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Conserved domains on  [gi|768006691|ref|XP_011524792|]
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protein KASH5 isoform X2 [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 ...
 173-347 1.89e-57

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: 190.39  E-value: 1.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  173 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 252
Cdd:pfam14662  17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  253 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 332
Cdd:pfam14662  97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176

                         170
                  ....*....|....*
gi 768006691  333 LRLEISRLEEQLSQT 347
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
EF-hand_9 pfam14658
EF-hand domain;
38-105 1.60e-26

EF-hand domain;


:

Pssm-ID: 405361  Cd Length: 66  Bit Score: 102.50  E-value: 1.60e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006691   38 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 105
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 ...
 173-347 1.89e-57

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: 190.39  E-value: 1.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  173 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 252
Cdd:pfam14662  17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  253 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 332
Cdd:pfam14662  97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176

                         170
                  ....*....|....*
gi 768006691  333 LRLEISRLEEQLSQT 347
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
EF-hand_9 pfam14658
EF-hand domain;
38-105 1.60e-26

EF-hand domain;


Pssm-ID: 405361  Cd Length: 66  Bit Score: 102.50  E-value: 1.60e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006691   38 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 105
Cdd:pfam14658   1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDA--LVDLDTFLRVMRDWI 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-385 2.70e-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: 63.54  E-value: 2.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKamdEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 260
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 340
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 768006691   341 EEQLSQTYEgpDELPEGAQlrrvgwtelLPPSLGLEIEAIRQEVA 385
Cdd:TIGR02168  942 QERLSEEYS--LTLEEAEA---------LENKIEDDEEEARRRLK 975
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-347 5.48e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE---ELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 333
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        170
                 ....*....|....
gi 768006691 334 RLEISRLEEQLSQT 347
Cdd:COG1196  448 AEEEAELEEEEEAL 461
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-345 2.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 197 LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLqEENGKLLAERDG 276
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKELKE 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006691 277 VKKRSQELAMEKDTLKRQLFECEhlicQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLS 345
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIE----KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
 
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 ...
 173-347 1.89e-57

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: 190.39  E-value: 1.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  173 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 252
Cdd:pfam14662  17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  253 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 332
Cdd:pfam14662  97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176

                         170
                  ....*....|....*
gi 768006691  333 LRLEISRLEEQLSQT 347
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
EF-hand_9 pfam14658
EF-hand domain;
38-105 1.60e-26

EF-hand domain;


Pssm-ID: 405361  Cd Length: 66  Bit Score: 102.50  E-value: 1.60e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006691   38 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 105
Cdd:pfam14658   1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDA--LVDLDTFLRVMRDWI 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-385 2.70e-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: 63.54  E-value: 2.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKamdEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 260
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 340
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 768006691   341 EEQLSQTYEgpDELPEGAQlrrvgwtelLPPSLGLEIEAIRQEVA 385
Cdd:TIGR02168  942 QERLSEEYS--LTLEEAEA---------LENKIEDDEEEARRRLK 975
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-347 5.48e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE---ELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 333
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        170
                 ....*....|....
gi 768006691 334 RLEISRLEEQLSQT 347
Cdd:COG1196  448 AEEEAELEEEEEAL 461
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-354 5.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 5.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-----------MDEELEDLKTLARSLEEQNRSL 242
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqdiarLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 243 LAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQT 322
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        170       180       190
                 ....*....|....*....|....*....|..
gi 768006691 323 LEEYRVTTQELRLEISRLEEQLSQTYEGPDEL 354
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEE 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-346 6.33e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA----MDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHL 256
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErleeLEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 257 VAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLE 336
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                        170
                 ....*....|
gi 768006691 337 ISRLEEQLSQ 346
Cdd:COG1196  437 EEEEEEALEE 446
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 180-347 7.51e-07

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: 52.38  E-value: 7.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   180 NAKLQRSMETAEEGSARLGEEILALRKQLHSTQ----QALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQH 255
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   256 LVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLF----ECEHLICQRDTILSERTR----------------- 314
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKREINELKRELDRlqeelqrlseeladlna 427

                          170       180       190
                   ....*....|....*....|....*....|...
gi 768006691   315 DVESLAQTLEEYRVTTQELRLEISRLEEQLSQT 347
Cdd:TIGR02169  428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-387 8.06e-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: 8.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAmdeELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLA-------QTLEEY 326
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqleLQIASL 398

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006691   327 RVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQEVATA 387
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-346 1.20e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 333
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                        170
                 ....*....|...
gi 768006691 334 RLEISRLEEQLSQ 346
Cdd:COG1196  392 LRAAAELAAQLEE 404
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 182-363 1.37e-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: 51.61  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   182 KLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAM--DEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAE 259
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   260 METLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEhlicqrdtilsertRDVESLAQTLEEYRVTTQELRLEISR 339
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE--------------EELEELEAALRDLESRLGDLKKERDE 893

                          170       180
                   ....*....|....*....|....
gi 768006691   340 LEEQLSQTYEGPDELPEGAQLRRV 363
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRK 917
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
181-368 1.46e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 260
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELE---QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQ-----ELRL 335
Cdd:COG4372  104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQ 183

                        170       180       190
                 ....*....|....*....|....*....|...
gi 768006691 336 EISRLEEQLSQTYEGPDELPEGAQLRRVGWTEL 368
Cdd:COG4372  184 ALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 181-365 2.10e-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: 50.15  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELE-DLKTLARSLEEQNRSLLAQARQAEKEQQH---- 255
Cdd:COG4942   44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQKEELAELLRALYRLGRQppla 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 256 ------------------------LVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSE 311
Cdd:COG4942  124 lllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768006691 312 RTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGW 365
Cdd:COG4942  204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
196-366 7.13e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 7.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 196 RLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSL--LAQARQAEKEQQHLVAEMETLQEENGKLLAE 273
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 274 RDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTI----LSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYE 349
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                        170
                 ....*....|....*..
gi 768006691 350 GPDELPEGAQLRRVGWT 366
Cdd:COG4717  235 ELEAAALEERLKEARLL 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-349 1.00e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  175 RLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFakamDEELEDLKTLAR---SLEEQNRSLLA---QARQ 248
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY----SWDEIDVASAEReiaELEAELERLDAssdDLAA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  249 AEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRv 328
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR- 768

                         170       180
                  ....*....|....*....|.
gi 768006691  329 ttQELRLEISRLEEQLSQTYE 349
Cdd:COG4913   769 --ENLEERIDALRARLNRAEE 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 176-362 3.01e-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: 46.98  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   176 LVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALqfaKAMDEELEDL-KTLARSLEEQNRSLLAQARQAEKEQQ 254
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   255 HLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELR 334
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391

                          170       180
                   ....*....|....*....|....*...
gi 768006691   335 LEISRLEEQLSQTYEGPDELPEGAQLRR 362
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRLS 419
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-362 3.11e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  199 EEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEE------QNRSLLAQAR--QAEKEQQHLVAEMETLQEENGKL 270
Cdd:COG4913   228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAarerlaELEYLRAALRlwFAQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  271 LAERDGVKKRSQELAMEKDTLKRQLF--------ECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEE 342
Cdd:COG4913   308 EAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                         170       180
                  ....*....|....*....|
gi 768006691  343 QLSQTYEGPDELPEGAQLRR 362
Cdd:COG4913   388 EAAALLEALEEELEALEEAL 407
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 197-354 7.54e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.19  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  197 LGEEILALRKQLHSTQQAlqfAKAMDEELE-DLKTLARSLEeQNRSLLAQARQ----AEKEQQHLVAEMETLQEENGKLL 271
Cdd:pfam15905 157 LSMELMKLRNKLEAKMKE---VMAKQEGMEgKLQVTQKNLE-HSKGKVAQLEEklvsTEKEKIEEKSETEKLLEYITELS 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  272 AERDGVKKRSQELAMEKDTLKRQLFECEHL---ICQRDTILSERTRDVESLAQTLE--------EYRVTTQELRLEISRL 340
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEELLKEKNDEIESLkqsLEEKEQELSKQIKDLNEKCKLLEsekeellrEYEEKEQTLNAELEEL 312

                         170
                  ....*....|....
gi 768006691  341 EEQLSQTYEGPDEL 354
Cdd:pfam15905 313 KEKLTLEEQEHQKL 326
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-350 8.62e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  195 ARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLaQARQAEKEQQHLVAEMETLQEENGKLLA-- 272
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDLAAle 691

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006691  273 -ERDGVKKRSQELAMEKDTLKRQLFECEHlicQRDTILSERTRdVESLAQTLEEYRVTTQELRLEiSRLEEQLSQTYEG 350
Cdd:COG4913   692 eQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDE-LQDRLEAAEDLARLELRALLE-ERFAAALGDAVER 765
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-345 2.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 197 LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLqEENGKLLAERDG 276
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKELKE 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006691 277 VKKRSQELAMEKDTLKRQLFECEhlicQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLS 345
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIE----KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
188-367 3.30e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 188 ETAEEGSAR----LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVA---EM 260
Cdd:PRK03918 161 ENAYKNLGEvikeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEI 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLIcQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 340
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319

                        170       180
                 ....*....|....*....|....*..
gi 768006691 341 EEQLSQTYEGPDELPEgaQLRRVGWTE 367
Cdd:PRK03918 320 EEEINGIEERIKELEE--KEERLEELK 344
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-345 4.82e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 175 RLVGENAKLQRSMETAEEGSARLGE------EILALRKQLHSTQQALQFAKAMDEELEDLKTlarslEEQNRSLlaqaRQ 248
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEElkkklkELEKRLEELEERHELYEEAKAKKEELERLKK-----RLTGLTP----EK 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 249 AEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEhlICQRD-------TILSERTRDVESLAQ 321
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP--VCGRElteehrkELLEEYTAELKRIEK 466

                        170       180
                 ....*....|....*....|....
gi 768006691 322 TLEEYRVTTQELRLEISRLEEQLS 345
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLK 490
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 181-358 5.41e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-MDEELEDLKTLARSLEEQNRS---------------LLA 244
Cdd:COG3883   40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeIEERREELGERARALYRSGGSvsyldvllgsesfsdFLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 245 QARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLE 324
Cdd:COG3883  120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199

                        170       180       190
                 ....*....|....*....|....*....|....
gi 768006691 325 EYRVTTQELRLEISRLEEQLSQTYEGPDELPEGA 358
Cdd:COG3883  200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
179-388 8.26e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 179 ENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVA 258
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 259 EMETLQEEnGKL---------------LAERDGvkkRSQELAMEKDTLKRQLFECEHLIcQRDTILSERTRDVESLAQTL 323
Cdd:PRK02224 444 EAEALLEA-GKCpecgqpvegsphvetIEEDRE---RVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERR 518

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006691 324 E--EYRVTTQELRLEisRLEEQLSQTYEGPDELPEGAQLRRVGWTELLppslgLEIEAIRQEVATAD 388
Cdd:PRK02224 519 EdlEELIAERRETIE--EKRERAEELRERAAELEAEAEEKREAAAEAE-----EEAEEAREEVAELN 578
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 219-344 9.39e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 219 KAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQhLVAEMETLQEEngKLLAERDGVKKRSQELAMEKDTLKRQLFEC 298
Cdd:COG1196  182 EATEENLERLEDILGELERQLEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEEL 258

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 768006691 299 EHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQL 344
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-356 1.29e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   184 QRSMETAEEGSARLGEEILALRKQLHSTQ----QALQFaKAMDEELEDLK--TLARSLEEQNRSLLAQARQAEKEQQhlv 257
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLErqaeKAERY-KELKAELRELElaLLVLRLEELREELEELQEELKEAEE--- 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   258 aEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLIC---QRDTILSERTRDVESLAQTLEEYRVTTQ--- 331
Cdd:TIGR02168  254 -ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQLEELEskl 332

                          170       180
                   ....*....|....*....|....*.
gi 768006691   332 -ELRLEISRLEEQLSQTYEGPDELPE 356
Cdd:TIGR02168  333 dELAEELAELEEKLEELKEELESLEA 358
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
183-362 1.41e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 183 LQRSMETAEEGSARLGEEILALRKQLHSTQQALQ-FAK-----AMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHL 256
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELEEAEAALEeFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 257 VAEMETLQEENGKLLAER--DGVKKRSQELAMEKDTLKRQLFEcEH-----LICQRDT----ILSERTRDVESLAQTLEE 325
Cdd:COG3206  246 RAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTP-NHpdviaLRAQIAAlraqLQQEAQRILASLEAELEA 324

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 768006691 326 YRVTTQELRLEISRLEEQLSQTyegPDELPEGAQLRR 362
Cdd:COG3206  325 LQAREASLQAQLAQLEARLAEL---PELEAELRRLER 358
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 191-295 1.82e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.48  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  191 EEGSARLGEEILALRKQLHSTQQalqfakamdeELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKL 270
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAR----------EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAET 210

                          90       100       110
                  ....*....|....*....|....*....|.
gi 768006691  271 LAE-RDGVKKRSQELAM-----EKDTlkRQL 295
Cdd:PRK11448  211 SQErKQKRKEITDQAAKrlelsEEET--RIL 239
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 204-354 2.11e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  204 LRKQLHSTQQALQFAK----AMDEELEDLKTLARSLE-------EQNRSLLAQARQAEKEQQHLVAEMETLQEENGKL-- 270
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKkenqSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNns 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  271 ----LAERDGVKKRS-QELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLS 345
Cdd:TIGR04523 441 eikdLTNQDSVKELIiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520


                  ....*....
gi 768006691  346 QTYEGPDEL 354
Cdd:TIGR04523 521 SLKEKIEKL 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-346 2.86e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 204 LRKQLHS----TQQALQFaKAMDEELEDLKTLARSLEEqnRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKK 279
Cdd:COG1196  198 LERQLEPlerqAEKAERY-RELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006691 280 RSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 346
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
210-342 4.03e-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: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 210 STQQALqfAKAMDEELEDLKTLARSLEEQNRsllAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKD 289
Cdd:COG2433  377 SIEEAL--EELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS 451

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768006691 290 TLKRQlfecEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEE 342
Cdd:COG2433  452 EARSE----ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
174-354 4.12e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ---AAQAELAQAQEELESLQEEAEELQEELEELQKER 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691 254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDtiLSERTRDVESLAQTLEEYRVTTQEL 333
Cdd:COG4372  125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS--EAEAEQALDELLKEANRNAEKEEEL 202

                        170       180
                 ....*....|....*....|.
gi 768006691 334 RLEISRLEEQLSQTYEGPDEL 354
Cdd:COG4372  203 AEAEKLIESLPRELAEELLEA 223
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 200-346 4.72e-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: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  200 EILALRKQlhsTQQAL-----QFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENG------ 268
Cdd:TIGR04523 296 EISDLNNQ---KEQDWnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqnei 372

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006691  269 -KLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 346
Cdd:TIGR04523 373 eKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 204-347 5.27e-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: 39.62  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691  204 LRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQE 283
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006691  284 LAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYR-----VTTQELRLEISRLEEQLSQT 347
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEI 326
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 173-334 5.30e-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: 39.82  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   173 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAM----DEELEDLKTLARSL------------- 235
Cdd:pfam12128  599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknaRLDLRRLFDEKQSEkdkknkalaerkd 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006691   236 --EEQNRSLLAQARQAEKEQQHLVAEM-ETLQEENGKLLAERDGVKKR--------SQELAMEKDTLKRQLFECEHlicQ 304
Cdd:pfam12128  679 saNERLNSLEAQLKQLDKKHQAWLEEQkEQKREARTEKQAYWQVVEGAldaqlallKAAIAARRSGAKAELKALET---W 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 768006691   305 RDTIL----------SERTRDVESLAQTLEEYRVTTQELR 334
Cdd:pfam12128  756 YKRDLaslgvdpdviAKLKREIRTLERKIERIAVRRQEVL 795
 
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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