|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-255 |
1.39e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 231
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180
....*....|....*....|....
gi 65301130 232 AELAMAKQSLATLTKDVPKRHSLA 255
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-246 |
1.40e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLV 150
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 151 SQMQQLYATLESREEQLRDFIR---NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM 227
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRaaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170
....*....|....*....
gi 65301130 228 KELEAELAMAKQSLATLTK 246
Cdd:COG1196 452 AELEEEEEALLELLAELLE 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-244 |
7.37e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQL--------------AQKEQELARAKEALQAMK 136
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeyellaelARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 137 ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF---IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHA 213
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190
....*....|....*....|....*....|.
gi 65301130 214 TALRSQLDLKDNRMKELEAELAMAKQSLATL 244
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEEL 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-246 |
1.24e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQmkemlakDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG1196 279 LELELEEAQAEEYELLA-------ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 231
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170
....*....|....*
gi 65301130 232 AELAMAKQSLATLTK 246
Cdd:COG1196 432 ELEEEEEEEEEALEE 446
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-239 |
7.23e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLV 150
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 151 SQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKEL 230
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
....*....
gi 65301130 231 EAELAMAKQ 239
Cdd:COG1196 494 LLLLEAEAD 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-246 |
2.14e-08 |
|
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: 56.61 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQ-------MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKG 144
Cdd:TIGR02169 693 LQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 145 EKTDLVSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATAL 216
Cdd:TIGR02169 773 DLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
170 180 190
....*....|....*....|....*....|
gi 65301130 217 RSQLDLKDNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLES 882
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-248 |
6.52e-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: 55.06 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEE-----SQGGKSSEVLSA---------TELRVQLAQKEQELARAKEALQAMKA 137
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISAlrkdlARLEAEVEQLEEriaqlskelTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 138 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 210
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 65301130 211 ---DHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:TIGR02168 863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
113-248 |
6.70e-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: 55.06 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 189
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301130 190 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:TIGR02168 768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-248 |
7.92e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEmLAKDLEESQGGKssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLvs 151
Cdd:COG4913 240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 231
Cdd:COG4913 315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170
....*....|....*..
gi 65301130 232 AELAMAKQSLATLTKDV 248
Cdd:COG4913 387 AEAAALLEALEEELEAL 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-246 |
8.62e-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: 54.68 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 59 RVRADGDCSQPVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-------EVLSATELRVQLAQKEQELARAKEA 131
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 132 LQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKE 208
Cdd:TIGR02168 798 LKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 65301130 209 ATD-------HATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR02168 878 LLNerasleeALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
113-247 |
1.57e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 192
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 65301130 193 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 247
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-250 |
2.43e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 86 LRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREE 165
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 166 QLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD 224
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180
....*....|....*....|....*.
gi 65301130 225 NRMKELEAELAMAKQSLATLTKDVPK 250
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAE 210
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
112-248 |
2.65e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 112 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKE 191
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 65301130 192 KDLLEREKWELRRQAKEatdhataLRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:COG4372 124 RQDLEQQRKQLEAQIAE-------LQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-237 |
3.42e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKE-QELARAKEALQAMKADRKRLKGEKTDL 149
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 150 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 229
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
....*...
gi 65301130 230 LEAELAMA 237
Cdd:COG4913 445 LRDALAEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-247 |
3.98e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLR-----QMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEK 146
Cdd:COG1196 218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 147 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLK 223
Cdd:COG1196 298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180
....*....|....*....|....
gi 65301130 224 DNRMKELEAELAMAKQSLATLTKD 247
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQ 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
72-247 |
6.92e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLE--ESQGGKSSEVLSATElrVQLAQKEQELARAKEALQAMkadRKRLKGEKTDL 149
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALE--QELAALEAELAELEKEIAEL---RAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 150 VSQMQQLYATLESREEQL-------RDFIRN------YEQHRKESEDAVKA----LAKEKDLLEREKWELRRQAKEATDH 212
Cdd:COG4942 107 AELLRALYRLGRQPPLALllspedfLDAVRRlqylkyLAPARREQAEELRAdlaeLAALRAELEAERAELEALLAELEEE 186
|
170 180 190
....*....|....*....|....*....|....*
gi 65301130 213 ATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 247
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-244 |
8.36e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS----EVLSATELRV-----QLAQKEQELARAKEA---LQAMKADR 139
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 140 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 219
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
170 180
....*....|....*....|....*
gi 65301130 220 LdlkDNRMKELEAELAMAKQSLATL 244
Cdd:COG4913 771 L---EERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-249 |
8.77e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 149
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLE--RQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 150 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAlrsqldLKDNRMKE 229
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK------LEEAELKE 437
|
170 180
....*....|....*....|
gi 65301130 230 LEAELAMAKQSLATLTKDVP 249
Cdd:TIGR02168 438 LQAELEELEEELEELQEELE 457
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
72-256 |
9.80e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 149
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 150 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 226
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
170 180 190
....*....|....*....|....*....|
gi 65301130 227 MKELEAELAMAKQSLATLTKDVPKRHSLAM 256
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-234 |
1.20e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 148
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 149 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 218
Cdd:PRK02224 298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377
|
170
....*....|....*.
gi 65301130 219 QLDLKDNRMKELEAEL 234
Cdd:PRK02224 378 AVEDRREEIEELEEEI 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
72-242 |
2.16e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKEL 230
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170
....*....|..
gi 65301130 231 EAELAMAKQSLA 242
Cdd:COG4372 217 AEELLEAKDSLE 228
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-248 |
2.73e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 67 SQPVLLREEVSRLQEEVHllrqMKEMLAKDLE---ESQGGKSSEV-LSATELRVQLAQKEQELARAKEALQAMKADRKRL 142
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDS----VKELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 143 KGEKTDLVSQMqqlyATLESREEQLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHATALRSQL 220
Cdd:TIGR04523 509 EEKVKDLTKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
170 180 190
....*....|....*....|....*....|....*
gi 65301130 221 DLKDNRMKELEAE-------LAMAKQSLATLTKDV 248
Cdd:TIGR04523 585 EEKQELIDQKEKEkkdlikeIEEKEKKISSLEKEL 619
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-248 |
5.96e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvsQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKALAKEK 192
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEER-LEELRELEEEL 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301130 193 DLLEREKWELRRQAKEATDHATA--------LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
113-271 |
7.83e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KE 191
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 192 KDLLE--REKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWV 269
Cdd:TIGR04523 496 KELKKlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEI 570
|
..
gi 65301130 270 VQ 271
Cdd:TIGR04523 571 EE 572
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
113-248 |
9.10e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELA-----RAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVKA 187
Cdd:TIGR02168 217 ELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 65301130 188 LAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-235 |
1.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 115 RVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDF------IRNYEQHRKE---SEDAV 185
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVasaereIAELEAELERldaSSDDL 687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 65301130 186 KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELA 235
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-245 |
1.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 154 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM--KELE 231
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242
|
170
....*....|....
gi 65301130 232 AELAMAKQSLATLT 245
Cdd:COG4717 243 ERLKEARLLLLIAA 256
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
71-246 |
1.23e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQ----GGK----------SSEVLSATELRVQLAQKEQELARAKEALQAMK 136
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEalleAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 137 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAL 216
Cdd:PRK02224 496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
170 180 190
....*....|....*....|....*....|
gi 65301130 217 RSQLDLKDNRMKELEAELAMAKQSLATLTK 246
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
74-244 |
1.35e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVSRLQEEVHLLrqmkemLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 153
Cdd:pfam02463 278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 154 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHATALRSQLDLKDNRMKE 229
Cdd:pfam02463 351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427
|
170
....*....|....*
gi 65301130 230 LEAELAMAKQSLATL 244
Cdd:pfam02463 428 ELEILEEEEESIELK 442
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
72-246 |
1.40e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQmkemlAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 149
Cdd:COG3206 187 LRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlq 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 150 ---VSQMQQLYATLESREEQLRdfiRNY-EQHRKesedaVKALAKEKDLLERekwELRRQAKEAtdhATALRSQLDLKDN 225
Cdd:COG3206 262 spvIQQLRAQLAELEAELAELS---ARYtPNHPD-----VIALRAQIAALRA---QLQQEAQRI---LASLEAELEALQA 327
|
170 180
....*....|....*....|.
gi 65301130 226 RMKELEAELAMAKQSLATLTK 246
Cdd:COG3206 328 REASLQAQLAQLEARLAELPE 348
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-246 |
1.76e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 95 KDLEESQGGKSSEVLsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNY 174
Cdd:TIGR04523 345 SQLKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQ 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301130 175 EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
55-318 |
2.28e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 55 AGVPRVRADGDCSQPV-LLREEVSRLQEEVHLLRQMKEMLAKDLEEsqggKSSEVLSAT-ELRVQLAQKEQELARAKEAL 132
Cdd:pfam15921 640 AGSERLRAVKDIKQERdQLLNEVKTSRNELNSLSEDYEVLKRNFRN----KSEEMETTTnKLKMQLKSAQSELEQTRNTL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 133 QAMK-ADRKRLK---GEKTDLVSQMQQLYAtLESREEQLrdfirnyeqhrkesEDAVKALAKEKDLLEREKWELRRQAKE 208
Cdd:pfam15921 716 KSMEgSDGHAMKvamGMQKQITAKRGQIDA-LQSKIQFL--------------EEAMTNANKEKHFLKEEKNKLSQELST 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 209 ATDHATALRSQLDL---KDNRMKELEA--ELAMAKQSLA-TLTKDVPKRHslampgetvlngnQEWVVQADLPLTAAIRQ 282
Cdd:pfam15921 781 VATEKNKMAGELEVlrsQERRLKEKVAnmEVALDKASLQfAECQDIIQRQ-------------EQESVRLKLQHTLDVKE 847
|
250 260 270
....*....|....*....|....*....|....*..
gi 65301130 283 SQQTLYHSHPP-HPADRQAVRVSPCHSRQPSVISDAS 318
Cdd:pfam15921 848 LQGPGYTSNSSmKPRLLQPASFTRTHSNVPSSQSTAS 884
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
72-259 |
2.80e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggksSEVLSATElrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQAR----SELEQLEE---ELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATalrsqldlkDNRMK 228
Cdd:COG4372 116 ELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA---------EQALD 186
|
170 180 190
....*....|....*....|....*....|.
gi 65301130 229 ELEAELAMAKQSLATLTKDVPKRHSLAMPGE 259
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-208 |
3.34e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 117 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 196
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90
....*....|..
gi 65301130 197 REKWELRRQAKE 208
Cdd:COG4942 97 AELEAQKEELAE 108
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
77-251 |
3.42e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 77 SRLQEEVHLLRQMKEMLAkDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKG---------EKT 147
Cdd:COG1579 17 SELDRLEHRLKELPAELA-ELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 148 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhatalrsqldlkDNRM 227
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEEL 151
|
170 180
....*....|....*....|....
gi 65301130 228 KELEAELAMAKQSLATLTKDVPKR 251
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPE 175
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
66-229 |
3.78e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 66 CSQPVLLREEVSRLQEEVHLLRQMKEMLAKdleesqggKSSEVLSATELRvqlAQKEQELARAKEAL---QAMKADRKRL 142
Cdd:pfam05483 359 CSLEELLRTEQQRLEKNEDQLKIITMELQK--------KSSELEEMTKFK---NNKEVELEELKKILaedEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 143 KGEKTDLVSQMQQLYATLESREEQLRDF------IRNYEQH-RKESEDAVKALAKEK----------DLLEREKWELrrq 205
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLeiqltaIKTSEEHyLKEVEDLKTELEKEKlknieltahcDKLLLENKEL--- 504
|
170 180
....*....|....*....|....*
gi 65301130 206 AKEATDHATALRS-QLDLKDNRMKE 229
Cdd:pfam05483 505 TQEASDMTLELKKhQEDIINCKKQE 529
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
97-248 |
4.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 97 LEESQGGKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 170
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301130 171 IRNYEQHRKESEDAVKALAKEKDLLerekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-249 |
5.22e-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: 45.83 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDleesqggkssevlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 231
Cdd:TIGR02169 421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
170
....*....|....*...
gi 65301130 232 AELAMAKQSLATLTKDVP 249
Cdd:TIGR02169 490 RELAEAEAQARASEERVR 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-215 |
8.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEE------SQGGKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADRKRLK 143
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPLPASA 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 65301130 144 GEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDHATA 215
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGLDEA 458
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-243 |
1.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATElrvqlaQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHATALR 217
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355
|
170 180
....*....|....*....|....*.
gi 65301130 218 SQLDLKDNRMKELEAELAMAKQSLAT 243
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVED 381
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
74-250 |
1.26e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATEL-----RVQLAQKE--QELARAKEALQAMKADRKRLKGEK 146
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdKLLLENKEltQEASDMTLELKKHQEDIINCKKQE 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 147 TDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVK---------ALAKEKDLLEREKW----------------- 200
Cdd:pfam05483 530 ERMLKQIE----NLEEKEMNLRDELESVREEFIQKGDEVKckldkseenARSIEYEVLKKEKQmkilenkcnnlkkqien 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 65301130 201 ------ELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 250
Cdd:pfam05483 606 knknieELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
72-236 |
1.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSatELRVQLAQKEQELARAKEALQ----AMKADRKRLKGEKT 147
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 148 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKeatdhatALRSQLDLKDNRM 227
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVE-------VARELYESLLQRL 374
|
....*....
gi 65301130 228 KELEAELAM 236
Cdd:COG3206 375 EEARLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-244 |
1.40e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 111 ATELRVQLAQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 184
Cdd:COG1196 215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301130 185 ----VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 244
Cdd:COG1196 293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
72-337 |
1.70e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKEQELARAKEALQAMKADRKRlKGEKTDLVS 151
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREELGERARALYR-SGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QM--QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 229
Cdd:COG3883 107 VLlgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 230 LEAELAMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCH 307
Cdd:COG3883 187 LSAEEAAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
250 260 270
....*....|....*....|....*....|
gi 65301130 308 SRQPSVISDASAAEGDRSSTPSDINSPRHR 337
Cdd:COG3883 267 AAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
87-247 |
2.10e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 87 RQMKEMLAKDlEESQGGKSSEVLSATELRvQLAQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 166
Cdd:pfam01576 2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 167 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 246
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152
|
.
gi 65301130 247 D 247
Cdd:pfam01576 153 E 153
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
113-241 |
2.22e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.67 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 192
Cdd:pfam20492 10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 65301130 193 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSL 241
Cdd:pfam20492 72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
80-196 |
2.72e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 41.42 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 80 QEEVHLLRQMKEMLAKDLEESQGgKSSEVLSATELRVQLAQKEQE-LARAKEALQAMKADRKRLKGEKtdLVSQMQQLYA 158
Cdd:pfam10368 32 KKEQELYEEIIELGMDEFDEIKK-LSDEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELID 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 65301130 159 TLESREEQLRDFIRNYEqhrkesedavKALAKEKDLLE 196
Cdd:pfam10368 109 AMEERYEAYDELYDAYK----------KALELDKELYE 136
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-219 |
3.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRqmkemlakdleesqggKSSEVLsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG4913 666 AEREIAELEAELERLD----------------ASSDDL--AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 219
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
60-233 |
4.34e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 60 VRADGDCSQPVLLREEVSrlQEEVHLLRQMKEMLAK--------DLEESQGGK-----SSEVLSATELRVQLAQKEQELA 126
Cdd:pfam15921 352 VLANSELTEARTERDQFS--QESGNLDDQLQKLLADlhkrekelSLEKEQNKRlwdrdTGNSITIDHLRRELDDRNMEVQ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 127 RAKEALQAMKADRK--------RLKGeKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLER 197
Cdd:pfam15921 430 RLEALLKAMKSECQgqmerqmaAIQG-KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDlTASLQEK 508
|
170 180 190
....*....|....*....|....*....|....*..
gi 65301130 198 EKwelrrqAKEATD-HATALRSQLDLKDNRMKELEAE 233
Cdd:pfam15921 509 ER------AIEATNaEITKLRSRVDLKLQELQHLKNE 539
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
72-222 |
5.34e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.93 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEEsqggkssEVLSATElrvqlAQK--EQEL---ARAKEALQAMKADRKRLKGEK 146
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEK-------QAEIARE-----AQQnyERELvlhAEDIKALQALREELNELKAEI 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301130 147 TDLVSQMQQLYATLESREEqlrdfirnyeqhrkesedavkALAKEKDLLEREKWELRRQAKEATDHATALRSQLDL 222
Cdd:pfam07926 74 AELKAEAESAKAELEESEE---------------------SWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-238 |
5.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEEsQGGKSSEVLSATELRVQLAQKEQ-ELARAKEALQAMKADRKRLKGEKTDLV 150
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERLKELEPFYNEYlELKDAEKELEREEKELKKLEEELDKAF 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 151 SQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMK 228
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
170
....*....|.
gi 65301130 229 ELEA-ELAMAK 238
Cdd:PRK03918 712 ELEKlEKALER 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-233 |
7.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVsRLQEEVHLLRQMKEmlAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:PTZ00121 1555 EEL-KKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 154 QQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATDHATALRSQLD--LKDNRMK 228
Cdd:PTZ00121 1632 KKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEeaKKAEELK 1708
|
....*
gi 65301130 229 ELEAE 233
Cdd:PTZ00121 1709 KKEAE 1713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
53-234 |
7.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 53 PRAGVPRVRADGDCsqpvllREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVlSATELRVQLAQKEQELARAKEAL 132
Cdd:PRK02224 460 PVEGSPHVETIEED------RERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 133 QAMKADRKRLKGEKTDLVSQMQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELR 203
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLR 612
|
170 180 190
....*....|....*....|....*....|.
gi 65301130 204 RQAKEATDHATALRSQLDLKDNRMKELEAEL 234
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
119-245 |
7.49e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 119 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 197
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 65301130 198 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 245
Cdd:cd22656 179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-233 |
7.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVSRLQEEVHLLRQMK--EMLAKDLEESQGGKSSEVLSATELRvqlaqKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKdNRMK 228
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIA 1760
|
....*
gi 65301130 229 ELEAE 233
Cdd:PTZ00121 1761 HLKKE 1765
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
114-249 |
7.72e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 114 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 193
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 65301130 194 lleREKWElrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:COG0542 460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
72-209 |
7.99e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHL---LRQMKEMLAKDLEESQGGKSSEVlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 148
Cdd:pfam07111 486 LREERNRLDAELQLsahLIQQEVGRAREQGEAERQQLSEV--AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAAS 563
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301130 149 L---VSQMQQLY--------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEA 209
Cdd:pfam07111 564 LrqeLTQQQEIYgqalqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEA 639
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
72-234 |
8.12e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVL---------SATELRVQLAQKEQELARAKEALQAMKADRKRL 142
Cdd:COG5185 287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEqeleeskreTETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 143 KGE--KTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKEsedAVKALAKEKDLLEREKWELRRQAKEATdhatalrSQL 220
Cdd:COG5185 367 VGEveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQAT-------SSN 436
|
170
....*....|....
gi 65301130 221 DLKDNRMKELEAEL 234
Cdd:COG5185 437 EEVSKLLNELISEL 450
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
71-246 |
8.42e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEvhllrQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLV 150
Cdd:pfam01576 196 LKKEEKGRQELE-----KAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 151 SQMQQLYATLESR-------EEQLRDFIRNYEQHRKESEDAVKALAKEKDL---LEREKWELRRQAKEATDHATALRSQL 220
Cdd:pfam01576 271 AQISELQEDLESEraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQEM 350
|
170 180
....*....|....*....|....*..
gi 65301130 221 DLKDNR-MKELEAELAMAKQSLATLTK 246
Cdd:pfam01576 351 RQKHTQaLEELTEQLEQAKRNKANLEK 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-249 |
9.34e-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: 41.59 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQ----GGKSSEV-----------------LSATELRVQLAQKE-QELARAK 129
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLeeevsriearlreieqkLNRLTLEKEYLEKEiQELQEQR 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 130 EALQAMKADRKRlkgEKTDLVSQMQQLYATLESREEQLRDfirnyeqhrkesedavkaLAKEKDLLEREKWELRRQAKEA 209
Cdd:TIGR02169 843 IDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRD------------------LESRLGDLKKERDELEAQLREL 901
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 65301130 210 TDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-191 |
9.75e-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: 40.90 E-value: 9.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 65301130 117 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 191
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
71-204 |
1.19e-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: 40.77 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQggksSEVLSATELRVQLAQKEQ-ELARAKEALQAMKADRKRLKGEKTDL 149
Cdd:smart00787 155 GLKEDYKLLMKELELLNSIKPKLRDRKDALE----EELRQLKQLEDELEDCDPtELDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 65301130 150 VSQMQQLYATLESREEQLRDFI-------RNYEQHRKESEDAVKALAKEKDLLEREK-WELRR 204
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNteiaeaeKKLEQCRGFTFKEIEKLKEQLKLLQSLTgWKITK 293
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
72-209 |
1.46e-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: 40.52 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLR-QMKEMLAKDLEESQGGKSSEVLSATEL-----------RVQLAQKEQ--ELARAKEALQAMKA 137
Cdd:COG4942 88 LEKEIAELRAELEAQKeELAELLRALYRLGRQPPLALLLSPEDFldavrrlqylkYLAPARREQaeELRADLAELAALRA 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301130 138 DRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEA 209
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
72-209 |
1.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEAL---------QAMKADRKRL 142
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 65301130 143 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEA 209
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
78-273 |
1.53e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 78 RLQEEVHLLRQMKEMLAKDLEesqggKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADrkrlkgektdlvsqMQQL 156
Cdd:PRK00409 496 RLGLPENIIEEAKKLIGEDKE-----KLNELIASLEeLERELEQKAEEAEALLKEAEKLKEE--------------LEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 157 YATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAtdhatalrsqldLKDNRMKELEAELAM 236
Cdd:PRK00409 557 KEKLQEEEDKLL------EEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS------------VKAHELIEARKRLNK 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 65301130 237 AKQSLATLTKDVPKRHSLAMPGETV-------------LNGNQEWVVQAD 273
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKVGDEVkylslgqkgevlsIPDDKEAIVQAG 668
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
117-238 |
1.53e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 117 QLAQKEQELARAKEALQAmKADRKRLKGEKtdlvsqmqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 196
Cdd:COG2268 238 RIAEAEAELAKKKAEERR-EAETARAEAEA-----------AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE 305
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 65301130 197 -----REKWELRRQAKEATDHATALRSQLDLKdnrmKELEAELAMAK 238
Cdd:COG2268 306 leadvRKPAEAEKQAAEAEAEAEAEAIRAKGL----AEAEGKRALAE 348
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-199 |
1.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSATELrvqlaqkEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELE--ELLEALDEEEL-------EEELEELEEELEELEEELEELREELAELEAEL 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 65301130 154 QQL-----YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK 199
Cdd:COG4717 463 EQLeedgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
54-238 |
1.95e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 54 RAGVPRVRADGDCSQPVLLREEvSRLQEEVHLlRQMKemlakDLEESQGGKSSEVLSATEL-RVQLAQKEQELARAKEAL 132
Cdd:pfam15921 286 KASSARSQANSIQSQLEIIQEQ-ARNQNSMYM-RQLS-----DLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 133 QAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrkesedavkALAKEKDlleREKWELRRQAKEATDH 212
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-------------------SLEKEQN---KRLWDRDTGNSITIDH 416
|
170 180
....*....|....*....|....*.
gi 65301130 213 ataLRSQLDLKDNRMKELEAELAMAK 238
Cdd:pfam15921 417 ---LRRELDDRNMEVQRLEALLKAMK 439
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
72-196 |
1.99e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:pfam10473 8 VLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTK 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 65301130 152 QMQQLYAT---LESREEQLRDFIRNYEQHR----KESEDAVKALAKE-KDLLE 196
Cdd:pfam10473 88 ELQKKQERvseLESLNSSLENLLEEKEQEKvqmkEESKTAVEMLQTQlKELNE 140
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-249 |
2.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 123 QELARAKEALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRkesedAVKALAKEKDLLEREKWEL 202
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAEL 144
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 65301130 203 RRQAKEATDHATALRSQLdlkdNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:COG4717 145 PERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLS 187
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-242 |
2.41e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEesQGGKSSEVLSA---------TELRVQLAQKEQELARAKEALQAMKADRKRL 142
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAG--LDDADAEAVEArreeledrdEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 143 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwelrrqakEATDHATALRSQLDL 222
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-----------NAEDFLEELREERDE 423
|
170 180
....*....|....*....|
gi 65301130 223 KDNRMKELEAELAMAKQSLA 242
Cdd:PRK02224 424 LREREAELEATLRTARERVE 443
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-235 |
2.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVH-LLRQMKEMLAKdleESQGGKSSEVLSATELRV-QLAQKEQELARAKEALQAMKADRKRLKG-EKTD 148
Cdd:PRK03918 312 IEKRLSRLEEEINgIEERIKELEEK---EERLEELKKKLKELEKRLeELEERHELYEEAKAKKEELERLKKRLTGlTPEK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 149 LVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAK----------------EKDLLEREKWELRRQAKEA 209
Cdd:PRK03918 389 LEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehRKELLEEYTAELKRIEKEL 468
|
170 180
....*....|....*....|....*.
gi 65301130 210 TDHATALRsqlDLKdNRMKELEAELA 235
Cdd:PRK03918 469 KEIEEKER---KLR-KELRELEKVLK 490
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
97-192 |
3.10e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 38.28 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 97 LEESQGGKSSEvlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDlvSQMQQLYATLESREEQLRDFIRNYEQ 176
Cdd:COG2825 35 LQESPEGKAAQ----KKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSE--EERQKKERELQKKQQELQRKQQEAQQ 108
|
90 100
....*....|....*....|....*...
gi 65301130 177 --HRKESE----------DAVKALAKEK 192
Cdd:COG2825 109 dlQKRQQEllqpilekiqKAIKEVAKEE 136
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-238 |
3.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATDHATALRSQLDLKDNRMKELE 231
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARERVEEAE 446
|
....*..
gi 65301130 232 AELAMAK 238
Cdd:PRK02224 447 ALLEAGK 453
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
59-169 |
3.92e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 59 RVRADGDcSQPvllrEEVSRLQEEVHLLRQMKEMLAKDLEESqggkSSEvlSATELRVQLAQKEQELARAKEALQAMKAD 138
Cdd:COG0542 401 RVRMEID-SKP----EELDELERRLEQLEIEKEALKKEQDEA----SFE--RLAELRDELAELEEELEALKARWEAEKEL 469
|
90 100 110
....*....|....*....|....*....|....
gi 65301130 139 RKRLKGEKTDLVSQ---MQQLYATLESREEQLRD 169
Cdd:COG0542 470 IEEIQELKEELEQRygkIPELEKELAELEEELAE 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
71-248 |
3.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 71 LLREEVSRLQEEVHLLRQMKEMLaKDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKAdrkrLKGEKTDLV 150
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELI-KEKEKELEEVLREI---NEISSELPELREELEKLEKEVKELEE----LKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 151 SQMQQLYATLESREE---QLRDFIRNYEQHRKESEDAVKAL------AKE----KDLLEREKWELRRQAKEATDHATALR 217
Cdd:PRK03918 245 KELESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELkelkekAEEyiklSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190
....*....|....*....|....*....|....*..
gi 65301130 218 ------SQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:PRK03918 325 gieeriKELEEKEERLEELKKKLKELEKRLEELEERH 361
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-243 |
4.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggksSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELE----EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 152 QMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMK 228
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
170
....*....|....*
gi 65301130 229 ELEAELAMAKQSLAT 243
Cdd:COG1196 561 AAIEYLKAAKAGRAT 575
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
113-245 |
4.51e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.94 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 113 ELRVQLAQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 179
Cdd:pfam00529 62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 180 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDN----RMKELEAELAMAKQSLATLT 245
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
111-241 |
4.78e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 111 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKT---DLVSQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKA 187
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQ-LEQLRA 592
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301130 188 LAKE-----------KDLLERekweLRRQAKEATDHATALRSQLDLKDNRMKELEAE---LAMAKQSL 241
Cdd:COG3096 593 RIKElaarapawlaaQDALER----LREQSGEALADSQEVTAAMQQLLEREREATVErdeLAARKQAL 656
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
115-248 |
5.00e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 38.90 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 115 RVQLAQKEQELARAKEALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 194
Cdd:pfam19220 47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 65301130 195 LEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-240 |
5.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 70 VLLRE-EVSRLQEEVHLLRQMKEMLAK-DLEEsqggkssevlsatelrvqLAQKEQELARAKEALQAMKADRKRLKGE-- 145
Cdd:PRK03918 488 VLKKEsELIKLKELAEQLKELEEKLKKyNLEE------------------LEKKAEEYEKLKEKLIKLKGEIKSLKKEle 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 146 -KTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE-----------KDLLEREKWELRRQAKEATDhA 213
Cdd:PRK03918 550 kLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKElepfyneylelKDAEKELEREEKELKKLEEE-L 628
|
170 180
....*....|....*....|....*..
gi 65301130 214 TALRSQLDLKDNRMKELEAELAMAKQS 240
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKK 655
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
88-203 |
5.41e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 38.42 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 88 QMKEMLAKDLEESQGgkSSEVLSATELRVQLAQKEQELARAKEAlqAMKADRKRLKGEKTDLVSQMQ-----------QL 156
Cdd:pfam02841 173 KAEEVLQEFLQSKEA--VEEAILQTDQALTAKEKAIEAERAKAE--AAEAEQELLREKQKEEEQMMEaqersyqehvkQL 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 65301130 157 YATLES-REEQLRDFIRNYEQHRKESEDAVKA-LAKEKDLLEREKWELR 203
Cdd:pfam02841 249 IEKMEAeREQLLAEQERMLEHKLQEQEELLKEgFKTEAESLQKEIQDLK 297
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
111-285 |
5.80e-03 |
|
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: 38.72 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 111 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY-------EQHRKESED 183
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSrekheelEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 184 AVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD---NRMKE------------------LEAELAMAKQSLA 242
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelERMKErakkagaqrkeeeaerkqLQAKLQQTEEELR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 65301130 243 TLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQ 285
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
77-233 |
7.16e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.22 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 77 SRLQEEVHLLRQMKEMLAKDLEE-SQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 155
Cdd:pfam08614 10 NRLLDRTALLEAENAKLQSEPESvLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301130 156 LYATLESREEQLRDFirnyeqhrkesEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAE 233
Cdd:pfam08614 90 LEKKLREDERRLAAL-----------EAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKE 156
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
72-248 |
7.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 37.97 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 72 LREEVSRLQEEVHLLRQMKEMLAKDLEEsqggkssevLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 149
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKE---------LAEKrdELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 150 VSQMQQLYATLESREEQLRDFIRN----------YEQHRKESEDAVKALAKEKDLLEREKwELRRQAKEAtdhatalRSQ 219
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAggsidklrkeIERLEWRQQTEVLSPEEEKELVEKIK-ELEKELEKA-------KKA 155
|
170 180
....*....|....*....|....*....
gi 65301130 220 LDLKDNrMKELEAELAMAKQSLATLTKDV 248
Cdd:COG1340 156 LEKNEK-LKELRAELKELRKEAEEIHKKI 183
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
107-235 |
8.59e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 37.19 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 107 EVLSA-----TELRVQLAQKEQELARAKEALQAMKADRKR-------LKGEKTDLVSQMQQLYATLESREEQLR---DFI 171
Cdd:pfam15619 4 RVLSArlhkiKELQNELAELQSKLEELRKENRLLKRLQKRqekalgkYEGTESELPQLIARHNEEVRVLRERLRrlqEKE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301130 172 RNYEQHRKESED----------AVKALAKEKDLLEREkwELRRQAKEATDHatalrsqLDLKDNRMKELEAELA 235
Cdd:pfam15619 84 RDLERKLKEKEAellrlrdqlkRLEKLSEDKNLAERE--ELQKKLEQLEAK-------LEDKDEKIQDLERKLE 148
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
130-248 |
9.16e-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: 37.69 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 130 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfiRNYEQHRKESEDavkalaKEKDLLEREKWELrrqaKEA 209
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEEL----RQLKQLEDELED------CDPTELDRAKEKL----KKL 216
|
90 100 110
....*....|....*....|....*....|....*....
gi 65301130 210 TDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
84-187 |
9.23e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.82 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 84 HLLRQMKEmLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESR 163
Cdd:COG4942 143 YLAPARRE-QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|....
gi 65301130 164 EEQLRDFIRNYEQHRKESEDAVKA 187
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPA 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-241 |
9.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 74 EEVSRLQEevhlLRQMKEmlAKDLEESQggKSSEVLSATELR-VQLAQKEQELARAKEAL----QAMKADRKRLKGEKTD 148
Cdd:PTZ00121 1185 EEVRKAEE----LRKAED--ARKAEAAR--KAEEERKAEEARkAEDAKKAEAVKKAEEAKkdaeEAKKAEEERNNEEIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 149 L----VSQMQQLYATLESREEQLRDFIRNYEQHRK-----ESEDAVKA-LAKEKDLLEREKWELRRQAKEATDHATALRS 218
Cdd:PTZ00121 1257 FeearMAHFARRQAAIKAEEARKADELKKAEEKKKadeakKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
170 180
....*....|....*....|...
gi 65301130 219 QLDLKDNRMKELEAELAMAKQSL 241
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEA 1359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-244 |
9.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.38 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 45 DAAGPGDRPRAGVPRVRADGDCSQPVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQE 124
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301130 125 LARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfiRNYEQHRKESEDAVKALAKEKDLLEREKWELRR 204
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE--LAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 65301130 205 QAKEATDHATALRSQLDLKDnrMKELEAELAMAKQSLATL 244
Cdd:COG1196 742 LEEEELLEEEALEELPEPPD--LEELERELERLEREIEAL 779
|
|
| |
