVGPNGSGKSNLadaIRWVLGEqsLKLLRGK 65
Cdd:cd03235   27 FLAIVGPNGAGKSTL---LKAILGL--LKPTSGS 55
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
 33-169 1.94e-03

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 37.57  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  33 TAVVGPNGSGKSNLADAIRWVLGEQSL-KLLRGKESQDVI---FSGSEGKgRAGFAQVSLSLNNEDgsmpidytHVTITR 108
Cdd:cd03241   24 TVLTGETGAGKSILLDALSLLLGGRASaDLIRSGAEKAVVegvFDISDEE-EAKALLLELGIEDDD--------DLIIRR 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818897332 109 RLYRDGTSEYLLNESPVRLADIQLLlaqanvGQRSYSVVGQGmiDHILVSTPEERKSFFDD 169
Cdd:cd03241   95 EISRKGRSRYFINGQSVTLKLLREL------GSLLVDIHGQH--DHQNLLNPERQLDLLDG 147
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 32-65 2.19e-03

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 37.38  E-value: 2.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 818897332  32 ITAVVGPNGSGKSNLadaIRWVLGEqsLKLLRGK 65
Cdd:COG1121   34 FVAIVGPNGAGKSTL---LKAILGL--LPPTSGT 62
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 5-74 3.72e-03

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 36.42  E-value: 3.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   5 KLELQGFKTFakkTELSFLPPSSqrcpITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSG 74
Cdd:cd03277    5 RIKLENFVTY---DETEFRPGPS----LNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRG 67
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 33-75 4.47e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 36.29  E-value: 4.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 818897332  33 TAVVGPNGSGKSNLADAIrwvLGEqsLKLLRGKesqdVIFSGS 75
Cdd:cd03250   34 VAIVGPVGSGKSSLLSAL---LGE--LEKLSGS----VSVPGS 67
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 31-93 4.50e-03

ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 36.04  E-value: 4.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818897332  31 PITAVVGPNGSGKSNLADAIRWVLGEQSLKLLRGKESQDVIFSGSEgkgragFAQVSLSLNNE 93
Cdd:cd03276   22 RVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGES------SAKITVTLKNQ 78
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
32-64 4.53e-03

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 36.25  E-value: 4.53e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 818897332  32 ITAVVGPNGSGKSNLadairwvlgeqsLKLLRG 64
Cdd:COG4559   29 LTAIIGPNGAGKSTL------------LKLLTG 49
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 6-55 4.73e-03

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 36.24  E-value: 4.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 818897332   6 LELQGF-KTFAKKT---ELSF-LPPSSqrcpITAVVGPNGSGKSNLadaIRWVLG 55
Cdd:COG4152    2 LELKGLtKRFGDKTavdDVSFtVPKGE----IFGLLGPNGAGKTTT---IRIILG 49
AAA_29 pfam13555
P-loop containing region of AAA domain;
32-54 4.76e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 34.11  E-value: 4.76e-03
                          10        20
                  ....*....|....*....|...
gi 818897332   32 ITAVVGPNGSGKSNLADAIRWVL 54
Cdd:pfam13555  24 NTLLTGPSGSGKSTLLDAIQTLL 46
recF PRK14079
recombination protein F; Provisional
 1-168 5.45e-03

recombination protein F; Provisional


Pssm-ID: 184491 [Multi-domain]  Cd Length: 349  Bit Score: 36.30  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332   1 MHLTKLELQGFKTFAKKTelsFLPPSSqrcpITAVVGPNGSGKSNLADAIRWVLGEQslkLLRGKESQDVIFSGSEGKGR 80
Cdd:PRK14079   1 MRLLSLRQLNYRNLAPPT---LAFPPG----VTAVVGENAAGKTNLLEAIYLALTGE---LPNGRLADLVRFGEGEAWVH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897332  81 AGF-AQVSLSlnnedgsmpidythvTITRRLYRdGTSEYLLNESPVRLADIqlllaqanvgQRSYSVVGQGMIDHILV-S 158
Cdd:PRK14079  71 AEVeTGGGLS---------------RLEVGLGP-GRRELKLDGVRVSLREL----------ARLPGAVLIRPEDLELVlG 124

                        170
                 ....*....|
gi 818897332 159 TPEERKSFFD 168
Cdd:PRK14079 125 PPEGRRAYLD 134
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-54 5.58e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 36.43  E-value: 5.58e-03
                          10        20
                  ....*....|....*....|...
gi 818897332   32 ITAVVGPNGSGKSNLADAIRWVL 54
Cdd:COG4913    26 GTLLTGDNGSGKSTLLDAIQTLL 48
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
3-51 9.24e-03

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 35.87  E-value: 9.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 818897332   3 LTKLE-LQGFKTFAKKTELSFLppssqrCPITAVVGPNGSGKSNLADAIR 51
Cdd:COG4694    2 ITKIKkLKNVGAFKDFGWLAFF------KKLNLIYGENGSGKSTLSRILR 45
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 32-50 9.85e-03

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 35.10  E-value: 9.85e-03
                         10
                 ....*....|....*....
gi 818897332  32 ITAVVGPNGSGKSNLADAI 50
Cdd:cd03214   27 IVGILGPNGAGKSTLLKTL 45
 
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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