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Conserved domains on  [gi|156637367|sp|A0MZ67|]
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RecName: Full=Shootin-1; AltName: Full=Shootin1

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

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 3.27e-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: 60.07  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   140 CQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQV 219
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   220 NLELEKDLRKKAEsfaQEMFIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQ-HQQKVKELEERLENEA 298
Cdd:TIGR02168  380 QLETLRSKVAQLE---LQIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQ 453

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 156637367   299 LHKEihNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  454 EELE--RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
PRK05771 super family cl35381
V-type ATP synthase subunit I; Validated
 13-236 8.01e-03

V-type ATP synthase subunit I; Validated


The actual alignment was detected with superfamily member PRK05771:

Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  13 ITSLKEQAIGEY-EDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQN--HLEIEKTCRESAEALATK 89
Cdd:PRK05771  33 IEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEeeLEKIEKEIKELEEEISEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  90 LNKENKTLKRISML-YMAKLGPDVI----TEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQ----IVSVQEEKKV 160
Cdd:PRK05771 113 ENEIKELEQEIERLePWGNFDLDLSlllgFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvVVVLKELSDE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 161 LAIELESLK------SKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsvLAVEEYEELQVNLELEKDLRKKAESF 234
Cdd:PRK05771 193 VEEELKKLGferlelEEEGTPSELIREIKEELEEIEKERESLLEELKE------LAKKYLEELLALYEYLEIELERAEAL 266


                 ..
gi 156637367 235 AQ 236
Cdd:PRK05771 267 SK 268
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-350 3.27e-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: 60.07  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   140 CQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQV 219
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   220 NLELEKDLRKKAEsfaQEMFIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQ-HQQKVKELEERLENEA 298
Cdd:TIGR02168  380 QLETLRSKVAQLE---LQIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQ 453

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 156637367   299 LHKEihNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  454 EELE--RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 141-350 1.95e-08

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: 56.70  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 141 QKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVN 220
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 221 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENE--A 298
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156637367 299 LHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 225-344 2.23e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 225 KDLRKKAESFAQEMFIEQNKLKRQshlllqsslpdqQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEN--EALHKE 302
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 156637367 303 IHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKR 344
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 39-321 3.87e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   39 DKIRQERDEAVKKLEEFQKIShmviEEVNFMQNHLEIEKTCRESAEALATKLNKEnktLKRISMLYMAKLGPDVITEEIN 118
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLE----EAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKRELERIRQEEIA 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  119 IDDDDPGTDTDAAAEtcvsvqcQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRK 198
Cdd:pfam17380 372 MEISRMRELERLQME-------RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  199 V----------LEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDE 268
Cdd:pfam17380 445 AremervrleeQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156637367  269 NAKLI----------------QQLEEERIQHQQKVKELEERLENEALHKEIHNLRQQLElLEDDKRELE 321
Cdd:pfam17380 525 RQKAIyeeerrreaeeerrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVE-SEKARAEYE 592
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 13-236 8.01e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  13 ITSLKEQAIGEY-EDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQN--HLEIEKTCRESAEALATK 89
Cdd:PRK05771  33 IEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEeeLEKIEKEIKELEEEISEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  90 LNKENKTLKRISML-YMAKLGPDVI----TEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQ----IVSVQEEKKV 160
Cdd:PRK05771 113 ENEIKELEQEIERLePWGNFDLDLSlllgFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvVVVLKELSDE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 161 LAIELESLK------SKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsvLAVEEYEELQVNLELEKDLRKKAESF 234
Cdd:PRK05771 193 VEEELKKLGferlelEEEGTPSELIREIKEELEEIEKERESLLEELKE------LAKKYLEELLALYEYLEIELERAEAL 266


                 ..
gi 156637367 235 AQ 236
Cdd:PRK05771 267 SK 268
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-350 3.27e-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: 60.07  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   140 CQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQV 219
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   220 NLELEKDLRKKAEsfaQEMFIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQ-HQQKVKELEERLENEA 298
Cdd:TIGR02168  380 QLETLRSKVAQLE---LQIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQ 453

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 156637367   299 LHKEihNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  454 EELE--RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 141-350 1.95e-08

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: 56.70  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 141 QKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVN 220
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 221 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENE--A 298
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156637367 299 LHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 140-349 2.52e-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: 57.39  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   140 CQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKC-----NRVSVLAVEEY 214
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRI 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   215 EELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQ-----------LEEERIQH 283
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKeienlngkkeeLEEELEEL 873

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156637367   284 QQKVKELEERLENeaLHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:TIGR02169  874 EAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-412 1.27e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 141 QKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVN 220
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 221 LELEKDLRKKAESFAQEMfIEQNKLKRQSHLLLQSSLpdQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEN---- 296
Cdd:COG1196  304 IARLEERRRELEERLEEL-EEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeee 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 297 -EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMS 375
Cdd:COG1196  381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 156637367 376 MIRKRshpsggstKKEKATQPETAEEVTDLKRQAVEE 412
Cdd:COG1196  461 LLELL--------AELLEEAALLEAALAELLEELAEA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-335 2.40e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   6 EEKQLQLITSLKEQAIGEYEDLRAENQKTKETCDKIRQERDEAVKKLEEFQkishmvieevnfmQNHLEIEktcresaEA 85
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-------------LELEELE-------LE 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  86 LATKLNKENKTLKRISMLymaklgpdviTEEINIDDDDPGTDTDAAAETcvsvqcQKQIKELRDQIVSVQEEKKVLAIEL 165
Cdd:COG1196  283 LEEAQAEEYELLAELARL----------EQDIARLEERRRELEERLEEL------EEELAELEEELEELEEELEELEEEL 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 166 ESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRvsvLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKL 245
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 246 KRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEA-----LHKEIHNLRQQLELLEDDKREL 320
Cdd:COG1196  424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEaalaeLLEELAEAAARLLLLLEAEADY 503

                        330
                 ....*....|....*
gi 156637367 321 EQKYQSSEEKARNLK 335
Cdd:COG1196  504 EGFLEGVKAALLLAG 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-350 2.69e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367    74 EIEK--TCRESAEALATKLNKENKTLkRISMLYMAKLGPDVITEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQI 151
Cdd:TIGR02168  678 EIEEleEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   152 VSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEkcnrvsvlaveeyeelqvnlELEKDLRKKA 231
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--------------------ELRAELTLLN 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   232 ESFAQEMFIEQNkLKRQSHLLLQSSlpdQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEneALHKEIHNLRQQLE 311
Cdd:TIGR02168  817 EEAANLRERLES-LERRIAATERRL---EDLEEQIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALA 890

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 156637367   312 LLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 130-347 4.49e-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: 52.46  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 130 AAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsvl 209
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 210 AVEEYEELQVNLELEKDLRKKAESFAQEMfIEQNKLKrqshLLLQSSLPDQ-----QLLKAL-DENAKLIQQLEEERIQH 283
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLA----LLLSPEDFLDavrrlQYLKYLaPARREQAEELRADLAEL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156637367 284 QQKVKELE-ERLENEALHKEIHNLRQQLELLEDDKR----ELEQKYQSSEEKARNLKHSVDELQKRVNQ 347
Cdd:COG4942  163 AALRAELEaERAELEALLAELEEERAALEALKAERQkllaRLEKELAELAAELAELQQEAEELEALIAR 231
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 130-350 1.18e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 130 AAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRkvlekcnrvsvl 209
Cdd:COG3883    4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ------------ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 210 avEEYEELQVNLElekDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPD-----QQLLKALDENAKLIQQLEEERIQHQ 284
Cdd:COG3883   72 --AEIAEAEAEIE---ERREELGERARALYRSGGSVSYLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELE 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156637367 285 QKVKELEERLEnealhkeihNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG3883  147 AKKAELEAKLA---------ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 130-349 1.59e-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: 51.60  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   130 AAAETCVSVQCQKQ-IKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSV 208
Cdd:TIGR02168  664 GSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   209 LAVEEYEELQVNLElekDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVK 288
Cdd:TIGR02168  744 QLEERIAQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156637367   289 ELEERLEN-----EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:TIGR02168  821 NLRERLESlerriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
211-409 1.63e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 211 VEEYeeLQVNLELEKDLRKKAESFAQEMFIE--------QNKLK--RQSHLLLQSSLPDQQLLKALDENAKLIQQLEEER 280
Cdd:COG3206  158 AEAY--LEQNLELRREEARKALEFLEEQLPElrkeleeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 281 IQHQQKVKELEERLENEAL-------HKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVP 353
Cdd:COG3206  236 AEAEARLAALRAQLGSGPDalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156637367 354 PPPPPPPPLPPPPPNPIRSLMSMIRKRShpsggstkkekATQPETAEEVTDLKRQA 409
Cdd:COG3206  316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREV 360
PRK12704 PRK12704
phosphodiesterase; Provisional
 225-344 2.23e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 225 KDLRKKAESFAQEMFIEQNKLKRQshlllqsslpdqQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEN--EALHKE 302
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 156637367 303 IHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKR 344
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
142-350 5.66e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  142 KQIKELRDQIVSVQEEKKVLAiELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRkvlekcnrvsvlaVEEYEELQVNL 221
Cdd:COG4913   235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRR-------------LELLEAELEEL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  222 ELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSlpDQQLLKALdenAKLIQQLEEERIQHQQKVKELEERLEN----- 296
Cdd:COG4913   301 RAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQL---EREIERLERELEERERRRARLEALLAAlglpl 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156637367  297 ----EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4913   376 pasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
PLN02939 PLN02939
transferase, transferring glycosyl groups
 154-341 1.07e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 48.74  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 154 VQEEKKVLAIELESLKSKLGEVM---EEVNKVKQEKAVLNSEVLE-QRKVLEKCNRVSVLAVEEYEELQVNLELEKDLRK 229
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLRElESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLD 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 230 KAESFAQE--MFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQleeeriqhqqKVKELEERLenEALHKEIHNlr 307
Cdd:PLN02939 311 RATNQVEKaaLVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQ----------KLKLLEERL--QASDHEIHS-- 376

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 156637367 308 qQLELLEDDKRELEQKYQS--SEEKARNLKHSVDEL 341
Cdd:PLN02939 377 -YIQLYQESIKEFQDTLSKlkEESKKRSLEHPADDM 411
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-311 1.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 139 QCQKQIKELRDQIVSVQEEKKvlaiELESLKSKLGEVMEEVNKVKQEKAVLN--SEVLEQRKVLEKCNRVSVLAVEEYEE 216
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 217 LQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPD-QQLLKALDENAKLIQQLEEERIQHQQKVKELEERLE 295
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230

                        170
                 ....*....|....*.
gi 156637367 296 NEALHKEIHNLRQQLE 311
Cdd:COG4717  231 QLENELEAAALEERLK 246
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 144-495 9.00e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 45.81  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  144 IKELR-DQIVSVQEEKKVLaieLESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEkcnrvsvLAVEEYEELQVNLE 222
Cdd:PTZ00108 1018 IKHVInGELVITNAKKKDL---VKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEA-------DDEDDEEELGAAVS 1087

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  223 LEKDLRKKAESFAQEMF---IEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERiqhqQKVKELEERLENEAL 299
Cdd:PTZ00108 1088 YDYLLSMPIWSLTKEKVeklNAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEVE----EKEIAKEQRLKSKTK 1163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  300 HKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSvdELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRK 379
Cdd:PTZ00108 1164 GKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRV--DSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVK 1241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  380 RSHPSGGSTKKEKATQPETAEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKAKPDSLKGSESAVDELKGILGTlnks 459
Cdd:PTZ00108 1242 RLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGS---- 1317

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 156637367  460 tssrslkSLGPENSETELERILRRRKLTAEADSSSP 495
Cdd:PTZ00108 1318 -------LAALKKKKKSEKKTARKKKSKTRVKQASA 1346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 23-347 1.01e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367    23 EYEDLRAENQKTKETCDKIRQERDEAVKKLEE-------FQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENK 95
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367    96 TLkrismlymaklgpdviTEEINIDDDDPGTDTDAAAEtcvsvqCQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEV 175
Cdd:TIGR02168  758 EL----------------EAEIEELEERLEEAEEELAE------AEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   176 MEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLL--- 252
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrse 895

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   253 ---LQSSLPD-----QQLLKALDENAKLIQQLEEERIQHQQKVKELEERLenealhkeihnlrqqLELLEDDKRELEQKY 324
Cdd:TIGR02168  896 leeLSEELREleskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---------------SEEYSLTLEEAEALE 960

                          330       340
                   ....*....|....*....|...
gi 156637367   325 QSSEEKARNLKHSVDELQKRVNQ 347
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLENKIKE 983
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-343 1.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 260 QQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVD 339
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170


                 ....
gi 156637367 340 ELQK 343
Cdd:COG4717  171 ELAE 174
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
164-326 1.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 164 ELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVlEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESfAQEMFIEQN 243
Cdd:COG4717  338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQELKEELEE-LEEQLEELL 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 244 KLKRQshllLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQK 323
Cdd:COG4717  416 GELEE----LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491


                 ...
gi 156637367 324 YQS 326
Cdd:COG4717  492 WAA 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-352 1.28e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367     8 KQLQLITSLKEQAIgEYEDLRAENQKTKETcdKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHL-EIEKTCresaEAL 86
Cdd:TIGR02169  198 QQLERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEIsELEKRL----EEI 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367    87 ATKLNKENKTLKRISMLYMAKLGPDVitEEINIDDDDPGTDTDAAAETcvSVQCQKQIKELRDQIVSVQEEKKVLAIELE 166
Cdd:TIGR02169  271 EQLLEELNKKIKDLGEEEQLRVKEKI--GELEAEIASLERSIAEKERE--LEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   167 SLKSKLGEVMEEVNKVKQEKAVLNSEVLEqrkvlekcnrVSVLAVEEYEELqvnleleKDLRKKAESFAQEMFIEQNKLK 246
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRAELEE----------VDKEFAETRDEL-------KDYREKLEKLKREINELKRELD 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   247 RQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEnealhkeihNLRQQLELLEDDKRELEQKYQS 326
Cdd:TIGR02169  410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE---------QLAADLSKYEQELYDLKEEYDR 480

                          330       340
                   ....*....|....*....|....*.
gi 156637367   327 SEEKARNLKHSVDELQKRVNQSENSV 352
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERV 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
7-341 2.15e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   7 EKQLQLITSLKEQAIGEYEDLRAENQKTKETCDKIRQ------ERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCR 80
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEElkkeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  81 ESAEALATKLNKENKTLKRISMLymaklgpdviTEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQIVSVQEEKKV 160
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 161 LAIE-----LESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEK----------CNRVsvLAVEEYEEL--QVNLEL 223
Cdd:PRK03918 384 LTPEklekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvCGRE--LTEEHRKELleEYTAEL 461

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 224 EKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLpdQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEA--LHK 301
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESEL--IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLikLKG 539

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 156637367 302 EIHNLRQQLE---LLEDDKRELEQKYQSSEEKARNLKHSVDEL 341
Cdd:PRK03918 540 EIKSLKKELEkleELKKKLAELEKKLDELEEELAELLKELEEL 582
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
168-344 3.30e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 168 LKSKLGEVMEEVNKVKQEKAVLNsevLEQRKVLEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKR 247
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 248 QSHLL--------LQSSLPD-QQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENE------ALHKEIHNLRQQLEL 312
Cdd:COG4717  124 LLQLLplyqeleaLEAELAElPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslATEEELQDLAEELEE 203

                        170       180       190
                 ....*....|....*....|....*....|..
gi 156637367 313 LEDDKRELEQKYQSSEEKARNLKHSVDELQKR 344
Cdd:COG4717  204 LQQRLAELEEELEEAQEELEELEEELEQLENE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-352 3.47e-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: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  141 QKQIKELRDQIVSVQEEKKVLAIELESLKSKLgevmeevnkvkqekavlnsEVLEQRKVLEKcnrvsvlAVEEYEELQVN 220
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAEL-------------------DALQERREALQ-------RLAEYSWDEID 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  221 L-ELEKDLRKKaesfaqemfieQNKLKRqshllLQSSLPD-QQLLKALDENAKLIQQLEEERIQHQQKVKELEERLenEA 298
Cdd:COG4913   663 VaSAEREIAEL-----------EAELER-----LDASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--EQ 724

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156637367  299 LHKEIHNLRQQLELLEDDKR-----ELEQKYQ------SSEEKARNLKHSVDELQKRVNQSENSV 352
Cdd:COG4913   725 AEEELDELQDRLEAAEDLARlelraLLEERFAaalgdaVERELRENLEERIDALRARLNRAEEEL 789
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 39-321 3.87e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   39 DKIRQERDEAVKKLEEFQKIShmviEEVNFMQNHLEIEKTCRESAEALATKLNKEnktLKRISMLYMAKLGPDVITEEIN 118
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLE----EAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKRELERIRQEEIA 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  119 IDDDDPGTDTDAAAEtcvsvqcQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRK 198
Cdd:pfam17380 372 MEISRMRELERLQME-------RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  199 V----------LEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDE 268
Cdd:pfam17380 445 AremervrleeQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156637367  269 NAKLI----------------QQLEEERIQHQQKVKELEERLENEALHKEIHNLRQQLElLEDDKRELE 321
Cdd:pfam17380 525 RQKAIyeeerrreaeeerrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVE-SEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 215-349 5.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 215 EELQVNLE-LEKDlRKKAESFAQemfIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQHQQKVKELEER 293
Cdd:COG1196  196 GELERQLEpLERQ-AEKAERYRE---LKEELKELEAELLLLK---LRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156637367 294 LEN-----EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:COG1196  269 LEElrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 139-314 7.56e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  139 QCQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQ 218
Cdd:pfam07888  70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  219 VNLELEKDLRKKAESFAQEMFIE----QNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEER- 293
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEEAErkqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKe 229

                         170       180
                  ....*....|....*....|.
gi 156637367  294 LENEALHKEIHNLRQQLELLE 314
Cdd:pfam07888 230 AENEALLEELRSLQERLNASE 250
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-350 1.12e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 164 ELESLKSKLGEVMEEVNKVKQEKAVLNSEvlEQRKVLekcnrvsvlaVEEYEELQVNLELEKDLRKKAESFAQEMfieqN 243
Cdd:COG3206  183 QLPELRKELEEAEAALEEFRQKNGLVDLS--EEAKLL----------LQQLSELESQLAEARAELAEAEARLAAL----R 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 244 KLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEER----------IQHQQKVKELEERLENEA------LHKEIHNLR 307
Cdd:COG3206  247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAqrilasLEAELEALQ 326

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 156637367 308 QQLELLEDDKRELEQKYQSSEEKARNLKhsvdELQKRVNQSEN 350
Cdd:COG3206  327 AREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARE 365
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 142-323 1.41e-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: 40.68  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 142 KQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNR--VSVLAVEEYEELQV 219
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 220 NLELEKDLRKKAESFAQEmfieqnklkrqshlllqsslpdqqLLKALDENAKLIQQLEEERIQHQQKVKELEERLEneal 299
Cdd:COG1579   97 EIESLKRRISDLEDEILE------------------------LMERIEELEEELAELEAELAELEAELEEKKAELD---- 148

                        170       180
                 ....*....|....*....|....
gi 156637367 300 hKEIHNLRQQLELLEDDKRELEQK 323
Cdd:COG1579  149 -EELAELEAELEELEAEREELAAK 171
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-351 1.63e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 160 VLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVNLeleKDLRKKAESFAQEMF 239
Cdd:COG4717  288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL---QELLREAEELEEELQ 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 240 IEQNKLKRQSHLLLQSSLPDQQLLKALDEnakliqqlEEERIQHQQKVKELEERLENEALHKEIHNLRQQLELLEDDKRE 319
Cdd:COG4717  365 LEELEQEIAALLAEAGVEDEEELRAALEQ--------AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE 436

                        170       180       190
                 ....*....|....*....|....*....|..
gi 156637367 320 LEQKYQSSEEKARNLKHSVDELQKRVNQSENS 351
Cdd:COG4717  437 LEEELEELEEELEELREELAELEAELEQLEED 468
PRK12704 PRK12704
phosphodiesterase; Provisional
 169-332 1.64e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 169 KSKLGEVMEEVNKVKQEkAVLNSEVLEQRKVLEkcnrvsvlAVEEYEELQvnLELEKDLR-KKAESFAQEMFIEQNK--L 245
Cdd:PRK12704  30 EAKIKEAEEEAKRILEE-AKKEAEAIKKEALLE--------AKEEIHKLR--NEFEKELReRRNELQKLEKRLLQKEenL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 246 KRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEN-------EAlhKEIhnLRQQLEllEDDKR 318
Cdd:PRK12704  99 DRKLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEA--KEI--LLEKVE--EEARH 169

                        170
                 ....*....|....
gi 156637367 319 ELEQKYQSSEEKAR 332
Cdd:PRK12704 170 EAAVLIKEIEEEAK 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 212-349 2.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 212 EEYEELQVNLElekdlRKKAESFAQEMFIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQHQQKVKELE 291
Cdd:COG1196  213 ERYRELKEELK-----ELEAELLLLKLRELEAELEELEAELEEL---EAELEELEAELAELEAELEELRLELEELELELE 284

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 156637367 292 ERLENE-ALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:COG1196  285 EAQAEEyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 251-347 2.12e-03

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: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 251 LLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEErlENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEK 330
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK--EEKALLKQLAALERRIAALARRIRALEQELAALEAE 84

                         90
                 ....*....|....*..
gi 156637367 331 ARNLKHSVDELQKRVNQ 347
Cdd:COG4942   85 LAELEKEIAELRAELEA 101
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-348 2.47e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  191 SEVLEQRKVLEKCNRvsvlAVEEYEELqvnleleKDLRKKAEsfaqemfieqnKLKRQshlllqsslpdQQLLKALDENA 270
Cdd:COG4913   215 EYMLEEPDTFEAADA----LVEHFDDL-------ERAHEALE-----------DAREQ-----------IELLEPIRELA 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156637367  271 KLIQQLEEERiqhqQKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQS 348
Cdd:COG4913   262 ERYAAARERL----AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-320 2.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  141 QKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVK-QEKAVLNSEVLEQRKVLEKCNRvsvlAVEEYEELQV 219
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER----RRARLEALLA 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  220 NLELEKDLrkKAESFAqemfieqnKLKRQSHLLLQSSLPDQQLL-KALDENAKLIQQLEEERIQHQQKVKELEERLENea 298
Cdd:COG4913   370 ALGLPLPA--SAEEFA--------ALRAEAAALLEALEEELEALeEALAEAEAALRDLRRELRELEAEIASLERRKSN-- 437

                         170       180
                  ....*....|....*....|...
gi 156637367  299 LHKEIHNLRQQL-ELLEDDKREL 320
Cdd:COG4913   438 IPARLLALRDALaEALGLDEAEL 460
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 261-352 2.58e-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: 39.91  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 261 QLLKALDENAKLIQQLEEERIQHQQKVKELEERLEN-------EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARN 333
Cdd:COG1579   49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAE 128

                         90
                 ....*....|....*....
gi 156637367 334 LKHSVDELQKRVNQSENSV 352
Cdd:COG1579  129 LEAELAELEAELEEKKAEL 147
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
144-333 2.88e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 144 IKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVL--AVEEYEElqvnl 221
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLlaAIADAED----- 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 222 ELEKdLRKKAESFAQEMFIEQNKL--KRQSHLLLQSSLPD----------QQLLKALDENAKLIQQLEEERIQHQQKVKE 289
Cdd:PRK02224 607 EIER-LREKREALAELNDERRERLaeKRERKRELEAEFDEarieearedkERAEEYLEQVEEKLDELREERDDLQAEIGA 685

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 156637367 290 LEERLEN-EAL---HKEIHNLRQQLELLEDDKRELEQKYQS--SEEKARN 333
Cdd:PRK02224 686 VENELEElEELrerREALENRVEALEALYDEAEELESMYGDlrAELRQRN 735
Rod_C pfam10493
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ...
 215-306 2.97e-03

Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.


Pssm-ID: 463114  Cd Length: 551  Bit Score: 40.43  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  215 EELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQsHLLLQSSLPDQQLLKALDENAKLIQQL-EEERIQHQQKVKELEER 293
Cdd:pfam10493 135 EKWLKNLAPDDEAREKAEALLKKLKRQYQRSKTE-NLLIAHGLNDEELLKLVGKPAELIVSLyEHSSIEQRYKNPGGRDY 213

                          90
                  ....*....|....*.
gi 156637367  294 LENEALHKEI---HNL 306
Cdd:pfam10493 214 PDIHAAVKEIaeiNEL 229
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 5-343 3.12e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367     5 DEEKQLQLITSLKEQAIGEYEDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKT------ 78
Cdd:TIGR00618  209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETqerinr 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367    79 ----------------CRESAEALATKLNKENKTLKRISMLYMAklgpdVITEEINIDDDDPGTDTDAAAETCVSVQCQK 142
Cdd:TIGR00618  289 arkaaplaahikavtqIEQQAQRIHTELQSKMRSRAKLLMKRAA-----HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   143 QI---------KELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKV----------KQEKAVLNSEVLEQRKVLEKC 203
Cdd:TIGR00618  364 ATsireiscqqHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsafrdlQGQLAHAKKQQELQQRYAELC 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   204 --------------NRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDE- 268
Cdd:TIGR00618  444 aaaitctaqcekleKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNp 523

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156637367   269 --NAKLIQQLEEERIQHQQKVKELEERLenEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQK 343
Cdd:TIGR00618  524 gpLTRRMQRGEQTYAQLETSEEDVYHQL--TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
210-321 3.30e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.03  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 210 AVEEYEELQVNLELEKDLRKKAESFAQ---EMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQK 286
Cdd:COG1566   95 AEAQLARLEAELGAEAEIAAAEAQLAAaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQA 174

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 156637367 287 VKELEERLENEALHKEIHNLRQQLELLEDDKRELE 321
Cdd:COG1566  175 QAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
155-323 3.84e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  155 QEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEqrkVLEKCNRVSVLAVEEYEELQVNLELEKDLRkkaesf 234
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDE---LEAQIRGNGGDRLEQLEREIERLERELEER------ 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  235 aqemfieQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEEriqhqqkVKELEERLENEA--LHKEIHNLRQQLEL 312
Cdd:COG4913   358 -------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA-------LEEELEALEEALaeAEAALRDLRRELRE 423

                         170
                  ....*....|.
gi 156637367  313 LEDDKRELEQK 323
Cdd:COG4913   424 LEAEIASLERR 434
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 6-351 4.56e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367     6 EEKQLQLITSLKEQAIGEYEDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKtcRESAEA 85
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ--ELLRDE 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367    86 LATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDDDPGTDTDAAAETcvsvqcQKQIKELRDQIVSVQEEKKVLAIEL 165
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL------KSELLKLERRKVDDEEKLKESEKEK 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   166 ESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKL 245
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   246 KRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEALHKEIHNLRQ--QLELLEDDKRELEQK 323
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELElkKSEDLLKETQLVKLQ 483

                          330       340
                   ....*....|....*....|....*...
gi 156637367   324 YQSSEEKARNLKHSVDELQKRVNQSENS 351
Cdd:pfam02463  484 EQLELLLSRQKLEERSQKESKARSGLKV 511
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-344 6.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 141 QKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVN 220
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 221 LELEKDLRKKAEsfaqemfiEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLEnealh 300
Cdd:PRK03918 272 KKEIEELEEKVK--------ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----- 338

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 156637367 301 kEIHNLRQQLELLEDDKRELEQKYQSSEEkARNLKHSVDELQKR 344
Cdd:PRK03918 339 -RLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKR 380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 212-409 7.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 212 EEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHL----LLQSSLpDQQLLKALDENAKLIQQLEEERiQHQQKV 287
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEaelaELEAEL-EELRLELEELELELEEAQAEEY-ELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 288 KELEERLenEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPP 367
Cdd:COG1196  298 ARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 156637367 368 NPIRSLMSMIRKRSHPSGGSTKKEKATQPETAEEVTDLKRQA 409
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-351 7.99e-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: 39.27  E-value: 7.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367   222 ELEKDLRK-KAESFAQEMFIEQNKLKRQSHLLLqSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEE-----RLE 295
Cdd:TIGR02168  197 ELERQLKSlERQAEKAERYKELKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQELEEkleelRLE 275

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 156637367   296 NEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENS 351
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-313 8.00e-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: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  141 QKQIKELR---DQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKC-NRVSVLAVEEYEE 216
Cdd:COG4913   674 EAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEE 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  217 LQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQS--------SLPDQQL---LKALDENAKLIQQLEEERI-QHQ 284
Cdd:COG4913   754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewPAETADLdadLESLPEYLALLDRLEEDGLpEYE 833

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 156637367  285 QKVKELEERLENE-------ALHKEIHNLRQQLELL 313
Cdd:COG4913   834 ERFKELLNENSIEfvadllsKLRRAIREIKERIDPL 869
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 13-236 8.01e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  13 ITSLKEQAIGEY-EDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQN--HLEIEKTCRESAEALATK 89
Cdd:PRK05771  33 IEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEeeLEKIEKEIKELEEEISEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367  90 LNKENKTLKRISML-YMAKLGPDVI----TEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQ----IVSVQEEKKV 160
Cdd:PRK05771 113 ENEIKELEQEIERLePWGNFDLDLSlllgFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvVVVLKELSDE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156637367 161 LAIELESLK------SKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsvLAVEEYEELQVNLELEKDLRKKAESF 234
Cdd:PRK05771 193 VEEELKKLGferlelEEEGTPSELIREIKEELEEIEKERESLLEELKE------LAKKYLEELLALYEYLEIELERAEAL 266


                 ..
gi 156637367 235 AQ 236
Cdd:PRK05771 267 SK 268
 
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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