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Conserved domains on  [gi|1191017796|ref|NP_001338486|]
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coiled-coil domain-containing protein 138 isoform 12 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12704 super family cl36166
phosphodiesterase; Provisional
172-296 2.33e-04

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 172 ISQIYDELFQihLKLQCETAAQQKFaEELQKRERFLLEREQLLFRHENALSKIkgvEEEVLTRFQIIKEQHDaEVEHLTE 251
Cdd:PRK12704   59 LLEAKEEIHK--LRNEFEKELRERR-NELQKLEKRLLQKEENLDRKLELLEKR---EEELEKKEKELEQKQQ-ELEKKEE 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191017796 252 VLKEK-NKETKRLR-----SSFDALKELNDTLKKQL-NEASEENRKIDIQAK 296
Cdd:PRK12704  132 ELEELiEEQLQELErisglTAEEAKEILLEKVEEEArHEAAVLIKEIEEEAK 183
 
Name Accession Description Interval E-value
PRK12704 PRK12704
phosphodiesterase; Provisional
172-296 2.33e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 172 ISQIYDELFQihLKLQCETAAQQKFaEELQKRERFLLEREQLLFRHENALSKIkgvEEEVLTRFQIIKEQHDaEVEHLTE 251
Cdd:PRK12704   59 LLEAKEEIHK--LRNEFEKELRERR-NELQKLEKRLLQKEENLDRKLELLEKR---EEELEKKEKELEQKQQ-ELEKKEE 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191017796 252 VLKEK-NKETKRLR-----SSFDALKELNDTLKKQL-NEASEENRKIDIQAK 296
Cdd:PRK12704  132 ELEELiEEQLQELErisglTAEEAKEILLEKVEEEArHEAAVLIKEIEEEAK 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
192-307 6.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 192 AQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTrfqiIKEQHDAEVEHLTEVLKEKNKETKRLRSSFDALK 271
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1191017796 272 ELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 307
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-307 8.34e-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: 8.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  189 ETAAQQKFAE-ELQKRERFLLEREQLLFRHE--NALSKIKGVEEEVLTRFQII----KEQHDAEVEHLTEVLKEKNKETK 261
Cdd:TIGR02168  371 ESRLEELEEQlETLRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQEIeellKKLEEAELKELQAELEELEEELE 450
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1191017796  262 RLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 307
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
185-335 1.00e-03

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: 42.13  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  185 KLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEQHDAEVEHLTEVLkEKNKETKRL- 263
Cdd:pfam12128  331 HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL-AKIREARDRq 409
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191017796  264 ----RSSFDALK-ELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRLKGSshAVHEMKSlKQEKA 335
Cdd:pfam12128  410 lavaEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDE--RIERARE-EQEAA 483
 
Name Accession Description Interval E-value
PRK12704 PRK12704
phosphodiesterase; Provisional
172-296 2.33e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 172 ISQIYDELFQihLKLQCETAAQQKFaEELQKRERFLLEREQLLFRHENALSKIkgvEEEVLTRFQIIKEQHDaEVEHLTE 251
Cdd:PRK12704   59 LLEAKEEIHK--LRNEFEKELRERR-NELQKLEKRLLQKEENLDRKLELLEKR---EEELEKKEKELEQKQQ-ELEKKEE 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191017796 252 VLKEK-NKETKRLR-----SSFDALKELNDTLKKQL-NEASEENRKIDIQAK 296
Cdd:PRK12704  132 ELEELiEEQLQELErisglTAEEAKEILLEKVEEEArHEAAVLIKEIEEEAK 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
192-307 6.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 192 AQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTrfqiIKEQHDAEVEHLTEVLKEKNKETKRLRSSFDALK 271
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1191017796 272 ELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 307
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-307 8.34e-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: 8.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  189 ETAAQQKFAE-ELQKRERFLLEREQLLFRHE--NALSKIKGVEEEVLTRFQII----KEQHDAEVEHLTEVLKEKNKETK 261
Cdd:TIGR02168  371 ESRLEELEEQlETLRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQEIeellKKLEEAELKELQAELEELEEELE 450
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1191017796  262 RLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 307
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
185-335 1.00e-03

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: 42.13  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  185 KLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEQHDAEVEHLTEVLkEKNKETKRL- 263
Cdd:pfam12128  331 HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL-AKIREARDRq 409
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191017796  264 ----RSSFDALK-ELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRLKGSshAVHEMKSlKQEKA 335
Cdd:pfam12128  410 lavaEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDE--RIERARE-EQEAA 483
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
171-317 1.25e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 171 QISQIYDELFQIHLKLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEQHDAevehLT 250
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE----LQ 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191017796 251 EVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRL 317
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
181-333 1.66e-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: 41.48  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  181 QIHLkLQCETAAQQkfAEELQKRERFLLEREQLLFRHENALSKIkgveEEVLTRFQIIKEQHDAevehLTEVLKEKNKET 260
Cdd:COG3096    882 QANL-LADETLADR--LEELREELDAAQEAQAFIQQHGKALAQL----EPLVAVLQSDPEQFEQ----LQADYLQAKEQQ 950
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  261 KRLRSSFDALKE----------------------LNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRkyefmTIQRLK 318
Cdd:COG3096    951 RRLKQQIFALSEvvqrrphfsyedavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-----VLASLK 1025
                          170
                   ....*....|....*.
gi 1191017796  319 GSSHAVHEM-KSLKQE 333
Cdd:COG3096   1026 SSRDAKQQTlQELEQE 1041
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
181-335 2.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 181 QIHLKLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEvLTRFQIIKEQHDAEVEHLTEVLKEKNKET 260
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEAL 367
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191017796 261 KRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRLKGSSHAVHEMKSLKQEKA 335
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
195-398 2.94e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  195 KFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLT--RFQIIKEQHDAEVEHLTEVLKEKNKETKRLRSSFDALKE 272
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDeiKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKN 1187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796  273 LNDTLKKQLNEAS---------EENRKIDIQ-----AKRVQARLDNLQRKYEFMtiqrLKGSSHAVHEMKSLKQEKAPVS 338
Cdd:TIGR01612 1188 IYDEIKKLLNEIAeiekdktslEEVKGINLSygknlGKLFLEKIDEEKKKSEHM----IKAMEAYIEDLDEIKEKSPEIE 1263
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191017796  339 KTYKVPLNGQV-YELLTVFMDWISDHHLSKVKHEESGMDGKKPQLKFA------SQRNDIQEKCVKH 398
Cdd:TIGR01612 1264 NEMGIEMDIKAeMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIedfseeSDINDIKKELQKN 1330
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
198-335 3.47e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 198 EELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQiiKEQHdaevEHLTEVLKEKNKETKRLRSSFDALKELNDTL 277
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEY----EELREEYLELSRELAGLRAELEELEKRREEI 692
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1191017796 278 KKQLNEASEENRKIdiqaKRVQARLDNLQRKYEFMTIQRLKgsshaVHEMKSLKQEKA 335
Cdd:PRK03918  693 KKTLEKLKEELEER----EKAKKELEKLEKALERVEELREK-----VKKYKALLKERA 741
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
157-316 3.81e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 157 PKSKASDKRSLLPHQISQIYDELFQIH-----LKLQCETaaQQKFAEELQKR---------ERFLLEREQLLFRHENalS 222
Cdd:pfam05622  53 SGTPGGKKYLLLQKQLEQLQEENFRLEtarddYRIKCEE--LEKEVLELQHRneeltslaeEAQALKDEMDILRESS--D 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 223 KIKGVEEEVLT-----------RFQI-IKEQHDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRK 290
Cdd:pfam05622 129 KVKKLEATVETykkkledlgdlRRQVkLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADK 208
                         170       180
                  ....*....|....*....|....*.
gi 1191017796 291 IDIQAKRVQARLDNLQRKYEFMTIQR 316
Cdd:pfam05622 209 LEFEYKKLEEKLEALQKEKERLIIER 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
183-310 5.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 183 HLKLQCETAAQQKFAEELQKRErfLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEQHDAEVEHLTEVLKEKNKETKR 262
Cdd:COG1196   264 ELEAELEELRLELEELELELEE--AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1191017796 263 LRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYE 310
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
171-311 5.63e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 171 QISQIYDELFQIHLKLQcetAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVltrfQIIKEQHDAEVEHLT 250
Cdd:COG1196   268 ELEELRLELEELELELE---EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELE 340
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191017796 251 EVLKEKNKETKRLRSsfdALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEF 311
Cdd:COG1196   341 ELEEELEEAEEELEE---AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
171-312 6.79e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017796 171 QISQIYDELFQIHLKLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIK------GVEEEVLTRFQIIKEQH-- 242
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkeNLEKEIDEKNKEIEELKqt 576
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191017796 243 ----DAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFM 312
Cdd:TIGR04523 577 qkslKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
 
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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