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Conserved domains on  [gi|768006709|ref|XP_011524796|]
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protein KASH5 isoform X5 [Homo sapiens]

Protein Classification

EF-hand_9 and KASH_CCD domain-containing protein( domain architecture ID 12169898)

protein containing domains EF-hand_9, KASH_CCD, and Androgen_recep

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 159-333 7.08e-56

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


:

Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 186.15  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  159 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 238
Cdd:pfam14662  17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  239 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 318
Cdd:pfam14662  97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176

                         170
                  ....*....|....*
gi 768006709  319 LRLEISRLEEQLSQT 333
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
EF-hand_9 pfam14658
EF-hand domain;
24-91 1.35e-26

EF-hand domain;


:

Pssm-ID: 405361  Cd Length: 66  Bit Score: 102.50  E-value: 1.35e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006709   24 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 91
Cdd:pfam14658   1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDA--LVDLDTFLRVMRDWI 66
 
Name Accession Description Interval E-value
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 159-333 7.08e-56

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 186.15  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  159 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 238
Cdd:pfam14662  17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  239 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 318
Cdd:pfam14662  97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176

                         170
                  ....*....|....*
gi 768006709  319 LRLEISRLEEQLSQT 333
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
EF-hand_9 pfam14658
EF-hand domain;
24-91 1.35e-26

EF-hand domain;


Pssm-ID: 405361  Cd Length: 66  Bit Score: 102.50  E-value: 1.35e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006709   24 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 91
Cdd:pfam14658   1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDA--LVDLDTFLRVMRDWI 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-335 5.63e-10

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: 62.38  E-value: 5.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   167 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKamdEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 246
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   247 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 326
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941


                   ....*....
gi 768006709   327 EEQLSQTYE 335
Cdd:TIGR02168  942 QERLSEEYS 950
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-340 8.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 160 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-----------MDEELEDLKTLARSLEEQNRSL 228
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqdiarLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 229 LAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQT 308
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        170       180       190
                 ....*....|....*....|....*....|..
gi 768006709 309 LEEYRVTTQELRLEISRLEEQLSQTYEGPDEL 340
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEE 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
183-379 5.43e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 183 LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLqEENGKLLAERDG 262
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKELKE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 263 VKKRSQELAMEKDTLKRQLFECEHLIC---QRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLsQTYEGPDE 339
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKA 369

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 768006709 340 LPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSN 379
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
 
Name Accession Description Interval E-value
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 159-333 7.08e-56

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 186.15  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  159 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 238
Cdd:pfam14662  17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  239 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 318
Cdd:pfam14662  97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176

                         170
                  ....*....|....*
gi 768006709  319 LRLEISRLEEQLSQT 333
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
EF-hand_9 pfam14658
EF-hand domain;
24-91 1.35e-26

EF-hand domain;


Pssm-ID: 405361  Cd Length: 66  Bit Score: 102.50  E-value: 1.35e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006709   24 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 91
Cdd:pfam14658   1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDA--LVDLDTFLRVMRDWI 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-335 5.63e-10

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: 62.38  E-value: 5.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   167 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKamdEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 246
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   247 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 326
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941


                   ....*....
gi 768006709   327 EEQLSQTYE 335
Cdd:TIGR02168  942 QERLSEEYS 950
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-340 8.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 160 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-----------MDEELEDLKTLARSLEEQNRSL 228
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqdiarLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 229 LAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQT 308
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        170       180       190
                 ....*....|....*....|....*....|..
gi 768006709 309 LEEYRVTTQELRLEISRLEEQLSQTYEGPDEL 340
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEE 440
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-378 8.57e-08

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: 55.46  E-value: 8.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   166 NAKLQRSMETAEEGSARLGEEILALRKQLHSTQ----QALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQH 241
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   242 LVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLfecehliCQRDTILSERTRDVESLAQTLEEYRVTTQELRL 321
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-------KDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 768006709   322 EISRLEEQLSQTYEGPDELPEGAQlrrvgwtellppSLGLEIEAIRQKQEVATADLS 378
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKE------------DKALEIKKQEWKLEQLAADLS 465
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-399 1.02e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 160 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA----MDEELEDLKTLARSLEEQNRSLLAQARQA 235
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 236 EKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVT 315
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 316 TQELRLEISRLEEQLSQTY--------EGPDELPEGAQLRRVGWTEL-LPPSLGLEIEAIRQKQEVATADLSNPLCGVWQ 386
Cdd:COG1196  451 EAELEEEEEALLELLAELLeeaalleaALAELLEELAEAAARLLLLLeAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530

                        250
                 ....*....|...
gi 768006709 387 WEEVIHETSEETE 399
Cdd:COG1196  531 GVEAAYEAALEAA 543
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 160-379 7.52e-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: 52.37  E-value: 7.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   160 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAmdeELEDLKTLARSLEEQNRSLLAQARQAEKEQ 239
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   240 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLA-------QTLEEY 312
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqleLQIASL 398

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006709   313 RVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSN 379
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-332 8.33e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 167 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA----MDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHL 242
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErleeLEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 243 VAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLE 322
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                        170
                 ....*....|
gi 768006709 323 ISRLEEQLSQ 332
Cdd:COG1196  437 EEEEEEALEE 446
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-332 1.57e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 160 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 239
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 240 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 319
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                        170
                 ....*....|...
gi 768006709 320 RLEISRLEEQLSQ 332
Cdd:COG1196  392 LRAAAELAAQLEE 404
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 168-349 2.05e-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: 50.84  E-value: 2.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   168 KLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAM--DEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAE 245
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   246 METLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEhlicqrdtilsertRDVESLAQTLEEYRVTTQELRLEISR 325
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE--------------EELEELEAALRDLESRLGDLKKERDE 893

                          170       180
                   ....*....|....*....|....
gi 768006709   326 LEEQLSQTYEGPDELPEGAQLRRV 349
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRK 917
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 167-351 3.41e-06

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: 49.38  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 167 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELE-DLKTLARSLEEQNRSLLAQARQAEKEQQH---- 241
Cdd:COG4942   44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQKEELAELLRALYRLGRQppla 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 242 ------------------------LVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSE 297
Cdd:COG4942  124 lllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768006709 298 RTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGW 351
Cdd:COG4942  204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
167-354 5.37e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 167 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 246
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELE---QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 247 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQ-----ELRL 321
Cdd:COG4372  104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQ 183

                        170       180       190
                 ....*....|....*....|....*....|...
gi 768006709 322 EISRLEEQLSQTYEGPDELPEGAQLRRVGWTEL 354
Cdd:COG4372  184 ALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
182-352 1.24e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 182 RLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSL--LAQARQAEKEQQHLVAEMETLQEENGKLLAE 259
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 260 RDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTI----LSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYE 335
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                        170
                 ....*....|....*..
gi 768006709 336 GPDELPEGAQLRRVGWT 352
Cdd:COG4717  235 ELEAAALEERLKEARLL 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
161-335 1.42e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  161 RLVGENAKLQRSMETAEEGSARLGEEILALRKQLHstqqALQFAKAMDEELEDLKTLAR---SLEEQNRSLLA---QARQ 234
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERRE----ALQRLAEYSWDEIDVASAEReiaELEAELERLDAssdDLAA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  235 AEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRv 314
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR- 768

                         170       180
                  ....*....|....*....|.
gi 768006709  315 ttQELRLEISRLEEQLSQTYE 335
Cdd:COG4913   769 --ENLEERIDALRARLNRAEE 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-348 4.03e-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: 46.60  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   162 LVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALqfaKAMDEELEDL-KTLARSLEEQNRSLLAQARQAEKEQQ 240
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   241 HLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELR 320
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391

                          170       180
                   ....*....|....*....|....*...
gi 768006709   321 LEISRLEEQLSQTYEGPDELPEGAQLRR 348
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRLS 419
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-348 4.74e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  185 EEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEE------QNRSLLAQAR--QAEKEQQHLVAEMETLQEENGKL 256
Cdd:COG4913   228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAarerlaELEYLRAALRlwFAQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  257 LAERDGVKKRSQELAMEKDTLKRQLF--------ECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEE 328
Cdd:COG4913   308 EAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                         170       180
                  ....*....|....*....|
gi 768006709  329 QLSQTYEGPDELPEGAQLRR 348
Cdd:COG4913   388 EAAALLEALEEELEALEEAL 407
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
183-379 5.43e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 183 LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLqEENGKLLAERDG 262
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKELKE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 263 VKKRSQELAMEKDTLKRQLFECEHLIC---QRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLsQTYEGPDE 339
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKA 369

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 768006709 340 LPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSN 379
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
181-336 1.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  181 ARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLaQARQAEKEQQHLVAEMETLQEENGKLLA-- 258
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDLAAle 691

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006709  259 -ERDGVKKRSQELAMEKDTLKRQLFECEHlicQRDTILSERTRdVESLAQTLEEYRVTTQELRLEiSRLEEQLSQTYEG 336
Cdd:COG4913   692 eQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDE-LQDRLEAAEDLARLELRALLE-ERFAAALGDAVER 765
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 191-391 4.40e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   191 RKQLHSTQQALqfakamdEELEDLktlARSLEEQNRSLLAQARQAEK------------------EQQHLVAEMETLQEE 252
Cdd:TIGR02168  178 ERKLERTRENL-------DRLEDI---LNELERQLKSLERQAEKAERykelkaelrelelallvlRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   253 NGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 332
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 768006709   333 TYEGPDELPEGAQLRRVGWTELLPpslglEIEAIRQKQEVATADLSNPLCGVWQWEEVI 391
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKE-----ELESLEAELEELEAELEELESRLEELEEQL 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
168-353 4.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 168 KLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVA--- 244
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElke 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 245 EMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLIcQRDTILSERTRDVESLAQTLEEYRVTTQELRLEIS 324
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317

                        170       180
                 ....*....|....*....|....*....
gi 768006709 325 RLEEQLSQTYEGPDELPEgaQLRRVGWTE 353
Cdd:PRK03918 318 RLEEEINGIEERIKELEE--KEERLEELK 344
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-373 6.09e-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: 42.74  E-value: 6.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   170 QRSMETAEEGSARLGEEILALRKQLHSTQ----QALQFaKAMDEELEDLK--TLARSLEEQNRSLLAQARQAEKEQQhlv 243
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLErqaeKAERY-KELKAELRELElaLLVLRLEELREELEELQEELKEAEE--- 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   244 aEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLIC---QRDTILSERTRDVESLAQTLEEYRVTTQ--- 317
Cdd:TIGR02168  254 -ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQLEELEskl 332

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 768006709   318 -ELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVA 373
Cdd:TIGR02168  333 dELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
161-331 7.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 161 RLVGENAKLQRSMETAEEGSARLGE------EILALRKQLHSTQQALQFAKAMDEELEDLKTlarslEEQNRSLlaqaRQ 234
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEElkkklkELEKRLEELEERHELYEEAKAKKEELERLKK-----RLTGLTP----EK 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 235 AEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEhlICQRD-------TILSERTRDVESLAQ 307
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP--VCGRElteehrkELLEEYTAELKRIEK 466

                        170       180
                 ....*....|....*....|....
gi 768006709 308 TLEEYRVTTQELRLEISRLEEQLS 331
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLK 490
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 167-344 8.65e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 167 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-MDEELEDLKTLARSLEEQNRS---------------LLA 230
Cdd:COG3883   40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeIEERREELGERARALYRSGGSvsyldvllgsesfsdFLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 231 QARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLE 310
Cdd:COG3883  120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199

                        170       180       190
                 ....*....|....*....|....*....|....
gi 768006709 311 EYRVTTQELRLEISRLEEQLSQTYEGPDELPEGA 344
Cdd:COG3883  200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 205-330 1.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 205 KAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQhLVAEMETLQEEngKLLAERDGVKKRSQELAMEKDTLKRQLFEC 284
Cdd:COG1196  182 EATEENLERLEDILGELERQLEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEEL 258

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 768006709 285 EHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQL 330
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
169-348 2.04e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 169 LQRSMETAEEGSARLGEEILALRKQLHSTQQALQ-FAK-----AMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHL 242
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELEEAEAALEeFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 243 VAEMETLQEENGKLLAER--DGVKKRSQELAMEKDTLKRQLFEcEH-----LICQRDT----ILSERTRDVESLAQTLEE 311
Cdd:COG3206  246 RAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTP-NHpdviaLRAQIAAlraqLQQEAQRILASLEAELEA 324

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 768006709 312 YRVTTQELRLEISRLEEQLSQTyegPDELPEGAQLRR 348
Cdd:COG3206  325 LQAREASLQAQLAQLEARLAEL---PELEAELRRLER 358
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 177-281 2.11e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  177 EEGSARLGEEILALRKQLHSTQQalqfakamdeELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKL 256
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAR----------EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAET 210

                          90       100       110
                  ....*....|....*....|....*....|.
gi 768006709  257 LAE-RDGVKKRSQELAM-----EKDTlkRQL 281
Cdd:PRK11448  211 SQErKQKRKEITDQAAKrlelsEEET--RIL 239
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-332 3.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 190 LRKQLHS----TQQALQFaKAMDEELEDLKTLARSLEEqnRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKK 265
Cdd:COG1196  198 LERQLEPlerqAEKAERY-RELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006709 266 RSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 332
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
196-328 4.19e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 196 STQQALqfAKAMDEELEDLKTLARSLEEQNRsllAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKD 275
Cdd:COG2433  377 SIEEAL--EELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS 451

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768006709 276 TLKRQlfecEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEE 328
Cdd:COG2433  452 EARSE----ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
165-376 4.56e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 165 ENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVA 244
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 245 EMETLQEEnGKL---------------LAERDGvkkRSQELAMEKDTLKRQLFECEHLIcQRDTILSERTRDVESLAQTL 309
Cdd:PRK02224 444 EAEALLEA-GKCpecgqpvegsphvetIEEDRE---RVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERR 518

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006709 310 E--EYRVTTQELRLEisRLEEQLSQTYEGPDELPEGAQLRRVGWTEllppslgLEIEAIRQKQEVATAD 376
Cdd:PRK02224 519 EdlEELIAERRETIE--EKRERAEELRERAAELEAEAEEKREAAAE-------AEEEAEEAREEVAELN 578
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 190-340 4.62e-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: 40.00  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  190 LRKQLHSTQQALQFAK----AMDEELEDLKTLARSLE-------EQNRSLLAQARQAEKEQQHLVAEMETLQEENGKL-- 256
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKkenqSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNns 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  257 ----LAERDGVKKRS-QELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLS 331
Cdd:TIGR04523 441 eikdLTNQDSVKELIiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520


                  ....*....
gi 768006709  332 QTYEGPDEL 340
Cdd:TIGR04523 521 SLKEKIEKL 529
PTZ00121 PTZ00121
MAEBL; Provisional
 165-446 5.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  165 ENAKLQRSMETAEEgsARLGEEIlalrKQLHSTQQALQFAKAmdEEL---EDLKTL--ARSLEEQNRSLLAQARQAEKEQ 239
Cdd:PTZ00121 1519 EEAKKADEAKKAEE--AKKADEA----KKAEEKKKADELKKA--EELkkaEEKKKAeeAKKAEEDKNMALRKAEEAKKAE 1590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  240 QHLVAEMETLQEENGKLLAERdgvKKRSQELAMEKDTLKRQLfECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 319
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEE---AKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  320 RL---EISRLEEQLSQTYEgpDELPEGAQLRRVGWTELLPPSL-GLEIEAIRQKQEVATADLSNPLcgvwQWEEVIHETS 395
Cdd:PTZ00121 1667 AKkaeEDKKKAEEAKKAEE--DEKKAAEALKKEAEEAKKAEELkKKEAEEKKKAEELKKAEEENKI----KAEEAKKEAE 1740

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768006709  396 EETEFPSEAPAG-GQRN-----FQGEPAHPEEGRKEPSMWLTRREEEEDAESQVTAD 446
Cdd:PTZ00121 1741 EDKKKAEEAKKDeEEKKkiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
160-377 8.86e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 8.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 160 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 239
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ---AAQAELAQAQEELESLQEEAEELQEELEELQKER 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 240 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRD--VESLAQTLEEYRVTTQ 317
Cdd:COG4372  125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKEEELAE 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709 318 ELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADL 377
Cdd:COG4372  205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 159-320 9.11e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   159 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAM----DEELEDLKTLARSL------------- 221
Cdd:pfam12128  599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknaRLDLRRLFDEKQSEkdkknkalaerkd 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709   222 --EEQNRSLLAQARQAEKEQQHLVAEM-ETLQEENGKLLAERDGVKKR--------SQELAMEKDTLKRQLFECEHlicQ 290
Cdd:pfam12128  679 saNERLNSLEAQLKQLDKKHQAWLEEQkEQKREARTEKQAYWQVVEGAldaqlallKAAIAARRSGAKAELKALET---W 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 768006709   291 RDTIL----------SERTRDVESLAQTLEEYRVTTQELR 320
Cdd:pfam12128  756 YKRDLaslgvdpdviAKLKREIRTLERKIERIAVRRQEVL 795
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 186-332 9.26e-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: 38.85  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  186 EILALRKQlhsTQQAL-----QFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENG------ 254
Cdd:TIGR04523 296 EISDLNNQ---KEQDWnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqnei 372

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006709  255 -KLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 332
Cdd:TIGR04523 373 eKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 190-333 9.50e-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: 38.85  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006709  190 LRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQE 269
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006709  270 LAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYR-----VTTQELRLEISRLEEQLSQT 333
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEI 326
 
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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