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Conserved domains on  [gi|148753319|gb|AAI43044|]
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C6orf174 protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SOGA pfam11365
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ...
 232-326 5.30e-35

Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.


:

Pssm-ID: 463264 [Multi-domain]  Cd Length: 95  Bit Score: 127.41  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  232 DNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEEANI 311
Cdd:pfam11365   1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80

                          90
                  ....*....|....*
gi 148753319  312 LGRKIVELEVENRGL 326
Cdd:pfam11365  81 LSGKVMKLQYENRVL 95
SOGA pfam11365
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ...
 352-440 4.07e-34

Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.


:

Pssm-ID: 463264 [Multi-domain]  Cd Length: 95  Bit Score: 125.10  E-value: 4.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  352 SLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKYKYKSGGHDSARHH------DNAKTEALQEELKAARLQINE 425
Cdd:pfam11365   1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDgegggsDSSREAELQEELKLARLQINE 80

                          90
                  ....*....|....*
gi 148753319  426 LSGKVMQLQYENRVL 440
Cdd:pfam11365  81 LSGKVMKLQYENRVL 95
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-384 1.77e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    78 KNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERkrlryaQTGEIDGELLRSLEQDLKVAKD 157
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELEQLRKELEELSR------QISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   158 VSvRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKElslkRRGSKDLPKSEKKAQQTPTEEDNEDLK 237
Cdd:TIGR02168  749 IA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----ELKALREALDELRAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   238 CQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAG--------GPPSTREAELKLRLRLVEEEA 309
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallnerASLEEALALLRSELEELSEEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   310 NILGRKIVELEVENRGLKAELDDLRGD------DFNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKR 383
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983


                   .
gi 148753319   384 I 384
Cdd:TIGR02168  984 L 984
 
Name Accession Description Interval E-value
SOGA pfam11365
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ...
 232-326 5.30e-35

Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.


Pssm-ID: 463264 [Multi-domain]  Cd Length: 95  Bit Score: 127.41  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  232 DNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEEANI 311
Cdd:pfam11365   1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80

                          90
                  ....*....|....*
gi 148753319  312 LGRKIVELEVENRGL 326
Cdd:pfam11365  81 LSGKVMKLQYENRVL 95
SOGA pfam11365
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ...
 352-440 4.07e-34

Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.


Pssm-ID: 463264 [Multi-domain]  Cd Length: 95  Bit Score: 125.10  E-value: 4.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  352 SLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKYKYKSGGHDSARHH------DNAKTEALQEELKAARLQINE 425
Cdd:pfam11365   1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDgegggsDSSREAELQEELKLARLQINE 80

                          90
                  ....*....|....*
gi 148753319  426 LSGKVMQLQYENRVL 440
Cdd:pfam11365  81 LSGKVMKLQYENRVL 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-434 6.52e-11

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: 65.85  E-value: 6.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   165 ELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRR-----GSKDLPKSEKKAQQTptEEDNEDLKCQ 239
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisaLRKDLARLEAEVEQL--EERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   240 LQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKG-EAGGPPSTREAELKLRLRLVEEEANILGRKIVE 318
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrEALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   319 LEVENRGLKAELDDLRGDdfNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKykyksggH 398
Cdd:TIGR02168  836 TERRLEDLEEQIEELSED--IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE-------L 906

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 148753319   399 DSARHHDNAKTEALQEELKAARLQINELSGKVMQLQ 434
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-384 1.77e-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: 64.31  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    78 KNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERkrlryaQTGEIDGELLRSLEQDLKVAKD 157
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELEQLRKELEELSR------QISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   158 VSvRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKElslkRRGSKDLPKSEKKAQQTPTEEDNEDLK 237
Cdd:TIGR02168  749 IA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----ELKALREALDELRAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   238 CQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAG--------GPPSTREAELKLRLRLVEEEA 309
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallnerASLEEALALLRSELEELSEEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   310 NILGRKIVELEVENRGLKAELDDLRGD------DFNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKR 383
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983


                   .
gi 148753319   384 I 384
Cdd:TIGR02168  984 L 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 69-336 1.54e-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: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  69 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 148
Cdd:COG1196  250 ELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 149 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLkrrgskdlpksEKKAQQTP 228
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----------EALRAAAE 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 229 TEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSfygdldsplpkgeaggppstREAELKLRLRLVEEE 308
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--------------------ALEEAAEEEAELEEE 457

                        250       260
                 ....*....|....*....|....*...
gi 148753319 309 ANILGRKIVELEVENRGLKAELDDLRGD 336
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEE 485
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 70-272 1.23e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   70 LREENETLKNEIDELRTEMDEMRDtffEEDACQLQEMRH----ELERANKNCRILQ-------YRLRKAERKRLRYAQTG 138
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQ---EEIAMEISRMRElerlQMERQQKNERVRQeleaarkVKILEEERQRKIQQQKV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  139 E---IDGELLRSLEQDLKVAKDVSVRlhhELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRgsK 215
Cdd:pfam17380 421 EmeqIRAEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR--K 495

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148753319  216 DLPKSEKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYR 272
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
69-392 6.78e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  69 KLREENETLKNEIDELRTEMDEMrdtffEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYaqtgEIDGELLRSL 148
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKL-----EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEFYEEY 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 149 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRqqliEVEIAKQALQNELEKMKELSLKRRGSKDLPKSEKKAQQTP 228
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 229 TEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEE 308
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAEL 461

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 309 ANILGRKIvELEVENRGLKAELDDLRGDDFNGSANPLMREQSESLSELRQHLQLV--------EDETELLRRNVADLEEQ 380
Cdd:PRK03918 462 KRIEKELK-EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGE 540

                        330
                 ....*....|..
gi 148753319 381 NKRITAELNKYK 392
Cdd:PRK03918 541 IKSLKKELEKLE 552
 
Name Accession Description Interval E-value
SOGA pfam11365
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ...
 232-326 5.30e-35

Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.


Pssm-ID: 463264 [Multi-domain]  Cd Length: 95  Bit Score: 127.41  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  232 DNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEEANI 311
Cdd:pfam11365   1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80

                          90
                  ....*....|....*
gi 148753319  312 LGRKIVELEVENRGL 326
Cdd:pfam11365  81 LSGKVMKLQYENRVL 95
SOGA pfam11365
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ...
 352-440 4.07e-34

Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.


Pssm-ID: 463264 [Multi-domain]  Cd Length: 95  Bit Score: 125.10  E-value: 4.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  352 SLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKYKYKSGGHDSARHH------DNAKTEALQEELKAARLQINE 425
Cdd:pfam11365   1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDgegggsDSSREAELQEELKLARLQINE 80

                          90
                  ....*....|....*
gi 148753319  426 LSGKVMQLQYENRVL 440
Cdd:pfam11365  81 LSGKVMKLQYENRVL 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-434 6.52e-11

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: 65.85  E-value: 6.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   165 ELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRR-----GSKDLPKSEKKAQQTptEEDNEDLKCQ 239
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisaLRKDLARLEAEVEQL--EERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   240 LQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKG-EAGGPPSTREAELKLRLRLVEEEANILGRKIVE 318
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrEALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   319 LEVENRGLKAELDDLRGDdfNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKykyksggH 398
Cdd:TIGR02168  836 TERRLEDLEEQIEELSED--IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE-------L 906

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 148753319   399 DSARHHDNAKTEALQEELKAARLQINELSGKVMQLQ 434
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-384 1.77e-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: 64.31  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    78 KNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERkrlryaQTGEIDGELLRSLEQDLKVAKD 157
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELEQLRKELEELSR------QISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   158 VSvRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKElslkRRGSKDLPKSEKKAQQTPTEEDNEDLK 237
Cdd:TIGR02168  749 IA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----ELKALREALDELRAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   238 CQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAG--------GPPSTREAELKLRLRLVEEEA 309
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallnerASLEEALALLRSELEELSEEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   310 NILGRKIVELEVENRGLKAELDDLRGD------DFNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKR 383
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983


                   .
gi 148753319   384 I 384
Cdd:TIGR02168  984 L 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-436 2.39e-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: 54.29  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   119 ILQYRLRK--AERKrlryaqtgeidgelLRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEkLRQQLIEVEIAKQA 196
Cdd:TIGR02168  167 ISKYKERRkeTERK--------------LERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALLV 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   197 LQ-NELEKMKELSLKRRGSKDLPKSEKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFY 275
Cdd:TIGR02168  232 LRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   276 GDLDSPLPKGEAggppstREAELKLRLRLVEEEANILGRKIVELEVENRGLKAELDDLRGDdfngsanplmreqsesLSE 355
Cdd:TIGR02168  312 ANLERQLEELEA------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE----------------LEE 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   356 LRQHLQLVEDETELLRRNVADLEEQNKRITAELNkyKYKSGGHDSARHHDNAKTEALQEELKAARLQINELSGKVMQLQY 435
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIE--RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447


                   .
gi 148753319   436 E 436
Cdd:TIGR02168  448 E 448
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 69-336 1.54e-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: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  69 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 148
Cdd:COG1196  250 ELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 149 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLkrrgskdlpksEKKAQQTP 228
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----------EALRAAAE 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 229 TEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSfygdldsplpkgeaggppstREAELKLRLRLVEEE 308
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--------------------ALEEAAEEEAELEEE 457

                        250       260
                 ....*....|....*....|....*...
gi 148753319 309 ANILGRKIVELEVENRGLKAELDDLRGD 336
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEE 485
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
69-214 1.10e-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: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   69 KLREENETLKNEIDELRTEMDEMRDTFFEEDACQLQEMRHELERANKncrilqyRLRKAERKRLRYAQtgeidgeLLRSL 148
Cdd:COG4913   306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLEA-------LLAAL 371

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148753319  149 EQDLKVAKDVSVRLHHElenVEEKRTTTEDENEKLRQQLIEVEIAKQALQNEL-EKMKEL-SLKRRGS 214
Cdd:COG4913   372 GLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELrELEAEIaSLERRKS 436
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 70-272 1.23e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   70 LREENETLKNEIDELRTEMDEMRDtffEEDACQLQEMRH----ELERANKNCRILQ-------YRLRKAERKRLRYAQTG 138
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQ---EEIAMEISRMRElerlQMERQQKNERVRQeleaarkVKILEEERQRKIQQQKV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  139 E---IDGELLRSLEQDLKVAKDVSVRlhhELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRgsK 215
Cdd:pfam17380 421 EmeqIRAEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR--K 495

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148753319  216 DLPKSEKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYR 272
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-272 1.24e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    69 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRYA-------QTGEID 141
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEELEaqleeleSKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   142 GELLRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEK-MKELSLKRRGSKDLPKS 220
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDR 415

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 148753319   221 EKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYR 272
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
69-443 3.28e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  69 KLREENETLKNEIDELRTEMDEMrdtffeEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIdgelLRSL 148
Cdd:COG4717   99 ELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEEL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 149 EQDLKVAKDVSVRLHHELENVEEKR-TTTEDENEKLRQQLIEVEIAKQALQNELEKMKElslkrrgskdlpKSEKKAQQT 227
Cdd:COG4717  169 EAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEE------------ELEQLENEL 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 228 PTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFE-----------HELQKYRSFYGDLDSPLPKGEAGGPPSTRE- 295
Cdd:COG4717  237 EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEEl 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 296 ---------AELKLRLRLVEEEANILGRKIVELEVENRGLKAELDDLRGDDFNGSANPLMRE-QSESLSELRQHLQLVED 365
Cdd:COG4717  317 eeeeleellAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEaGVEDEEELRAALEQAEE 396

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148753319 366 ETELLRRnvadLEEQNKRITAELNKYKYKSGGHDSARHhdNAKTEALQEELKAARLQINELSGKVMQLQYENRVLMSN 443
Cdd:COG4717  397 YQELKEE----LEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEED 468
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 79-434 5.39e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 5.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    79 NEIDELRTEmdemRDTFFEEDAC---QLQEMRHELERANKncrilQYRLRKAERKRLRYAQTG----------EIDGELL 145
Cdd:pfam15921  356 SELTEARTE----RDQFSQESGNlddQLQKLLADLHKREK-----ELSLEKEQNKRLWDRDTGnsitidhlrrELDDRNM 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   146 --RSLEQDLKVAKD----------VSVRLHHE-LENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELslkrr 212
Cdd:pfam15921  427 evQRLEALLKAMKSecqgqmerqmAAIQGKNEsLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL----- 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   213 gSKDLPKSEKKAQQTPTE----EDNEDLKCQ-----------LQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGD 277
Cdd:pfam15921  502 -TASLQEKERAIEATNAEitklRSRVDLKLQelqhlknegdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   278 ldsplpKGEAGGPPSTREAELKLRL---RLVEEEANIL----GRKIVELEVENRGLKAELDDL--RGDDFNGSANPLMRE 348
Cdd:pfam15921  581 ------HGRTAGAMQVEKAQLEKEIndrRLELQEFKILkdkkDAKIRELEARVSDLELEKVKLvnAGSERLRAVKDIKQE 654

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   349 QSESLSEL---RQHLQLVEDETELLRRNVAD-----------LEEQNKRITAELNKYKYKSGGHDSARHHDNAKTEALQE 414
Cdd:pfam15921  655 RDQLLNEVktsRNELNSLSEDYEVLKRNFRNkseemetttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK 734

                          410       420
                   ....*....|....*....|
gi 148753319   415 ELKAARLQINELSGKVMQLQ 434
Cdd:pfam15921  735 QITAKRGQIDALQSKIQFLE 754
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
69-392 6.78e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  69 KLREENETLKNEIDELRTEMDEMrdtffEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYaqtgEIDGELLRSL 148
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKL-----EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEFYEEY 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 149 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRqqliEVEIAKQALQNELEKMKELSLKRRGSKDLPKSEKKAQQTP 228
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 229 TEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEE 308
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAEL 461

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 309 ANILGRKIvELEVENRGLKAELDDLRGDDFNGSANPLMREQSESLSELRQHLQLV--------EDETELLRRNVADLEEQ 380
Cdd:PRK03918 462 KRIEKELK-EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGE 540

                        330
                 ....*....|..
gi 148753319 381 NKRITAELNKYK 392
Cdd:PRK03918 541 IKSLKKELEKLE 552
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 70-426 2.55e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    70 LREENETLKNEIDELRTEMDEMRDtffeedacQLQEMRHELERANKNCRILQYRLRKAERKrlryaqtgeidgelLRSLE 149
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASR--------KIGEIEKEIEQLEQEEEKLKERLEELEED--------------LSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   150 QDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIakQALQNELEKMKELSLKRRGS-----KDLPKSEKKA 224
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARlreieQKLNRLTLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   225 QQTPTE-----EDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGppstreAELK 299
Cdd:TIGR02169  829 EYLEKEiqelqEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL------RELE 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   300 LRLRLVEEEANILGRKIVELEVENRGLKAELDDLRGDDFNGSANPlmrEQSESLSELRQHLQLVEDETELLRRNVADLEE 379
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP---EEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 148753319   380 QNKRITAELNKYKyksgghdsarhhdnAKTEALQEELKAARLQINEL 426
Cdd:TIGR02169  980 EYEEVLKRLDELK--------------EKRAKLEEERKAILERIEEY 1012
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 125-434 3.94e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 125 RKAER-KRLRyAQTGEIDGEL----LRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQN 199
Cdd:COG1196  210 EKAERyRELK-EELKELEAELlllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 200 ELekmkelslkRRGSKDLPKSEKkaQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELqkyrsfygdld 279
Cdd:COG1196  289 EE---------YELLAELARLEQ--DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----------- 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 280 splpkgeaggppstreAELKLRLRLVEEEANILGRKIVELEVENRGLKAELDDLRGDDFNgsanpLMREQSESLSELRQH 359
Cdd:COG1196  347 ----------------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-----ALRAAAELAAQLEEL 405

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148753319 360 LQLVEDETELLRRNVADLEEQNKRITAELNKYKYKSgghdSARHHDNAKTEALQEELKAARLQINELSGKVMQLQ 434
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 70-211 5.09e-04

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 42.44  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   70 LREENETLKNEIDELRTEMDEMRDTFFEEdacqLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTgeidgelLRSLE 149
Cdd:pfam09787  59 LREEIQKLRGQIQQLRTELQELEAQQQEE----AESSREQLQELEEQLATERSARREAEAELERLQEE-------LRYLE 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148753319  150 QDLKVAKDVSVRLHHELENVEEK----------RTTTEDENEKLRQQLIEVEIAKQALQNELEKMKE---LSLKR 211
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKlrnqltsksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNslvLQLER 202
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 76-310 5.33e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   76 TLKNEIDELRTEMDEmRDTFFEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSLEQDLKVA 155
Cdd:pfam10174 342 ILQTEVDALRLRLEE-KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGL 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  156 KDVSVRLHHELENVEEKRTTTED---ENEKLRQQLIEveiakQALQNELEKMKELSLKRRGSKDLPK--SEKKAQQTPTE 230
Cdd:pfam10174 421 KERVKSLQTDSSNTDTALTTLEEalsEKERIIERLKE-----QREREDRERLEELESLKKENKDLKEkvSALQPELTEKE 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  231 EDNEDLKcqlqfvkEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEEAN 310
Cdd:pfam10174 496 SSLIDLK-------EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVA 568
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-388 5.69e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  61 EEMQEEmekLREENETLKNEIDELRTEMDEMRDtffeedacQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEI 140
Cdd:COG1196  308 EERRRE---LEERLEELEEELAELEEELEELEE--------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 141 DGELLRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRgskdlpkS 220
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-------E 449

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 221 EKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKL 300
Cdd:COG1196  450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 301 RLRLVEEEANI---LGRKIVELEVENRGLKAELDDLRGDDFNGSAN--PLMREQSESLSELRQHLQLVEDETELLRRNVA 375
Cdd:COG1196  530 IGVEAAYEAALeaaLAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDLR 609

                        330
                 ....*....|...
gi 148753319 376 DLEEQNKRITAEL 388
Cdd:COG1196  610 EADARYYVLGDTL 622
PTZ00121 PTZ00121
MAEBL; Provisional
 78-392 1.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   78 KNEIDELRtEMDEMRDTffeEDACQLQEMRHELERANKNCRILQyRLRKAERKRLRYAQTGEIDGELLRSleQDLKVAKD 157
Cdd:PTZ00121 1545 KKKADELK-KAEELKKA---EEKKKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKA--EEAKKAEE 1617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  158 VSVRLHhELENVEEKRTTTEDENEKLRQQLIEVEIAKQAlqNELEKMKELSLKRRGSKDlpksEKKAQQTPTEEDNEDLK 237
Cdd:PTZ00121 1618 AKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKA 1690

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  238 CQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAggpPSTREAElklRLRLVEEEANilgrKIV 317
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE---EDKKKAE---EAKKDEEEKK----KIA 1760

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148753319  318 ELEVEnrglkaelDDLRGDDFNGSANPLMREQSESLSELRQhlQLVEDETELLRRNVADLEEQNKRITAELNKYK 392
Cdd:PTZ00121 1761 HLKKE--------EEKKAEEIRKEKEAVIEEELDEEDEKRR--MEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 69-383 1.46e-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: 41.75  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    69 KLREENETLKNEIDELRTEMDEMRDTFFEEDACQLQEMRHELERANKNCRI-LQYRLRKAERKRLRYAQTGEIDGellrs 147
Cdd:pfam12128  238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELnQLLRTLDDQWKEKRDELNGELSA----- 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   148 leQDLKVAKDvsvrlHHELENVEEKRTTTEDENeklrqqlieVEIAKQALQNELEKMKELSLKRRGSKDLPKSEKKAQQ- 226
Cdd:pfam12128  313 --ADAAVAKD-----RSELEALEDQHGAFLDAD---------IETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAk 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   227 TPTEEDNEDLKCqlqfvKEEAALMRKKMAKIDKEKDRfehELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVE 306
Cdd:pfam12128  377 YNRRRSKIKEQN-----NRDIAGIKDKLAKIREARDR---QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGE 448

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148753319   307 EEANILGRKIVELEVENRGLKAELDDlRGDDFNGSANplmREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKR 383
Cdd:pfam12128  449 LKLRLNQATATPELLLQLENFDERIE-RAREEQEAAN---AEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 69-433 1.73e-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: 41.54  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   69 KLREENETLKNEIDELRTEMDEMRDTF-------------FEEDACQLQEMRHELERANKNCRILQYRLR--KAERKRLR 133
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEIsntqtqlnqlkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  134 YAQTGEIDGEL----------LRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIE-------------- 189
Cdd:TIGR04523 302 NQKEQDWNKELkselknqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieklkkenqs 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  190 -------VEIAKQALQNELEKMKELSLKRRG---SKDLPKSEKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDK 259
Cdd:TIGR04523 382 ykqeiknLESQINDLESKIQNQEKLNQQKDEqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  260 EKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTRE-AELKLRLRLVEEEANILGRKIVELEVENRGLKAEL-------- 330
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKkekeskis 541

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  331 ---DDLRGDDFNGSANPL---MREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKYKYKSGGHDSARHH 404
Cdd:TIGR04523 542 dleDELNKDDFELKKENLekeIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621

                         410       420
                  ....*....|....*....|....*....
gi 148753319  405 DNAKTEALQEELKaarlQINELSGKVMQL 433
Cdd:TIGR04523 622 AKKENEKLSSIIK----NIKSKKNKLKQE 646
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 69-200 2.32e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    69 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRY--------AQTGEI 140
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYRE-KLEKLKREINELKRELDRLQEELQRLSEELADLnaaiagieAKINEL 439

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148753319   141 DGEL------LRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNE 200
Cdd:TIGR02169  440 EEEKedkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-447 2.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 175 TTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRGSKDLPKSEkkaqqtpteednEDLKCQLQFVKEEAALMRKKM 254
Cdd:PRK03918 142 ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRT------------ENIEELIKEKEKELEEVLREI 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 255 AKIDKEKDRFEHELQKYRSFYGDLDSplpkgeaggppsTRE--AELKLRLRLVEEEANILGRKIVELEVENRGLKAELDD 332
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEE------------LKEeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 333 LRGddfNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKykyksgghdsaRHHDNAKTEAL 412
Cdd:PRK03918 278 LEE---KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-----------LEEKEERLEEL 343

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148753319 413 QEELKAARLQINELSGKVMQLQyENRVLMSNMQRY 447
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYE-EAKAKKEELERL 377
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 70-273 2.87e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   70 LREENETLKNEIDELRTEMDEMRDtffeedacqlqEMRHELERANKNCRILQYRLRKAERKRLRYAQTG-------EIDG 142
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGD-----------EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCnnlkkqiENKN 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  143 ELLRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQalqnelekmKELSLKRRGSKDLPKSEK 222
Cdd:pfam05483 608 KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ---------KEIEDKKISEEKLLEEVE 678

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148753319  223 KAQQTPTE----EDNEDLKCQLQfVKEEAALMRKKMAKIDKEKDRFEHELQKYRS 273
Cdd:pfam05483 679 KAKAIADEavklQKEIDKRCQHK-IAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-436 3.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  72 EENETLKNEIDELRTEMDEMRDtffeedacQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRS---L 148
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLD--------ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleeL 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 149 EQDLKVAKDVSVRLhHELENVEEKRttTEDENEKLRQQLIEVEIAKQALQNELEKMKEL--SLKRRGS---KDLPKSEKK 223
Cdd:PRK03918 358 EERHELYEEAKAKK-EELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARigELKKEIKelkKAIEELKKA 434

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 224 AQQTP------TEEDNEDLKcqlqfvkeeaALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKgeagGPPSTREAE 297
Cdd:PRK03918 435 KGKCPvcgrelTEEHRKELL----------EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK----ESELIKLKE 500

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 298 LKLRLRLVEEEANILGRKIVELEVEN-RGLKAELDDLRGDDFN-----GSANPLMREQSESLSELRQ-HLQLVEDETELL 370
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSlkkelEKLEELKKKLAELEKKLDElEEELAELLKELE 580

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148753319 371 RRNVADLEEQNKRItAELNKYKYKSGGHDSARHHDNAKTEAL---QEELKAARLQINELSGKVMQLQYE 436
Cdd:PRK03918 581 ELGFESVEELEERL-KELEPFYNEYLELKDAEKELEREEKELkklEEELDKAFEELAETEKRLEELRKE 648
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 231-426 6.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 231 EDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLdsplpkgeaggppSTREAELKLRLRLVEEEAN 310
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------------ARRIRALEQELAALEAELA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 311 ILGRKIVELEVENRGLKAELDD-----------------LRGDDFNGSANPLM-------------REQSESLSELRQHL 360
Cdd:COG4942   87 ELEKEIAELRAELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALR 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148753319 361 QLVEDETELLRRNVADLEEQNKRITAELNKYKYKSGGHDSARHHDNAKTEALQEELKAARLQINEL 426
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 69-380 6.33e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319    69 KLREENETlKNEIDELRtemDEMRDTFFEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 148
Cdd:TIGR02169  202 RLRREREK-AERYQALL---KEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   149 EQDLK-VAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRGSKDLPKSEKKAQQT 227
Cdd:TIGR02169  278 NKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   228 PTEEDN---EDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAE-LKLRLR 303
Cdd:TIGR02169  358 EYAELKeelEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgIEAKIN 437

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148753319   304 LVEEEANILGRKIVELEVENRGLKAELDDLRgddfngsanplmreqsESLSELRQHLQLVEDETELLRRNVADLEEQ 380
Cdd:TIGR02169  438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYE----------------QELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 156-390 7.14e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 39.65  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   156 KDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVE-IAKQALQNE----LEKMKELSLKRRGSKDLPKSEKKAQQTPTE 230
Cdd:TIGR01612 1121 KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEdVADKAISNDdpeeIEKKIENIVTKIDKKKNIYDEIKKLLNEIA 1200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   231 EDNEDlKCQLQFVKE-----EAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLV 305
Cdd:TIGR01612 1201 EIEKD-KTSLEEVKGinlsyGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETF 1279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   306 ------EEEANILGRKIVE--LEVENRGLKAELDDLRGDDFNGSANPLMREQSESL---SELRQHLQLVEDETELLRRN- 373
Cdd:TIGR01612 1280 nishddDKDHHIISKKHDEniSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQkhnSDINLYLNEIANIYNILKLNk 1359

                          250       260
                   ....*....|....*....|....*...
gi 148753319   374 -----------VADLEEQNKRITAELNK 390
Cdd:TIGR01612 1360 ikkiidevkeyTKEIEENNKNIKDELDK 1387
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-366 9.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319   72 EENETLKnEIDELRTEMDEMRDTffEEDACQLQEMRHELERANKNC-RILQYRLRKAERKRLRYAQTGEIDGELLRSLEQ 150
Cdd:COG4913   219 EEPDTFE-AADALVEHFDDLERA--HEALEDAREQIELLEPIRELAeRYAAARERLAELEYLRAALRLWFAQRRLELLEA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  151 DLkvakdvsVRLHHELENVEEKRTTTEDENEKLRQQLIEVEiaKQALQNELEKMKELslkrrgskdlpksekkaqqtptE 230
Cdd:COG4913   296 EL-------EELRAELARLEAELERLEARLDALREELDELE--AQIRGNGGDRLEQL----------------------E 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  231 EDNEDLKcqlqfvkeeaalmrkkmakidKEKDRFEHELQKYRSFYGDLDSPLPKGEAG-----GPPSTREAELKLRLRLV 305
Cdd:COG4913   345 REIERLE---------------------RELEERERRRARLEALLAALGLPLPASAEEfaalrAEAAALLEALEEELEAL 403

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148753319  306 EEEANILGRKIVELEVENRGLKAELDDLRGddfNGSANPlmREQSESLSELRQHLQLVEDE 366
Cdd:COG4913   404 EEALAEAEAALRDLRRELRELEAEIASLER---RKSNIP--ARLLALRDALAEALGLDEAE 459
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-388 9.20e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319  71 REENETLKNEIDELRTEMDEMRDTF------FEEDACQLQEMRHELERANKNCRILQYRLRKAeRKRLRYAQTGEIDGEl 144
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFgdapvdLGNAEDFLEELREERDELREREAELEATLRTA-RERVEEAEALLEAGK- 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 145 LRSLEQDLKVAKDVSVrlhheLENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRGSKDLpkSEKKA 224
Cdd:PRK02224 454 CPECGQPVEGSPHVET-----IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL--EELIA 526

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 225 QQTPTEEDNEDlkcQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEaggppSTREAELKLRLRL 304
Cdd:PRK02224 527 ERRETIEEKRE---RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK-----ERIESLERIRTLL 598

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148753319 305 VEEEAniLGRKIVELEvENRGLKAELDDLRGDDfngsanplMREQSESLSELRQHLQlvEDETELLRRNVADLEEQNKRI 384
Cdd:PRK02224 599 AAIAD--AEDEIERLR-EKREALAELNDERRER--------LAEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQV 665


                 ....
gi 148753319 385 TAEL 388
Cdd:PRK02224 666 EEKL 669
 
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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