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Conserved domains on  [gi|1952581435|ref|XP_038668775|]
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sarcolemma associated protein a isoform X10 [Scyliorhinus canicula]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 6-363 7.13e-12

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 67.40  E-value: 7.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435    6 SPSKDRSSEDTTDYQMDEQELNESLNKvslLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEA 85
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   86 QELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA--- 162
Cdd:TIGR02169  736 KERLEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrie 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  163 LRQTAVEAATGRES-DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQ 241
Cdd:TIGR02169  812 ARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESR 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  242 SNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHA 319
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRV 963

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952581435  320 ENETQKFQ-------KQYEADQTMYLELKEKLDKTQKENESITDELENCKE 363
Cdd:TIGR02169  964 EEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-363 7.13e-12

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: 67.40  E-value: 7.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435    6 SPSKDRSSEDTTDYQMDEQELNESLNKvslLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEA 85
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   86 QELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA--- 162
Cdd:TIGR02169  736 KERLEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrie 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  163 LRQTAVEAATGRES-DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQ 241
Cdd:TIGR02169  812 ARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESR 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  242 SNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHA 319
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRV 963

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952581435  320 ENETQKFQ-------KQYEADQTMYLELKEKLDKTQKENESITDELENCKE 363
Cdd:TIGR02169  964 EEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-336 1.52e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  48 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQkcfemqALLEEERKTAKKQVEESTRQIQALQAH 127
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEELELELEEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 128 LHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASE 201
Cdd:COG1196   290 EYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 202 YESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLT 281
Cdd:COG1196   370 AEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581435 282 KDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 336
Cdd:COG1196   449 EEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 5-373 1.41e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   5 LSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKE 84
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  85 AQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---ILREDKEIEIIETRDQLASTHKEIV 161
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtKFKNNKEVELEELKKILAEDEKLLD 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 162 ALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKL 235
Cdd:pfam05483 423 EKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV---------------EDLKTELEKEKLKN 487

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 236 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVK 315
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581435 316 LAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 373
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
prfA PRK00591
peptide chain release factor 1; Validated
 73-124 2.45e-03

peptide chain release factor 1; Validated


Pssm-ID: 234801 [Multi-domain]  Cd Length: 359  Bit Score: 39.68  E-value: 2.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952581435  73 REKQELQQELKEAQELAISSKQKcfEMQALLEEERKTAKKQVEESTRQIQAL 124
Cdd:PRK00591   52 REYKQAQEDLEEAKEMLEEESDP--EMREMAKEELKELEERLEELEEELKIL 101
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-363 7.13e-12

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: 67.40  E-value: 7.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435    6 SPSKDRSSEDTTDYQMDEQELNESLNKvslLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEA 85
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   86 QELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA--- 162
Cdd:TIGR02169  736 KERLEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrie 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  163 LRQTAVEAATGRES-DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQ 241
Cdd:TIGR02169  812 ARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESR 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  242 SNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHA 319
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRV 963

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952581435  320 ENETQKFQ-------KQYEADQTMYLELKEKLDKTQKENESITDELENCKE 363
Cdd:TIGR02169  964 EEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-336 1.52e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  48 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQkcfemqALLEEERKTAKKQVEESTRQIQALQAH 127
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEELELELEEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 128 LHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASE 201
Cdd:COG1196   290 EYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 202 YESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLT 281
Cdd:COG1196   370 AEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581435 282 KDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 336
Cdd:COG1196   449 EEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-370 1.19e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 103 LEEERKTAKK----QVEESTRQIQALQAHLHKLQKDIEILRED---KEIEIIETRDQLASTHKEIVALRQTAVEAatgrE 175
Cdd:COG1196   205 LERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEEL----E 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 176 SDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 255
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERR---------------RELEERLEELEEELAELEEELEELEEELEELEEE 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 256 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQT 335
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1952581435 336 MYLELKEKLDKTQKENESITDELENCKENLKLLQQ 370
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-308 5.03e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  20 QMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQE---LAISSKQKC 96
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  97 FEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEA 170
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeaeeelEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 171 ATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCD 250
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581435 251 SLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQE 308
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 106-371 2.05e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  106 ERKTAKKQVEESTRQIQALQAHLHKLQK---DIEILREDKEIEIIETRDQLASTHKEIVALRQTaVEAATGRESDIAILQ 182
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKeleELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  183 GELHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEK 262
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEA----EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  263 LQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLE 339
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1952581435  340 LKEKLDKTQKENESITDELENCKENLKLLQQK 371
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 72-359 2.39e-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: 53.15  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   72 EREK----QELQQELKEAQELAISSKQKCFEMQ-ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEIL----REDK 142
Cdd:TIGR02169  206 EREKaeryQALLKEKREYEGYELLKEKEALERQkEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLG 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  143 EIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKD 222
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEK----ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  223 KQKGEAVqLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK 302
Cdd:TIGR02169  362 LKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581435  303 EqrlqETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELE 359
Cdd:TIGR02169  441 E----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-371 2.98e-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: 52.75  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   76 QELQQELKEAQeLAISSKQKCFemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilredkeieiiETRDQLAS 155
Cdd:TIGR02168  216 KELKAELRELE-LALLVLRLEE-----LREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  156 THKEIVALrQTAVEAATgreSDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKL 235
Cdd:TIGR02168  279 LEEEIEEL-QKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE--------ELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  236 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK---EQRLQETNGL 312
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEEL 426

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581435  313 RVKLahAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 371
Cdd:TIGR02168  427 LKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-350 3.03e-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: 52.76  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   25 ELNESLNKVSLLKDLLAEARA-SSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 103
Cdd:TIGR02169  195 EKRQQLERLRREREKAERYQAlLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  104 EEERKTAKKQVEESTRQIqalQAHLHKLQKDIEILrEDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQG 183
Cdd:TIGR02169  275 EELNKKIKDLGEEEQLRV---KEKIGELEAEIASL-ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  184 ELHKVQTELEQWRQTASEYESEIfnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKL 263
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAEL--------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  264 QWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRlqetnglrvklahaenetQKFQKQYEADQTMYLELKEK 343
Cdd:TIGR02169  423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------------------SKYEQELYDLKEEYDRVEKE 484


                   ....*..
gi 1952581435  344 LDKTQKE 350
Cdd:TIGR02169  485 LSKLQRE 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-323 1.08e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   9 KDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQel 88
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-- 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  89 aisskqkcfEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdKEIEIIETRDQLASTHKEIVALRQTAV 168
Cdd:COG1196   330 ---------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALRAAAELA 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 169 EAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKND 248
Cdd:COG1196   400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581435 249 CDSLRQEKVLLTEKLQWFEEELRCAQQ--QSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENET 323
Cdd:COG1196   479 LAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 23-295 2.22e-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: 50.06  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   23 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQcahvqtgDSEREKQELQQELKEAQELAISSKQKcfemQAL 102
Cdd:TIGR02168  718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEELAEAEAE----IEE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  103 LEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK---EIEIIETRDQLASTHKEIVALRQTaVEAATGRESDIA 179
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLeslERRIAATERRLEDLEEQIEELSED-IESLAAEIEELE 865

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  180 ILQGELHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLL 259
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALL----RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1952581435  260 TEKL-QWFEEELRCAQQQSVKLTKDASGLEVSRKALE 295
Cdd:TIGR02168  942 QERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-295 3.58e-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: 49.28  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   20 QMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQE--LAISSKQKCF 97
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   98 EMQ-ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE---IEIIETRDQLASTHKEIVALRQTAVEAATG 173
Cdd:TIGR02168  301 EQQkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  174 RE---SDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEavqLQGKLDELQKQSNGLKNDCD 250
Cdd:TIGR02168  381 LEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELEELEEELEELQEELE 457

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1952581435  251 SLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALE 295
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 5-373 1.41e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   5 LSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKE 84
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  85 AQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---ILREDKEIEIIETRDQLASTHKEIV 161
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtKFKNNKEVELEELKKILAEDEKLLD 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 162 ALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKL 235
Cdd:pfam05483 423 EKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV---------------EDLKTELEKEKLKN 487

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 236 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVK 315
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581435 316 LAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 373
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 70-293 2.18e-05

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: 46.30  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  70 DSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIET 149
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 150 RDQLASTHKEIValRQTAVEAATGRESDIAIL--QGELHKVQTELeQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGE 227
Cdd:COG4942    96 RAELEAQKEELA--ELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581435 228 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 293
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-193 3.09e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   5 LSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKE 84
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  85 AQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE--DKEIEIIETRDQLASTHKEIVA 162
Cdd:COG1196   384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeeEALEEAAEEEAELEEEEEALLE 463

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1952581435 163 LRQTAVEAATGRESDIAILQGELHKVQTELE 193
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEELAEAAARLL 494
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
23-202 1.48e-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: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  23 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLK--YELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ 100
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 101 ALLEEERKTAKKQVEEStrQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAAtgrESD 177
Cdd:COG3206   247 AQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNHPDVIALRAQIAALRAQLQQEAQRILASL---EAE 321

                         170       180
                  ....*....|....*....|....*
gi 1952581435 178 IAILQGELHKVQTELEQWRQTASEY 202
Cdd:COG3206   322 LEALQAREASLQAQLAQLEARLAEL 346
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-255 3.40e-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: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   72 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEILREDKeIEIIETRD 151
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLA--EYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEE 692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  152 QLASTHKEIVALRQ---TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgea 228
Cdd:COG4913    693 QLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--- 769

                          170       180
                   ....*....|....*....|....*..
gi 1952581435  229 vQLQGKLDELQKQSNGLKNDCDSLRQE 255
Cdd:COG4913    770 -NLEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-196 8.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   23 EQELNESLNKVSLLKDLLAEARASSRKHE--------SELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQ 94
Cdd:COG4913    301 RAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   95 KCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkEIEIIETRDqlASTHKEIVALRQTAVEAATGR 174
Cdd:COG4913    381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA--EIASLERRK--SNIPARLLALRDALAEALGLD 456

                          170       180
                   ....*....|....*....|..
gi 1952581435  175 ESDIAILqGELHKVQTELEQWR 196
Cdd:COG4913    457 EAELPFV-GELIEVRPEEERWR 477
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 24-373 9.35e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 9.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   24 QELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELkEAQELAISSKQKCFEMQALL 103
Cdd:pfam15921  454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-EATNAEITKLRSRVDLKLQE 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  104 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiIETRDQLASTHKEIVALRQtaVEAATgresdiaiLQG 183
Cdd:pfam15921  533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-----IENMTQLVGQHGRTAGAMQ--VEKAQ--------LEK 597

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  184 ELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDeLQKQSNGLKNDCDSLRQEKVLLTEKL 263
Cdd:pfam15921  598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNELNSLSEDY 676

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  264 QWFEEELRC-AQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKfQKQYEADQTMYLELKE 342
Cdd:pfam15921  677 EVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEE 755

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1952581435  343 KLDKTQKENESITDELENCKENLKLLQQKGN 373
Cdd:pfam15921  756 AMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-305 9.52e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 105 EERKTAKKQVEESTRQIQALQAHLHKLQKDIEIL---REDKEIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAIL 181
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALlkqLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 182 QGELHKVQTELEQ-----WRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAvqLQGKLDELQKQSNGLKNDCDSLRQEK 256
Cdd:COG4942    96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALRAELEAER 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1952581435 257 VLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 305
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-371 1.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   18 DYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDS---------------EREKQELQQEL 82
Cdd:COG4913    282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlereierlERELEERERRR 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   83 KEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEiEIIETRDQLASTHK---- 158
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-ELEAEIASLERRKSnipa 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  159 EIVALRQTAVEAATGRESDIAILqGELHKVQTELEQWRQTA--------------SEYE---SEIFNLQTKLQ------- 214
Cdd:COG4913    441 RLLALRDALAEALGLDEAELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYaaaLRWVNRLHLRGrlvyerv 519

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  215 LQTQQQKDKQKGEAVQLQGKL---------------------------DELQ------------KQSNGL--KNDCDSLR 253
Cdd:COG4913    520 RTGLPDPERPRLDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspEELRrhpraitragqvKGNGTRheKDDRRRIR 599

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  254 QEKVL---LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLkeQRLQETNGLRVKLAHAENETQKFQKQY 330
Cdd:COG4913    600 SRYVLgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAEL 677

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1952581435  331 ---EADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 371
Cdd:COG4913    678 erlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 26-371 1.66e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  26 LNESLNKVSLLKDLLAEAR-ASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQAL-L 103
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNdLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeL 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 104 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIE-------IIETRDQLASTHKEIVALRQT 166
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlSEKQKEleqnnkkIKELEKQLNQLKSEISDLNNQ 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 167 AVEAATGR-ESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQSNGL 245
Cdd:TIGR04523 304 KEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES--------ENSEKQRELEEKQNEIEKL 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 246 KNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ----------ETNGLRVK 315
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELI 455

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581435 316 LAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 371
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
prfA PRK00591
peptide chain release factor 1; Validated
 73-124 2.45e-03

peptide chain release factor 1; Validated


Pssm-ID: 234801 [Multi-domain]  Cd Length: 359  Bit Score: 39.68  E-value: 2.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952581435  73 REKQELQQELKEAQELAISSKQKcfEMQALLEEERKTAKKQVEESTRQIQAL 124
Cdd:PRK00591   52 REYKQAQEDLEEAKEMLEEESDP--EMREMAKEELKELEERLEELEEELKIL 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
78-276 2.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  78 LQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTH 157
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 158 KEIVALRQTAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES---EIFNLQTKLQLQTQQQKDKQKGEAVQLQGK 234
Cdd:COG4717   123 KLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEE 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952581435 235 LDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 276
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-271 2.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   38 DLLAEARASSRKHES---ELDHLKYELQCAHVQTGdsEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQV 114
Cdd:COG4913    252 ELLEPIRELAERYAAareRLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAE----LERLEARLDALREEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  115 EESTRQIQALQ-AHLHKLQKDIEILREDKEiEIIETRDQLASthkeivALRQTAVEAATGREsdiailqgELHKVQTELE 193
Cdd:COG4913    326 DELEAQIRGNGgDRLEQLEREIERLERELE-ERERRRARLEA------LLAALGLPLPASAE--------EFAALRAEAA 390

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581435  194 QWRQTASEYESEIFNlqtklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELR 271
Cdd:COG4913    391 ALLEALEEELEALEE------------------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 66-345 2.85e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   66 VQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALqahlhklqKDIEILREDKEIE 145
Cdd:pfam15921  590 VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV--------KDIKQERDQLLNE 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  146 IIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESeifnlqtklqlqtqqqkdkQK 225
Cdd:pfam15921  662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG-------------------SD 722

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  226 GEAVQLQGKldeLQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKE 303
Cdd:pfam15921  723 GHAMKVAMG---MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGELEVLRSQE 799

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1952581435  304 QRLQE-TNGLRVKLAHAENETQKFQK--QYEADQTMYLELKEKLD 345
Cdd:pfam15921  800 RRLKEkVANMEVALDKASLQFAECQDiiQRQEQESVRLKLQHTLD 844
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 23-206 5.29e-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: 38.59  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  23 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELqcahvqtGDSEREKQELQQELKEAQELAISSKQKCFEMQAL 102
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 103 LEEERKTAKKQV---------------------EESTRQIQALQAHLHKLQKDIEILREDKEI------EIIETRDQLAS 155
Cdd:COG4942    99 LEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEA 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952581435 156 THKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEI 206
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
99-348 5.98e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435  99 MQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIeiIETRDQLASTHKEIVALRQTAVEAatgrESDI 178
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEA----RAEL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 179 AILQGELHKVQTELEQWRQTASEyeseifnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 258
Cdd:COG3206   236 AEAEARLAALRAQLGSGPDALPE-------------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435 259 LTEKLQwfeeelRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKeQRLQETNGLRVKLAhaenetqKFQKQYEADQTMYL 338
Cdd:COG3206   303 LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLE-ARLAELPELEAELR-------RLEREVEVARELYE 368

                         250
                  ....*....|
gi 1952581435 339 ELKEKLDKTQ 348
Cdd:COG3206   369 SLLQRLEEAR 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
24-141 6.57e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   24 QELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 103
Cdd:COG4913    678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1952581435  104 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRED 141
Cdd:COG4913    758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
PRK11281 PRK11281
mechanosensitive channel MscK;
64-208 6.90e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581435   64 AHVQTGDSEREKQELQQELKEAQElaisskqkcfemQALLEEERKTAKKQVEESTRQIQALQahlhKLQKDIEILRedKE 143
Cdd:PRK11281    27 ARAASNGDLPTEADVQAQLDALNK------------QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLK--QQ 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581435  144 IEiiETRDQLASTHKEIVALRQTAVEAATGRESDIAI--LQGELHKVQTELEQWRQTASEYESEIFN 208
Cdd:PRK11281    89 LA--QAPAKLRQAQAELEALKDDNDEETRETLSTLSLrqLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
 
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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