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Conserved domains on  [gi|2462569957|ref|XP_054196436|]
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protein phosphatase 1 regulatory subunit 21 isoform X1 [Homo sapiens]

Protein Classification

KLRAQ and TTKRSYEDQ domain-containing protein( domain architecture ID 10562896)

KLRAQ and TTKRSYEDQ domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTKRSYEDQ super family cl16016
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
255-408 6.43e-93

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.


The actual alignment was detected with superfamily member pfam10212:

Pssm-ID: 463001  Cd Length: 523  Bit Score: 290.96  E-value: 6.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957 255 IAGQALAFVQDLVTALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLE 334
Cdd:pfam10212   1 LAGQALSFIQDLVSALLNFHTYTEQRVQIFPIDSAIDPISPLNQKFSQYLHENASYVRPLEEGFLQLHESITEDTVTTLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957 335 TTVKLKTFSEHLTSYICFLRKILPYQLKSLEEECESSLCTSALRARNLELSQDMKKMTAVFEKLQTYIALLALP 408
Cdd:pfam10212  81 TAVKLKDFSDHFHSYVCFLKKILPYQLKSLEEECESSLCTATLTARNMELHNDMKKMTAVFEKLQTYISLLALP 154
KLRAQ pfam10205
Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain ...
11-111 9.87e-40

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: 138.44  E-value: 9.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  11 QKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKK- 89
Cdd:pfam10205   1 QKLAQEYSKLRAQNSVLKKAVLDEQQKNNSLKESLKEKEQSLRKSEQEMDSLTFRNQQLTKRVTLLQEELELSEKKESGg 80
                          90       100
                  ....*....|....*....|....*
gi 2462569957  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 1.96e-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: 53.79  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   2 ASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  82 LSEpRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:COG1196   362 EAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957 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 ...
255-408 6.43e-93

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: 290.96  E-value: 6.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957 255 IAGQALAFVQDLVTALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLE 334
Cdd:pfam10212   1 LAGQALSFIQDLVSALLNFHTYTEQRVQIFPIDSAIDPISPLNQKFSQYLHENASYVRPLEEGFLQLHESITEDTVTTLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957 335 TTVKLKTFSEHLTSYICFLRKILPYQLKSLEEECESSLCTSALRARNLELSQDMKKMTAVFEKLQTYIALLALP 408
Cdd:pfam10212  81 TAVKLKDFSDHFHSYVCFLKKILPYQLKSLEEECESSLCTATLTARNMELHNDMKKMTAVFEKLQTYISLLALP 154
KLRAQ pfam10205
Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain ...
11-111 9.87e-40

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: 138.44  E-value: 9.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  11 QKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKK- 89
Cdd:pfam10205   1 QKLAQEYSKLRAQNSVLKKAVLDEQQKNNSLKESLKEKEQSLRKSEQEMDSLTFRNQQLTKRVTLLQEELELSEKKESGg 80
                          90       100
                  ....*....|....*....|....*
gi 2462569957  90 ---NKKSGESSSQLSQEQKSVFDED 111
Cdd:pfam10205  81 qwfGKNKGDSESQKKEEETSVLDEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-225 1.96e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   2 ASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  82 LSEpRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:COG1196   362 EAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957 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 3.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   84 EprgKKNKKSGESSSQLSQEQKSVFDE--DLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:TIGR02168  837 E---RRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462569957  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 7.33e-07

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: 51.30  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLtfrNLQLAKRVELLQDELALS 83
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  84 EPRGKKNKK----SGESSSQ----------LSQEQKSVFDEdLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLET 149
Cdd:COG4942   114 YRLGRQPPLalllSPEDFLDavrrlqylkyLAPARREQAEE-LRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462569957 150 EAAQHQAVVDGLTRK---YMETIEKLQNDKAKLEVKSQTLEKEAKECRLRT 197
Cdd:COG4942   193 LKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAAAAERT 243
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
11-223 4.85e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  11 QKLAQEYSKLRAqnqvLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKKN 90
Cdd:PRK03918  289 KEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  91 KKSGESSSQLSQEQKSVFD---EDLQKKIEENERlhiqffeADEQHKHVEAELRSRLATLETEAAQHQAVVD-------- 159
Cdd:PRK03918  365 EEAKAKKEELERLKKRLTGltpEKLEKELEELEK-------AKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgk 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957 160 --------------GLTRKYMETIEKLQNDKAKLEVKSQTLEKEAKECR--LRTEECQLQLKTLHEDLSgRLEESLSIIN 223
Cdd:PRK03918  438 cpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLK-ELEEKLKKYN 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4-172 1.15e-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: 41.59  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   84 EPrgkkNKKSGESSSQlsqEQKSVfdEDLQKKIEENERlHIQFFE-----ADEQHKHVEA---ELRSRLATLETEAAQHQ 155
Cdd:TIGR02169  937 ED----PKGEDEEIPE---EELSL--EDVQAELQRVEE-EIRALEpvnmlAIQEYEEVLKrldELKEKRAKLEEERKAIL 1006
                          170       180
                   ....*....|....*....|.
gi 2462569957  156 AVVDGLTRK----YMETIEKL 172
Cdd:TIGR02169 1007 ERIEEYEKKkrevFMEAFEAI 1027
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
9-188 7.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   9 KYQKLAQEYSKLRAQNQVLKKGVVDEQA---NSAALKEQLKMKDQSLRKLQQEMDSLTFRNL-QLAKRVELLQ------- 77
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEpfyneyl 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  78 ------DELALSEPRGKKNKKSGESSSQLSQEQKSVFdEDLQKKIEENERLHiqffeADEQHKHVE---AELRSRLATLE 148
Cdd:PRK03918  606 elkdaeKELEREEKELKKLEEELDKAFEELAETEKRL-EELRKELEELEKKY-----SEEEYEELReeyLELSRELAGLR 679
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462569957 149 TEAAQHQAVVDGLtrkyMETIEKLQNDKAKLEVKSQTLEK 188
Cdd:PRK03918  680 AELEELEKRREEI----KKTLEKLKEELEEREKAKKELEK 715
 
Name Accession Description Interval E-value
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
255-408 6.43e-93

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: 290.96  E-value: 6.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957 255 IAGQALAFVQDLVTALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLE 334
Cdd:pfam10212   1 LAGQALSFIQDLVSALLNFHTYTEQRVQIFPIDSAIDPISPLNQKFSQYLHENASYVRPLEEGFLQLHESITEDTVTTLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957 335 TTVKLKTFSEHLTSYICFLRKILPYQLKSLEEECESSLCTSALRARNLELSQDMKKMTAVFEKLQTYIALLALP 408
Cdd:pfam10212  81 TAVKLKDFSDHFHSYVCFLKKILPYQLKSLEEECESSLCTATLTARNMELHNDMKKMTAVFEKLQTYISLLALP 154
KLRAQ pfam10205
Predicted coiled-coil domain-containing protein; This is the N-terminal 100 amino acid domain ...
11-111 9.87e-40

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: 138.44  E-value: 9.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  11 QKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKK- 89
Cdd:pfam10205   1 QKLAQEYSKLRAQNSVLKKAVLDEQQKNNSLKESLKEKEQSLRKSEQEMDSLTFRNQQLTKRVTLLQEELELSEKKESGg 80
                          90       100
                  ....*....|....*....|....*
gi 2462569957  90 ---NKKSGESSSQLSQEQKSVFDED 111
Cdd:pfam10205  81 qwfGKNKGDSESQKKEEETSVLDEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-225 1.96e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   2 ASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  82 LSEpRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:COG1196   362 EAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957 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 3.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   84 EprgKKNKKSGESSSQLSQEQKSVFDE--DLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGL 161
Cdd:TIGR02168  837 E---RRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462569957  162 TRKY---METIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSGRLEESLSIINEKV 226
Cdd:TIGR02168  914 RRELeelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4-226 4.02e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 4.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  84 EPRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVvdgltR 163
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-----E 403
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462569957 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 7.33e-07

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: 51.30  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLtfrNLQLAKRVELLQDELALS 83
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  84 EPRGKKNKK----SGESSSQ----------LSQEQKSVFDEdLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLET 149
Cdd:COG4942   114 YRLGRQPPLalllSPEDFLDavrrlqylkyLAPARREQAEE-LRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462569957 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 3.99e-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: 46.20  E-value: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    1 MASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDEL 80
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   81 AlseprgKKNKKSGESSSQLsqeqksvfdEDLQKKIEENERLhiqFFEADEQhkhvEAELRSRLATLETEAAQHQAVVDG 160
Cdd:TIGR02168  361 E------ELEAELEELESRL---------EELEEQLETLRSK---VAQLELQ----IASLNNEIERLEARLERLEDRRER 418
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462569957  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 1.89e-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: 43.90  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    5 ELQGKYQKLAQEYSKLRAQNQVLKKgvvdeqaNSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSE 84
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   85 ---------PRGKKNKKSGESSSQLSQE-----------QKSVFDEDLQKKIEENERLHIQ--FFEADEQHKHVEAE--- 139
Cdd:TIGR02169  779 ealndlearLSHSRIPEIQAELSKLEEEvsriearlreiEQKLNRLTLEKEYLEKEIQELQeqRIDLKEQIKSIEKEien 858
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462569957  140 LRSRLATLETEAAQHQAVVDGLTRKYME---TIEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLS 212
Cdd:TIGR02169  859 LNGKKEELEEELEELEAALRDLESRLGDlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2-192 2.92e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   2 ASAELQgkYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELA 81
Cdd:COG3883    12 AFADPQ--IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  82 LsepRGKKNKKSGESSSQLSQ--EQKSVFD-------------------EDLQKKIEENERLHIQFFEADEQHKHVEAEL 140
Cdd:COG3883    90 E---RARALYRSGGSVSYLDVllGSESFSDfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAEL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462569957 141 RSRLATLETEAAQHQAVVDGLTRKymetIEKLQNDKAKLEVKSQTLEKEAKE 192
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAE----EAAAEAQLAELEAELAAAEAAAAA 214
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
11-223 4.85e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  11 QKLAQEYSKLRAqnqvLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKKN 90
Cdd:PRK03918  289 KEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  91 KKSGESSSQLSQEQKSVFD---EDLQKKIEENERlhiqffeADEQHKHVEAELRSRLATLETEAAQHQAVVD-------- 159
Cdd:PRK03918  365 EEAKAKKEELERLKKRLTGltpEKLEKELEELEK-------AKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgk 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957 160 --------------GLTRKYMETIEKLQNDKAKLEVKSQTLEKEAKECR--LRTEECQLQLKTLHEDLSgRLEESLSIIN 223
Cdd:PRK03918  438 cpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLK-ELEEKLKKYN 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4-172 1.15e-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: 41.59  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    4 AELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALS 83
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   84 EPrgkkNKKSGESSSQlsqEQKSVfdEDLQKKIEENERlHIQFFE-----ADEQHKHVEA---ELRSRLATLETEAAQHQ 155
Cdd:TIGR02169  937 ED----PKGEDEEIPE---EELSL--EDVQAELQRVEE-EIRALEpvnmlAIQEYEEVLKrldELKEKRAKLEEERKAIL 1006
                          170       180
                   ....*....|....*....|.
gi 2462569957  156 AVVDGLTRK----YMETIEKL 172
Cdd:TIGR02169 1007 ERIEEYEKKkrevFMEAFEAI 1027
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5-225 1.37e-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: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957    5 ELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTF-RNLQLAKRVELLQDELALS 83
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASL 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   84 EPRGKKNKKSGESSSQLSQEQKSVFD------EDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAA----- 152
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrde 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  153 --QHQAVVDGLTRKYMET-----------------IEKLQNDKAKLEVKSQTLEKEAKECRLRTEECQLQLKTLHEDLSG 213
Cdd:TIGR02169  387 lkDYREKLEKLKREINELkreldrlqeelqrlseeLADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
                          250
                   ....*....|....*...
gi 2462569957  214 ------RLEESLSIINEK 225
Cdd:TIGR02169  467 yeqelyDLKEEYDRVEKE 484
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-224 1.60e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957 110 EDLQKKIEENERLHIQFFEADEQHKHVEaELRSRLATLETEAAQHQAVVDGLTrkymETIEKLQNDKAKLEVKSQTLEKE 189
Cdd:PRK02224  485 EDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKR----ERAEELRERAAELEAEAEEKREA 559
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462569957 190 AKECRLRTEECQLQLKTLHEDLS---------GRLEESLSIINE 224
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAelkerieslERIRTLLAAIAD 603
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
5-143 4.60e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   5 ELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMK----------DQSLRKLQQEMDSLTFRNLQLA---- 70
Cdd:pfam05667 346 DLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKkktldllpdaEENIAKLQALVDASAQRLVELAgqwe 425
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462569957  71 -KRVELLQDELALSEprgKKNKKSGESSSQLSQEQKsvFDEDLQKKIEENERlhiqffeADEQHKHVEAELRSR 143
Cdd:pfam05667 426 kHRVPLIEEYRALKE---AKSNKEDESQRKLEEIKE--LREKIKEVAEEAKQ-------KEELYKQLVAEYERL 487
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
20-199 5.16e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   20 LRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMD--SLTFRNLQLAKR---VELLQDELALSEPRGKKNKKSG 94
Cdd:pfam12128  602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfaRTALKNARLDLRrlfDEKQSEKDKKNKALAERKDSAN 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   95 ESSSQLSQEQKsVFDEDLQKKIEENERlhiQFFEA----DEQHKHVEAELRSRLATLETEAA----QHQAVVDGLTRKYM 166
Cdd:pfam12128  682 ERLNSLEAQLK-QLDKKHQAWLEEQKE---QKREArtekQAYWQVVEGALDAQLALLKAAIAarrsGAKAELKALETWYK 757
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462569957  167 ETIEKLQNDK---AKLEVKSQTLEKEAKECRLRTEE 199
Cdd:pfam12128  758 RDLASLGVDPdviAKLKREIRTLERKIERIAVRRQE 793
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
9-188 7.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   9 KYQKLAQEYSKLRAQNQVLKKGVVDEQA---NSAALKEQLKMKDQSLRKLQQEMDSLTFRNL-QLAKRVELLQ------- 77
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEpfyneyl 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957  78 ------DELALSEPRGKKNKKSGESSSQLSQEQKSVFdEDLQKKIEENERLHiqffeADEQHKHVE---AELRSRLATLE 148
Cdd:PRK03918  606 elkdaeKELEREEKELKKLEEELDKAFEELAETEKRL-EELRKELEELEKKY-----SEEEYEELReeyLELSRELAGLR 679
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462569957 149 TEAAQHQAVVDGLtrkyMETIEKLQNDKAKLEVKSQTLEK 188
Cdd:PRK03918  680 AELEELEKRREEI----KKTLEKLKEELEEREKAKKELEK 715
PTZ00121 PTZ00121
MAEBL; Provisional
12-217 8.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   12 KLAQEYSKLRAQNQVLKKGVVDEQANSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVE---------LLQDELAL 82
Cdd:PTZ00121  1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEearieevmkLYEEEKKM 1607
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462569957   83 SEPRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEQHKHVEAELRSRLATLETEAAQHQAVVDGLT 162
Cdd:PTZ00121  1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462569957  163 RKYMETIEKLQNDKAKLE-VKSQTLEKEAKECRLRTEECQLQLKTlhEDLSGRLEE 217
Cdd:PTZ00121  1688 KKAAEALKKEAEEAKKAEeLKKKEAEEKKKAEELKKAEEENKIKA--EEAKKEAEE 1741
 
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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