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Conserved domains on  [gi|529006532|ref|XP_005224777|]
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nuclear distribution protein nudE homolog 1 isoform X2 [Bos taurus]

Protein Classification

SPEC and NUDE_C domain-containing protein( domain architecture ID 10522326)

SPEC and NUDE_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-297 2.16e-54

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


:

Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 176.13  E-value: 2.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVDAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  204 TAVQATgsvpSTPIAHRGPSSSLNtpgTFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170
                  ....*....|....
gi 529006532  284 GRASGPASGRGSKN 297
Cdd:pfam04880 146 SRRGNSRSLYGSRP 159
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 6.21e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 6.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    26 KQRAENTQEELREFQEESREYEAELETQLQQTEsKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   106 -------IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 529006532   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-297 2.16e-54

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 176.13  E-value: 2.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVDAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  204 TAVQATgsvpSTPIAHRGPSSSLNtpgTFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170
                  ....*....|....
gi 529006532  284 GRASGPASGRGSKN 297
Cdd:pfam04880 146 SRRGNSRSLYGSRP 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 6.21e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 6.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    26 KQRAENTQEELREFQEESREYEAELETQLQQTEsKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   106 -------IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 529006532   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-188 2.32e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGY 90
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        170
                 ....*....|....*...
gi 529006532 171 DEARDLRQELAVQQKQEK 188
Cdd:COG1196  460 ALLELLAELLEEAALLEA 477
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 19-188 4.86e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 47.75  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  19 KDLAMTYKQRAENTQEELREFQEESREYEAELETQlqqtESKNRDLLMENN--HLRMELETIKEKFKTQHSEgyrQISAL 96
Cdd:cd22656  127 LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETL----EKALKDLLTDEGgaIARKEIKDLQKELEKLNEE---YAAKL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  97 EDDLAQTKAIKDKLQKYIRELEQANDDLERAKratiMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLLESVQRl 169
Cdd:cd22656  200 KAKIDELKALIADDEAKLAAALRLIADLTAAD----TDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLLEDDIS- 274

                        170
                 ....*....|....*....
gi 529006532 170 kDEARDLRQELAVQQKQEK 188
Cdd:cd22656  275 -KIPAAILAKLELEKAIEK 292
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-190 6.13e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 48.30  E-value: 6.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    20 DLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    93 -ISALEDDLAQTKAIKDKLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 529006532   154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-253 1.37e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMEnnhlrmeleTIKEKFKTQHSEGY-------RQISALED 98
Cdd:COG3883   50 NEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGE---------RARALYRSGGSVSYldvllgsESFSDFLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  99 DLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:COG3883  120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529006532 179 ELAVQQKQEKPRTPMPSSVDAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGTFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883  200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-168 2.40e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  28 RAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELetikekfktqhsEGYRQISALEDDLAQTKAIK 107
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKELAEQLKELE 509

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006532 108 DKLQKY-IRELEQANDDLERAK------RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:PRK03918 510 EKLKKYnLEELEKKAEEYEKLKekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 142-204 1.67e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 39.58  E-value: 1.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006532 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVDAERTDT 204
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 34-186 6.45e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.07  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    34 EELREFQEESREYEAELETQLQQTE----------SKNRDLLMEN------NHLRME------------LETIKEKFKTQ 85
Cdd:smart00787  73 KELKKYISEGRDLFKEIEEETLINNpplfkeyfsaSPDVKLLMDKqfqlvkTFARLEakkmwyewrmklLEGLKEGLDEN 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    86 HS---EGYRQISA----LEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSL-EDFEQRLNQAIERNAFLESELD 157
Cdd:smart00787 153 LEglkEDYKLLMKelelLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLEELEE 232

                          170       180
                   ....*....|....*....|....*....
gi 529006532   158 EKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEKK 261
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-297 2.16e-54

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 176.13  E-value: 2.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVDAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  204 TAVQATgsvpSTPIAHRGPSSSLNtpgTFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170
                  ....*....|....
gi 529006532  284 GRASGPASGRGSKN 297
Cdd:pfam04880 146 SRRGNSRSLYGSRP 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 6.21e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 6.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    26 KQRAENTQEELREFQEESREYEAELETQLQQTEsKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   106 -------IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 529006532   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-188 2.32e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGY 90
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        170
                 ....*....|....*...
gi 529006532 171 DEARDLRQELAVQQKQEK 188
Cdd:COG1196  460 ALLELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 3.99e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477


                 ..
gi 529006532 186 QE 187
Cdd:COG1196  478 AL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-188 8.09e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 8.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ----RLKDEARDLRQELA 181
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerleRLEEELEELEEALA 431


                 ....*..
gi 529006532 182 VQQKQEK 188
Cdd:COG1196  432 ELEEEEE 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-186 8.68e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 8.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    34 EELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKF---KTQHSEGYRQISALEDDLAQTKAIKDKL 110
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006532   111 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-188 1.11e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  24 TYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRM------ELETIKEKFKTQHSEGYRQISALE 97
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  98 DDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELA 399

                        170
                 ....*....|.
gi 529006532 178 QELAVQQKQEK 188
Cdd:COG1196  400 AQLEELEEAEE 410
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-188 1.26e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  27 QRAENTQEELREFQEESREYEAELET-QLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 106 IKDKLQKYIRELEQANDDLERAKR----ATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELA 181
Cdd:COG4717  161 LEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQ---EELEELEEELEQLENELE 237


                 ....*..
gi 529006532 182 VQQKQEK 188
Cdd:COG4717  238 AAALEER 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-181 4.17e-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: 51.98  E-value: 4.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLmENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 173
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974


                   ....*...
gi 529006532   174 RDLRQELA 181
Cdd:TIGR02168  975 KRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-187 4.57e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  27 QRAENTQEELR-EFQEESREYEA------ELETQLQQTESKNRDLLMENNHLRMELETIKE---KFKTQHSEGYRQISAL 96
Cdd:COG1196  263 AELEAELEELRlELEELELELEEaqaeeyELLAELARLEQDIARLEERRRELEERLEELEEelaELEEELEELEEELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  97 EDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDL 176
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                        170
                 ....*....|.
gi 529006532 177 RQELAVQQKQE 187
Cdd:COG1196  423 LEELEEALAEL 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 4.65e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHL------RMELETIKEKFKTQHSEGYRQISALEDD 99
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELeelaeeLLEALRAAAELAAQLEELEEAEEALLER 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 100 LAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQE 179
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495


                 ....*...
gi 529006532 180 LAVQQKQE 187
Cdd:COG1196  496 LLEAEADY 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-188 6.21e-07

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: 6.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELET---QLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQ 102
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 103 TKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAV 182
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488


                 ....*.
gi 529006532 183 QQKQEK 188
Cdd:COG1196  489 AAARLL 494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-198 7.86e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEA---ELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQ---------- 92
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalll 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  93 ----ISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4942  127 spedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 529006532 169 -----------LKDEARDLRQELAVQQKQEKPRTPMPSSVD 198
Cdd:COG4942  207 elaelaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAG 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-188 1.35e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  27 QRAENTQEELREFQEESREYeAELETQLQQTESKNRDLLMENNHLRMELETIKEKfkTQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG4717   71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPER 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 107 KDKLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAF-----LESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLateeeLQDLAEELEELQQRLAELEEELEEAQEELE 223


                 ....*..
gi 529006532 182 VQQKQEK 188
Cdd:COG4717  224 ELEEELE 230
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1-201 1.74e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    1 MADSGKTFSSEEEEANYWKDLAMTykQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLlmenNHLRMELETIKE 80
Cdd:COG4913   257 IRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARL----DALREELDELEA 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   81 kfktQHSE-GYRQISALEDDLAQTKAIKDKLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEK 159
Cdd:COG4913   331 ----QIRGnGGDRLEQLEREIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 529006532  160 EN----LLESVQRLKDEARDLRQELAVQQKQekpRTPMPSSVDAER 201
Cdd:COG4913   404 EEalaeAEAALRDLRRELRELEAEIASLERR---KSNIPARLLALR 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-191 2.14e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 2.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532     1 MADSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEA---ELETQLQQTESKNRDLLMENNHLRMELET 77
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    78 IKEKFktqhSEGYRqiSALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQrLNqaiERNAFLESELD 157
Cdd:TIGR02168  941 LQERL----SEEYS--LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE-LK---ERYDFLTAQKE 1010

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 529006532   158 E----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-173 2.98e-06

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: 49.30  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEA-----------------ELETQLQQTESKNRDLLMENNHLRM 73
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    74 ELETIKEKFKTQHSEgyrqISALEDDLAQTKAIK------DKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIE 147
Cdd:TIGR02169  918 RLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993

                          170       180
                   ....*....|....*....|....*.
gi 529006532   148 RNAFLESELDEKENLLESVQRLKDEA 173
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKREV 1019
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-188 3.03e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREyeaeLETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQTKA 105
Cdd:COG1196  294 LAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEE----LEEAEAELAEAEE 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEE 442


                 ...
gi 529006532 186 QEK 188
Cdd:COG1196  443 ALE 445
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 30-188 3.79e-06

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: 48.48  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   30 ENTQEELREFQEESREYEAELE---TQLQQTESKNRDLLMENNHLRMELETIK-EKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSekqKELEQNNKKIKELEKQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  106 IKDKLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404


                  ....
gi 529006532  185 KQEK 188
Cdd:TIGR04523 405 KLNQ 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-180 4.43e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 4.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    27 QRAENTQEELREFQEES-----REYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKfKTQHSEGYRQISALEDDLA 101
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529006532   102 QTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 19-188 4.86e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 47.75  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  19 KDLAMTYKQRAENTQEELREFQEESREYEAELETQlqqtESKNRDLLMENN--HLRMELETIKEKFKTQHSEgyrQISAL 96
Cdd:cd22656  127 LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETL----EKALKDLLTDEGgaIARKEIKDLQKELEKLNEE---YAAKL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  97 EDDLAQTKAIKDKLQKYIRELEQANDDLERAKratiMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLLESVQRl 169
Cdd:cd22656  200 KAKIDELKALIADDEAKLAAALRLIADLTAAD----TDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLLEDDIS- 274

                        170
                 ....*....|....*....
gi 529006532 170 kDEARDLRQELAVQQKQEK 188
Cdd:cd22656  275 -KIPAAILAKLELEKAIEK 292
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-190 6.13e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 48.30  E-value: 6.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    20 DLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    93 -ISALEDDLAQTKAIKDKLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 529006532   154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-181 6.45e-06

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: 6.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    27 QRAENTQEELREFQEESREYEA--------ELETQLQQTESKnrdllmennhlRMELETIKEKFKTQHSEGYRQISALED 98
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGyellkekeALERQKEAIERQ-----------LASLEEELEKLTEEISELEKRLEEIEQ 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    99 DLAQ-TKAIKDK-------LQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EK 159
Cdd:TIGR02169  273 LLEElNKKIKDLgeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRR 352

                          170       180
                   ....*....|....*....|..
gi 529006532   160 ENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELE 374
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-188 1.08e-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: 47.37  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532     1 MADSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLlmenNHLRMELETIK- 79
Cdd:TIGR02169  711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    80 --------------EKFKTQHSEGYRQISALEDDLA---QTKAIKDK----LQKYIRELE-------QANDDLERAKRAT 131
Cdd:TIGR02169  787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLNrltLEKEYLEKeiqeLQEQRIDLKeqiksieKEIENLNGKKEEL 866

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 529006532   132 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-181 1.30e-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: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    12 EEEANYWKDLAMTYKQRAENTQEELREFQEESREYE---AELETQLQQTESKNRDLLMENNHLRMELETIKEKFK-TQHS 87
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELEsrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErLEDR 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    88 EGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ 167
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495

                          170
                   ....*....|....
gi 529006532   168 RLKDEARDLRQELA 181
Cdd:TIGR02168  496 RLQENLEGFSEGVK 509
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-253 1.37e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMEnnhlrmeleTIKEKFKTQHSEGY-------RQISALED 98
Cdd:COG3883   50 NEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGE---------RARALYRSGGSVSYldvllgsESFSDFLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  99 DLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:COG3883  120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529006532 179 ELAVQQKQEKPRTPMPSSVDAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGTFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883  200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-181 1.41e-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: 46.98  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEK---FKTQHS 87
Cdd:TIGR02169  771 EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIK 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    88 EGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQaiernafLESELDEKENLLEsvq 167
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRLS--- 920

                          170
                   ....*....|....
gi 529006532   168 RLKDEARDLRQELA 181
Cdd:TIGR02169  921 ELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-187 1.58e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  37 REFQEESREYEAEL--------ETQLQQTESKNRDLLMENNHLRMELETIK---EKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                 ..
gi 529006532 186 QE 187
Cdd:COG1196  376 EA 377
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-191 1.87e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  74 ELETIKEKFKTQhSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRA--TIMSLEDFEQRLNQAIERNAF 151
Cdd:COG4717   72 ELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 529006532 152 LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-186 5.42e-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: 44.75  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  95 ALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 174
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93

                         90
                 ....*....|..
gi 529006532 175 DLRQELAVQQKQ 186
Cdd:COG4942   94 ELRAELEAQKEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-181 6.28e-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: 45.05  E-value: 6.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    24 TYKQRAENTQEELREFQEESREYEAELETqlqqtesknrdLLMENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQT 103
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEE-----------LRLEVSELEEEIEELQKELYALANE----ISRLEQQKQIL 307

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006532   104 KAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 91-163 8.83e-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: 43.98  E-value: 8.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006532  91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG4942   34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-187 9.81e-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: 44.28  E-value: 9.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQTKA 105
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELES 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEAR--DLRQELAVQ 183
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEEL 452


                   ....
gi 529006532   184 QKQE 187
Cdd:TIGR02168  453 QEEL 456
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 28-187 1.21e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.73  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   28 RAENTQEELREFQEEsreyEAELetqLQQTESKNRDLLMEnnhlRMELETIKEKFKTQHSEGYRQISALEDDLAQTKAIK 107
Cdd:pfam07888  28 RAELLQNRLEECLQE----RAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELESRVAELKEELRQSREKH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  108 DKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEARdlrqELAVQQKQE 187
Cdd:pfam07888  97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK----KAGAQRKEE 169
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 19-188 1.22e-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: 43.95  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    19 KDLAMTYKQRAENTQEEL-REFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALE 97
Cdd:pfam15921  244 EDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    98 DDLAQtkaIKDKLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLR 177
Cdd:pfam15921  324 STVSQ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKRE 390

                          170
                   ....*....|.
gi 529006532   178 QELAVQQKQEK 188
Cdd:pfam15921  391 KELSLEKEQNK 401
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 30-185 2.15e-04

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: 43.17  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   30 ENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGyrqiSALEDDLA-QTKAIKD 108
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ----KALEEDLQiATKTICQ 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  109 KLQKYIRELEQANddleRAK----------RATIMSLEDF----EQRLNQAIERNAFLESELDEKENLLESVQRLKD--- 171
Cdd:pfam05483 329 LTEEKEAQMEELN----KAKaahsfvvtefEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnke 404

                         170
                  ....*....|....*
gi 529006532  172 -EARDLRQELAVQQK 185
Cdd:pfam05483 405 vELEELKKILAEDEK 419
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-168 2.40e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  28 RAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELetikekfktqhsEGYRQISALEDDLAQTKAIK 107
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKELAEQLKELE 509

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006532 108 DKLQKY-IRELEQANDDLERAK------RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:PRK03918 510 EKLKKYnLEELEKKAEEYEKLKekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-171 2.52e-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: 41.83  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLM------ENNHLRMELETIKekfktqhsegyRQISALEDD 99
Cdd:COG1579   44 EARLEAAKTELEDLEKEIKRLELEIE-EVEARIKKYEEQLGnvrnnkEYEALQKEIESLK-----------RRISDLEDE 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006532 100 LAQTKAIKDKLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 171
Cdd:COG1579  112 ILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
mukB PRK04863
chromosome partition protein MukB;
13-186 3.45e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   13 EEANYWKDLAmtykqraENTQEELREFQEESREYEAELETQLQQTESKnrdLLMENNHlrmeletikekfKTQHSEGYRQ 92
Cdd:PRK04863  424 ERAKQLCGLP-------DLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAA------------HSQFEQAYQL 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   93 ISALEDDLAQTKA---IKDKLQKY----------------IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLE 153
Cdd:PRK04863  482 VRKIAGEVSRSEAwdvARELLRRLreqrhlaeqlqqlrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELE 557

                         170       180       190
                  ....*....|....*....|....*....|...
gi 529006532  154 SELDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK04863  558 QLQEELEARLESLSESVSEARERRMALRQQLEQ 590
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-174 3.53e-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: 41.45  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESreyeAELETQLQQTESKNRDLLMENNHLRMELETIK---EKFKTQHSEG--YRQISALEDDL 100
Cdd:COG1579   23 EHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVrnNKEYEALQKEI 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529006532 101 AQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 174
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-189 4.39e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    34 EELREFQEESREyeAELETQLQQTESKNRDLLmennhlrmELETIKEKFKTQHSEGYRQISALEDDLAQTKAIKDKLQKY 113
Cdd:TIGR02168  213 ERYKELKAELRE--LELALLVLRLEELREELE--------ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006532   114 IRELEQANDDLERAkratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:TIGR02168  283 IEELQKELYALANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-180 5.75e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  12 EEEANYWKDLAMTYKQRAENTQEELREFQEEsreyEAELETQLQQTEsKNRDLLMENNHLRMELETIKEKFKTQH----- 86
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAelnde 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  87 -----SEGYRQISALEDD-----LAQTKAIKDKLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:PRK02224 625 rrerlAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALE 704

                        170       180
                 ....*....|....*....|....*..
gi 529006532 154 SELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK02224 705 NRVEALEALYDEAEELESMYGDLRAEL 731
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 38-84 6.10e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 41.36  E-value: 6.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 529006532  38 EFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIK---EKFKT 84
Cdd:PRK03992   1 ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKselEKLKS 50
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
138-193 7.22e-04

Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 39.95  E-value: 7.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 529006532 138 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 193
Cdd:COG3166   43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-192 7.28e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  19 KDLAMTYKQRAENTQEELREFQEESREYEAELET------QLQQTESKNRDLLMENNHLRMELETIKEKFKTQHS---EG 89
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKlekevkELEELKEEIEELEKELESLEGSKRKLEEKIRELEErieEL 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  90 YRQISALEDDLAQTKAIKDKLQKYIReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------EL 156
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkEL 350

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 529006532 157 DEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTP 192
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-188 8.86e-04

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: 41.16  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   25 YKQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDdlaQTK 104
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIE-RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR---SIN 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  105 AIKDKLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQEL- 180
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDFELk 555

                         170
                  ....*....|....
gi 529006532  181 ------AVQQKQEK 188
Cdd:TIGR04523 556 kenlekEIDEKNKE 569
COG5022 COG5022
Myosin heavy chain [General function prediction only];
6-197 1.50e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    6 KTFSSEEEEAnywkdLAMTYKQRAENTQEELREFQEESREYeaeleTQLQQTESKNRDLLMENNHLRMELETIKEKFKTQ 85
Cdd:COG5022   859 KRFSLLKKET-----IYLQSAQRVELAERQLQELKIDVKSI-----SSLKLVNLELESEIIELKKSLSSDLIENLEFKTE 928

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   86 HSEGY------RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAkratIMSLEDFEQRLNQAIERNAFLESELDEK 159
Cdd:COG5022   929 LIARLkkllnnIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDL----LKKSTILVREGNKANSELKNFKKELAEL 1004

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 529006532  160 ENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSV 197
Cdd:COG5022  1005 SKQYGALQESTKQLKELPVEVAELQSASKIISSESTEL 1042
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 11-173 1.53e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.33  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  11 EEEEANYWKDLAMTYKQRAENTQE-------ELREFQEESREYEAELETQLQQTESKNRDLLME----NNHLRMELETIK 79
Cdd:COG5185  281 NENANNLIKQFENTKEKIAEYTKSidikkatESLEEQLAAAEAEQELEESKRETETGIQNLTAEieqgQESLTENLEAIK 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  80 EKFKtqHSEGYRQISALEDDLaqtKAIKDKLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEK 159
Cdd:COG5185  361 EEIE--NIVGEVELSKSSEEL---DSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQA 432

                        170
                 ....*....|....
gi 529006532 160 ENLLESVQRLKDEA 173
Cdd:COG5185  433 TSSNEEVSKLLNEL 446
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 91-190 1.57e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   91 RQISALEDDLAQTKAIKDKLqkyiRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG3096   502 RRYRSQQALAQRLQQLRAQL----AELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573

                          90       100
                  ....*....|....*....|
gi 529006532  171 DEARDLRQELAVQQKQEKPR 190
Cdd:COG3096   574 AEAVEQRSELRQQLEQLRAR 593
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 142-204 1.67e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 39.58  E-value: 1.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006532 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVDAERTDT 204
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-185 1.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  10 SEEEEanywKDLAMTYKQRAENTQEELREFQEESREYEAE---LETQLQQTE--SKNRDLLMENNHLRMELETIKEKFKT 84
Cdd:PRK03918 446 TEEHR----KELLEEYTAELKRIEKELKEIEEKERKLRKElreLEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELE 521

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  85 QHSEGYR-----------QISALEDDLAQTKAIKDKLQKYIRELEQANDDLE----RAKRATIMSLEDFE---QRLNQAI 146
Cdd:PRK03918 522 KKAEEYEklkekliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAellkELEELGFESVEELEerlKELEPFY 601

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 529006532 147 ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 39-234 1.84e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.71  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   39 FQEESREYEA---ELETQLQQTESKnrdllmennhlRMELETIKEKFKTQHSEGYRQISALEDDLAQTKAIKDKLQKYIR 115
Cdd:pfam00529  49 FQLDPTDYQAaldSAEAQLAKAQAQ-----------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  116 ELEQANDDLERAK-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprt 191
Cdd:pfam00529 118 QLAQAQIDLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ----- 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 529006532  192 pmPSSVDAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGTFRR 234
Cdd:pfam00529 193 --IAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-176 1.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  27 QRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG1196  682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006532 107 KDKLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 176
Cdd:COG1196  762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-186 2.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  25 YKQRAENTQEELREFQEESREYE------AELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgYRQISALED 98
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-VKELEELKE 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  99 DLAQTKAIKDKLQKYIRELEQANDDLER---AKRATIMSLEDFEQRLNQaIERNAFLESELDE-KENLLESVQRLKDEAR 174
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEErieELKKEIEELEEKVKELKE-LKEKAEEYIKLSEfYEEYLDELREIEKRLS 317

                        170
                 ....*....|..
gi 529006532 175 DLRQELAVQQKQ 186
Cdd:PRK03918 318 RLEEEINGIEER 329
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 21-188 2.38e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    21 LAMTYKQRA-ENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHsegyRQISALEDD 99
Cdd:pfam01576  485 LNLSTRLRQlEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ----RELEALTQQ 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   100 LAQTKAIKDKLQKYIRELEQANDDLERA---KRATIMSLEDFEQRLNQ--AIERNAFL---------ESELDEKENLLES 165
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDldhQRQLVSNLEKKQKKFDQmlAEEKAISAryaeerdraEAEAREKETRALS 640

                          170       180
                   ....*....|....*....|...
gi 529006532   166 VQRLKDEARDLRQELAVQQKQEK 188
Cdd:pfam01576  641 LARALEEALEAKEELERTNKQLR 663
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-186 2.44e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  12 EEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELET----------QLQQTESKNRDLLMENNHLRMELETIKEK 81
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerfgdapvDLGNAEDFLEELREERDELREREAELEAT 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  82 FKT---------------------QHSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKratimSLEDFEQ 140
Cdd:PRK02224 435 LRTarerveeaealleagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-----DLVEAED 509

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 529006532 141 RLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREA 559
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-196 3.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   33 QEELREFQEESREYEAELEtQLQQTESKNRDLLMENNHLRMELETIKEKFKTQhsegyRQISALE----------DDLAQ 102
Cdd:COG4913   616 EAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEaelerldassDDLAA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  103 TKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIER--------NAFLESELDEK--------------E 160
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRALLEERfaaalgdaverelrE 769

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 529006532  161 NLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSS 196
Cdd:COG4913   770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-186 3.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLN--QAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLAA 689

                          90
                  ....*....|....*...
gi 529006532  169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4913   690 LEEQLEELEAELEELEEE 707
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-190 3.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  21 LAMTYKQRAENTQEELREFQEESREYEAELE---TQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgyrqISALE 97
Cdd:COG4372   25 LIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE----LAQAQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  98 DDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR--LKDEARD 175
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAE 180

                        170
                 ....*....|....*
gi 529006532 176 LRQELAVQQKQEKPR 190
Cdd:COG4372  181 AEQALDELLKEANRN 195
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 19-187 3.51e-03

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: 39.32  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   19 KDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDL------LMENNHL---RMELETIKEKFKTQHSEG 89
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELeelkkiLAEDEKLldeKKQFEKIAEELKGKEQEL 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   90 YRQISALEDDL----AQTKAIKDKLQKYIRELEQANDDLERAKRATI--------MSLED-----------FEQRLNQAI 146
Cdd:pfam05483 442 IFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltahcdkLLLENkeltqeasdmtLELKKHQED 521

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 529006532  147 ERNAFLESE--LDEKENLLESVQRLKDEARDLRQELaVQQKQE 187
Cdd:pfam05483 522 IINCKKQEErmLKQIENLEEKEMNLRDELESVREEF-IQKGDE 563
PRK12704 PRK12704
phosphodiesterase; Provisional
 22-172 3.58e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  22 AMTYKQRAE-NTQEEL----REFQEESREYEAEL---ETQLQQTESKNRDLLMENNHLRMELETIKEkfktqhsegyrQI 93
Cdd:PRK12704  51 AEAIKKEALlEAKEEIhklrNEFEKELRERRNELqklEKRLLQKEENLDRKLELLEKREEELEKKEK-----------EL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  94 SALEDDLAQTKA-IKDKLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESV 166
Cdd:PRK12704 120 EQKQQELEKKEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAI 198


                 ....*.
gi 529006532 167 QRLKDE 172
Cdd:PRK12704 199 QRCAAD 204
PRK14160 PRK14160
heat shock protein GrpE; Provisional
 1-188 3.77e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237629 [Multi-domain]  Cd Length: 211  Bit Score: 38.20  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   1 MADSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEE--SREYEAELETQLQQTESKNRDLLMENNHLRMELETI 78
Cdd:PRK14160   1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEeiIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  79 KEKFK--TQHSEGYRQISALEDDLAQTKAIKDKLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 151
Cdd:PRK14160  81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 529006532 152 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
30-185 4.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  30 ENTQEELREFQEESREYEAELETQLQQTESKNRDLLmENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQTKAIKDK 109
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEE 644

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006532 110 LQKYIRELEQANDDLE-RAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK03918 645 LRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEE---LEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
26-181 5.27e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532  26 KQRAENTQEELREFQEESREYEAELETQLQQTESKnRDLLMENNHLRMEL-ETIKEkFKTQHSEGYRQISALEDDLAQTK 104
Cdd:COG1340   21 REEIEELKEKRDELNEELKELAEKRDELNAQVKEL-REEAQELREKRDELnEKVKE-LKEERDELNEKLNELREELDELR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532 105 AIKDKLQKY---IRELEQANDDLERAKRATIMSLEDfEQRLNQAIERnafLESELDEKE----------NLLESVQRLKD 171
Cdd:COG1340   99 KELAELNKAggsIDKLRKEIERLEWRQQTEVLSPEE-EKELVEKIKE---LEKELEKAKkalekneklkELRAELKELRK 174

                        170
                 ....*....|
gi 529006532 172 EARDLRQELA 181
Cdd:COG1340  175 EAEEIHKKIK 184
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 34-186 6.45e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.07  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    34 EELREFQEESREYEAELETQLQQTE----------SKNRDLLMEN------NHLRME------------LETIKEKFKTQ 85
Cdd:smart00787  73 KELKKYISEGRDLFKEIEEETLINNpplfkeyfsaSPDVKLLMDKqfqlvkTFARLEakkmwyewrmklLEGLKEGLDEN 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    86 HS---EGYRQISA----LEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSL-EDFEQRLNQAIERNAFLESELD 157
Cdd:smart00787 153 LEglkEDYKLLMKelelLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLEELEE 232

                          170       180
                   ....*....|....*....|....*....
gi 529006532   158 EKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEKK 261
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 97-176 7.17e-03

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 35.74  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532   97 EDDLAQTKAIKDKLQKYIRELEQANDDLERA---------KRATIMSLEDFEQRlnqAIERNAF-LESELDEKENLLESV 166
Cdd:pfam15898   7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83

                          90
                  ....*....|
gi 529006532  167 QRLKDEARDL 176
Cdd:pfam15898  84 QRLKDENGAL 93
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 26-180 9.08e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 37.85  E-value: 9.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLL----------MENNHLRMELETIKEKFKTQHSEGYRQISA 95
Cdd:pfam01576  351 RQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQaelrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAE 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006532    96 LEDdlaqtkaikdKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARD 175
Cdd:pfam01576  431 LAE----------KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500


                   ....*
gi 529006532   176 LRQEL 180
Cdd:pfam01576  501 LQEQL 505
YabA COG4467
Regulator of replication initiation timing YabA [Replication, recombination and repair];
19-90 9.36e-03

Regulator of replication initiation timing YabA [Replication, recombination and repair];


Pssm-ID: 443564 [Multi-domain]  Cd Length: 107  Bit Score: 35.23  E-value: 9.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006532  19 KDLAMTYKQRAENTQEELREFQEesreyeaeLETQLQQTESKNRDLLMENNHLRMELETI----KEKFKTQHSEGY 90
Cdd:COG4467    4 KELFDRLSELEEQLGELLKELGE--------LKDEVAELLEENARLRIENEHLRERLEELekkkEKKAEKDIGEGY 71
 
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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