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Conserved domains on  [gi|24308420|ref|NP_694539|]
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protein phosphatase 1 regulatory subunit 21 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
255-760 0e+00

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.


:

Pssm-ID: 463001  Cd Length: 523  Bit Score: 858.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   255 IAGQALAFVQDLVTALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLE 334
Cdd:pfam10212   1 LAGQALSFIQDLVSALLNFHTYTEQRVQIFPIDSAIDPISPLNQKFSQYLHENASYVRPLEEGFLQLHESITEDTVTTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   335 TTVKLKTFSEHLTSYICFLRKILPYQLKSLEEECESSLCTSALRARNLELSQDMKKMTAVFEKLQTYIALLALPSTEPDG 414
Cdd:pfam10212  81 TAVKLKDFSDHFHSYVCFLKKILPYQLKSLEEECESSLCTATLTARNMELHNDMKKMTAVFEKLQTYISLLALPSTKPEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   415 LLRTNYSSVLTNVGAALHGFHDVMKDISKHYSQKAAIEHELPTATQKLITTNDCILSSVVALTNGAGKIASFFSNNLDYF 494
Cdd:pfam10212 161 LPRTNYSAVFTQLAACLHGLHDAVKEISKHYNQKASLEQELPTATQKLKTTNECILSSLVSLTNSTGKIATFFSNNLDFF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   495 IASLSYGPKAASGFISPLSAECMLQYKKKAAAYMKSLRKPLLESVPYEEALANRRILLSSTESREGLAQQVQQSLEKISK 574
Cdd:pfam10212 241 TSSAGYGPKGGTGFLNPLSAECMLQYKKKAVAYISSLKKPCPESVPYEEALSNRRVLLSSTESREGLAQQVQQSQEKIAK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   575 LEQEKEHWMLEAQLAKIKLEKENQRIAD----KLKNTGSAQLVGLAQENAAVSNTAGQDEATAKAVL-EPIQSTSLV--- 646
Cdd:pfam10212 321 LEQEKEHWMLEAQLLKIKLEKENQRIADlekqLLKGSTSGQLPELVQSKATLPLTAKQGSEASSISEkEPTPSTSLIgml 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   647 ---------PDVESREDLIKNHYMARIVELTSQLQLADSKSVHFYAECRALSKRLALAEKSKEALTEEMKLASQNISRLQ 717
Cdd:pfam10212 401 tvttdseesSDEESREQLIKSHYMARIAELTSQLQLADSKAVHFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQ 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 24308420   718 DELTTTKRSYEDQLSMMSDHLCSMNETLSKQREEIDTLKMSSK 760
Cdd:pfam10212 481 DELTTTKRSYEDQLSMMSDHLCSMNETLTKQREEIDTLKMASK 523
KLRAQ pfam10205
Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain ...
11-111 3.48e-38

Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain of a family of proteins conserved from nematodes to humans. It carries a characteriztic KLRAQ sequence-motif. The function is not known.


:

Pssm-ID: 462996 [Multi-domain]  Cd Length: 105  Bit Score: 137.29  E-value: 3.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    11 QKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKK- 89
Cdd:pfam10205   1 QKLAQEYSKLRAQNSVLKKAVLDEQQKNNSLKESLKEKEQSLRKSEQEMDSLTFRNQQLTKRVTLLQEELELSEKKESGg 80
                          90       100
                  ....*....|....*....|....*
gi 24308420    90 ---NKKSGESSSQLSQEQKSVFDED 111
Cdd:pfam10205  81 qwfGKNKGDSESQKKEEETSVLDEE 105
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-225 5.68e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 5.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   2 ASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  82 LSEpRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:COG1196 362 EAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308420 162 TrkymETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEK 225
Cdd:COG1196 441 E----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
 
Name Accession Description Interval E-value
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
255-760 0e+00

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.


Pssm-ID: 463001  Cd Length: 523  Bit Score: 858.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   255 IAGQALAFVQDLVTALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLE 334
Cdd:pfam10212   1 LAGQALSFIQDLVSALLNFHTYTEQRVQIFPIDSAIDPISPLNQKFSQYLHENASYVRPLEEGFLQLHESITEDTVTTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   335 TTVKLKTFSEHLTSYICFLRKILPYQLKSLEEECESSLCTSALRARNLELSQDMKKMTAVFEKLQTYIALLALPSTEPDG 414
Cdd:pfam10212  81 TAVKLKDFSDHFHSYVCFLKKILPYQLKSLEEECESSLCTATLTARNMELHNDMKKMTAVFEKLQTYISLLALPSTKPEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   415 LLRTNYSSVLTNVGAALHGFHDVMKDISKHYSQKAAIEHELPTATQKLITTNDCILSSVVALTNGAGKIASFFSNNLDYF 494
Cdd:pfam10212 161 LPRTNYSAVFTQLAACLHGLHDAVKEISKHYNQKASLEQELPTATQKLKTTNECILSSLVSLTNSTGKIATFFSNNLDFF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   495 IASLSYGPKAASGFISPLSAECMLQYKKKAAAYMKSLRKPLLESVPYEEALANRRILLSSTESREGLAQQVQQSLEKISK 574
Cdd:pfam10212 241 TSSAGYGPKGGTGFLNPLSAECMLQYKKKAVAYISSLKKPCPESVPYEEALSNRRVLLSSTESREGLAQQVQQSQEKIAK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   575 LEQEKEHWMLEAQLAKIKLEKENQRIAD----KLKNTGSAQLVGLAQENAAVSNTAGQDEATAKAVL-EPIQSTSLV--- 646
Cdd:pfam10212 321 LEQEKEHWMLEAQLLKIKLEKENQRIADlekqLLKGSTSGQLPELVQSKATLPLTAKQGSEASSISEkEPTPSTSLIgml 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   647 ---------PDVESREDLIKNHYMARIVELTSQLQLADSKSVHFYAECRALSKRLALAEKSKEALTEEMKLASQNISRLQ 717
Cdd:pfam10212 401 tvttdseesSDEESREQLIKSHYMARIAELTSQLQLADSKAVHFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQ 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 24308420   718 DELTTTKRSYEDQLSMMSDHLCSMNETLSKQREEIDTLKMSSK 760
Cdd:pfam10212 481 DELTTTKRSYEDQLSMMSDHLCSMNETLTKQREEIDTLKMASK 523
KLRAQ pfam10205
Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain ...
11-111 3.48e-38

Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain of a family of proteins conserved from nematodes to humans. It carries a characteriztic KLRAQ sequence-motif. The function is not known.


Pssm-ID: 462996 [Multi-domain]  Cd Length: 105  Bit Score: 137.29  E-value: 3.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    11 QKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKK- 89
Cdd:pfam10205   1 QKLAQEYSKLRAQNSVLKKAVLDEQQKNNSLKESLKEKEQSLRKSEQEMDSLTFRNQQLTKRVTLLQEELELSEKKESGg 80
                          90       100
                  ....*....|....*....|....*
gi 24308420    90 ---NKKSGESSSQLSQEQKSVFDED 111
Cdd:pfam10205  81 qwfGKNKGDSESQKKEEETSVLDEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-225 5.68e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 5.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   2 ASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  82 LSEpRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:COG1196 362 EAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308420 162 TrkymETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEK 225
Cdd:COG1196 441 E----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-226 7.55e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     84 EprgKKNKKSGESSSQLSQEQKSVFD--EDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:TIGR02168  837 E---RRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24308420    162 TRKY---METIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEKV 226
Cdd:TIGR02168  914 RRELeelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
4-197 2.30e-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: 50.53  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLtfrNLQLAKRVELLQDELALS 83
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELLRAL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  84 EPRGKKNKK----SGESSSQ----------LSQEQKSVFDEdLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLET 149
Cdd:COG4942 114 YRLGRQPPLalllSPEDFLDavrrlqylkyLAPARREQAEE-LRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24308420 150 EAAQHQAVVDGLTRK---YMETIEKLQNDKAKLEVKSQTLEKEAKECRLRT 197
Cdd:COG4942 193 LKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAAAAERT 243
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
11-223 1.56e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   11 QKLAQEYSKLRAqnqvLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKKN 90
Cdd:PRK03918 289 KEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   91 KKSGESSSQLSQEQKSVFD---EDLQKKIEENERlhiqffeADEQHKHVEAELRSRLATLETEAAQHQAVVD-------- 159
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGltpEKLEKELEELEK-------AKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgk 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  160 --------------GLTRKYMETIEKLQNDKAKLEVKSQTLEKEAKECR--LRTEECQLQLKTLHEDLSgRLEESLSIIN 223
Cdd:PRK03918 438 cpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLK-ELEEKLKKYN 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-756 2.60e-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: 41.58  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      4 AELQGKYQKL------AQEYSKLRAQNQVLKKGVVDEQANSaaLKEQLKMKDQSLRKLQQEMDSLTfRNLQlAKRVELLQ 77
Cdd:TIGR02168  196 NELERQLKSLerqaekAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELT-AELQ-ELEEKLEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     78 DELALSEPRGKKNKKSGESssQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEA---ELRSRLATLETEAAQH 154
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKEL--YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    155 QAVVDGLTrkymETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSgRLEESLSIINEKVPFNDTKYS 234
Cdd:TIGR02168  350 KEELESLE----AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    235 QynalnvpLHNRRHQLKMRDIAGQALAFVQDLVTALLNFHTYTEQRIQIfpvDSAIDTISPLNQKFSQYLHENASYVRPL 314
Cdd:TIGR02168  425 E-------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLDSL 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    315 EEgMLHLFESITEDTVTVLEttvKLKTFSEHLTSYIcflrkilpyQLKSLEEECESSLCTsALRARnlelSQDmkkmtAV 394
Cdd:TIGR02168  495 ER-LQENLEGFSEGVKALLK---NQSGLSGILGVLS---------ELISVDEGYEAAIEA-ALGGR----LQA-----VV 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    395 FEKLQTyiALLALPSTEPDGLLRTNYSSVLTNVGAALHGFHDVMKDISKHYSQKAAIEHELPTATQKLITTndcILSSVV 474
Cdd:TIGR02168  552 VENLNA--AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY---LLGGVL 626
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    475 ALTNGAGKIASFFSNNLDYFIASLSYGPKAASGFISPLSAEC---MLQYK----------KKAAAYMKSLRKPL------ 535
Cdd:TIGR02168  627 VVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssILERRreieeleekiEELEEKIAELEKALaelrke 706
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    536 LESVPYEEALANRRILLSSTESREG------LAQQVQQSLEKISKLEQEKEHWMLEAQLAKIKLEKENQRIADKLKNTGS 609
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    610 AQLVGLAQENAAVSNTAGQDEATAKAVLEPIQSTSLVPDVESREDLIK------NHYMARIVELTSQLQLADSKSVHFYA 683
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAaterrlEDLEEQIEELSEDIESLAAEIEELEE 866
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24308420    684 ECRALSKRLALAEKSKEALTEEMKLAS---QNISRLQDELTTTKRSYEDQLSMMSDHLCSMNETLSKQREEIDTLK 756
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4-172 3.94e-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: 40.82  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     84 EPrgkkNKKSGESSSQlsqEQKSVfdEDLQKKIEENERlHIQFFE-----ADEQHKHVEA---ELRSRLATLETEAAQHQ 155
Cdd:TIGR02169  937 ED----PKGEDEEIPE---EELSL--EDVQAELQRVEE-EIRALEpvnmlAIQEYEEVLKrldELKEKRAKLEEERKAIL 1006
                          170       180
                   ....*....|....*....|.
gi 24308420    156 AVVDGLTRK----YMETIEKL 172
Cdd:TIGR02169 1007 ERIEEYEKKkrevFMEAFEAI 1027
 
Name Accession Description Interval E-value
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
255-760 0e+00

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.


Pssm-ID: 463001  Cd Length: 523  Bit Score: 858.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   255 IAGQALAFVQDLVTALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLE 334
Cdd:pfam10212   1 LAGQALSFIQDLVSALLNFHTYTEQRVQIFPIDSAIDPISPLNQKFSQYLHENASYVRPLEEGFLQLHESITEDTVTTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   335 TTVKLKTFSEHLTSYICFLRKILPYQLKSLEEECESSLCTSALRARNLELSQDMKKMTAVFEKLQTYIALLALPSTEPDG 414
Cdd:pfam10212  81 TAVKLKDFSDHFHSYVCFLKKILPYQLKSLEEECESSLCTATLTARNMELHNDMKKMTAVFEKLQTYISLLALPSTKPEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   415 LLRTNYSSVLTNVGAALHGFHDVMKDISKHYSQKAAIEHELPTATQKLITTNDCILSSVVALTNGAGKIASFFSNNLDYF 494
Cdd:pfam10212 161 LPRTNYSAVFTQLAACLHGLHDAVKEISKHYNQKASLEQELPTATQKLKTTNECILSSLVSLTNSTGKIATFFSNNLDFF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   495 IASLSYGPKAASGFISPLSAECMLQYKKKAAAYMKSLRKPLLESVPYEEALANRRILLSSTESREGLAQQVQQSLEKISK 574
Cdd:pfam10212 241 TSSAGYGPKGGTGFLNPLSAECMLQYKKKAVAYISSLKKPCPESVPYEEALSNRRVLLSSTESREGLAQQVQQSQEKIAK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   575 LEQEKEHWMLEAQLAKIKLEKENQRIAD----KLKNTGSAQLVGLAQENAAVSNTAGQDEATAKAVL-EPIQSTSLV--- 646
Cdd:pfam10212 321 LEQEKEHWMLEAQLLKIKLEKENQRIADlekqLLKGSTSGQLPELVQSKATLPLTAKQGSEASSISEkEPTPSTSLIgml 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   647 ---------PDVESREDLIKNHYMARIVELTSQLQLADSKSVHFYAECRALSKRLALAEKSKEALTEEMKLASQNISRLQ 717
Cdd:pfam10212 401 tvttdseesSDEESREQLIKSHYMARIAELTSQLQLADSKAVHFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQ 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 24308420   718 DELTTTKRSYEDQLSMMSDHLCSMNETLSKQREEIDTLKMSSK 760
Cdd:pfam10212 481 DELTTTKRSYEDQLSMMSDHLCSMNETLTKQREEIDTLKMASK 523
KLRAQ pfam10205
Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain ...
11-111 3.48e-38

Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain of a family of proteins conserved from nematodes to humans. It carries a characteriztic KLRAQ sequence-motif. The function is not known.


Pssm-ID: 462996 [Multi-domain]  Cd Length: 105  Bit Score: 137.29  E-value: 3.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    11 QKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKK- 89
Cdd:pfam10205   1 QKLAQEYSKLRAQNSVLKKAVLDEQQKNNSLKESLKEKEQSLRKSEQEMDSLTFRNQQLTKRVTLLQEELELSEKKESGg 80
                          90       100
                  ....*....|....*....|....*
gi 24308420    90 ---NKKSGESSSQLSQEQKSVFDED 111
Cdd:pfam10205  81 qwfGKNKGDSESQKKEEETSVLDEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-225 5.68e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 5.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   2 ASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  82 LSEpRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:COG1196 362 EAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308420 162 TrkymETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEK 225
Cdd:COG1196 441 E----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-226 7.55e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     84 EprgKKNKKSGESSSQLSQEQKSVFD--EDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:TIGR02168  837 E---RRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24308420    162 TRKY---METIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEKV 226
Cdd:TIGR02168  914 RRELeelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4-226 1.27e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  84 EPRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVvdgltR 163
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-----E 403
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24308420 164 KYMETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEKV 226
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
4-197 2.30e-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: 50.53  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLtfrNLQLAKRVELLQDELALS 83
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELLRAL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  84 EPRGKKNKK----SGESSSQ----------LSQEQKSVFDEdLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLET 149
Cdd:COG4942 114 YRLGRQPPLalllSPEDFLDavrrlqylkyLAPARREQAEE-LRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24308420 150 EAAQHQAVVDGLTRK---YMETIEKLQNDKAKLEVKSQTLEKEAKECRLRT 197
Cdd:COG4942 193 LKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAAAAERT 243
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-211 1.07e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      1 MASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDEL 80
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     81 AlseprgKKNKKSGESSSQLsqeqksvfdEDLQKKIEENERLhiqFFEADEQhkhvEAELRSRLATLETEAAQHQAVVDG 160
Cdd:TIGR02168  361 E------ELEAELEELESRL---------EELEEQLETLRSK---VAQLELQ----IASLNNEIERLEARLERLEDRRER 418
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24308420    161 LTRKYMETIEKLQ-NDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDL 211
Cdd:TIGR02168  419 LQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5-212 7.14e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 7.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      5 ELQGKYQKLAQEYSKLRAQNQVLKKgvvdeqaNSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSE 84
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     85 ---------PRGKKNKKSGESSSQLSQE-----------QKSVFDEDLQKKIEENERLHIQ--FFEADEQHKHVEAE--- 139
Cdd:TIGR02169  779 ealndlearLSHSRIPEIQAELSKLEEEvsriearlreiEQKLNRLTLEKEYLEKEIQELQeqRIDLKEQIKSIEKEien 858
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24308420    140 LRSRLATLETEAAQHQAVVDGLTRKYME---TIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLS 212
Cdd:TIGR02169  859 LNGKKEELEEELEELEAALRDLESRLGDlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
11-223 1.56e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   11 QKLAQEYSKLRAqnqvLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKKN 90
Cdd:PRK03918 289 KEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420   91 KKSGESSSQLSQEQKSVFD---EDLQKKIEENERlhiqffeADEQHKHVEAELRSRLATLETEAAQHQAVVD-------- 159
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGltpEKLEKELEELEK-------AKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgk 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  160 --------------GLTRKYMETIEKLQNDKAKLEVKSQTLEKEAKECR--LRTEECQLQLKTLHEDLSgRLEESLSIIN 223
Cdd:PRK03918 438 cpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLK-ELEEKLKKYN 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-756 2.60e-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: 41.58  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      4 AELQGKYQKL------AQEYSKLRAQNQVLKKGVVDEQANSaaLKEQLKMKDQSLRKLQQEMDSLTfRNLQlAKRVELLQ 77
Cdd:TIGR02168  196 NELERQLKSLerqaekAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELT-AELQ-ELEEKLEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     78 DELALSEPRGKKNKKSGESssQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEA---ELRSRLATLETEAAQH 154
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKEL--YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    155 QAVVDGLTrkymETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSgRLEESLSIINEKVPFNDTKYS 234
Cdd:TIGR02168  350 KEELESLE----AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    235 QynalnvpLHNRRHQLKMRDIAGQALAFVQDLVTALLNFHTYTEQRIQIfpvDSAIDTISPLNQKFSQYLHENASYVRPL 314
Cdd:TIGR02168  425 E-------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLDSL 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    315 EEgMLHLFESITEDTVTVLEttvKLKTFSEHLTSYIcflrkilpyQLKSLEEECESSLCTsALRARnlelSQDmkkmtAV 394
Cdd:TIGR02168  495 ER-LQENLEGFSEGVKALLK---NQSGLSGILGVLS---------ELISVDEGYEAAIEA-ALGGR----LQA-----VV 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    395 FEKLQTyiALLALPSTEPDGLLRTNYSSVLTNVGAALHGFHDVMKDISKHYSQKAAIEHELPTATQKLITTndcILSSVV 474
Cdd:TIGR02168  552 VENLNA--AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY---LLGGVL 626
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    475 ALTNGAGKIASFFSNNLDYFIASLSYGPKAASGFISPLSAEC---MLQYK----------KKAAAYMKSLRKPL------ 535
Cdd:TIGR02168  627 VVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssILERRreieeleekiEELEEKIAELEKALaelrke 706
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    536 LESVPYEEALANRRILLSSTESREG------LAQQVQQSLEKISKLEQEKEHWMLEAQLAKIKLEKENQRIADKLKNTGS 609
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    610 AQLVGLAQENAAVSNTAGQDEATAKAVLEPIQSTSLVPDVESREDLIK------NHYMARIVELTSQLQLADSKSVHFYA 683
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAaterrlEDLEEQIEELSEDIESLAAEIEELEE 866
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24308420    684 ECRALSKRLALAEKSKEALTEEMKLAS---QNISRLQDELTTTKRSYEDQLSMMSDHLCSMNETLSKQREEIDTLK 756
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4-172 3.94e-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: 40.82  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     84 EPrgkkNKKSGESSSQlsqEQKSVfdEDLQKKIEENERlHIQFFE-----ADEQHKHVEA---ELRSRLATLETEAAQHQ 155
Cdd:TIGR02169  937 ED----PKGEDEEIPE---EELSL--EDVQAELQRVEE-EIRALEpvnmlAIQEYEEVLKrldELKEKRAKLEEERKAIL 1006
                          170       180
                   ....*....|....*....|.
gi 24308420    156 AVVDGLTRK----YMETIEKL 172
Cdd:TIGR02169 1007 ERIEEYEKKkrevFMEAFEAI 1027
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-224 4.13e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420  110 EDLQKKIEENERLHIQFFEADEQHKHVEaELRSRLATLETEAAQHQAVVDGLTrkymETIEKLQNDKAKLEVKSQTLEKE 189
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKR----ERAEELRERAAELEAEAEEKREA 559
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 24308420  190 AKECRLRTEECQLQLKTLHEDLS---------GRLEESLSIINE 224
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAelkerieslERIRTLLAAIAD 603
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5-225 5.00e-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: 40.44  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420      5 ELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTF-RNLQLAKRVELLQDELALS 83
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASL 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420     84 EPRGKKNKKSGESSSQLSQEQKSVFD------EDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAA----- 152
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrde 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308420    153 --QHQAVVDGLTRK-----------------YMETIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSG 213
Cdd:TIGR02169  387 lkDYREKLEKLKREinelkreldrlqeelqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
                          250
                   ....*....|....*...
gi 24308420    214 ------RLEESLSIINEK 225
Cdd:TIGR02169  467 yeqelyDLKEEYDRVEKE 484
 
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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