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Conserved domains on  [gi|385198095|ref|NP_001245228|]
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shootin-1 isoform d [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 ...
 140-350 2.31e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   140 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 219
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   220 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 299
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198095   300 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
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 ...
 140-350 2.31e-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: 56.99  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   140 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 219
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   220 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 299
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198095   300 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 141-350 7.11e-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: 7.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 141 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 220
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 221 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENE--T 298
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198095 299 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 225-344 8.03e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 225 KDLRKKAESFAQEMFIEQNKLKRQshlllqssipdqQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN--ETLHKE 302
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 385198095 303 IHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 344
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 ...
 216-349 2.53e-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: 40.93  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   216 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQ-----------QLLKALDENAKL-TQQLEEERIQH 283
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRShEAQLQEMRQKH 354

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385198095   284 QQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 349
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 ...
 140-350 2.31e-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: 56.99  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   140 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 219
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   220 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 299
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198095   300 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 140-349 2.40e-07

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: 53.92  E-value: 2.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   140 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKC-----NRVSMLAVEEY 214
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRI 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   215 EEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQ-----------LEEERIQH 283
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKeienlngkkeeLEEELEEL 873

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198095   284 QQKVKELEEQLENetLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 349
Cdd:TIGR02169  874 EAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 141-350 7.11e-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: 7.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 141 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 220
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 221 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENE--T 298
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198095 299 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-352 2.54e-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: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 141 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKcnrvsmLAVEEYEEMQVN 220
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE------LEEELEELEEEL 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 221 LELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQL-ENETL 299
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeELEEL 426

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 385198095 300 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSV 352
Cdd:COG1196  427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-350 2.61e-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: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 141 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLE-KCNRVSMLAVEEYEEMQV 219
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 220 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENET- 298
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEe 404

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198095 299 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG1196  405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 130-349 4.28e-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: 49.67  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   130 GAAETCVSVQCQKQ-IKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRvsm 208
Cdd:TIGR02168  664 GSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--- 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   209 lAVEEYEEMQVNLELE-KDLRKKAESFAQEMFIEQNKLKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQ--- 284
Cdd:TIGR02168  741 -EVEQLEERIAQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEEL---EAQIEQLKEELKALREALDELRAELTlln 816

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   285 ---QKVKELEEQLENET--LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 349
Cdd:TIGR02168  817 eeaANLRERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-325 5.23e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   4 SDEEKQLQLitslkEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKishmvieevnfmqnhlEIEKTcRESA 83
Cdd:COG1196  219 KEELKELEA-----ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA----------------ELEEL-RLEL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095  84 EALATKLNKENKTLKRISMlymaklgpDVITEEINIDDEDSTTDTDGAAEtcvsVQCQKQIKELRDQIVSVQEEKKILAI 163
Cdd:COG1196  277 EELELELEEAQAEEYELLA--------ELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEELEELEE 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 164 ELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRvsmLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQN 243
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 244 KLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKK 318
Cdd:COG1196  422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALleaalAELLEELAEAAARLLLLLEAEA 501


                 ....*..
gi 385198095 319 ELELKYQ 325
Cdd:COG1196  502 DYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-416 5.32e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 141 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 220
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 221 LELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN---- 296
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEE---LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeee 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 297 -ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMS 375
Cdd:COG1196  381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 385198095 376 MIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDR 416
Cdd:COG1196  461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
PRK12704 PRK12704
phosphodiesterase; Provisional
 225-344 8.03e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 225 KDLRKKAESFAQEMFIEQNKLKRQshlllqssipdqQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN--ETLHKE 302
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 385198095 303 IHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 344
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-350 2.25e-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: 47.36  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095    74 EIEK--TCRESAEALATKLNKENKTLkRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQI 151
Cdd:TIGR02168  678 EIEEleEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   152 VSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlaveeyeemqvnlELEKDLRKKA 231
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--------------------ELRAELTLLN 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   232 ESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEEriqhQQKVKELEEQLENETlhKEIHNLKQQLE 311
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALL--NERASLEEALA 890

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 385198095   312 LLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 139-349 1.22e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 139 QCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCN-RVSMLAVEEYEEM 217
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReELGERARALYRSG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 218 QVNLELEKDLrkKAESFAQemFIEQnklkrqshLLLQSSIPDQQlLKALDENAKLTQQLEEERIQHQQKVKELEEQLenE 297
Cdd:COG3883  100 GSVSYLDVLL--GSESFSD--FLDR--------LSALSKIADAD-ADLLEELKADKAELEAKKAELEAKLAELEALK--A 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198095 298 TLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 349
Cdd:COG3883  165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-340 2.88e-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: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095  192 EVLEQRKVLEKCNRvsmlAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEqnklkrqshlLLQSSIpdQQLLKALDENAK 271
Cdd:COG4913   246 DAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFAQRRLE----------LLEAEL--EELRAELARLEA 309

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385198095  272 LTQQLEEERIQHQQKVKELEEQLENETLhKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDE 340
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGG-DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
211-409 2.91e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 211 VEEYeeMQVNLELEKDLRKKAESFAQEMFIE--------QNKLK--RQSHLLLQSSIPDQQLLKALDENAKLTQQLEEER 280
Cdd:COG3206  158 AEAY--LEQNLELRREEARKALEFLEEQLPElrkeleeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 281 IQHQQKVKELEEQLENETL-------HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVP 353
Cdd:COG3206  236 AEAEARLAALRAQLGSGPDalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385198095 354 PPPPPPPPLPPPPPNPIRSLMSMIRKRShpsgsgakkekATQPETTEEVTDLKRQA 409
Cdd:COG3206  316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREV 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-413 4.66e-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: 43.12  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   142 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLE-QRKVLEKCNRVSmlaveeyeemqvn 220
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEIS------------- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   221 lELEKDLRKKAESFAQemfIEQNKLKRQSHLllqssipdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENetLH 300
Cdd:TIGR02168  299 -RLEQQKQILRERLAN---LERQLEELEAQL--------EELESKLDELAEELAELEEKLEELKEELESLEAELEE--LE 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   301 KEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKR 380
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444

                          250       260       270
                   ....*....|....*....|....*....|...
gi 385198095   381 SHPSGSGAKKEKATQPETTEEVTDLKRQAVEEM 413
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQAL 477
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-349 4.82e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095  191 SEVLEQRKVLEKCNRVSMLaVEEYEEMQVNLELEKD-------LRKKAESFaQEMFIEQNKLKRQSHLL--LQSSIPDQQ 261
Cdd:COG4913   215 EYMLEEPDTFEAADALVEH-FDDLERAHEALEDAREqiellepIRELAERY-AAARERLAELEYLRAALrlWFAQRRLEL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095  262 LLKALDENAKLTQQLEEERIQHQQKVKELEEQLENetLHKEIHNLK-QQLELLEEDKKELELKYQNSEEKARNLKHSVDE 340
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDE--LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA 370


                  ....*....
gi 385198095  341 LQKRVNQSE 349
Cdd:COG4913   371 LGLPLPASA 379
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
210-323 9.59e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.57  E-value: 9.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 210 AVEEYEEMQVNLELEKDLRKKAESFAQ---EMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQK 286
Cdd:COG1566   95 AEAQLARLEAELGAEAEIAAAEAQLAAaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQA 174

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 385198095 287 VKELEEQLENETLHKEIHNLKQQLELLEEDKKELELK 323
Cdd:COG1566  175 QAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-311 1.01e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 139 QCQKQIKELRDQ---IVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKtvlnsEVLEQRKVLEKCNRVSMLAVEEYE 215
Cdd:COG4717   75 ELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 216 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPD-QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQL 294
Cdd:COG4717  150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                        170
                 ....*....|....*..
gi 385198095 295 ENETLHKEIHNLKQQLE 311
Cdd:COG4717  230 EQLENELEAAALEERLK 246
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 216-349 2.53e-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: 40.93  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   216 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQ-----------QLLKALDENAKL-TQQLEEERIQH 283
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRShEAQLQEMRQKH 354

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385198095   284 QQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 349
Cdd:pfam01576  355 TQALEELTEQLEQakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-343 2.86e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 260 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVD 339
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170


                 ....
gi 385198095 340 ELQK 343
Cdd:COG4717  171 ELAE 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 23-341 4.08e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095    23 EYEDLRAENQKTKEKCDKIRQERDEAVKKLEE-------FQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENK 95
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095    96 TLKRISMLYMAKLgpdviteEINIDDEDSTTDTDGAAETCVSVQcQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEV 175
Cdd:TIGR02168  758 ELEAEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQL-KEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   176 IEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQshlLLQS 255
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE---LREL 906

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095   256 SIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENEtlhkeihnLKQQLELLEEDKKELELKYQNSEEKARNLK 335
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE--------YSLTLEEAEALENKIEDDEEEARRRLKRLE 978


                   ....*.
gi 385198095   336 HSVDEL 341
Cdd:TIGR02168  979 NKIKEL 984
PRK12704 PRK12704
phosphodiesterase; Provisional
 158-332 4.33e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 158 KKILAIELENLKSKLVEVIEEVNKvkqektvlNSEVLEQRKVLEkcnrvsmlAVEEYEEMQvnLELEKDLR-KKAESFAQ 236
Cdd:PRK12704  26 KKIAEAKIKEAEEEAKRILEEAKK--------EAEAIKKEALLE--------AKEEIHKLR--NEFEKELReRRNELQKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095 237 EMFIEQNK--LKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEnetlhkEIHNL-----KQQ 309
Cdd:PRK12704  88 EKRLLQKEenLDRKLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE------RISGLtaeeaKEI 158

                        170       180
                 ....*....|....*....|....*
gi 385198095 310 L--ELLEEDKKELELKYQNSEEKAR 332
Cdd:PRK12704 159 LleKVEEEARHEAAVLIKEIEEEAK 183
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
260-349 9.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198095  260 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEED----------KKELELKYQNSEE 329
Cdd:COG4913   627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASsddlaaleeqLEELEAELEELEE 706

                          90       100
                  ....*....|....*....|
gi 385198095  330 KARNLKHSVDELQKRVNQSE 349
Cdd:COG4913   707 ELDELKGEIGRLEKELEQAE 726
 
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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