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Conserved domains on  [gi|1473292296|ref|WP_117761688|]
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MULTISPECIES: hypothetical protein [Lachnospiraceae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 345-430 1.44e-31

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


:

Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 115.70  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 345 FKLTGYCSCSICTGQWSGGsTASGTTPTAGRTIAMG--GVPFGTKLMING-QVYTVEDRGTAYG--HVDIFCSSHSEALS 419
Cdd:cd14667     1 FTATAYTSCEGCCGGGPGG-TASGGLPVGGGTIAVDpsVIPLGTKVYIEGyGVYVVEDTGGAIKgnRIDIYMDSHAEALA 79

                          90
                  ....*....|.
gi 1473292296 420 FGVQYADVYQL 430
Cdd:cd14667    80 FGRRYVEVYIL 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 46-251 5.12e-30

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 119.55  E-value: 5.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQYMYE 125
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSSGNGYMAMLFSSKSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:COG3883    98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1473292296 206 AAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
 
Name Accession Description Interval E-value
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 345-430 1.44e-31

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 115.70  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 345 FKLTGYCSCSICTGQWSGGsTASGTTPTAGRTIAMG--GVPFGTKLMING-QVYTVEDRGTAYG--HVDIFCSSHSEALS 419
Cdd:cd14667     1 FTATAYTSCEGCCGGGPGG-TASGGLPVGGGTIAVDpsVIPLGTKVYIEGyGVYVVEDTGGAIKgnRIDIYMDSHAEALA 79

                          90
                  ....*....|.
gi 1473292296 420 FGVQYADVYQL 430
Cdd:cd14667    80 FGRRYVEVYIL 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 46-251 5.12e-30

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 119.55  E-value: 5.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQYMYE 125
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSSGNGYMAMLFSSKSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:COG3883    98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1473292296 206 AAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 344-430 1.27e-21

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 88.63  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 344 RFKLTGYCSCSICTGQWsGGSTASGTTPTAGRTIAMGG--VPFGTKLMINGQ-VYTVEDRGTA--YGHVDIFCSSHSEAL 418
Cdd:COG3584     1 TVTATAYTAGPECTGKG-GGITASGTRLRPGGVIAVDPdvIPLGTKVYIEGYgYAVAEDTGGAikGNRIDIYMPSVSEAL 79

                          90
                  ....*....|..
gi 1473292296 419 SFGVQYADVYQL 430
Cdd:COG3584    80 NWGRRTVTVYIL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-249 2.59e-07

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: 53.14  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   50 QSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKA------KEEEQYEAMKLRIQym 123
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarleAEVEQLEERIAQLS-- 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  124 YENSSGNGYMAMLFSSKSISELiSRAEYIQKISdfdrDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQE 203
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEE-ELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1473292296  204 L---YAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKE 249
Cdd:TIGR02168  829 LerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 46-252 1.61e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.69  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRI-QYMY 124
Cdd:pfam06160  88 LDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFsQFEE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 125 ENSSGNGYMAMLFSSKSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAI--VELQQQSSDQQEAIQ 202
Cdd:pfam06160 168 LTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALehLNVDKEIQQLEEQLE 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473292296 203 ELYAaayqelRTYSAELDDAksseSALVDEINSKADAINDLIrqakEEEI 252
Cdd:pfam06160 248 ENLA------LLENLELDEA----EEALEEIEERIDQLYDLL----EKEV 283
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-250 1.98e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQdqydakqnELVQIQADLEDAKAKEEEQYEAMKLRIQYMYE 125
Cdd:PRK02224  215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--------TLEAEIEDLRETIAETEREREELAEEVRDLRE 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 nssgngymamlfsskSISELISRAEYIQKISDFDR----DLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAI 201
Cdd:PRK02224  287 ---------------RLEELEEERDDLLAEAGLDDadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1473292296 202 QELYAAAyQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEE 250
Cdd:PRK02224  352 DDLEERA-EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
 
Name Accession Description Interval E-value
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 345-430 1.44e-31

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 115.70  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 345 FKLTGYCSCSICTGQWSGGsTASGTTPTAGRTIAMG--GVPFGTKLMING-QVYTVEDRGTAYG--HVDIFCSSHSEALS 419
Cdd:cd14667     1 FTATAYTSCEGCCGGGPGG-TASGGLPVGGGTIAVDpsVIPLGTKVYIEGyGVYVVEDTGGAIKgnRIDIYMDSHAEALA 79

                          90
                  ....*....|.
gi 1473292296 420 FGVQYADVYQL 430
Cdd:cd14667    80 FGRRYVEVYIL 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 46-251 5.12e-30

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 119.55  E-value: 5.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQYMYE 125
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSSGNGYMAMLFSSKSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:COG3883    98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1473292296 206 AAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-251 4.10e-27

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: 111.39  E-value: 4.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   1 MKKKKLFSLVLATVLTAATvlpcygastkEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNR 80
Cdd:COG4942     1 MRKLLLLALLLALAAAAQA----------DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  81 LQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQYMYENSSgNGYMAMLFSSKSISELISRAEYIQKISDFDR 160
Cdd:COG4942    71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-QPPLALLLSPEDFLDAVRRLQYLKYLAPARR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 161 DLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELYAAAYQELRTYSAELDDAKSSESALVDEINSKADAI 240
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229

                         250
                  ....*....|.
gi 1473292296 241 NDLIRQAKEEE 251
Cdd:COG4942   230 ARLEAEAAAAA 240
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 344-430 1.27e-21

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 88.63  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 344 RFKLTGYCSCSICTGQWsGGSTASGTTPTAGRTIAMGG--VPFGTKLMINGQ-VYTVEDRGTA--YGHVDIFCSSHSEAL 418
Cdd:COG3584     1 TVTATAYTAGPECTGKG-GGITASGTRLRPGGVIAVDPdvIPLGTKVYIEGYgYAVAEDTGGAikGNRIDIYMPSVSEAL 79

                          90
                  ....*....|..
gi 1473292296 419 SFGVQYADVYQL 430
Cdd:COG3584    80 NWGRRTVTVYIL 91
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 345-428 6.88e-20

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins; This family includes two subfamilies of conserved double-psi beta-barrel (DPBB) domain proteins, such as membrane-bound lytic murein transglycosylase A (MltA)-like proteins and YuiC-like proteins. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439261 [Multi-domain]  Cd Length: 92  Bit Score: 83.85  E-value: 6.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 345 FKLTGYCSCSICTGQWSGGsTASGTTPTAGRTIAmggV-----PFGTKLMING----QVYTVEDRGTA--YGHVDIFCSS 413
Cdd:cd22784     1 VTVTAYTPDEEQTDGGPGI-TASGVTLRGYGTVA---VdrdliPLGTKVKIEGpgsgGEYVVLDRGGAikGNRIDIYFPS 76

                          90
                  ....*....|....*
gi 1473292296 414 HSEALSFGVQYADVY 428
Cdd:cd22784    77 EKEAKKFGRQKVTVT 91
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 348-428 7.47e-15

double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of conserved double-psi beta-barrel (DPBB) fold proteins, such as Bacillus subtilis protein YuiC, cell wall shaping protein YabE, cell wall-binding protein YocH, as well as Clostridium tetani phosphatase-associated protein PapQ. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a double-psi beta-barrel (DPBB) fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439263 [Multi-domain]  Cd Length: 96  Bit Score: 69.94  E-value: 7.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 348 TGYCSCSICtGQWSGGSTASGTTPTAGRTIAMGG--VPFGTKLMINGqvY---TVEDRGTAYGH--VDIFCSSHSEALSF 420
Cdd:cd22786     9 TAYSPCSSS-GGGCYGITASGTPLKRKGTIAVDPsvIPLGTKVYIPG--YgyaVVADTGGAIKGnrIDLYFPTHEEAINW 85


                  ....*...
gi 1473292296 421 GVQYADVY 428
Cdd:cd22786    86 GRKTVEVY 93
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
47-248 2.16e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 56.18  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  47 DSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQY-----DAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQ 121
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 122 YMYEN-SSGNGYMAMLFSSKSISELISRAeyiqkisdfdRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEA 200
Cdd:COG3206   244 ALRAQlGSGPDALPELLQSPVIQQLRAQL----------AELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR 313

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1473292296 201 IQELYAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAK 248
Cdd:COG3206   314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 46-221 2.25e-08

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: 54.55  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEqyeamklriqymYE 125
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------------YE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSSGNG-----YMAMLfssksiSELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEA 200
Cdd:COG1579    80 EQLGNVrnnkeYEALQ------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153

                         170       180
                  ....*....|....*....|.
gi 1473292296 201 IQELYAAAYQELRTYSAELDD 221
Cdd:COG1579   154 LEAELEELEAEREELAAKIPP 174
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-250 6.49e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 6.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQ--DQYDAKQNELVQIQADLEDAkakeEEQYEAMKLriqym 123
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAEL----EAELERLDA----- 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  124 yenssgngymamlfSSKSISELISRAEYIQKIsdfdrdlMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQE 203
Cdd:COG4913    683 --------------SSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1473292296  204 LYAAAYQEL--RTYSAELDDAksSESALVDEINSKADAINDLIRQAKEE 250
Cdd:COG4913    742 LARLELRALleERFAAALGDA--VERELRENLEERIDALRARLNRAEEE 788
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-251 1.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQyEAMKLRIQYMYE 125
Cdd:COG1196   276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSSGNgymAMLFSSKSISELISRAEYIQKISDFDRDLMQEyedtVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:COG1196   355 EAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1473292296 206 AAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
46-250 1.93e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.22  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQL-------DDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMK- 117
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKRDELNEELkelaekrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNe 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 118 LRIQYMYENSSGNGYMAMLFSSKSISELISRAEYIQKISDFD-----------RDLMQEYEdTVDQVKEKETQVQEEQAA 186
Cdd:COG1340    90 LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSpeeekelvekiKELEKELE-KAKKALEKNEKLKELRAE 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473292296 187 IVELQQQSSDQQEAIQELYAAA----------YQELRTYSAELDDAKssesALVDEINSKADAINDLIRQAKEE 250
Cdd:COG1340   169 LKELRKEAEEIHKKIKELAEEAqelheemielYKEADELRKEADELH----KEIVEAQEKADELHEEIIELQKE 238
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-251 2.47e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSelnQQLDDLQNRLQELQDQ---YDAKQNELVQIQADLEDAKAKEEE-QYEAMKLRIQ 121
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNL---KELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEElREELEKLEKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 122 YMYENSsgngYMAMLFSSKSISELISRAEYIqkisdfdRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAI 201
Cdd:COG4717   125 LQLLPL----YQELEALEAELAELPERLEEL-------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473292296 202 QELYAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-249 2.59e-07

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: 53.14  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   50 QSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKA------KEEEQYEAMKLRIQym 123
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarleAEVEQLEERIAQLS-- 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  124 YENSSGNGYMAMLFSSKSISELiSRAEYIQKISdfdrDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQE 203
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEE-ELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1473292296  204 L---YAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKE 249
Cdd:TIGR02168  829 LerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-252 2.85e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  42 AQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKaKEEEQYEAMKLRIQ 121
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-ERRRELEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 122 ymyenssgngymamlfssKSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAI 201
Cdd:COG1196   323 ------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1473292296 202 QELYAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEEI 252
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-246 3.31e-07

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: 52.75  E-value: 3.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   49 IQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEE---QYEAMKLRIQYMYE 125
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  126 NSSG--NGYMAMLFSSKSISELISRAEyiQKISDFDRDLMQEYEDTVDQVKEK-ETQVQEEQAAIVELQQQSSDQQ---E 199
Cdd:TIGR02168  380 QLETlrSKVAQLELQIASLNNEIERLE--ARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQeelE 457

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1473292296  200 AIQELYAAAYQELRTYSAELDDAKSSEsalvDEINSKADAINDLIRQ 246
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAEREL----AQLQARLDSLERLQEN 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-252 3.25e-06

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: 49.67  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   29 KEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKaK 108
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE-R 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  109 EEEQYEAMKLRIQymyenssgngymamlfssKSISELISRAEYIQKISDfdrDLMQEYEDTVDQVKEKETQVQEEQAAIV 188
Cdd:TIGR02168  317 QLEELEAQLEELE------------------SKLDELAEELAELEEKLE---ELKEELESLEAELEELEAELEELESRLE 375

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473292296  189 ELQQQSSDQQEAIQELYAAAYQ---ELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEEI 252
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-252 5.84e-06

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: 48.91  E-value: 5.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   50 QSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQ---DQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQymyen 126
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----- 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  127 ssgngymamlfssksisELISRAEYIQKisdFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQsSDQQEAIQELYA 206
Cdd:TIGR02169  865 -----------------ELEEELEELEA---ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELK 923

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1473292296  207 AAYQELRTYSAELDDAKSSESALVDEINSKADAinDLIRQAKEEEI 252
Cdd:TIGR02169  924 AKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--QAELQRVEEEI 967
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-234 1.34e-05

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: 47.74  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   28 TKEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADL---ED 104
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallRS 894

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  105 AKAKEEEQYEAMKLRIQYMYENSSGngymamlfSSKSISELISRAEYI-QKISDFDRDLMQEYEDTVDQVKEKETQVQEE 183
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEE--------LREKLAQLELRLEGLeVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473292296  184 QAaivELQQQSSDQQEAIQEL-------------YAAAYQELRTYSAELDDAKSSESALVDEIN 234
Cdd:TIGR02168  967 EE---EARRRLKRLENKIKELgpvnlaaieeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-247 1.58e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQY-DAKQNELVQIQADLEDAKAKEEEQYEAmklriqymy 124
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR--------- 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  125 enssgngymamlfssksiselisRAEYIQKIsdfdRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQEL 204
Cdd:COG4913    361 -----------------------RARLEALL----AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1473292296  205 YAAAYQELRTYSAELDDAKSSESAlvdeINSKADAINDLIRQA 247
Cdd:COG4913    414 LRDLRRELRELEAEIASLERRKSN----IPARLLALRDALAEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-249 1.75e-05

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: 47.36  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   26 ASTKEKISNAQAEQAAAQSQLDSIQSRIDELNSKkgqseeyLSELNQQLDDLQNRLQELQDQYDAKQNELVqiqaDLEDA 105
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAE-------LTLLNEEAANLRERLESLERRIAATERRLE----DLEEQ 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  106 KAKEEEQYEAMKLRIQYMyenssgngymamlfsSKSISELISRAEYIQKISDFDRDLMQ----EYEDTVDQVKEKETQVQ 181
Cdd:TIGR02168  847 IEELSEDIESLAAEIEEL---------------EELIEELESELEALLNERASLEEALAllrsELEELSEELRELESKRS 911

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1473292296  182 EEQAAIVELQQQSSDQQEAIQELYAAAyQELRT-----YSAELDDAKSSESALVDEINSKADAINDLIRQAKE 249
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVRI-DNLQErlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
52-252 5.29e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  52 RIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAM-KLRIQYMYENSSGN 130
Cdd:COG1340    30 KRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELdELRKELAELNKAGG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 131 gymamlfSSKSISELISRAEYIQKISDFD-----------RDLMQEYEdTVDQVKEKETQVQEEQAAIVELQQQSSDQQE 199
Cdd:COG1340   110 -------SIDKLRKEIERLEWRQQTEVLSpeeekelvekiKELEKELE-KAKKALEKNEKLKELRAELKELRKEAEEIHK 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 200 AIQELYaaayQELRTYSAELDDAKSSesalVDEINSKADAINDLIRQAKE-------EEI 252
Cdd:COG1340   182 KIKELA----EEAQELHEEMIELYKE----ADELRKEADELHKEIVEAQEkadelheEII 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-213 7.35e-05

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: 45.43  E-value: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   26 ASTKEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQ-------NRLQELQDQYDAKQNELVQI 98
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeelreleSKRSELRRELEELREKLAQL 927

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   99 QADLEDAKAKEEEQYEAMKLRIQYMYENSSGNgYMAMLFSSKSISELISRAE-YIQKISDFDRDLMQEYEDTVDQVKEKE 177
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLEnKIKELGPVNLAAIEEYEELKERYDFLT 1006

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1473292296  178 TQVQEEQAAIVELQQQSSDQQEAIQELYAAAYQELR 213
Cdd:TIGR02168 1007 AQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVN 1042
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 30-239 8.72e-05

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: 45.06  E-value: 8.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   30 EKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKE 109
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  110 EEqYEAMKLRIQYMYENSSGNGymamlfssKSISELISRAEyiQKISDFDRDLmqeyEDTVDQVKEKETQVQEEQAAIVE 189
Cdd:TIGR02169  402 NE-LKRELDRLQEELQRLSEEL--------ADLNAAIAGIE--AKINELEEEK----EDKALEIKKQEWKLEQLAADLSK 466

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1473292296  190 LQQQSSDQQEAIQELyaaaYQELRTYSAELDDAKSSESALVDEINSKADA 239
Cdd:TIGR02169  467 YEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-251 9.92e-05

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: 44.67  E-value: 9.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQnrlqelQDQYDAKQNELVQIQADLEDAK----AKEEEQYEAMKLRIQ 121
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLErsiaEKERELEDAEERLAK 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  122 YMYENSSGNGYMAMLfsSKSISELisRAEYIQKISDFDrDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAI 201
Cdd:TIGR02169  327 LEAEIDKLLAEIEEL--EREIEEE--RKRRDKLTEEYA-ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1473292296  202 QEL---YAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:TIGR02169  402 NELkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-276 1.16e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQYMYE 125
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSSGNGYMAMLFSSksisELISRAEYIQKISDFDRDLmQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:COG1196   398 LAAQLEELEEAEEA----LLERLERLEEELEELEEAL-AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473292296 206 AAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEEIAAQKKAEEEAAAAAAAQQAAAEAE 276
Cdd:COG1196   473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 345-417 1.53e-04

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and similar proteins; MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. This model corresponds to the DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis. It is involved in substrate binding and catalysis.


Pssm-ID: 439262 [Multi-domain]  Cd Length: 97  Bit Score: 40.70  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 345 FKLTGYcscsictgqWSGGSTASGTTPTAGRTIAM--GGVPFGTKLMI--------------NGqVYTVEDRGTAY--GH 406
Cdd:cd22785     1 VLITGY---------YTPPRGALGVPLTPFRSVAVdpSVIPLGSVVYIpaldgvklpdgephDG-LFIAQDTGGAIkgKH 70

                          90
                  ....*....|.
gi 1473292296 407 VDIFCSSHSEA 417
Cdd:cd22785    71 IDVFTGSGDEA 81
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 46-252 1.61e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.69  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRI-QYMY 124
Cdd:pfam06160  88 LDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFsQFEE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 125 ENSSGNGYMAMLFSSKSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAI--VELQQQSSDQQEAIQ 202
Cdd:pfam06160 168 LTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALehLNVDKEIQQLEEQLE 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473292296 203 ELYAaayqelRTYSAELDDAksseSALVDEINSKADAINDLIrqakEEEI 252
Cdd:pfam06160 248 ENLA------LLENLELDEA----EEALEEIEERIDQLYDLL----EKEV 283
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-250 1.98e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQdqydakqnELVQIQADLEDAKAKEEEQYEAMKLRIQYMYE 125
Cdd:PRK02224  215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--------TLEAEIEDLRETIAETEREREELAEEVRDLRE 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 nssgngymamlfsskSISELISRAEYIQKISDFDR----DLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAI 201
Cdd:PRK02224  287 ---------------RLEELEEERDDLLAEAGLDDadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1473292296 202 QELYAAAyQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEE 250
Cdd:PRK02224  352 DDLEERA-EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 46-251 2.32e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKaKEEEQYeamKLRIQYMye 125
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK-KENQSY---KQEIKNL-- 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 nssgngymamlfsSKSISELISRAEYIQKISdfdrdlmQEYEdtvDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:TIGR04523 390 -------------ESQINDLESKIQNQEKLN-------QQKD---EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1473292296 206 AAAY-----------------QELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEE 251
Cdd:TIGR04523 447 NQDSvkeliiknldntresleTQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-263 2.70e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLsELNQQLDDLQ-----NRLQELQDQYDAKQNELVQIQADLEDAKAK---EEEQYEAMK 117
Cdd:COG1196   195 LGELERQLEPLERQAEKAERYR-ELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAElaeLEAELEELR 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 118 LRIQymyenssgngymamlfsskSISELISRAeyiqkisdfdRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQ 197
Cdd:COG1196   274 LELE-------------------ELELELEEA----------QAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473292296 198 QEAIQELYAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKEEEIAAQKKAEEEAA 263
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 46-250 2.98e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEdaKAKEEEQYEAMKLRIQYMYE 125
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN--KDDFELKKENLEKEIDEKNK 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 NSS--GNGYMAMLFSSKSISELIsrAEYIQKISDFDRDLmQEYEDTVDQVKEKETQVQEEQAAIVELQQQssdqqeaIQE 203
Cdd:TIGR04523 569 EIEelKQTQKSLKKKQEEKQELI--DQKEKEKKDLIKEI-EEKEKKISSLEKELEKAKKENEKLSSIIKN-------IKS 638

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473292296 204 LYAAAYQELRTYSAELDDAKSSESALVDEIN---SKADAINDLIRQAKEE 250
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKeskTKIDDIIELMKDWLKE 688
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
24-241 3.96e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  24 YGASTKEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQY----------DAKQN 93
Cdd:PRK02224  231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERddllaeagldDADAE 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  94 ELVQIQADLEDAKAKEEEQYEAMKLRIQYMYENSSGNgymamlfsSKSISELISRAEYIQKISDfdrDLMQEYEDTVDQV 173
Cdd:PRK02224  311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL--------REDADDLEERAEELREEAA---ELESELEEAREAV 379

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1473292296 174 KEKETQVQEEQAAIVELQQQSSDQQEAIQElyAAAYQELRTysAELDDAKSSESALVDEINSKADAIN 241
Cdd:PRK02224  380 EDRREEIEELEEEIEELRERFGDAPVDLGN--AEDFLEELR--EERDELREREAELEATLRTARERVE 443
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-251 4.93e-04

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: 42.75  E-value: 4.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   53 IDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQ------IQADLEDAKAKE--------EEQYEAMKL 118
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGYEllkekealERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  119 RIQYMYENSSGngymamlfSSKSISELISRAEYI-QKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQ 197
Cdd:TIGR02169  245 QLASLEEELEK--------LTEEISELEKRLEEIeQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473292296  198 QEAIQELYAAAYQELRTYSAELDDAKSS-------ESALVDEINSKADAINDLIRQAKEEE 251
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREieeerkrRDKLTEEYAELKEELEDLRAELEEVD 377
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-291 5.98e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQYEAMKLRIQymye 125
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE---- 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 126 nSSGNGYMAMLFSSKSISELISRAEYIQKIsdfDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELY 205
Cdd:COG1196   380 -ELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 206 AAAYQELRTYSAELDDAKSSESALVDEINSKADAIN-DLIRQAKEEEIAAQKKAEEEAAAAAAAQQAAAEAEAEAARKQA 284
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAArLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535


                  ....*..
gi 1473292296 285 AEAARVA 291
Cdd:COG1196   536 YEAALEA 542
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-249 7.27e-04

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: 41.98  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   46 LDSIQSRIDELNSK-------KGQSEEY-------------------------LSELNQQLDDLQNRLQELQDQYDAKQN 93
Cdd:TIGR02169  186 IERLDLIIDEKRQQlerlrreREKAERYqallkekreyegyellkekealerqKEAIERQLASLEEELEKLTEEISELEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   94 ELVQIQADLEDAKAKEEEQYEAMKLRIQymyenssgngymamlfssKSISELISRAEYIQKISDFDRDLMQEYEDTVDQV 173
Cdd:TIGR02169  266 RLEEIEQLLEELNKKIKDLGEEEQLRVK------------------EKIGELEAEIASLERSIAEKERELEDAEERLAKL 327

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473292296  174 KEKETQVQEEQAAIVELQQQSSDQQEAIQELYAAAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAKE 249
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
46 PHA02562
endonuclease subunit; Provisional
 48-249 1.01e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  48 SIQSRIDELNskkgqsEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEQY-EAMKLRIQYMYEN 126
Cdd:PHA02562  163 SVLSEMDKLN------KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYdELVEEAKTIKAEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 127 SSGNGYMAMLfssksISELISRAEYIQKISDFDRDL-----------------------MQEYEDTV-------DQVKEK 176
Cdd:PHA02562  237 EELTDELLNL-----VMDIEDPSAALNKLNTAAAKIkskieqfqkvikmyekggvcptcTQQISEGPdritkikDKLKEL 311

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1473292296 177 ETQVQEEQAAIVELQQQSS---DQQEAIQELYAAAYQELRTYSAELDDAKSSESA---LVDEINSKADAINDLIRQAKE 249
Cdd:PHA02562  312 QHSLEKLDTAIDELEEIMDefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKLQDELDK 390
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 28-251 1.14e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  28 TKEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLS----------ELNQQLDDLQNRLQELQDQYDAKQNELVQ 97
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSnlkkkiqknkSLESQISELKKQNNQLKDNIEKKQQEINE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  98 IQADLEDAKAK----EEEQYEAMKLRIQYMYENSSGNGYMAMLfsSKSISELISRAEYI--QKISDFDRDLMQEYEDTVD 171
Cdd:TIGR04523 244 KTTEISNTQTQlnqlKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEK 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 172 QVKEKETQVQEEQAAIVELQQQSSDQQEAIQELYA---AAYQELRTYSAELDDAKSSESALVDEINSKADAINDLIRQAK 248
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401


                  ...
gi 1473292296 249 EEE 251
Cdd:TIGR04523 402 NQE 404
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 67-250 1.58e-03

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: 39.91  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  67 LSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKeeeqyeamklriqymyenssgngymamlfssksiselI 146
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-------------------------------------I 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 147 SRAEyiQKISDfDRDLMQEYEDTVDQVK-EKE-TQVQEEQAAIVELQQQSSDQQEAIQELYAAAYQELRTYSAELDDAKS 224
Cdd:COG1579    62 KRLE--LEIEE-VEARIKKYEEQLGNVRnNKEyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                         170       180
                  ....*....|....*....|....*.
gi 1473292296 225 SESALVDEINSKADAINDLIRQAKEE 250
Cdd:COG1579   139 ELEEKKAELDEELAELEAELEELEAE 164
PRK11281 PRK11281
mechanosensitive channel MscK;
47-236 2.51e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   47 DSIQSRIDELNSKKGQSEE---YLSELNQQLDDLQN------RLQELQDQYDAKQNELVQIQADLEDAKAKE----EEQY 113
Cdd:PRK11281    39 ADVQAQLDALNKQKLLEAEdklVQQDLEQTLALLDKidrqkeETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetRETL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  114 EAMKLR-IQYMYENSSG---------NGYMAMLFSSKSISE-----LISRAEYIQKIsdfDRDLMQEYEDTVDQVKEKET 178
Cdd:PRK11281   119 STLSLRqLESRLAQTLDqlqnaqndlAEYNSQLVSLQTQPEraqaaLYANSQRLQQI---RNLLKGGKVGGKALRPSQRV 195

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473292296  179 QVQEEQAAI---VELQQQSSDQQEAIQELYAAAYQELRTYSAELDdakSSESALVDEINSK 236
Cdd:PRK11281   196 LLQAEQALLnaqNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLE---HQLQLLQEAINSK 253
mukB PRK04863
chromosome partition protein MukB;
46-228 2.97e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYdAKQNELVQIQADLEDAKAKEEEQYEAMKL--RIQYM 123
Cdd:PRK04863   302 LAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEERLEEQNEVVEEadEQQEE 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  124 YENSSGNgymamlfSSKSISELIS--------------RA-EYIQKISDFDR--DLMQEYEDTVDQVKE--KETQVQEEQ 184
Cdd:PRK04863   381 NEARAEA-------AEEEVDELKSqladyqqaldvqqtRAiQYQQAVQALERakQLCGLPDLTADNAEDwlEEFQAKEQE 453

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1473292296  185 A--AIVELQQQSSDQQEAIQElYAAAYQELRTYSAELDDAKSSESA 228
Cdd:PRK04863   454 AteELLSLEQKLSVAQAAHSQ-FEQAYQLVRKIAGEVSRSEAWDVA 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
46-250 3.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELN---QQLDDLQNRLQELQdqydaKQNELVQIQADLEDAKAKE-EEQYEAMKLRIQ 121
Cdd:PRK03918  202 LEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELE-----KELESLEGSKRKLEEKIRElEERIEELKKEIE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 122 YMYENssgngymamlfsSKSISELISRAEYIQKISDFdrdlMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAI 201
Cdd:PRK03918  277 ELEEK------------VKELKELKEKAEEYIKLSEF----YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473292296 202 QEL----------------YAAAYQELRTYSAELDDAKSSESAL-VDEINSKADAindlIRQAKEE 250
Cdd:PRK03918  341 EELkkklkelekrleeleeRHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEE----LEKAKEE 402
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-251 3.84e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   72 QQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKAKEEEqyeamkLRIQYmyensSGNGYmamlfssksiselisraey 151
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDE------LEAQI-----RGNGG------------------- 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  152 iqkisdfdrdlmqeyedtvDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELYAAAY---QELRTYSAELDDAKSSESA 228
Cdd:COG4913    338 -------------------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPasaEEFAALRAEAAALLEALEE 398

                          170       180
                   ....*....|....*....|...
gi 1473292296  229 LVDEINSKADAINDLIRQAKEEE 251
Cdd:COG4913    399 ELEALEEALAEAEAALRDLRREL 421
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 53-199 4.07e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.97  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  53 IDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYdakQNELVQIQADLEDAKAKEEEQYEAmKLRIQymyenssgngy 132
Cdd:pfam09787  49 LEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQ---QEEAESSREQLQELEEQLATERSA-RREAE----------- 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473292296 133 mamlfssksiSELISRAEYIQKISDfdrDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQE 199
Cdd:pfam09787 114 ----------AELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSE 167
TolA_bind_tri pfam16331
TolA binding protein trimerization; This is the N-terminal domain of the YbgF protein. YbgF ...
 48-104 5.70e-03

TolA binding protein trimerization; This is the N-terminal domain of the YbgF protein. YbgF binds to TolA. This domain mediates trimerization.


Pssm-ID: 435282 [Multi-domain]  Cd Length: 72  Bit Score: 35.25  E-value: 5.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1473292296  48 SIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLED 104
Cdd:pfam16331   1 SLEDRLARLERILEARNQGLLELQQQLDDLQQEVRELRGQIEELQYQLEQLQERQRD 57
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 46-148 6.13e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQ--------SEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQAdledAKAKEEEQYEAMK 117
Cdd:COG0542   413 LDELERRLEQLEIEKEAlkkeqdeaSFERLAELRDELAELEEELEALKARWEAEKELIEEIQE----LKEELEQRYGKIP 488

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1473292296 118 -LRIQYMYENSSGNGYMAMLF---SSKSISELISR 148
Cdd:COG0542   489 eLEKELAELEEELAELAPLLReevTEEDIAEVVSR 523
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-190 7.30e-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: 38.90  E-value: 7.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296   28 TKEKISNAQAEQAAAQSQLDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDAKA 107
Cdd:TIGR02169  845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  108 KEEEQYEAMKlriQYMYENSSGNGYMAMLFSSKSISELISRAEY-IQKISDFDRDLMQEYEDTV---DQVKEKETQVQEE 183
Cdd:TIGR02169  925 KLEALEEELS---EIEDPKGEDEEIPEEELSLEDVQAELQRVEEeIRALEPVNMLAIQEYEEVLkrlDELKEKRAKLEEE 1001


                   ....*..
gi 1473292296  184 QAAIVEL 190
Cdd:TIGR02169 1002 RKAILER 1008
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 48-251 8.17e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.46  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  48 SIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDaKAKEEEQYEAmklriqymyens 127
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-LEKQLNQLKS------------ 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 128 sgngymamlfsskSISELISraeyiQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSSDQQEAIQELYA- 206
Cdd:TIGR04523 296 -------------EISDLNN-----QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESe 357

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473292296 207 --AAYQELRTYSAELDDAKSSESALVDEINSKADAINDL---IRQAKEEE 251
Cdd:TIGR04523 358 nsEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLN 407
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 47-252 8.31e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.46  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  47 DSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDAKQNELVQIQADLEDaKAKEEEQyeamklriqymyen 126
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE-KQKELEQ-------------- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 127 ssgngymamlfSSKSISELISRAEYIQ-KISDFDRdlmQEYEDTVDQVKEKETQVQEEqaaIVELQQQSSDQQEAIQELy 205
Cdd:TIGR04523 279 -----------NNKKIKELEKQLNQLKsEISDLNN---QKEQDWNKELKSELKNQEKK---LEEIQNQISQNNKIISQL- 340

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1473292296 206 aaaYQELRTYSAELDDAKSSESALVDEINSKADAINDLIR--QAKEEEI 252
Cdd:TIGR04523 341 ---NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKenQSYKQEI 386
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-243 8.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296  46 LDSIQSRIDELNSKKGQSEEYLSELNQQLDDLQNRLQELQDQYDA----------KQNELVQIQADLEDAKAKEEEQYEA 115
Cdd:PRK02224  407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELED 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473292296 116 MKLRIQymyenssgngymamlfsskSISELISRAEYIQKISDFDRDLMQEYEDTVDQVKEKETQVQEEQAAIVELQQQSS 195
Cdd:PRK02224  487 LEEEVE-------------------EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1473292296 196 DQQEAIQELYAAAyQELRTYSAE-LDDAKSSESALvDEINSKADAINDL 243
Cdd:PRK02224  548 ELEAEAEEKREAA-AEAEEEAEEaREEVAELNSKL-AELKERIESLERI 594
 
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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