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Conserved domains on  [gi|767980551|ref|XP_011535065|]
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pleckstrin homology domain-containing family D member 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-208 2.28e-09

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: 58.41  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  23 QELRMEQEQikRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLH 102
Cdd:COG1196  216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE------AQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551 103 SNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRL 182
Cdd:COG1196  288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                        170       180
                 ....*....|....*....|....*.
gi 767980551 183 REAEGALRSLEQGLNSKVRNKEKEER 208
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALR 393
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-208 2.28e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  23 QELRMEQEQikRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLH 102
Cdd:COG1196  216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE------AQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551 103 SNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRL 182
Cdd:COG1196  288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                        170       180
                 ....*....|....*....|....*.
gi 767980551 183 REAEGALRSLEQGLNSKVRNKEKEER 208
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALR 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-208 2.69e-08

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: 55.45  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENE 82
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    83 NHLQTLanqseqpppsgglHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREfyssqsqALQNSLQELTAEKQ 162
Cdd:TIGR02168  810 AELTLL-------------NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-------SLAAEIEELEELIE 869

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 767980551   163 QAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEER 208
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
 5-163 3.76e-05

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 45.04  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    5 ERLNQVLEAEKQQFEEVVQELRMEQEQIKReleLTARCLKGVEQEKKELRHL----TESLQQtlEELSIEKKK--TLEML 78
Cdd:pfam15967 243 ENLPPVICQDVENFQKFVKEQKQVQEEISR---MSSKAMLKVQDDIKALKQLlsvaASGLQR--NSLAIDKLKieTAQEL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   79 EENENHLQTLAN----QSEQPPPSGGLHSNLRQIEEKMQQLLEEkllaekrmkeneersraLEEEREFYSSQSQALQNSL 154
Cdd:pfam15967 318 KNADIALRTQKTppglQHENTAPADYFRSLVEQFEVQLQQYRQQ-----------------IEELENHLTTQSSSSHITP 380


                  ....*....
gi 767980551  155 QELTAEKQQ 163
Cdd:pfam15967 381 QDLSLAMQK 389
PTZ00121 PTZ00121
MAEBL; Provisional
 5-232 3.87e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    5 ERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENH 84
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   85 LQTLANQSEQPPPSGGLHSNLRQIEEkmqqllEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQElTAEKQQA 164
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEE------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-EEDKKKA 1677

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767980551  165 ERELKAEVKVRMDLERRLREAEGAlRSLEQGLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAK 232
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-208 2.28e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  23 QELRMEQEQikRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLH 102
Cdd:COG1196  216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE------AQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551 103 SNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRL 182
Cdd:COG1196  288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                        170       180
                 ....*....|....*....|....*.
gi 767980551 183 REAEGALRSLEQGLNSKVRNKEKEER 208
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-232 4.46e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENE 82
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  83 NHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQ 162
Cdd:COG1196  316 ERLEELEEELAE------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551 163 QAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAK 232
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-212 1.41e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   4 LERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENEN 83
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  84 HLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREfyssqsqALQNSLQELTAEKQQ 163
Cdd:COG1196  387 ELLEALRAAAE------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE-------EEEEALEEAAEEEAE 453

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767980551 164 AERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRAD 212
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-208 2.69e-08

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: 55.45  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENE 82
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    83 NHLQTLanqseqpppsgglHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREfyssqsqALQNSLQELTAEKQ 162
Cdd:TIGR02168  810 AELTLL-------------NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-------SLAAEIEELEELIE 869

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 767980551   163 QAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEER 208
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-235 9.76e-08

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: 53.52  E-value: 9.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENE 82
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    83 NHLQTLANQSEQPPPS----------------------GGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEER 140
Cdd:TIGR02168  775 EELAEAEAEIEELEAQieqlkeelkalrealdelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   141 EFYSSQSQALQNS-------LQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGL----NSKVRNKEKEERM 209
Cdd:TIGR02168  855 ESLAAEIEELEELieeleseLEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelrEKLAQLELRLEGL 934

                          250       260
                   ....*....|....*....|....*..
gi 767980551   210 RADVSHLK-RFFEECIRNAELEAKMPV 235
Cdd:TIGR02168  935 EVRIDNLQeRLSEEYSLTLEEAEALEN 961
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 3-219 2.81e-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: 51.69  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   3 ELERLNQVLEAEKQQFEEVVQELrmeqEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEEne 82
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQL----AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE-- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  83 nHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLA-EKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEK 161
Cdd:COG4942  109 -LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980551 162 QQAERELKAEVKVRMDLERRLREAEGALRSL---EQGLNSKVRNKEKEERMRADVSHLKRF 219
Cdd:COG4942  188 AALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPAAGF 248
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-222 3.66e-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: 51.60  E-value: 3.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENE 82
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    83 NHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQ 162
Cdd:TIGR02168  365 AELEELESRLEE------LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980551   163 QA-----ERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKvrnKEKEERMRADVSHLKRFFEE 222
Cdd:TIGR02168  439 QAeleelEEELEELQEELERLEEALEELREELEEAEQALDAA---ERELAQLQARLDSLERLQEN 500
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3-195 6.02e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 6.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    3 ELERLNQVLEAEKQQFE--EVVQELRMEQEQIKRELELTARCLKGV-----EQEKKELRHLTESLQQTLEELSIEKKKTL 75
Cdd:COG4913   236 DLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   76 EMLEENENHLQTLANQSEQpppSGGlhSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALE----EEREFYSSQSQALQ 151
Cdd:COG4913   316 ARLDALREELDELEAQIRG---NGG--DRLEQLEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAA 390

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767980551  152 NSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQG 195
Cdd:COG4913   391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-218 8.37e-06

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: 47.36  E-value: 8.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     2 FELERLNQVLEAEKQQFEEVvQELRMEQEQIkrELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEEN 81
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERY-KELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    82 ENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKL-LAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAE 160
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980551   161 KQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKE----ERMRADVSHLKR 218
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneiERLEARLERLED 414
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 9-236 1.63e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     9 QVLEAEKQQFE-----EVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSiekKKTLEMLEENEN 83
Cdd:TIGR02169  214 QALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN---KKIKDLGEEEQL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    84 HLQTlanqseqpppsgglhsNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQ 163
Cdd:TIGR02169  291 RVKE----------------KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767980551   164 AERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVR-----NKEKEERMRADVSHLKRFFEECIRNAELEAKMPVI 236
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleklKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
 5-163 3.76e-05

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 45.04  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    5 ERLNQVLEAEKQQFEEVVQELRMEQEQIKReleLTARCLKGVEQEKKELRHL----TESLQQtlEELSIEKKK--TLEML 78
Cdd:pfam15967 243 ENLPPVICQDVENFQKFVKEQKQVQEEISR---MSSKAMLKVQDDIKALKQLlsvaASGLQR--NSLAIDKLKieTAQEL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   79 EENENHLQTLAN----QSEQPPPSGGLHSNLRQIEEKMQQLLEEkllaekrmkeneersraLEEEREFYSSQSQALQNSL 154
Cdd:pfam15967 318 KNADIALRTQKTppglQHENTAPADYFRSLVEQFEVQLQQYRQQ-----------------IEELENHLTTQSSSSHITP 380


                  ....*....
gi 767980551  155 QELTAEKQQ 163
Cdd:pfam15967 381 QDLSLAMQK 389
PTZ00121 PTZ00121
MAEBL; Provisional
 5-232 3.87e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    5 ERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENH 84
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   85 LQTLANQSEQPPPSGGLHSNLRQIEEkmqqllEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQElTAEKQQA 164
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEE------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-EEDKKKA 1677

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767980551  165 ERELKAEVKVRMDLERRLREAEGAlRSLEQGLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAK 232
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-222 4.30e-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: 45.43  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    21 VVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsgg 100
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ------ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   101 LHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTA---EKQQAERELKAEV-KVRM 176
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAaNLRE 824

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 767980551   177 DLERRLREAEGALRSLEQGLNSKVRNKEKEERMRADVSHLKRFFEE 222
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-218 5.54e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENE 82
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    83 NHLQTLANQseqpppsgglhsnLRQIEEKMQQLleEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQ 162
Cdd:TIGR02169  765 ARIEELEED-------------LHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   163 QAERELKAEVKVRMDLERRLREAEGALRSLE---QGLNSKVRNKEKEER-MRADVSHLKR 218
Cdd:TIGR02169  830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRdLESRLGDLKK 889
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3-201 1.11e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKelrhlTESLQQTLEELSIEkkktLEMLEENE 82
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAE----LERLDASS 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   83 NHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALqnsLQELTAEKQ 162
Cdd:COG4913   685 DDLAALEEQLEE------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---LRALLEERF 755

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767980551  163 QAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVR 201
Cdd:COG4913   756 AAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-224 1.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  34 RELELTARCLKGVEQEKKELRHLTESLQQTLEELSiEKKKTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQ 113
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551 114 QLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKvrmDLERRLREAEGALRSLE 193
Cdd:COG4717  143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE---ELQQRLAELEEELEEAQ 219

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767980551 194 QGLNSKVRNKEKEERMRADVSHLKRFFEECI 224
Cdd:COG4717  220 EELEELEEELEQLENELEAAALEERLKEARL 250
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 5-148 2.16e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   5 ERLNQVLEAEKQQFEEVV---QELRMEQEQIKRELEltaRCLKGVEQEKKELRHLTESLQQTLEELSIE-----KKKTLE 76
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIaslEELERELEQKAEEAE---ALLKEAEKLKEELEEKKEKLQEEEDKLLEEaekeaQQAIKE 581

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980551  77 MLEENENHLQTLANQSEQPPPSGGLHsnlrQIEEKMQQLLEEKLLAEKRMKENEERSRALEE-EREFYSSQSQ 148
Cdd:PRK00409 582 AKKEADEIIKELRQLQKGGYASVKAH----ELIEARKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQ 650
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
3-192 3.00e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   3 ELERLNQVLEAEKQQfEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTE--SLQQTLEELSIEKKKTLEMLEE 80
Cdd:COG4717   72 ELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  81 NENHLQTLANQSEQPPpsgGLHSNLRQIEEKMQQLLEEKLLA-EKRMKENEERSRALEEEREFYSSQSQALQNSLQELTA 159
Cdd:COG4717  151 LEERLEELRELEEELE---ELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767980551 160 EKQQAERELKAEvkvrmDLERRLREAEGALRSL 192
Cdd:COG4717  228 ELEQLENELEAA-----ALEERLKEARLLLLIA 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 13-234 7.39e-04

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: 40.90  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  13 AEKQQFEEVVQELRMEQEQIKRELELtarcLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQS 92
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKE----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  93 EQpppsggLHSNLRQIEEKMQQLL------------------EEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSL 154
Cdd:COG4942   93 AE------LRAELEAQKEELAELLralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551 155 QELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKvrnKEKEERMRADVSHLKRFFEECIRNAELEAKMP 234
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL---AAELAELQQEAEELEALIARLEAEAAAAAERT 243
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
9-206 1.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    9 QVLEAEKQQFEEVVQELRMEQEQIKRELELTArclkgveqekkELRHLTESLQQTLEELsIEKKKTLEMLEENENHLQTL 88
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQ-----------ERREALQRLAEYSWDE-IDVASAEREIAELEAELERL 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   89 ANQSeqpppsgglhSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAEREL 168
Cdd:COG4913   681 DASS----------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767980551  169 KAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKE 206
Cdd:COG4913   751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
46 PHA02562
endonuclease subunit; Provisional
 1-216 3.70e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   1 MFELERLNQVLEAEKQqfeEVVQELRMEQEQIKREL-ELTARCLKGVEQEKKELRHLTEsLQQTLEELSIEKK---KTLE 76
Cdd:PHA02562 204 IEEQRKKNGENIARKQ---NKYDELVEEAKTIKAEIeELTDELLNLVMDIEDPSAALNK-LNTAAAKIKSKIEqfqKVIK 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  77 MLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQE 156
Cdd:PHA02562 280 MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980551 157 ltAEKQQAE-RELKAEVKVRmdlerrlREAEGALRSLEQGLNSKVRNKEKEERMRADVSHL 216
Cdd:PHA02562 360 --AKKVKAAiEELQAEFVDN-------AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDL 411
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-167 3.70e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551     3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEEL---------SIEKKK 73
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELerkieeleaQIEKKR 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    74 --------TLEMLEENENHLQTLANQSEQPPPS----GGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEERE 141
Cdd:TIGR02169  917 krlselkaKLEALEEELSEIEDPKGEDEEIPEEelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996

                          170       180
                   ....*....|....*....|....*.
gi 767980551   142 FYSSQSQALQNSLQELTAEKQQAERE 167
Cdd:TIGR02169  997 KLEEERKAILERIEEYEKKKREVFME 1022
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-171 3.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   9 QVLEAEkQQFEEVVQELRMEQEQIKRELELTARclkgveQEKKELRHLTEslqqtlEELSIEKKKtlemLEENENHLQtl 88
Cdd:PRK12704  32 KIKEAE-EEAKRILEEAKKEAEAIKKEALLEAK------EEIHKLRNEFE------KELRERRNE----LQKLEKRLL-- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  89 anQSEQpppsgglhsnlrQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQE---LTAEK---- 161
Cdd:PRK12704  93 --QKEE------------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgLTAEEakei 158

                        170
                 ....*....|..
gi 767980551 162 --QQAERELKAE 171
Cdd:PRK12704 159 llEKVEEEARHE 170
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
3-194 4.70e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   3 ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTArclkgVEQEKKELRHLTESLQQTLEELSIEkkktLEMLEENE 82
Cdd:COG3206  172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAE----LAEAEARL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  83 NHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEERE---------------FYSSQS 147
Cdd:COG3206  243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAalraqlqqeaqrilaSLEAEL 322

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767980551 148 QALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQ 194
Cdd:COG3206  323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-173 4.81e-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: 38.47  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    1 MFELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEElsieKKKTLEML-- 78
Cdd:pfam05667 323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKV----KKKTLDLLpd 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   79 -EENENHLQTLANQSEQpppsgglhsNLRQIEEKMQQ----LLEE-KLLAEKRMKENEERSRALEEEREFYSSQSQAlqn 152
Cdd:pfam05667 399 aEENIAKLQALVDASAQ---------RLVELAGQWEKhrvpLIEEyRALKEAKSNKEDESQRKLEEIKELREKIKEV--- 466

                         170       180
                  ....*....|....*....|.
gi 767980551  153 slQELTAEKQQAERELKAEVK 173
Cdd:pfam05667 467 --AEEAKQKEELYKQLVAEYE 485
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 93-173 4.84e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.78  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   93 EQPPPSGGLHSNLRQIEEKMQQLLE---EKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELK 169
Cdd:PRK11448  136 PPEDPENLLHALQQEVLTLKQQLELqarEKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215


                  ....
gi 767980551  170 AEVK 173
Cdd:PRK11448  216 QKRK 219
PTZ00121 PTZ00121
MAEBL; Provisional
 4-212 6.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    4 LERLNQVLEAEKQQFEEVV----QELRMEQEQIKRELE--LTARCLKGVEQEKKELRHL----------TESLQQTLEEL 67
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMklyeEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQLkkkeaeekkkAEELKKAEEEN 1659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   68 SIEKKKTLEMLEENENHLQTLANQSEQPppsgglhsnlRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQS 147
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDE----------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767980551  148 QALQNSLQELTAEKQQAERELKAE---VKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRAD 212
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEeekKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
16-194 6.90e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  16 QQFEEVVQELRMEQEQIKRELELTARcLKGVEQEKKELRHLTESLQQTLEELSIEKK--KTLEMLEENENHLQTLANQSE 93
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  94 QpppsggLHSNLRQIEEKMQQLLEeklLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVK 173
Cdd:COG4717  150 E------LEERLEELRELEEELEE---LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                        170       180
                 ....*....|....*....|.
gi 767980551 174 VRMDLERRLREAEGALRSLEQ 194
Cdd:COG4717  221 ELEELEEELEQLENELEAAAL 241
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 16-212 7.21e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.23  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    16 QQFEEVVQELRMEQEQIKRELELTArclkgveqEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQP 95
Cdd:pfam01576   33 KKHQQLCEEKNALQEQLQAETELCA--------EAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQH 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    96 ppSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVR 175
Cdd:pfam01576  105 --IQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLK 182

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 767980551   176 MDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRAD 212
Cdd:pfam01576  183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD 219
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-175 9.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 9.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   2 FELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEEN 81
Cdd:COG1196  666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551  82 ENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEkrmkenEErSRALEEEREFYSSQSQALQNSLQELtaek 161
Cdd:COG1196  746 ELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAI------EE-YEELEERYDFLSEQREDLEEARETL---- 814

                        170
                 ....*....|....
gi 767980551 162 QQAERELKAEVKVR 175
Cdd:COG1196  815 EEAIEEIDRETRER 828
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 8-209 9.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 37.69  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551    8 NQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQT 87
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980551   88 LANQSEQPPPS-GGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAER 166
Cdd:TIGR04523 375 LKKENQSYKQEiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767980551  167 ELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERM 209
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
 
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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