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Conserved domains on  [gi|1034641777|ref|XP_016864316|]
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coiled-coil domain-containing protein 149 isoform X2 [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 ...
 26-338 2.71e-140

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: 407.10  E-value: 2.71e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHL 105
Cdd:pfam09789   1 KRKLQSKVEALLILSKELEKCRQERDQYKLMAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 106 GEEIKELQQRLGEVQGDNKLLRMTIAKQRLG---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVK 182
Cdd:pfam09789  81 RLEVEELRQKLNEAQGDIKLLREQIARQRLGgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 183 EERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSS 262
Cdd:pfam09789 161 TERDAYKCKAHRLNHELNYILGGDESRIVDIDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNG 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641777 263 SALTGVLSAKQVQDLLsedHGCSLPATPQ-SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 338
Cdd:pfam09789 241 SSGGLVISAKQVKELL---ESGSLSNTPQaTISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
 
Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
 26-338 2.71e-140

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: 407.10  E-value: 2.71e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHL 105
Cdd:pfam09789   1 KRKLQSKVEALLILSKELEKCRQERDQYKLMAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 106 GEEIKELQQRLGEVQGDNKLLRMTIAKQRLG---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVK 182
Cdd:pfam09789  81 RLEVEELRQKLNEAQGDIKLLREQIARQRLGgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 183 EERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSS 262
Cdd:pfam09789 161 TERDAYKCKAHRLNHELNYILGGDESRIVDIDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNG 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641777 263 SALTGVLSAKQVQDLLsedHGCSLPATPQ-SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 338
Cdd:pfam09789 241 SSGGLVISAKQVKELL---ESGSLSNTPQaTISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-250 1.21e-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: 57.76  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKkyrELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLG 106
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  107 EEIKELQQRLgevqgdnKLLRMTIAKQRLGDEAIGVRHFAAHER-EDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:TIGR02168  803 EALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034641777  186 SSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-253 5.19e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDSQDRNKHL 105
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----------EQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 106 GEEIKELQQRLGEV------QGDNKLLRMTIAKQRLGDEAIGVRHFAA--HEREDLVQQLERAKEQIESLEHDLQASVDE 177
Cdd:COG4942    96 RAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAE 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034641777 178 LQDVKEERSSYQDKVERLNQELNHILSGHENRIidvdalcmenRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 253
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKEL----------AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
mukB PRK04863
chromosome partition protein MukB;
26-250 4.92e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLR------ERHQSlKKKYRELIDgdpslppEKRKQANLAQllRDSQ 99
Cdd:PRK04863   448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiagevSRSEA-WDVARELLR-------RLREQRHLAE--QLQQ 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  100 DRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEAIGVRHFAAHE--REDLVQQLERAKEQIESLEH---D 170
Cdd:PRK04863   518 LRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSEARERRMALRQqleQ 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  171 LQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:PRK04863   591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDELAARKQALDEEIER 663
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 101-239 7.06e-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: 38.46  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  101 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEAIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 168
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034641777  169 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 239
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
 
Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
 26-338 2.71e-140

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: 407.10  E-value: 2.71e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHL 105
Cdd:pfam09789   1 KRKLQSKVEALLILSKELEKCRQERDQYKLMAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 106 GEEIKELQQRLGEVQGDNKLLRMTIAKQRLG---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVK 182
Cdd:pfam09789  81 RLEVEELRQKLNEAQGDIKLLREQIARQRLGgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 183 EERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSS 262
Cdd:pfam09789 161 TERDAYKCKAHRLNHELNYILGGDESRIVDIDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNG 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641777 263 SALTGVLSAKQVQDLLsedHGCSLPATPQ-SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 338
Cdd:pfam09789 241 SSGGLVISAKQVKELL---ESGSLSNTPQaTISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-250 1.21e-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: 57.76  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKkyrELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLG 106
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  107 EEIKELQQRLgevqgdnKLLRMTIAKQRLGDEAIGVRHFAAHER-EDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:TIGR02168  803 EALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034641777  186 SSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 26-242 4.66e-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: 49.12  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELdtcQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKqanLAQLLRDSQDRNKHL 105
Cdd:pfam07888  61 KERYKRDREQWERQRREL---ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIREL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 106 GEEIKELQQRLGEVQGDnkLLRMTIAKQRlgdeAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:pfam07888 135 EEDIKTLTQRVLERETE--LERMKERAKK----AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641777 186 SSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 242
Cdd:pfam07888 209 LQLQDTITTLTQKLTTA----HRKEAENEALLEELRSLQERLNASERKVEGLGEELS 261
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-253 5.19e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDSQDRNKHL 105
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----------EQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 106 GEEIKELQQRLGEV------QGDNKLLRMTIAKQRLGDEAIGVRHFAA--HEREDLVQQLERAKEQIESLEHDLQASVDE 177
Cdd:COG4942    96 RAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAE 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034641777 178 LQDVKEERSSYQDKVERLNQELNHILSGHENRIidvdalcmenRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 253
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKEL----------AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
84-250 1.04e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  84 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEaigvRHFAAHEREDLVQQLERAKEQ 163
Cdd:COG4717    79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 164 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 242
Cdd:COG4717   155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230


                  ....*...
gi 1034641777 243 KYKNALER 250
Cdd:COG4717   231 QLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
97-250 1.08e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   97 DSQDRNKHLGEEIKELQQRLGEVQ---GDNKLLRMTIAKQRLGDEAIGVRHF-------AAHEREDLVQQLER------- 159
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQRLAEYSWdeidvasAEREIAELEAELERldassdd 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  160 ---AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNH---ILSGHENRIIDVDALCMENRYLQERL------ 227
Cdd:COG4913    687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALLEERFAAALGdavere 766

                          170       180
                   ....*....|....*....|....*
gi 1034641777  228 --KQLHEEVNLLKSNIAKYKNALER 250
Cdd:COG4913    767 lrENLEERIDALRARLNRAEEELER 791
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-208 1.23e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   21 EYLVCKRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIdgdpslppekrkqanlAQLLRDSQD 100
Cdd:COG4913    275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----------------AQIRGNGGD 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  101 RNKHLGEEIKELQQRLGEVQGdnkllrmtiAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQD 180
Cdd:COG4913    339 RLEQLEREIERLERELEERER---------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409

                          170       180
                   ....*....|....*....|....*...
gi 1034641777  181 VKEERSSYQDKVERLNQELNHILSGHEN 208
Cdd:COG4913    410 AEAALRDLRRELRELEAEIASLERRKSN 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-195 3.39e-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: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLppeKRKQANLAQLLRDSQDRNKHL 105
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARLERLEDRRERL 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  106 GEEIKELQQRLGEVQgdNKLLRMTIAkqrlgdEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:TIGR02168  420 QQEIEELLKKLEEAE--LKELQAELE------ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491

                          170
                   ....*....|
gi 1034641777  186 SSYQDKVERL 195
Cdd:TIGR02168  492 DSLERLQENL 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-203 3.41e-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: 46.60  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDSQDRNKHLG 106
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL----------EEELEELEAALRDLESRLGDLK 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  107 EEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHER---------------------EDLVQQLERAKEQIE 165
Cdd:TIGR02169  889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElseiedpkgedeeipeeelslEDVQAELQRVEEEIR 968

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034641777  166 SLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIL 203
Cdd:TIGR02169  969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-339 3.81e-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: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 146 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRII----DVDALCM 218
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELArleqDIARLEE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 219 ENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgVLSAKQVQDLLSEDHGCSLPATpQSISDLKS 298
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE-EELEELAE 386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034641777 299 LATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
57-252 5.24e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   57 ANQLRERHQSLKKKYRELIDGDPSLPPEKRKQAnlAQLLRDSQDRNKH----LGEEIKELQQRLGEVQGdnKLLRMTIAK 132
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAelarLEAELERLEARLDALRE--ELDELEAQI 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  133 QRLGDEAIGV----RHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEN 208
Cdd:COG4913    333 RGNGGDRLEQlereIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034641777  209 RIIDvdalcmenryLQERLKQLHEEVNLLKSNIAKY-KNALERRK 252
Cdd:COG4913    413 ALRD----------LRRELRELEAEIASLERRKSNIpARLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-339 7.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  58 NQLRERHQSLKK------KYRELIDGdpslppEKRKQANLAQL-LRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI 130
Cdd:COG1196   196 GELERQLEPLERqaekaeRYRELKEE------LKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAEL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 131 AKQRLGDEAIGVRHFAAHERE-DLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENR 209
Cdd:COG1196   270 EELRLELEELELELEEAQAEEyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 210 IIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgvlsAKQVQDLLSEDHgcslpat 289
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-----EEAEEALLERLE------- 417

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034641777 290 pQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG1196   418 -RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 13-265 8.53e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  13 ARAATWDSEYLVCKRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLA 92
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----------EERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  93 QLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLG-DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDL 171
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 172 QASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERR 251
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         250
                  ....*....|....
gi 1034641777 252 KNSKGQGKSSSSAL 265
Cdd:COG1196   483 LEELAEAAARLLLL 496
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-198 1.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKQAnLAQLLRDSQDRNKHLG 106
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-LEAELAELPERLEELE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 107 EEIKELQQRLGEVQGDNKLLRMtiAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 186
Cdd:COG4717   153 ERLEELRELEEELEELEAELAE--LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230

                         170
                  ....*....|..
gi 1034641777 187 SYQDKVERLNQE 198
Cdd:COG4717   231 QLENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-201 1.85e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRElIDGDpslppekrkqaNLAQLLRDSqdrnKHLG 106
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-NGGD-----------RLEQLEREI----ERLE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  107 EEIKELQQRLGEVQGDNKLLRMTIAK-----QRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDV 181
Cdd:COG4913    352 RELEERERRRARLEALLAALGLPLPAsaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431

                          170       180
                   ....*....|....*....|
gi 1034641777  182 KEERSSYQDKVERLNQELNH 201
Cdd:COG4913    432 ERRKSNIPARLLALRDALAE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-199 2.05e-04

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: 44.29  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   25 CKRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRK-QANLAQL---LRDSQD 100
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlRAELEEVdkeFAETRD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  101 RNKHLGEEIKELQQRLGEVQG--DNKLLRMTIAKQRLGD-----EAIGVRHFA-AHEREDLVQQLERAKEQIESLEHDLQ 172
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRelDRLQEELQRLSEELADlnaaiAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS 465

                          170       180
                   ....*....|....*....|....*..
gi 1034641777  173 ASVDELQDVKEERSSYQDKVERLNQEL 199
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQREL 492
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-253 9.16e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLkKKYRELIDGDPSLPPEKRKQANL-AQL--LRDSQDRN 102
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELeAELerLDASSDDL 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  103 KHLGEEIKELQQRLGEVQGDNKLLRMTIAKqrlgdeaigvrhfAAHEREDLVQQLERAKEQIESLEHD------------ 170
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEIGR-------------LEKELEQAEEELDELQDRLEAAEDLarlelralleer 754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  171 -LQASVDEL-----QDVKEERSSYQDKVERLNQELNHILSGH----ENRIIDVDALCMENRYLQERLKQLHEEvnllksN 240
Cdd:COG4913    755 fAAALGDAVerelrENLEERIDALRARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDRLEED------G 828

                          250
                   ....*....|...
gi 1034641777  241 IAKYKNALERRKN 253
Cdd:COG4913    829 LPEYEERFKELLN 841
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 160-339 9.62e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 160 AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSghenriidvdalcmENRYLQERLKQLHEEVNLLKS 239
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA--------------ELEALQAEIDKLQAEIAEAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 240 NIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcslpatpqSISDLKSLATAlletiheKNMVIQHQRQ 319
Cdd:COG3883    80 EIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLD------------RLSALSKIADA-------DADLLEELKA 140

                         170       180
                  ....*....|....*....|
gi 1034641777 320 TNKILGNRVAELEKKLRTLE 339
Cdd:COG3883   141 DKAELEAKKAELEAKLAELE 160
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
13-202 1.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   13 ARAATWDSEYLVCKRKLESKKEALLILSKELDTCQQERDQYKlmaNQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLA 92
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ---DRLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   93 QLLRDSQDRNKhlgEEIKELQQRLGEVQGDNKLlRMTIAKQRLGDEAIGVRHFAAH----EREDLVQQLERAKEQIESLE 168
Cdd:COG4913    769 ENLEERIDALR---ARLNRAEEELERAMRAFNR-EWPAETADLDADLESLPEYLALldrlEEDGLPEYEERFKELLNENS 844

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034641777  169 HDLQASVdeLQDVKEERSSYQDKVERLNQELNHI 202
Cdd:COG4913    845 IEFVADL--LSKLRRAIREIKERIDPLNDSLKRI 876
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 146-339 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 146 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIidvdalcmenRYLQE 225
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQEL----------AALEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 226 RLKQLHEEVNLLKSNIAKYKNALERRkNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcSLPATPQSISDLKSLATALLE 305
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVR-----RLQYLKYLAPARREQAEELRA 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034641777 306 TIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALE 191
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-250 2.12e-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: 40.81  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDsqdrnkhL 105
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----------QKELYALANEISR-------L 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  106 GEEIKELQQRLGEVQGDNKLLRMTIA--KQRLGDeaigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKE 183
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEelESKLDE--------LAEELAELEEKLEELKEELESLEAELEELEAELEELES 372

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641777  184 ERSSYQDKVERLNQELNHILSghenriiDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLEL-------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-339 2.36e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 154 VQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsgheNRIIDVDALCMENRYLQERLKQLHEE 233
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPER 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 234 VNLLKSNIAKYKNALERRKNSKGQgkssssaltgvlsAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIHEKNMV 313
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAE-------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                         170       180
                  ....*....|....*....|....*.
gi 1034641777 314 IQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEAAA 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-341 2.62e-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: 40.81  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  151 EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQL 230
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  231 HEEVNLLKSNIAKyknaLERRKNSKGQGKSSSSALTGVLsAKQVQDLLSEdhgcsLPATPQSISDLKSLATALLETIHE- 309
Cdd:TIGR02168  315 ERQLEELEAQLEE----LESKLDELAEELAELEEKLEEL-KEELESLEAE-----LEELEAELEELESRLEELEEQLETl 384

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034641777  310 KNMVIQHQRQTNKIlGNRVAELEKKLRTLEVS 341
Cdd:TIGR02168  385 RSKVAQLELQIASL-NNEIERLEARLERLEDR 415
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 151-456 2.79e-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: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  151 EDLVQQLERAKEQIESL---EHDLQASVDELQDVKEERSSYQDKVerLNQELNH---ILSGHENRIIDVDALcmENRYLQ 224
Cdd:TIGR01612  807 EDAKQNYDKSKEYIKTIsikEDEIFKIINEMKFMKDDFLNKVDKF--INFENNCkekIDSEHEQFAELTNKI--KAEISD 882

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  225 ERLKQLHEEVNLLKSNIAKYKNALERRknskgqgkssssaLTGVLSAKQVQDLLSEdhgCSlpATPQSISDLKSLATAL- 303
Cdd:TIGR01612  883 DKLNDYEKKFNDSKSLINEINKSIEEE-------------YQNINTLKKVDEYIKI---CE--NTKESIEKFHNKQNILk 944

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  304 ------LETIHEKNMVIQ-HQRQTNKILGNRVAELEKklrtlevsglwslpggkdtiLFSDPTLPSGQRSRSPLLKFVEQ 376
Cdd:TIGR01612  945 eilnknIDTIKESNLIEKsYKDKFDNTLIDKINELDK--------------------AFKDASLNDYEAKNNELIKYFND 1004

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  377 PTENKADPKDGEAQKQEEDESCAAAEALTAPEDagrpavnspANQSRGNQCKLFHPSLPQLpSEEEVNSLGREIIKLTKE 456
Cdd:TIGR01612 1005 LKANLGKNKENMLYHQFDEKEKATNDIEQKIED---------ANKNIPNIEIAIHTSIYNI-IDEIEKEIGKNIELLNKE 1074
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-199 3.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  27 RKLESKKEALLILSKELDTCQQERDQYklmaNQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNK--- 103
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlea 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 104 ---HLGEEIKELQQRLGEVQgdNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQD 180
Cdd:COG4717   140 elaELPERLEELEERLEELR--ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                         170
                  ....*....|....*....
gi 1034641777 181 VKEERSSYQDKVERLNQEL 199
Cdd:COG4717   218 AQEELEELEEELEQLENEL 236
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
 60-227 3.57e-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: 39.26  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  60 LRERHQSLKKKYRELIDG--------DPSLPPEKRKQANLAQLLRDSQDRN--KHLGEE-IKELQQRLGEVQ-GDNKLLR 127
Cdd:pfam01963  21 LPPSVYPLPPAIEEALEAadtvvvelDLSRYTDPATQAALPKLGLLPDGKTlsDLLSPElYARLQKALAKRGlPLAALDR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 128 M------------TIAKQRLGDEAIGV-RHFA--AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKV 192
Cdd:pfam01963 101 MkpwlaalllslaELAKQKAGLDPDLVdRYLAktAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLDELEKGEDLL 180

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034641777 193 ERLnqeLNHILSGHENRIIDVDALCMENRYLQERL 227
Cdd:pfam01963 181 ETL---VEAWAEGDLEALELEAELKEAYPELYEVL 212
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 84-179 4.20e-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: 39.67  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  84 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQ--RLGDEAIGVRHFAAHERE--DLVQQLER 159
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgsKAEDSSLLKQKLEEHLEKlhEAQSELQK 381

                          90       100
                  ....*....|....*....|....
gi 1034641777 160 AKEQIESLEHDLQAS----VDELQ 179
Cdd:pfam05622 382 KKEQIEELEPKQDSNlaqkIDELQ 405
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 26-343 4.39e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  26 KRKLESKKEALLILSKELDT----CQQERDQYKLMA---NQLRERHQSLKKKYRELIDGDPSLppeKRKQANLAQLLRDS 98
Cdd:pfam05557  19 KQMELEHKRARIELEKKASAlkrqLDRESDRNQELQkriRLLEKREAEAEEALREQAELNRLK---KKYLEALNKKLNEK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  99 QDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHERedlVQQLERAKEQIESLEHDLQASVDEL 178
Cdd:pfam05557  96 ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAK---ASEAEQLRQNLEKQQSSLAEAEQRI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 179 QDVKEERSSYQDK---VERLNQELNhilsghenRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSK 255
Cdd:pfam05557 173 KELEFEIQSQEQDseiVKNSKSELA--------RIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777 256 GQGKSSSSALTGVLSAKQVQDLLSEDHGCSLPaTPQSISdlkslatalletihekNMVIQHQrQTNKILGNRVAELEKKL 335
Cdd:pfam05557 245 EEAATLELEKEKLEQELQSWVKLAQDTGLNLR-SPEDLS----------------RRIEQLQ-QREIVLKEENSSLTSSA 306


                  ....*...
gi 1034641777 336 RTLEVSGL 343
Cdd:pfam05557 307 RQLEKARR 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-339 4.54e-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: 40.04  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  149 EREDLVQQLERAKEQIESLEhdlqasvDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLK 228
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELE-------KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  229 QLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTgvlsaKQVQDLLSEdhgcslpatpqsISDLKSLATALLETIH 308
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-----AQIEQLKEE------------LKALREALDELRAELT 813

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034641777  309 EKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLE 844
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 107-336 4.66e-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: 40.03  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  107 EEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 186
Cdd:TIGR00606  744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  187 SYQ--DKVERLNQELNHILS-GHENRiidvdaLCMENRylQERLKQLHEEVNLLKSNIAKYKNALERRKNSkgqgkssss 263
Cdd:TIGR00606  824 VQQvnQEKQEKQHELDTVVSkIELNR------KLIQDQ--QEQIQHLKSKTNELKSEKLQIGTNLQRRQQF--------- 886

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034641777  264 altgvlsAKQVQDLLSEDHGCsLPATPQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLR 336
Cdd:TIGR00606  887 -------EEQLVELSTEVQSL-IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
mukB PRK04863
chromosome partition protein MukB;
26-250 4.92e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLR------ERHQSlKKKYRELIDgdpslppEKRKQANLAQllRDSQ 99
Cdd:PRK04863   448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiagevSRSEA-WDVARELLR-------RLREQRHLAE--QLQQ 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  100 DRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEAIGVRHFAAHE--REDLVQQLERAKEQIESLEH---D 170
Cdd:PRK04863   518 LRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSEARERRMALRQqleQ 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  171 LQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:PRK04863   591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDELAARKQALDEEIER 663
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-242 6.06e-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: 39.67  E-value: 6.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777   38 ILSKELDTCQQERDQyklmanqlRERHQSLKKKYRElIDGDPSLppeKRKQANLAQLlrdsQDRNKHLGEEIKELQQRlg 117
Cdd:TIGR02169  195 EKRQQLERLRREREK--------AERYQALLKEKRE-YEGYELL---KEKEALERQK----EAIERQLASLEEELEKL-- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  118 EVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQdkverlnQ 197
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE-------A 329

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034641777  198 ELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 242
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 101-239 7.06e-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: 38.46  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641777  101 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEAIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 168
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034641777  169 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 239
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
 
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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