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Conserved domains on  [gi|145337709|ref|NP_177964|]
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ROP interactive partner 2 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-252 1.17e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    62 SQKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTPAperddipgdghQETDVFEVLDEKA 141
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES-----------RLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   142 KESEKTKNdELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKktdtemscaKAKEDEIASKVSQIGEELEESNET 221
Cdd:TIGR02168  386 SKVAQLEL-QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEE 455

                          170       180       190
                   ....*....|....*....|....*....|.
gi 145337709   222 TAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQ 486
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-252 1.17e-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: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    62 SQKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTPAperddipgdghQETDVFEVLDEKA 141
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES-----------RLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   142 KESEKTKNdELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKktdtemscaKAKEDEIASKVSQIGEELEESNET 221
Cdd:TIGR02168  386 SKVAQLEL-QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEE 455

                          170       180       190
                   ....*....|....*....|....*....|.
gi 145337709   222 TAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQ 486
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
139-247 1.37e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.86  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 139 EKAKESEKTKND-ELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKvsqiGEELEE 217
Cdd:COG2433  394 EPEAEREKEHEErELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISR 469

                         90       100       110
                 ....*....|....*....|....*....|
gi 145337709 218 SNETTAKLKKKLESVEEAKETLEAEMKKLK 247
Cdd:COG2433  470 LDREIERLERELEEERERIEELKRKLERLK 499
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 139-255 2.14e-05

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 43.83  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  139 EKAKESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTemscAKAKEDEIASKVSQIGEELEES 218
Cdd:pfam12718  17 EELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEK----LKTNNENLTRKIQLLEEELEES 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 145337709  219 NETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWRK 255
Cdd:pfam12718  93 DKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEK 129
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
64-247 6.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  64 KKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKkpntpAPERDDIPGDGHQETDVFEVLDEKAKE 143
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-----VKELKELKEKAEEYIKLSEFYEEYLDE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 144 SEKTKNdELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTA 223
Cdd:PRK03918 309 LREIEK-RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387

                        170       180
                 ....*....|....*....|....
gi 145337709 224 KLKKKLESVEEAKETLEAEMKKLK 247
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKIT 411
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 135-255 7.79e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.69  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   135 EVLDEKAkESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTD-TEMSCAKAK----EDEIASKVS 209
Cdd:smart00787 147 EGLDENL-EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKlkklLQEIMIKVK 225

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 145337709   210 qigeELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWRK 255
Cdd:smart00787 226 ----KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-252 1.17e-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: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    62 SQKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTPAperddipgdghQETDVFEVLDEKA 141
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES-----------RLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   142 KESEKTKNdELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKktdtemscaKAKEDEIASKVSQIGEELEESNET 221
Cdd:TIGR02168  386 SKVAQLEL-QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEE 455

                          170       180       190
                   ....*....|....*....|....*....|.
gi 145337709   222 TAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQ 486
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
139-247 1.37e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.86  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 139 EKAKESEKTKND-ELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKvsqiGEELEE 217
Cdd:COG2433  394 EPEAEREKEHEErELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISR 469

                         90       100       110
                 ....*....|....*....|....*....|
gi 145337709 218 SNETTAKLKKKLESVEEAKETLEAEMKKLK 247
Cdd:COG2433  470 LDREIERLERELEEERERIEELKRKLERLK 499
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 68-246 1.64e-06

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: 48.38  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  68 SRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKpntpaperddipgdGHQETDVFEVLDEKAKESEK- 146
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------------KRLELEIEEVEARIKKYEEQl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 147 ---TKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMscaKAKEDEIASKVSQIGEELEESNETTA 223
Cdd:COG1579   83 gnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELE 159

                        170       180
                 ....*....|....*....|...
gi 145337709 224 KLKKKLesvEEAKETLEAEMKKL 246
Cdd:COG1579  160 ELEAER---EELAAKIPPELLAL 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 68-252 1.01e-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: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    68 SRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTP---APERDDIPGDGHQETDVFEVLDEKAKES 144
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   145 EKtKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTAK 224
Cdd:TIGR02168  757 TE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180
                   ....*....|....*....|....*...
gi 145337709   225 LKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEE 863
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 139-255 2.14e-05

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 43.83  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  139 EKAKESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTemscAKAKEDEIASKVSQIGEELEES 218
Cdd:pfam12718  17 EELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEK----LKTNNENLTRKIQLLEEELEES 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 145337709  219 NETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWRK 255
Cdd:pfam12718  93 DKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEK 129
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-242 2.47e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  64 KKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRkkskkpntpapERDDIpgdghqetdvfevldEKAKE 143
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----------LELEL---------------EEAQA 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 144 SEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTA 223
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170
                 ....*....|....*....
gi 145337709 224 KLKKKLESVEEAKETLEAE 242
Cdd:COG1196  369 EAEAELAEAEEELEELAEE 387
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 60-253 3.66e-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: 45.44  E-value: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    60 PLSQKKLGSRISGL---ESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTpapERDDIPGDGHQETDVFEV 136
Cdd:TIGR02169  152 PVERRKIIDEIAGVaefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA---ERYQALLKEKREYEGYEL 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   137 LDEK--AKESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKK-TDTEMSCAKAKEDEIASKVSQI-- 211
Cdd:TIGR02169  229 LKEKeaLERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLer 308

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 145337709   212 -----GEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQW 253
Cdd:TIGR02169  309 siaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-255 4.15e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  66 LGSRISGLESQLGQA------QEELRLLKQQLAKAEAAKKRAQEELHRKKSKkpntpaperddipgdghQETDVFEVLDE 139
Cdd:COG1196  198 LERQLEPLERQAEKAeryrelKEELKELEAELLLLKLRELEAELEELEAELE-----------------ELEAELEELEA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 140 KAKESEKTKN---DELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELE 216
Cdd:COG1196  261 ELAELEAELEelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 145337709 217 ESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWRK 255
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-249 4.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  63 QKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKpntpAPERDDIpgdghqetdvfevldEKAK 142
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL----AEAEEEL---------------EELA 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 143 ESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETT 222
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                        170       180
                 ....*....|....*....|....*..
gi 145337709 223 AKLKKKLESVEEAKETLEAEMKKLKVQ 249
Cdd:COG1196  466 AELLEEAALLEAALAELLEELAEAAAR 492
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 63-255 1.27e-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: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   63 QKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNtpaperddipgdghqetdVFEVLDEKAK 142
Cdd:TIGR04523 213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK------------------IKKQLSEKQK 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  143 ESEKTkNDELASKEDQINVLKARLYDLEKERVSlsEENETLKDQLKKTDTEMscakakeDEIASKVSQIGEELEESNETT 222
Cdd:TIGR04523 275 ELEQN-NKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKL-------EEIQNQISQNNKIISQLNEQI 344

                         170       180       190
                  ....*....|....*....|....*....|...
gi 145337709  223 AKLKKKLESVEEAKETLEAEMKKLKVQTEQWRK 255
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 151-248 1.84e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 151 ELASKEDQINVLKARLYDLEKERVSLSEENET--------LKDQLKKTDTEMSCAKAK---EDEIASKVSQIGEELEESN 219
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELAELEEELEALKARweaEKELIEEIQELKEELEQRY 484

                         90       100
                 ....*....|....*....|....*....
gi 145337709 220 ETTAKLKKKLESVEEAKETLEAeMKKLKV 248
Cdd:COG0542  485 GKIPELEKELAELEEELAELAP-LLREEV 512
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-253 2.06e-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: 43.13  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    45 GLDRRSPRSGGPHTDPLSQKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKkskkpntpaperddip 124
Cdd:TIGR02169  658 GSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI---------------- 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   125 gdghqETDVFEVLDEKAKESEKTKN--DELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKktDTEMSCAKAKED 202
Cdd:TIGR02169  722 -----EKEIEQLEQEEEKLKERLEEleEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN--DLEARLSHSRIP 794

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 145337709   203 EIASKVSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQW 253
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 139-247 2.44e-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: 42.70  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  139 EKAKESEKT-KNDELASKEDQINVLKARL--YDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEEL 215
Cdd:TIGR04523 526 IEKLESEKKeKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605

                          90       100       110
                  ....*....|....*....|....*....|..
gi 145337709  216 EESNETTAKLKKKLESVEEAKETLEAEMKKLK 247
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-255 4.78e-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: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   153 ASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTAKLKKKLESV 232
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110
                   ....*....|....*....|....*....|
gi 145337709   233 EEAKE-------TLEAEMKKLKVQTEQWRK 255
Cdd:TIGR02169  750 EQEIEnvkselkELEARIEELEEDLHKLEE 779
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 185-252 4.86e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 4.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337709 185 DQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 64-251 5.53e-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: 41.54  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   64 KKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTpaperDDIPGDGHQETDVFEVLDEKAKE 143
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-----DNTRESLETQLKVLSRSINKIKQ 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  144 SEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCA----KAKEDEIASK------------ 207
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKeskiSDLEDELNKDdfelkkenleke 562

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 145337709  208 VSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTE 251
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
64-247 6.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  64 KKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKkpntpAPERDDIPGDGHQETDVFEVLDEKAKE 143
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-----VKELKELKEKAEEYIKLSEFYEEYLDE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 144 SEKTKNdELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTA 223
Cdd:PRK03918 309 LREIEK-RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387

                        170       180
                 ....*....|....*....|....
gi 145337709 224 KLKKKLESVEEAKETLEAEMKKLK 247
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKIT 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-254 6.55e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    62 SQKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNtpaperddipgdghqetdvFEVLDEKA 141
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------------------LEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   142 KESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNET 221
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190
                   ....*....|....*....|....*....|...
gi 145337709   222 TAKLKKKLESVEEAKETLEAEMKKLKVQTEQWR 254
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 63-252 9.05e-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: 41.21  E-value: 9.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    63 QKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNtpaPERDDIPGDGHQETDVFEVLDEKAK 142
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND---LEARLSHSRIPEIQAELSKLEEEVS 808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   143 ESEKTkndeLASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASK-------VSQIGEEL 215
Cdd:TIGR02169  809 RIEAR----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaaLRDLESRL 884

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 145337709   216 EESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
150-255 2.03e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 150 DELASKEDQINVLKARLYDLEKERVSLSEENETLKDqLKKTDTEMscakakeDEIASKVSQIGEELEESNETTAKLKKKL 229
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRI-------ERLEERREDLEELIAERRETIEEKRERA 539

                         90       100
                 ....*....|....*....|....*.
gi 145337709 230 ESVEEAKETLEAEMkklkvqtEQWRK 255
Cdd:PRK02224 540 EELRERAAELEAEA-------EEKRE 558
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-247 2.41e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   128 HQETDVFEVLDEKAKESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASK 207
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 145337709   208 VSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLK 247
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 74-254 2.41e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 39.63  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   74 ESQLGQAQEELRLLKQQLAKAEAAKKRAQ---EELHRKKSK----KPNTPAPERDDIPGDGHQETDVFEVLDEKAKESEK 146
Cdd:pfam05701 225 EKELKQAEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAElaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEE 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  147 TK-NDELASkeDQINVLK---ARL-YDLEKERVSLSEENET----------LKDQLKKTDTEMSCAKAKEDEIASKVSQI 211
Cdd:pfam05701 305 VKaNIEKAK--DEVNCLRvaaASLrSELEKEKAELASLRQRegmasiavssLEAELNRTKSEIALVQAKEKEAREKMVEL 382

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 145337709  212 GEELE----ESNETTAKLKKKLESVEEAKEtlEAEMKKLKVQTEQWR 254
Cdd:pfam05701 383 PKQLQqaaqEAEEAKSLAQAAREELRKAKE--EAEQAKAAASTVESR 427
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-252 2.48e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  63 QKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTpapeRDDIPGDGHQETDVFEVLDEKAK 142
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 143 ESEKTKNDE------LASKE-----DQINVLKaRLYDLEKERV-SLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQ 210
Cdd:COG3883   94 ALYRSGGSVsyldvlLGSESfsdflDRLSALS-KIADADADLLeELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 145337709 211 IGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:COG3883  173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
153-252 2.53e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 153 ASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTAKLKKKLESV 232
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106

                         90       100
                 ....*....|....*....|
gi 145337709 233 EEAKETLEAEMKKLKVQTEQ 252
Cdd:COG4372  107 QEEAEELQEELEELQKERQD 126
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 64-250 2.53e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  64 KKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKS----------KKPNTPAPERDDIPGDGHQETDV 133
Cdd:COG4942   58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyRLGRQPPLALLLSPEDFLDAVRR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 134 FEVLDEKAKEsektkndelasKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGE 213
Cdd:COG4942  138 LQYLKYLAPA-----------RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145337709 214 ELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQT 250
Cdd:COG4942  207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 151-247 3.29e-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: 38.37  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 151 ELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMscakakeDEIASKVSQIGEELEESNETTAKLKKKLE 230
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLG 83

                         90
                 ....*....|....*....
gi 145337709 231 SVEEAKE--TLEAEMKKLK 247
Cdd:COG1579   84 NVRNNKEyeALQKEIESLK 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 131-254 3.32e-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: 39.28  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   131 TDVFEVLDEKAKESEKTKN--DELASK-----EDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDE 203
Cdd:TIGR02169  254 EKLTEEISELEKRLEEIEQllEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 145337709   204 IASKVSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWR 254
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 150-252 3.50e-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: 38.37  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 150 DELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAK------AKEDEIAS----------KVSQIGE 213
Cdd:COG1579   38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyeALQKEIESlkrrisdledEILELME 117

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145337709 214 ELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:COG1579  118 RIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-252 3.94e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  62 SQKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKpntpaperddipgdghqetdvfevldEKA 141
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL--------------------------QAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 142 KESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNET 221
Cdd:COG4372   93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172

                        170       180       190
                 ....*....|....*....|....*....|.
gi 145337709 222 TAKLKKklESVEEAKETLEAEMKKLKVQTEQ 252
Cdd:COG4372  173 LQALSE--AEAEQALDELLKEANRNAEKEEE 201
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 177-265 4.83e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 177 SEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWRKA 256
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98


                 ....*....
gi 145337709 257 ADAAAAVLS 265
Cdd:COG4942   99 LEAQKEELA 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
63-249 6.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  63 QKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKkpntpaperddipgdghqetdvfevLDEKAK 142
Cdd:COG4372   19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE-------------------------LEQARS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 143 ESEKTKNdELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNETT 222
Cdd:COG4372   74 ELEQLEE-ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152

                        170       180
                 ....*....|....*....|....*..
gi 145337709 223 AKLKKKLESVEEAKETLEAEMKKLKVQ 249
Cdd:COG4372  153 KELEEQLESLQEELAALEQELQALSEA 179
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 191-249 6.41e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 6.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145337709 191 DTEMSCAKAKEDEIASKVSQIGEELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQ 249
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE 73
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 135-255 7.79e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.69  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   135 EVLDEKAkESEKTKNDELASKEDQINVLKARLYDLEKERVSLSEENETLKDQLKKTD-TEMSCAKAK----EDEIASKVS 209
Cdd:smart00787 147 EGLDENL-EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKlkklLQEIMIKVK 225

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 145337709   210 qigeELEESNETTAKLKKKLESVEEAKETLEAEMKKLKVQTEQWRK 255
Cdd:smart00787 226 ----KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 64-246 9.15e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 37.73  E-value: 9.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709    64 KKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTPAPERDdipgdghqetdvfevLDEKAKE 143
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE---------------LESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709   144 SE---KTKNDELASKEDQINVLKARL-YDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIG------- 212
Cdd:TIGR02168  913 LRrelEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaai 992

                          170       180       190
                   ....*....|....*....|....*....|....
gi 145337709   213 EELEESNETTAKLKKKLESVEEAKETLEAEMKKL 246
Cdd:TIGR02168  993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
70-247 9.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 9.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  70 ISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRKKSKKPNTPAPERDDIPGDGHQETDVFEVLDEKAKESEKTKN 149
Cdd:COG4717  286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 150 DELaskEDQINVLKAR-----------LYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEiaskvSQIGEELEES 218
Cdd:COG4717  366 EEL---EQEIAALLAEagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEEL 437

                        170       180
                 ....*....|....*....|....*....
gi 145337709 219 NETTAKLKKKLESVEEAKETLEAEMKKLK 247
Cdd:COG4717  438 EEELEELEEELEELREELAELEAELEQLE 466
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
63-247 9.77e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 9.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709  63 QKKLGSRISGLESQLGQAQEELRLLKQQLAKAEAAKKRAQEELHRkkskkpntpaperddipgdgHQET-DVFEVLDEKA 141
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE--------------------HEERrEELETLEAEI 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337709 142 KESEKTKNDELASKEDqinvLKARLYDLEKERVSLSEENETLKDQLKKTDTEMSCAKAKEDEIASKVSQIGEELEESNET 221
Cdd:PRK02224 261 EDLRETIAETEREREE----LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336

                        170       180
                 ....*....|....*....|....*.
gi 145337709 222 TAKLKKKLESVEEAKETLEAEMKKLK 247
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELR 362
 
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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