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Conserved domains on  [gi|385198097|ref|NP_001245229|]
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shootin-1 isoform e [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-290 9.89e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 9.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 159
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 239
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198097   240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-290 9.89e-09

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: 58.14  E-value: 9.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 159
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 239
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198097   240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-290 3.81e-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: 52.07  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 160
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 161 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENE--T 238
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198097 239 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 165-284 4.56e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 165 KDLRKKAESFAQEMFIEQNKLKRQshlllqssipdqQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN--ETLHKE 242
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 385198097 243 IHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 284
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 156-289 8.10e-04

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: 42.08  E-value: 8.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   156 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQ-----------QLLKALDENAKL-TQQLEEERIQH 223
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRShEAQLQEMRQKH 354

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385198097   224 QQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:pfam01576  355 TQALEELTEQLEQakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-290 9.89e-09

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: 58.14  E-value: 9.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 159
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 239
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198097   240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 80-289 8.45e-08

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: 55.07  E-value: 8.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKC-----NRVSMLAVEEY 154
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRI 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   155 EEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQ-----------LEEERIQH 223
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKeienlngkkeeLEEELEEL 873

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198097   224 QQKVKELEEQLENetLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:TIGR02169  874 EAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-290 3.81e-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: 52.07  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 160
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 161 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENE--T 238
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198097 239 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-292 1.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKcnrvsmLAVEEYEEMQVN 160
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE------LEEELEELEEEL 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 161 LELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQL-ENETL 239
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeELEEL 426

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 385198097 240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSV 292
Cdd:COG1196  427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-290 1.40e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLE-KCNRVSMLAVEEYEEMQV 159
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENET- 238
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEe 404

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198097 239 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:COG1196  405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 70-289 1.41e-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: 51.21  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    70 GAAETCVSVQCQKQ-IKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRvsm 148
Cdd:TIGR02168  664 GSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--- 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   149 lAVEEYEEMQVNLELE-KDLRKKAESFAQEMFIEQNKLKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQ--- 224
Cdd:TIGR02168  741 -EVEQLEERIAQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEEL---EAQIEQLKEELKALREALDELRAELTlln 816

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   225 ---QKVKELEEQLENET--LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:TIGR02168  817 eeaANLRERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-356 2.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 160
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 161 LELEKDLRKKAESFAQEMfIEQNKLKRQSHLLLQSSIpdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN---- 236
Cdd:COG1196  304 IARLEERRRELEERLEEL-EEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeee 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 237 -ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMS 315
Cdd:COG1196  381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 385198097 316 MIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDR 356
Cdd:COG1196  461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-265 3.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRvsmLAVEEYEEMQVN 160
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE---ELLEALRAAAEL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 161 LELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN---- 236
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALleaa 478

                        170       180       190
                 ....*....|....*....|....*....|
gi 385198097 237 -ETLHKEIHNLKQQLELLEEDKKELELKYQ 265
Cdd:COG1196  479 lAELLEELAEAAARLLLLLEAEADYEGFLE 508
PRK12704 PRK12704
phosphodiesterase; Provisional
 165-284 4.56e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 165 KDLRKKAESFAQEMFIEQNKLKRQshlllqssipdqQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN--ETLHKE 242
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 385198097 243 IHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 284
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-290 8.73e-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: 48.51  E-value: 8.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    14 EIEK--TCRESAEALATKLNKENKTLkRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQI 91
Cdd:TIGR02168  678 EIEEleEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    92 VSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlaveeyeemqvnlELEKDLRKKA 171
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--------------------ELRAELTLLN 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   172 ESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEEriqhQQKVKELEEQLENETlhKEIHNLKQQLE 251
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALL--NERASLEEALA 890

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 385198097   252 LLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 79-291 4.58e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  79 QCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCN-RVSMLAVEEYEEM 157
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReELGERARALYRSG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 158 QVNLELEKDLrkKAESFAQemFIEQnklkrqshLLLQSSIPDQQlLKALDENAKLTQQLEEERIQHQQKVKELEEQLenE 237
Cdd:COG3883  100 GSVSYLDVLL--GSESFSD--FLDR--------LSALSKIADAD-ADLLEELKADKAELEAKKAELEAKLAELEALK--A 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 385198097 238 TLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENS 291
Cdd:COG3883  165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
132-280 1.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  132 EVLEQRKVLEKCNRvsmlAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEqnklkrqshlLLQSSIpdQQLLKALDENAK 211
Cdd:COG4913   246 DAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFAQRRLE----------LLEAEL--EELRAELARLEA 309

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385198097  212 LTQQLEEERIQHQQKVKELEEQLENETLhKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDE 280
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGG-DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
PLN02939 PLN02939
transferase, transferring glycosyl groups
 94-281 1.77e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.12  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  94 VQEEKKILAIELENLKSKLVEVI---EEVNKVKQEKTVLNSEV--LEQRKVL--EKCNRVSMLAVEEYEEMQVNLELEKD 166
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLreLESKFIVaqEDVSKLSPLQYDCWWEKVENLQDLLD 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 167 -LRKKAESFAqeMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTqqleeeriqhQQKVKELEEQLENEtlHKEIHN 245
Cdd:PLN02939 311 rATNQVEKAA--LVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELL----------QQKLKLLEERLQAS--DHEIHS 376

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 385198097 246 lkqQLELLEEDKKELE--LKYQNSEEKARNLKHSVDEL 281
Cdd:PLN02939 377 ---YIQLYQESIKEFQdtLSKLKEESKKRSLEHPADDM 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 82-353 1.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    82 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLE-QRKVLEKCNRVSmlaveeyeemqvn 160
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEIS------------- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   161 lELEKDLRKKAESFAQemfIEQNKLKRQSHLllqssipdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENetLH 240
Cdd:TIGR02168  299 -RLEQQKQILRERLAN---LERQLEELEAQL--------EELESKLDELAEELAELEEKLEELKEELESLEAELEE--LE 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   241 KEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKR 320
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444

                          250       260       270
                   ....*....|....*....|....*....|...
gi 385198097   321 SHPSGSGAKKEKATQPETTEEVTDLKRQAVEEM 353
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQAL 477
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-289 2.26e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  131 SEVLEQRKVLEKCNRVSMLaVEEYEEMQVNLELEKD-------LRKKAESFaQEMFIEQNKLKRQSHLL--LQSSIPDQQ 201
Cdd:COG4913   215 EYMLEEPDTFEAADALVEH-FDDLERAHEALEDAREqiellepIRELAERY-AAARERLAELEYLRAALrlWFAQRRLEL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  202 LLKALDENAKLTQQLEEERIQHQQKVKELEEQLENetLHKEIHNLK-QQLELLEEDKKELELKYQNSEEKARNLKHSVDE 280
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDE--LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA 370


                  ....*....
gi 385198097  281 LQKRVNQSE 289
Cdd:COG4913   371 LGLPLPASA 379
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
151-349 2.89e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 151 VEEYeeMQVNLELEKDLRKKAESFAQEMFIE--------QNKLK--RQSHLLLQSSIPDQQLLKALDENAKLTQQLEEER 220
Cdd:COG3206  158 AEAY--LEQNLELRREEARKALEFLEEQLPElrkeleeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 221 IQHQQKVKELEEQLENETL-------HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVP 293
Cdd:COG3206  236 AEAEARLAALRAQLGSGPDalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385198097 294 PPPPPPPPLPPPPPNPIRSLMSMIRKRShpsgsgakkekATQPETTEEVTDLKRQA 349
Cdd:COG3206  316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREV 360
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
79-251 3.42e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  79 QCQKQIKELRDQ---IVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKtvlnsEVLEQRKVLEKCNRVSMLAVEEYE 155
Cdd:COG4717   75 ELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 156 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPD-QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQL 234
Cdd:COG4717  150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                        170
                 ....*....|....*..
gi 385198097 235 ENETLHKEIHNLKQQLE 251
Cdd:COG4717  230 EQLENELEAAALEERLK 246
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
150-263 7.39e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.57  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 150 AVEEYEEMQVNLELEKDLRKKAESFAQ---EMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQK 226
Cdd:COG1566   95 AEAQLARLEAELGAEAEIAAAEAQLAAaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQA 174

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 385198097 227 VKELEEQLENETLHKEIHNLKQQLELLEEDKKELELK 263
Cdd:COG1566  175 QAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 156-289 8.10e-04

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: 42.08  E-value: 8.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   156 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQ-----------QLLKALDENAKL-TQQLEEERIQH 223
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRShEAQLQEMRQKH 354

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385198097   224 QQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:pfam01576  355 TQALEELTEQLEQakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
200-283 1.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 200 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVD 279
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170


                 ....
gi 385198097 280 ELQK 283
Cdd:COG4717  171 ELAE 174
PRK12704 PRK12704
phosphodiesterase; Provisional
 98-272 1.90e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  98 KKILAIELENLKSKLVEVIEEVNKvkqektvlNSEVLEQRKVLEkcnrvsmlAVEEYEEMQvnLELEKDLR-KKAESFAQ 176
Cdd:PRK12704  26 KKIAEAKIKEAEEEAKRILEEAKK--------EAEAIKKEALLE--------AKEEIHKLR--NEFEKELReRRNELQKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 177 EMFIEQNK--LKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEnetlhkEIHNL-----KQQ 249
Cdd:PRK12704  88 EKRLLQKEenLDRKLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE------RISGLtaeeaKEI 158

                        170       180
                 ....*....|....*....|....*
gi 385198097 250 L--ELLEEDKKELELKYQNSEEKAR 272
Cdd:PRK12704 159 LleKVEEEARHEAAVLIKEIEEEAK 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 82-235 4.96e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  82 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKcNRVSMLAV---EEYEEMQ 158
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVrnnKEYEALQ 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385198097 159 VNLELEKDLRKKAESFAQEMFIEQNKLKrqshlllqssipdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLE 235
Cdd:COG1579   96 KEIESLKRRISDLEDEILELMERIEELE-------------EELAELEAELAELEAELEEKKAELDEELAELEAELE 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
200-289 5.49e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  200 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEED----------KKELELKYQNSEE 269
Cdd:COG4913   627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASsddlaaleeqLEELEAELEELEE 706

                          90       100
                  ....*....|....*....|
gi 385198097  270 KARNLKHSVDELQKRVNQSE 289
Cdd:COG4913   707 ELDELKGEIGRLEKELEQAE 726
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-249 5.54e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVK-QEKTVLNSEVLEQRKVLEKCNRvsmlAVEEYEEMQV 159
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER----RRARLEALLA 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  160 NLELEKDLrkKAESFAqemfieqnKLKRQShlllqssipdQQLLKALDEnakLTQQLEEERIQHQQKVKELEEQLenETL 239
Cdd:COG4913   370 ALGLPLPA--SAEEFA--------ALRAEA----------AALLEALEE---ELEALEEALAEAEAALRDLRREL--REL 424

                         170
                  ....*....|
gi 385198097  240 HKEIHNLKQQ 249
Cdd:COG4913   425 EAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-349 8.98e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 8.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 152 EEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHL----LLQSSIpDQQLLKALDENAKLTQQLEEERiQHQQKV 227
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEaelaELEAEL-EELRLELEELELELEEAQAEEY-ELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097 228 KELEEQLENETlhKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPP 307
Cdd:COG1196  298 ARLEQDIARLE--ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 385198097 308 NPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQA 349
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-362 9.16e-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: 38.90  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097    82 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEvlEQRKVLEKCNRVSMlaveEYEEMQVNL 161
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEA----EIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   162 ELEKDLRKKAESFAQEMFIEQNKLKRQsHLLLQSSIPDQQLLKAL---------DENAKLTQQLEEERIQHQ---QKVKE 229
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAE-IEELEREIEEERKRRDKlteeyaelkEELEDLRAELEEVDKEFAetrDELKD 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   230 LEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVpPPPPPPPPLPP 304
Cdd:TIGR02169  390 YREKLEKlkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-EQLAADLSKYE 468

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 385198097   305 PPPNPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDlkRQAVEEMMDRIKKGVH 362
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG--GRAVEEVLKASIQGVH 524
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-292 9.26e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097   81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLvevieevnkvkqektvlnsEVLEQRKVLEKcnrvsmlAVEEYEEMQVN 160
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAEL-------------------DALQERREALQ-------RLAEYSWDEID 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198097  161 L-ELEKDLRKKaesfaqemfieQNKLKRqshllLQSSIPD-QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENet 238
Cdd:COG4913   663 VaSAEREIAEL-----------EAELER-----LDASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-- 724

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385198097  239 LHKEIHNLKQQLELLEEDKKEL-----------ELKYQNSEEKARNLKHSVDELQKRVNQSENSV 292
Cdd:COG4913   725 AEEELDELQDRLEAAEDLARLElralleerfaaALGDAVERELRENLEERIDALRARLNRAEEEL 789
 
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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