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Conserved domains on  [gi|300797073|ref|NP_001177992|]
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coiled-coil domain-containing protein 27 [Rattus norvegicus]

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 ...
 419-617 6.14e-07

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: 52.76  E-value: 6.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   419 ESQLRKVTTENELLVKELRERKQQIQDMTDKFSNLREEKK--HQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNA 496
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   497 QTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQAEQQTHVILEATQARLEKLRNKIIQ----AVFSVSGTKSLSTEIS 572
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkeFAETRDELKDYREKLE 395

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300797073   573 D------------NYILESLQRIISERSDFYNQLKQKGVKVPPLQQSDVSLPGKIKK 617
Cdd:TIGR02169  396 KlkreinelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 419-617 6.14e-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: 6.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   419 ESQLRKVTTENELLVKELRERKQQIQDMTDKFSNLREEKK--HQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNA 496
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   497 QTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQAEQQTHVILEATQARLEKLRNKIIQ----AVFSVSGTKSLSTEIS 572
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkeFAETRDELKDYREKLE 395

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300797073   573 D------------NYILESLQRIISERSDFYNQLKQKGVKVPPLQQSDVSLPGKIKK 617
Cdd:TIGR02169  396 KlkreinelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 374-557 2.14e-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: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQrhtdfqeSQLRKVTTENELLVKELRERKQQIQDMTDKFSNL 453
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 454 REEKKHQEI-MGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQA 532
Cdd:COG1196  322 EEELAELEEeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                        170       180
                 ....*....|....*....|....*
gi 300797073 533 EQQTHVILEATQARLEKLRNKIIQA 557
Cdd:COG1196  402 LEELEEAEEALLERLERLEEELEEL 426
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 363-553 4.54e-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: 43.57  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   363 KKSYSMTESFEEELMAQLEEYERMLMDFQNELELTRSKYSLAtgaITSLQrHTDFQESQLRKVTTENELLVKELRERKQQ 442
Cdd:pfam15921  488 KMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK---LQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKV 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   443 IQDMTDKFSNLRE-EKKHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELE-----------NLVNTDKD 510
Cdd:pfam15921  564 IEILRQQIENMTQlVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdlelekvKLVNAGSE 643

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 300797073   511 HLRRWKELNDDL-QMRNEmIQQAEQQTHVILEATQARLEKLRNK 553
Cdd:pfam15921  644 RLRAVKDIKQERdQLLNE-VKTSRNELNSLSEDYEVLKRNFRNK 686
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
374-551 5.31e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSkyslatgAITSLQRHTDFQESQLRKVTTENELL----------VKELRERKQQI 443
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELreerdelrerEAELEATLRTA 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 444 QDMTDKFSNLREEKK----HQEIMGLIEKENLT-LRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHlrrwkel 518
Cdd:PRK02224 439 RERVEEAEALLEAGKcpecGQPVEGSPHVETIEeDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI------- 511

                        170       180       190
                 ....*....|....*....|....*....|...
gi 300797073 519 nDDLQMRNEMIQQAEQQTHVILEATQARLEKLR 551
Cdd:PRK02224 512 -ERLEERREDLEELIAERRETIEEKRERAEELR 543
mS26_Tt cd23695
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ...
 427-541 4.28e-03

Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.


Pssm-ID: 467909 [Multi-domain]  Cd Length: 496  Bit Score: 40.19  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 427 TENELLVKELRERKQQIqdmTDKFSNLREEKKHQeiMGLIEKENLTLRqkvADLKTELENSEHTIEELNAQTKELENLvn 506
Cdd:cd23695  191 TELFKLLKEYQDAKAII---IEDFRESSEEGAEK--LEKLEKAFATLL---KNYKEELEEPEKQLEFMQKRLLDLYNL-- 260

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 300797073 507 tdkdhLRRWKELNDDLQMRNEMIQQAEQQTHVILE 541
Cdd:cd23695  261 -----LRLWGQYITIVKMPDSVVRDIMNKTQARPE 290
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 419-617 6.14e-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: 6.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   419 ESQLRKVTTENELLVKELRERKQQIQDMTDKFSNLREEKK--HQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNA 496
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   497 QTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQAEQQTHVILEATQARLEKLRNKIIQ----AVFSVSGTKSLSTEIS 572
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkeFAETRDELKDYREKLE 395

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300797073   573 D------------NYILESLQRIISERSDFYNQLKQKGVKVPPLQQSDVSLPGKIKK 617
Cdd:TIGR02169  396 KlkreinelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 374-557 2.14e-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: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQrhtdfqeSQLRKVTTENELLVKELRERKQQIQDMTDKFSNL 453
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 454 REEKKHQEI-MGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQA 532
Cdd:COG1196  322 EEELAELEEeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                        170       180
                 ....*....|....*....|....*
gi 300797073 533 EQQTHVILEATQARLEKLRNKIIQA 557
Cdd:COG1196  402 LEELEEAEEALLERLERLEEELEEL 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 374-554 8.64e-06

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: 48.22  E-value: 8.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTDFQESQLRKVTTENELLVKELRERKQQIQDMTDKFSNL 453
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 454 REEKKHQ----EIMGLIEKENLTLRQK--------VADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDD 521
Cdd:COG4942  103 KEELAELlralYRLGRQPPLALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190
                 ....*....|....*....|....*....|...
gi 300797073 522 LQMRNEMIQQAEQQTHVILEATQARLEKLRNKI 554
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAEL 215
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
370-514 1.67e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.93  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 370 ESFEEELMAQLEEYermlmdfQNELELTRSKYSLATGA-ITSLQRHTDFQESQLRKVTTENELLVKELRERKQQIQDMTD 448
Cdd:COG2433  376 LSIEEALEELIEKE-------LPEEEPEAEREKEHEEReLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300797073 449 KFSNLREEKKhQEImgLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVntDKDHLRR 514
Cdd:COG2433  449 ELSEARSEER-REI--RKDREISRLDREIERLERELEEERERIEELKRKLERLKELW--KLEHSGE 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 370-550 1.85e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   370 ESFEEELMAQLEEYERMLMDFQNEL---ELTRSKYSLATGAITSLQRHTDFQESQ--LRKVTTENELLVKELRERKQQIQ 444
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEARIeelEEDLHKLEEALNDLEARLSHSRIPEIQaeLSKLEEEVSRIEARLREIEQKLN 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   445 DMTDKFSNLREEKKH-QEIMGL-------IEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRrwk 516
Cdd:TIGR02169  823 RLTLEKEYLEKEIQElQEQRIDlkeqiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR--- 899

                          170       180       190
                   ....*....|....*....|....*....|....
gi 300797073   517 ELNDDLQMRNEMIQQAEQQTHVILEATQARLEKL 550
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 370-550 2.48e-05

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: 47.32  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073  370 ESFEEELMAQLEEYERMLMD--FQNEL--ELTRSKYSLATgAITSLQRHTDFQESQLRKVTTENELLVKELRERKQQIQD 445
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETiiKNNSEikDLTNQDSVKEL-IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073  446 MTDKFSNLREEKKhqeimgLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLrRWKELNDDLQMR 525
Cdd:TIGR04523 494 KEKELKKLNEEKK------ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-KKENLEKEIDEK 566

                         170       180
                  ....*....|....*....|....*
gi 300797073  526 NEMIQQAEqQTHVILEATQARLEKL 550
Cdd:TIGR04523 567 NKEIEELK-QTQKSLKKKQEEKQEL 590
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
376-535 2.50e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 376 LMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTDFQESQLRKVTTENEL--LVKELRERKQQIQDMTDKFS-- 451
Cdd:COG3206  210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqLRAQLAELEAELAELSARYTpn 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 452 -----NLREEKkhQEIMGLIEKEnltLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDDLQMRN 526
Cdd:COG3206  290 hpdviALRAQI--AALRAQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364


                 ....*....
gi 300797073 527 EMIQQAEQQ 535
Cdd:COG3206  365 ELYESLLQR 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 363-552 4.32e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   363 KKSYSMTESFEEELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTDFQESQLRKVTTENELLVKELRERKQQ 442
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   443 IQDMTDKFSNLREEKKHqeimglIEKENLTLRQKVADLKTELENSE--HTIEELNAQTKELENLVNTDKDHLRRWKELND 520
Cdd:TIGR02168  395 IASLNNEIERLEARLER------LEDRRERLQQEIEELLKKLEEAElkELQAELEELEEELEELQEELERLEEALEELRE 468

                          170       180       190
                   ....*....|....*....|....*....|..
gi 300797073   521 DLQMRNEMIQQAEQQthviLEATQARLEKLRN 552
Cdd:TIGR02168  469 ELEEAEQALDAAERE----LAQLQARLDSLER 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-597 5.58e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTD-------FQESQLRKVTTENELLVKELRERKQQIQDM 446
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEelsrqisALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   447 TDKFSNLREEK-KHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELE----NLVNTDKDHLRRWKELNDD 521
Cdd:TIGR02168  760 EAEIEELEERLeEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRERLESLERRIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   522 LQMRNEMIQQAEQQ----THVIlEATQARLEKLRNKIIQAVFSVSGTKSLSTEISDNYIL--ESLQRIISERSDFYNQLK 595
Cdd:TIGR02168  840 LEDLEEQIEELSEDieslAAEI-EELEELIEELESELEALLNERASLEEALALLRSELEElsEELRELESKRSELRRELE 918


                   ..
gi 300797073   596 QK 597
Cdd:TIGR02168  919 EL 920
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 373-561 8.53e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 373 EEELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTD-FQESQLRKVTTENELLVKELRERKQQIQDMTDKFS 451
Cdd:COG1196  339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEeLAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 452 NLREEKKHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQ 531
Cdd:COG1196  419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                        170       180       190
                 ....*....|....*....|....*....|
gi 300797073 532 AEQQTHVILEATQARLEKLRNKIIQAVFSV 561
Cdd:COG1196  499 AEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 374-516 2.89e-04

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: 42.60  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTDFQESQLRKVTTENEL--LVKELRERKQQIQDMTDKFS 451
Cdd:COG1579   34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESLKRRISDLEDEIL 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300797073 452 NLRE-----EKKHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTD----KDHLRRWK 516
Cdd:COG1579  114 ELMErieelEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllalYERIRKRK 187
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 363-553 4.54e-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: 43.57  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   363 KKSYSMTESFEEELMAQLEEYERMLMDFQNELELTRSKYSLAtgaITSLQrHTDFQESQLRKVTTENELLVKELRERKQQ 442
Cdd:pfam15921  488 KMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK---LQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKV 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   443 IQDMTDKFSNLRE-EKKHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELE-----------NLVNTDKD 510
Cdd:pfam15921  564 IEILRQQIENMTQlVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdlelekvKLVNAGSE 643

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 300797073   511 HLRRWKELNDDL-QMRNEmIQQAEQQTHVILEATQARLEKLRNK 553
Cdd:pfam15921  644 RLRAVKDIKQERdQLLNE-VKTSRNELNSLSEDYEVLKRNFRNK 686
SEC1 COG5158
Proteins involved in synaptic transmission and general secretion, Sec1 family [Intracellular ...
 376-608 5.14e-04

Proteins involved in synaptic transmission and general secretion, Sec1 family [Intracellular trafficking and secretion];


Pssm-ID: 227487  Cd Length: 582  Bit Score: 43.18  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 376 LMAQLEEYERMLMDFQNEL---ELTRSKYSLATGAITSLQRHTDFQE------SQLRKVTTENELLVKELRERKQQIQDM 446
Cdd:COG5158  243 MLHDLLGINNNIVTIPSSSvngPEKKFSLSDKDDPFWNDNKFLNFGEvgeklkKLAKELKTKAQLRHKENAKSVNDIKEF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 447 TDKFSNLREEK----KH----QEIMGLIEKENLTLRQKVADLKTELENSEHTIEELnaqTKELENLVNTDKD-------H 511
Cdd:COG5158  323 VDKLPELQKRSrslnKHltlaSELLKVVEERYLDDFSEIEQNLSTGNDVKSDISDL---IELLESGVEEDDKlrllilyS 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 512 LRRWKELNDDLQMRNEMIQQ----AEQQTHVILEATQARLEKLRNKIIQavfsvSGTKSLSTEISDNYILESLQRIISER 587
Cdd:COG5158  400 LTKDGLIKDIDELRLLRIQGygieALNFFQRLKELGFLTLKDSKTISLK-----RGDKDSLFQWFNTYSLSREHQGVPDL 474

                        250       260
                 ....*....|....*....|...
gi 300797073 588 SDFYNQL--KQKGVKVPPLQQSD 608
Cdd:COG5158  475 ENVYSGLipLKKDIPIDLLVRRL 497
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
374-551 5.31e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSkyslatgAITSLQRHTDFQESQLRKVTTENELL----------VKELRERKQQI 443
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELreerdelrerEAELEATLRTA 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 444 QDMTDKFSNLREEKK----HQEIMGLIEKENLT-LRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHlrrwkel 518
Cdd:PRK02224 439 RERVEEAEALLEAGKcpecGQPVEGSPHVETIEeDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI------- 511

                        170       180       190
                 ....*....|....*....|....*....|...
gi 300797073 519 nDDLQMRNEMIQQAEQQTHVILEATQARLEKLR 551
Cdd:PRK02224 512 -ERLEERREDLEELIAERRETIEEKRERAEELR 543
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
412-554 5.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 412 QRHTDFQESQLRKVTTENEL-----LVKELRERKQQIQDMTDKFSNLREEKKHQEIMGLIEKENLTLRQKVA---DLKTE 483
Cdd:COG4717   85 EKEEEYAELQEELEELEEELeeleaELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEelrELEEE 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300797073 484 LENSEHTIEELNAQTKELENLVNTDKdhLRRWKELNDDLQMRNEMIQQAEQQthviLEATQARLEKLRNKI 554
Cdd:COG4717  165 LEELEAELAELQEELEELLEQLSLAT--EEELQDLAEELEELQQRLAELEEE----LEEAQEELEELEEEL 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
428-606 8.65e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 428 ENELLVKELRERKQQIQDMTDKFSNLREEKKHqeimglIEKENLTLRQKVADLKTELENSEHTIE--ELNAQTKELENLV 505
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEE------LEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 506 NTDKDHLRRWKELNDDLQMRNEMIQQAEQQTHVILEATQARLEKLRNKIIQAVFSVSGTKSLSTEisdnyILESLQRIIS 585
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE-----ELEEAQEELE 223

                        170       180
                 ....*....|....*....|.
gi 300797073 586 ERSDFYNQLKQKGVKVPPLQQ 606
Cdd:COG4717  224 ELEEELEQLENELEAAALEER 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 363-551 1.23e-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: 41.67  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 363 KKSYSMTESFEEELMAQLEEYERMLmdfqneleltrskySLATGAITSLQRHTDFQESQLRKVTTENELLVKELRERKQQ 442
Cdd:COG4942   40 EKELAALKKEEKALLKQLAALERRI--------------AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 443 IQDMTDK---------------FSNLREEKKHQEIMGLIEKEnltLRQKVADLKTELENSEHTIEELNAQTKELENLVNT 507
Cdd:COG4942  106 LAELLRAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 300797073 508 DKDHLrrwKELNDDLQMRNEMIQQAEQQthviLEATQARLEKLR 551
Cdd:COG4942  183 LEEER---AALEALKAERQKLLARLEKE----LAELAAELAELQ 219
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-535 1.68e-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: 41.58  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHtdfqesqlrkvttenellVKELRERKQQIQDMTDKFSNL 453
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE------------------IERLEARLERLEDRRERLQQE 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   454 REEkkhqEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQAE 533
Cdd:TIGR02168  423 IEE----LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498


                   ..
gi 300797073   534 QQ 535
Cdd:TIGR02168  499 EN 500
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
374-553 1.95e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 374 EELMAQLEEYERMLMDFQNELELTRSKYSLATGAITSLQRHTDFQE--SQLRKVTTENELLVKELRERKQQI----QDMT 447
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEliAERRETIEEKRERAEELRERAAELeaeaEEKR 557

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 448 DKFSNLREE-KKHQEIMGLIEKENLTLRQ------KVADLKTELENSEHTIEELNAQTKELENLVNTDKDHLR----RWK 516
Cdd:PRK02224 558 EAAAEAEEEaEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekreRKR 637

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 300797073 517 ELNDDLQ-MRNEMIQQAEQQTHVILEATQARLEKLRNK 553
Cdd:PRK02224 638 ELEAEFDeARIEEAREDKERAEEYLEQVEEKLDELREE 675
PRK12704 PRK12704
phosphodiesterase; Provisional
 434-555 2.27e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 434 KELRERKQQIQDMtDKFSNLREE--KKHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEEL-NAQTKELENLVNTDKD 510
Cdd:PRK12704  75 KELRERRNELQKL-EKRLLQKEEnlDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAE 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 300797073 511 HLRrwKELNDdlQMRNEMIQQAEQQTHVILEATQARLEKLRNKII 555
Cdd:PRK12704 154 EAK--EILLE--KVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 419-557 2.38e-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: 41.20  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073   419 ESQLRKvTTEN----ELLVKELRERKQQIQ---DMTDKFSNLREEKKHQEIMGLI--------EKENLT-----LRQKVA 478
Cdd:TIGR02168  178 ERKLER-TRENldrlEDILNELERQLKSLErqaEKAERYKELKAELRELELALLVlrleelreELEELQeelkeAEEELE 256

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300797073   479 DLKTELENSEHTIEELNAQTKELENLVNTDKDHLRRWKELNDDLQMRNEMIQQAEQQTHVILEATQARLEKLRNKIIQA 557
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
mS26_Tt cd23695
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ...
 427-541 4.28e-03

Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.


Pssm-ID: 467909 [Multi-domain]  Cd Length: 496  Bit Score: 40.19  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 427 TENELLVKELRERKQQIqdmTDKFSNLREEKKHQeiMGLIEKENLTLRqkvADLKTELENSEHTIEELNAQTKELENLvn 506
Cdd:cd23695  191 TELFKLLKEYQDAKAII---IEDFRESSEEGAEK--LEKLEKAFATLL---KNYKEELEEPEKQLEFMQKRLLDLYNL-- 260

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 300797073 507 tdkdhLRRWKELNDDLQMRNEMIQQAEQQTHVILE 541
Cdd:cd23695  261 -----LRLWGQYITIVKMPDSVVRDIMNKTQARPE 290
PRK12704 PRK12704
phosphodiesterase; Provisional
 440-581 4.94e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 440 KQQIQDMTDKFSNLREEKKHqEIMGLIEKENLTLRQKVADLKTELENsehTIEELNAQTKELENLVNTDKDHLRRWKELN 519
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKK-EAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELL 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300797073 520 DDLQMRNEMIQQAEQQTHVILEATQARLEKLRNKIIQAVFSVSGtksLSTEISDNYILESLQ 581
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG---LTAEEAKEILLEKVE 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-557 6.65e-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: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073 432 LVKELRERKQQIQdmtdkfsnLREEKKHQEIMGLIEKENLTLRQKVADLKTELENSEHTIEELNAQTKELENLVNTDKDH 511
Cdd:COG1196  218 LKEELKELEAELL--------LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 300797073 512 LR----RWKELNDDLQMRNEMIQQAEQQthviLEATQARLEKLRNKIIQA 557
Cdd:COG1196  290 EYellaELARLEQDIARLEERRRELEER----LEELEEELAELEEELEEL 335
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 375-595 7.21e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.34  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073  375 ELMAQLEEYERMLMdfQNELELTRSKySLATGAITSLQRHTDFQESQLRKVTTENELLVKELRERKQQIQDMTDkfsNLR 454
Cdd:pfam05557   6 ESKARLSQLQNEKK--QMELEHKRAR-IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE---LNR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797073  455 EEKKHQEIMGLIEKEN-----------LTLRQKVADLKTELENSEhtiEELNAQTKELENLvntdkdhLRRWKELNDDLQ 523
Cdd:pfam05557  80 LKKKYLEALNKKLNEKesqladareviSCLKNELSELRRQIQRAE---LELQSTNSELEEL-------QERLDLLKAKAS 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300797073  524 MRNEMIQQAEQQTHVILEATQaRLEKLRNKIIQAVFSVSGTKSLSTEISDNYILESLQRIISERSDFYNQLK 595
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQ-RIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENI 220
 
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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