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Conserved domains on  [gi|767929950|ref|XP_011512209|]
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coiled-coil domain-containing protein 149 isoform X3 [Homo sapiens]

Protein Classification

coiled-coil domain-containing family 149 protein( domain architecture ID 12102062)

coiled-coil domain-containing family 149 (CCDC149) protein is a DUF2353 domain-containing protein similar to Homo sapiens CCDC149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
 1-283 1.52e-121

Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.


:

Pssm-ID: 462902 [Multi-domain]  Cd Length: 314  Bit Score: 357.80  E-value: 1.52e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    1 MANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789  31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   81 G---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767929950  237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
 
Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
 1-283 1.52e-121

Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.


Pssm-ID: 462902 [Multi-domain]  Cd Length: 314  Bit Score: 357.80  E-value: 1.52e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    1 MANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789  31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   81 G---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767929950  237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-195 1.26e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    18 ELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLgevqgdnKLLRMTIAKQRLGDEAIGVRHFAAHER-E 96
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRlE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    97 DLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLH 176
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921

                          170
                   ....*....|....*....
gi 767929950   177 EEVNLLKSNIAKYKNALER 195
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
29-195 3.47e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEaigvRHFAAHEREDLVQQLERAKEQ 108
Cdd:COG4717   79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 109 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:COG4717  155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230


                 ....*...
gi 767929950 188 KYKNALER 195
Cdd:COG4717  231 QLENELEA 238
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 46-184 2.89e-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: 39.62  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    46 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEAIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 113
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767929950   114 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 184
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
mukB PRK04863
chromosome partition protein MukB;
31-195 4.13e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   31 RKQANLAQllRDSQDRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEAIGVRHFAAHE--REDLVQQLER 104
Cdd:PRK04863  506 REQRHLAE--QLQQLRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSE 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  105 AKEQIESLEH---DLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNL 181
Cdd:PRK04863  577 ARERRMALRQqleQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDE 649

                         170
                  ....*....|....
gi 767929950  182 LKSNIAKYKNALER 195
Cdd:PRK04863  650 LAARKQALDEEIER 663
 
Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
 1-283 1.52e-121

Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.


Pssm-ID: 462902 [Multi-domain]  Cd Length: 314  Bit Score: 357.80  E-value: 1.52e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    1 MANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789  31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   81 G---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767929950  237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-195 1.26e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    18 ELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLgevqgdnKLLRMTIAKQRLGDEAIGVRHFAAHER-E 96
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRlE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    97 DLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLH 176
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921

                          170
                   ....*....|....*....
gi 767929950   177 EEVNLLKSNIAKYKNALER 195
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 4-187 2.54e-06

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: 49.89  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    4 QLRERHQSLKKKYRELIDGDPSLPPEKRKqanLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDnkLLRMTIAKQRlgde 83
Cdd:pfam07888  91 QSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETE--LERMKERAKK---- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   84 AIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCM 163
Cdd:pfam07888 162 AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA----HRKEAENEALLE 237

                         170       180
                  ....*....|....*....|....
gi 767929950  164 ENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELS 261
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
29-195 3.47e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEaigvRHFAAHEREDLVQQLERAKEQ 108
Cdd:COG4717   79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 109 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:COG4717  155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230


                 ....*...
gi 767929950 188 KYKNALER 195
Cdd:COG4717  231 QLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-195 5.52e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   42 DSQDRNKHLGEEIKELQQRLGEVQ---GDNKLLRMTIAKQRLGDEAIGVRHF-------AAHEREDLVQQLER------- 104
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQRLAEYSWdeidvasAEREIAELEAELERldassdd 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  105 ---AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNH---ILSGHENRIIDVDALCMENRYLQERL------ 172
Cdd:COG4913   687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALLEERFAAALGdavere 766

                         170       180
                  ....*....|....*....|....*
gi 767929950  173 --KQLHEEVNLLKSNIAKYKNALER 195
Cdd:COG4913   767 lrENLEERIDALRARLNRAEEELER 791
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 91-284 2.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  91 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRII----DVDALCM 163
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELArleqDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 164 ENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgVLSAKQVQDLLSEDHGCSLPATpQSISDLKS 243
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE-EELEELAE 386

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767929950 244 LATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-284 3.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   3 NQLRERHQSLKK------KYRELIDGdpslppEKRKQANLAQL-LRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI 75
Cdd:COG1196  196 GELERQLEPLERqaekaeRYRELKEE------LKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAEL 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  76 AKQRLGDEAigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRI 155
Cdd:COG1196  270 EELRLELEE------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 156 IDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLS--AKQVQDLLSEDHgcslpa 233
Cdd:COG1196  344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEelEEAEEALLERLE------ 417

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767929950 234 tpQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG1196  418 --RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 91-284 8.70e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  91 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIidvdalcmenRYLQE 170
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQEL----------AALEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 171 RLKQLHEEVNLLKSNIAKYKNALERRkNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcSLPATPQSISDLKSLATALLE 250
Cdd:COG4942   84 ELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVR-----RLQYLKYLAPARREQAEELRA 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767929950 251 TIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG4942  158 DLAELAALRAELEAERAELEALLAELEEERAALE 191
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
99-284 9.26e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 9.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  99 VQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsgheNRIIDVDALCMENRYLQERLKQLHEE 178
Cdd:COG4717   73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPER 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 179 VNLLKSNIAKYKNALERRKNSKGQgkssssaltgvlsAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIHEKNMV 258
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAE-------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                        170       180
                 ....*....|....*....|....*.
gi 767929950 259 IQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG4717  215 LEEAQEELEELEEELEQLENELEAAA 240
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-198 9.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 9.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  27 PPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgdeaigvrhfaaHEREDLVQQLERAK 106
Cdd:COG4372   20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------------SELEQLEEELEELN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 107 EQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNI 186
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                        170
                 ....*....|..
gi 767929950 187 AKYKNALERRKN 198
Cdd:COG4372  167 AALEQELQALSE 178
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 52-313 1.25e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  52 EEIKELQQRLGEVQGDNKLLRMTIAKQRlgdeaiGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 131
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALK------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 132 SYQDKVERLNQELNHIL---------------------SGHENRIIDVDALcmeNRYLQERLKQLHEEVNLLKSNIAKYK 190
Cdd:COG4942   94 ELRAELEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYL---APARREQAEELRADLAELAALRAELE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950 191 NALERRKNSKGQGKSSSSALTgvlSAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIheKNMVIQHQRQTNKILG 270
Cdd:COG4942  171 AERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAERTPA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767929950 271 NRVAELEKKLRtlevsglWSLPGlsyNVSVGFGRGKDTILFSD 313
Cdd:COG4942  246 AGFAALKGKLP-------WPVSG---RVVRRFGERDGGGGRNK 278
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 52-281 1.38e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    52 EEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 131
Cdd:TIGR00606  744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   132 SYQ--DKVERLNQELNHILS-GHENRiidvdaLCMENRylQERLKQLHEEVNLLKSNIAKYKNALERRKNSkgqgkssss 208
Cdd:TIGR00606  824 VQQvnQEKQEKQHELDTVVSkIELNR------KLIQDQ--QEQIQHLKSKTNELKSEKLQIGTNLQRRQQF--------- 886

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767929950   209 altgvlsAKQVQDLLSEDHGCsLPATPQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLR 281
Cdd:TIGR00606  887 -------EEQLVELSTEVQSL-IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-286 1.48e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    96 EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQL 175
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   176 HEEVNLLKSNIAKyknaLERRKNSKGQGKSSSSALTGVLsAKQVQDLLSEdhgcsLPATPQSISDLKSLATALLETIHE- 254
Cdd:TIGR02168  315 ERQLEELEAQLEE----LESKLDELAEELAELEEKLEEL-KEELESLEAE-----LEELEAELEELESRLEELEEQLETl 384

                          170       180       190
                   ....*....|....*....|....*....|..
gi 767929950   255 KNMVIQHQRQTNKIlGNRVAELEKKLRTLEVS 286
Cdd:TIGR02168  385 RSKVAQLELQIASL-NNEIERLEARLERLEDR 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-285 1.58e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI--AKQRLGDEAIGVRHF------AAHEREDLVQQ 101
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLeaeveqLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   102 LERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHenriidvDALCMENRYLQERLKQLHEEVNL 181
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-------DELRAELTLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   182 LKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQ--DLLSE--DHGCSLPATPQSISDLKSLATALLETIHEKNM 257
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieELESEleALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260
                   ....*....|....*....|....*...
gi 767929950   258 VIQHQRQTNKILGNRVAELEKKLRTLEV 285
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEV 936
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
 5-172 1.66e-03

TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.


Pssm-ID: 426534  Cd Length: 262  Bit Score: 40.42  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    5 LRERHQSLKKKYRELIDG--------DPSLPPEKRKQANLAQLLRDSQDRN--KHLGEE-IKELQQRLGEVQ-GDNKLLR 72
Cdd:pfam01963  21 LPPSVYPLPPAIEEALEAadtvvvelDLSRYTDPATQAALPKLGLLPDGKTlsDLLSPElYARLQKALAKRGlPLAALDR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   73 M------------TIAKQRLGDEAIGV-RHFA--AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKV 137
Cdd:pfam01963 101 MkpwlaalllslaELAKQKAGLDPDLVdRYLAktAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLDELEKGEDLL 180

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767929950  138 ERLnqeLNHILSGHENRIIDVDALCMENRYLQERL 172
Cdd:pfam01963 181 ETL---VEAWAEGDLEALELEAELKEAYPELYEVL 212
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 29-124 1.84e-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: 40.83  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQ--RLGDEAIGVRHFAAHERE--DLVQQLER 104
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgsKAEDSSLLKQKLEEHLEKlhEAQSELQK 381

                          90       100
                  ....*....|....*....|....
gi 767929950  105 AKEQIESLEHDLQAS----VDELQ 124
Cdd:pfam05622 382 KKEQIEELEPKQDSNlaqkIDELQ 405
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 46-184 2.89e-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: 39.62  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    46 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEAIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 113
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767929950   114 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 184
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-197 3.41e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950    2 ANQLRERHQSLKKKYRELIDGDPSLPPEKRKQ----------------ANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQ 65
Cdd:COG4913   257 IRELAERYAAARERLAELEYLRAALRLWFAQRrlelleaeleelraelARLEAELERLEARLDALREELDELEAQIRGNG 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   66 GDnkllRMTIAKQRLGDeaigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELN 145
Cdd:COG4913   337 GD----RLEQLEREIER--------LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767929950  146 HILSGHENRIIDvdalcmenryLQERLKQLHEEVNLLKSNIAKY-KNALERRK 197
Cdd:COG4913   405 EALAEAEAALRD----------LRRELRELEAEIASLERRKSNIpARLLALRD 447
mukB PRK04863
chromosome partition protein MukB;
31-195 4.13e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   31 RKQANLAQllRDSQDRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEAIGVRHFAAHE--REDLVQQLER 104
Cdd:PRK04863  506 REQRHLAE--QLQQLRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSE 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  105 AKEQIESLEH---DLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNL 181
Cdd:PRK04863  577 ARERRMALRQqleQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDE 649

                         170
                  ....*....|....
gi 767929950  182 LKSNIAKYKNALER 195
Cdd:PRK04863  650 LAARKQALDEEIER 663
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-140 4.68e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950     2 ANQLRERHQSLKKKYRELIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQgdNKLLRMTIAkqrlg 81
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASL---NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELE----- 443

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767929950    82 dEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERL 140
Cdd:TIGR02168  444 -ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-198 5.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   3 NQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRdsqdRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgd 82
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELE--- 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950  83 eaigvrhfaaHEREDLVQQLERAKEQIESLEhDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRIIDVD 159
Cdd:PRK03918 266 ----------ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLeeeINGIEERIKELE 334

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767929950 160 ALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 198
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-157 8.71e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 8.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950   1 MANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKqrl 80
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE--- 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767929950  81 gdeaigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:COG4372  120 ----------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-144 9.53e-03

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: 38.51  E-value: 9.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767929950     4 QLRERHQSLKKKYRELIDgdpSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDE 83
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRA---ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767929950    84 AIGVRHFA-AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQEL 144
Cdd:TIGR02169  431 GIEAKINElEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
 
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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