|
Name |
Accession |
Description |
Interval |
E-value |
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-233 |
4.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKdgdysALQNKLQARDALVKTCTDDKNKLQndvs 117
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSDDLA---- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 118 aqmseihRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEyeslQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLEN 197
Cdd:COG4913 689 -------ALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
170 180 190
....*....|....*....|....*....|....*..
gi 528485282 198 RNADSVVQHVDLDLDQSNKR-KEKEDTAERHTVAARR 233
Cdd:COG4913 758 ALGDAVERELRENLEERIDAlRARLNRAEEELERAMR 794
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-219 |
2.86e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 40 ARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDVSAQ 119
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 120 MSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESlqcgRQIAELKAEYEESKKRVEEEAAKLRQSLLENRN 199
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180
....*....|....*....|
gi 528485282 200 ADSVVQHVDLDLDQSNKRKE 219
Cdd:COG1196 475 LEAALAELLEELAEAAARLL 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
41-191 |
5.52e-06 |
|
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: 49.35 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 41 RLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCT-------DDKNKLQ 113
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANkekhflkEEKNKLS 775
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528485282 114 NDVSAQMSEIHRLKEQVKELRQevirqedQQREVRKNSTNLEKKLEYESLQCgrqiaelkAEYEESKKRVEEEAAKLR 191
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRS-------QERRLKEKVANMEVALDKASLQF--------AECQDIIQRQEQESVRLK 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-248 |
2.12e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 40 ARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDVSAQ 119
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 120 MSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEK---KLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLE 196
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 528485282 197 NRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRNDVPVLKDDLGKPGS 248
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
21-231 |
2.71e-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: 46.30 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 21 LLVVIVILSFNYWSVSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDA 100
Cdd:COG4942 4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 101 LVKTCTDDKNKLQNDVSAQMSEI--------------------------------HRLKEQVKELRQEVIRQEDQQREVR 148
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 149 KNSTNLEKKL-EYESLQcgRQIAELKAEYEESKKRVEEEAAKLRQSLLENRNADSVVQHVDLDLDQSNKRKEKEDTAERH 227
Cdd:COG4942 164 ALRAELEAERaELEALL--AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 528485282 228 TVAA 231
Cdd:COG4942 242 RTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
38-226 |
3.29e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 38 KHARLLDELAEVQTQVKRTDAARSR---LEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKtctddKNKLQN 114
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 115 DVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGRQIAELKAEYEEskkrVEEEAAKLRQSL 194
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----LQQRLAELEEEL 215
|
170 180 190
....*....|....*....|....*....|..
gi 528485282 195 LENRNAdsvVQHVDLDLDQSNKRKEKEDTAER 226
Cdd:COG4717 216 EEAQEE---LEELEEELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-234 |
3.38e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 40 ARLLDELAEVQTQVKRTDAARSRLEKRNsELMMQVDTHRKQIDLKDgdYSALQNKLQARDALVKTCTDDKNKLQNDVSAQ 119
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEKAERYR-ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 120 MSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESL---QCGRQIAELKAEYEESKKRVEEEAAKLRQSLLE 196
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190
....*....|....*....|....*....|....*...
gi 528485282 197 NRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRN 234
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
38-196 |
4.46e-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: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQN--- 114
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 115 ------DVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKL-----EYESLQCGRQ--IAELKAEYEESKK 181
Cdd:COG1579 84 nvrnnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELaeleaELEEKKAELDeeLAELEAELEELEA 163
|
170
....*....|....*
gi 528485282 182 RVEEEAAKLRQSLLE 196
Cdd:COG1579 164 EREELAAKIPPELLA 178
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-196 |
1.27e-04 |
|
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: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 30 FNYWSVSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGD-YSALQNKLQARDALVKTCTDD 108
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 109 KNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGRQIAELKAE---YEESKKRVEE 185
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiasLERRKSNIPA 440
|
170
....*....|.
gi 528485282 186 EAAKLRQSLLE 196
Cdd:COG4913 441 RLLALRDALAE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-220 |
4.01e-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: 43.13 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 40 ARLLDELAEVQTQVKRTDA--ARSRLEKRNSELMMQVDTHRK---QIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQN 114
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 115 DVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEK---KLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLR 191
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
170 180 190
....*....|....*....|....*....|....*
gi 528485282 192 ------QSLLENRNADSVVQHVDLDLDQSNKRKEK 220
Cdd:TIGR02169 928 aleeelSEIEDPKGEDEEIPEEELSLEDVQAELQR 962
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-234 |
4.05e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 35 VSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDA-------LVKTCTD 107
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 108 DKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGR----------QIAELKAEYE 177
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqieelseDIESLAAEIE 862
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528485282 178 ESKKRVEEEAAKLrQSLLENRnaDSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRN 234
Cdd:TIGR02168 863 ELEELIEELESEL-EALLNER--ASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-233 |
4.49e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 45 ELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQardalvktctddknKLQNDVSAQMSEIH 124
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE--------------ELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 125 RLKEQVKELrqevirqEDQQREVRKNSTNLEKKLeyesLQCGRQIAELKAE---YEESKKRVEEEAAKLRQSLLENRNAD 201
Cdd:TIGR02168 362 ELEAELEEL-------ESRLEELEEQLETLRSKV----AQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKL 430
|
170 180 190
....*....|....*....|....*....|..
gi 528485282 202 SVVQHVDLDLDQSNKRKEKEDTAERHTVAARR 233
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEA 462
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-233 |
4.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 37 TKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDV 116
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 117 SAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLE----------YESLQCGRQIAELKAEYEESKKRVEEE 186
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeaeeeleelaEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528485282 187 AAKLRQSLLENRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARR 233
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-243 |
5.19e-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: 42.75 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 45 ELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDK-NKLQNDVSAQMSEI 123
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 124 HRLKEQVKELRQEVIRQEDQQRE-------VRKNSTNLEKKLEYESL---QCGRQIAELKAEYEESKKRVEEEAAK---L 190
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEEERKrrdKLTEEYAELKEELEDLRAELEEVDKEfaeT 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528485282 191 RQSLLENRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRNDVPVLKDDL 243
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-192 |
8.53e-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: 42.08 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 38 KHARLLDELAEVQTQVKRT----DAARSRLEKRNSELMMQVDT---------HRK----------QIDLKDGD------- 87
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNkanlEKAKQALESENAELQAELRTlqqakqdseHKRkklegqlqelQARLSESErqraela 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 88 --YSALQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHrlkeQVKELRQEVIRQE----DQQREVRKNSTNLEKKLEYE 161
Cdd:pfam01576 433 ekLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ----DTQELLQEETRQKlnlsTRLRQLEDERNSLQEQLEEE 508
|
170 180 190
....*....|....*....|....*....|....
gi 528485282 162 SL---QCGRQIAELKAEYEESKKRVEEEAAKLRQ 192
Cdd:pfam01576 509 EEakrNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
41-196 |
8.63e-04 |
|
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: 40.66 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 41 RLLDELAE----VQTQVKRTDAARSRLEKRNSELMMQVDTHRKQI--------DLKDgDYSALQNKLQARDALVKTCTDD 108
Cdd:pfam15619 25 SKLEELRKenrlLKRLQKRQEKALGKYEGTESELPQLIARHNEEVrvlrerlrRLQE-KERDLERKLKEKEAELLRLRDQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 109 KNKLQNDVSAQ-MSEIHRLKEQVKELRQEVirqEDQQREVRknstNLEKKLEYESLQCGRQIAELKAEYEESKKRV---E 184
Cdd:pfam15619 104 LKRLEKLSEDKnLAEREELQKKLEQLEAKL---EDKDEKIQ----DLERKLELENKSFRRQLAAEKKKHKEAQEEVkilQ 176
|
170
....*....|..
gi 528485282 185 EEAAKLRQSLLE 196
Cdd:pfam15619 177 EEIERLQQKLKE 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
42-192 |
1.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 42 LLDELAEVQTQVKRTDAARSRLEKRN---------SELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKL 112
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 113 QNDVSAQM--SEIHRLKEQVKELRQ-------EVIRQEDQQREVRKNSTNLEKKL------EYESLQcgRQIAELKAEYE 177
Cdd:COG3206 260 LQSPVIQQlrAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIlasleaELEALQ--AREASLQAQLA 337
|
170
....*....|....*
gi 528485282 178 ESKKRVEEEAAKLRQ 192
Cdd:COG3206 338 QLEARLAELPELEAE 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-226 |
1.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKT-----------CTDDKNK- 111
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakkAEEDKNMa 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 112 ------LQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQR----------EVRKNSTNLEKKLEYESlqcgRQIAELKAE 175
Cdd:PTZ00121 1580 lrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelkkaeEEKKKVEQLKKKEAEEK----KKAEELKKA 1655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 528485282 176 YEESKKRVEEEAAKLRQsllENRNADSVVQHVDLDLDQSNKRKEKEDTAER 226
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-189 |
1.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 42 LLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDgDYSALQNKLQARDALVKTCTDDKNKLQN---DVSA 118
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAALEQAEEYQELKEELEELEEQLEEllgELEE 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528485282 119 QMSEI--HRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYesLQCGRQIAELKAEYEESKKRVEEEAAK 189
Cdd:COG4717 421 LLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELRELAEE 491
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
73-232 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 73 QVDTHRKQIDLKDGDysaLQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKN-- 150
Cdd:COG1579 14 ELDSELDRLEHRLKE---LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 151 STNLEKKLEYESlqcgRQIAELKAEYEESKKRVEEEAAKLR--QSLLENRNADSVVQHVDLDLDQSNKRKEKED-TAERH 227
Cdd:COG1579 91 YEALQKEIESLK----RRISDLEDEILELMERIEELEEELAelEAELAELEAELEEKKAELDEELAELEAELEElEAERE 166
|
....*
gi 528485282 228 TVAAR 232
Cdd:COG1579 167 ELAAK 171
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
38-267 |
1.97e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 40.97 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQidLKDGDYSALQNKLQA-RDALVKTctddknklQNDV 116
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALETNGQAqRDAILEE--------SRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 117 SAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNS--TNLEKKLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSL 194
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGllDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528485282 195 LenrNADSVVQHVDLDLDQS-NKRKEKEDTAerhtvAARRNDVPVLKDDLGKPGSDAGMPGIEDSEVGKIDDSQ 267
Cdd:NF012221 1699 A---QGEQNQANAEQDIDDAkADAEKRKDDA-----LAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ 1764
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-235 |
2.12e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 121 SEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEK---KLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLEN 197
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110
....*....|....*....|....*....|....*...
gi 528485282 198 RNADSVVQHVDLDLDQSNKRKeKEDTAERHTVAARRND 235
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEEL-AEAEAEIEELEAQIEQ 793
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
16-185 |
2.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 16 FILIALLVVIVILSFNYW---SVSTKHARLLDELAEVQTQVKRTDAARSRLEKR---NSELMMQVDTHRKQIDLKDGDYS 89
Cdd:PRK12704 6 IILIALVALVVGAVIGYFvrkKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALleaKEEIHKLRNEFEKELRERRNELQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 90 ALQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNL-------------EK 156
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaeeakeillekvEE 165
|
170 180
....*....|....*....|....*....
gi 528485282 157 KLEYESLQCGRQIaELKAEyEESKKRVEE 185
Cdd:PRK12704 166 EARHEAAVLIKEI-EEEAK-EEADKKAKE 192
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
113-192 |
2.30e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 113 QNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKL------EYESLQCGRQIAELKAEYEESKKRVEEE 186
Cdd:COG2433 405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEE 484
|
....*.
gi 528485282 187 AAKLRQ 192
Cdd:COG2433 485 RERIEE 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-185 |
4.59e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKtctddknKLQNDVSAQMSEI 123
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE-------KLKKENQSYKQEI 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528485282 124 HRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKklEYESLQcgRQIAELKAEYEESKKRVEE 185
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ--EKELLE--KEIERLKETIIKNNSEIKD 444
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
12-151 |
4.83e-03 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 38.72 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 12 RLPSFILIALLVVIVILSF-----NYWSVSTkharllDELAEVQTQVkrtDAARSRLEKRNSELmmQVDTHRKQID--LK 84
Cdd:NF038305 77 RFLSWILSLLLGLLFLLLIplhlnNTRRLST------QALQQINQQA---GQQETQLQQQLNQL--QAQTSPQQLNqlLK 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485282 85 DGDYSALQNKLQARDALVKtctDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQedQQREVRKNS 151
Cdd:NF038305 146 SEQKQGQALASGQLPEEQK---EQLQQFKSNPQALDKFLAQQLTQIRTQAEEAEKQ--ARLEALKSS 207
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
44-148 |
5.44e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.27 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLkdgdysALQnklQARDALVKTCTDDKNKLQNDVSAQMSEI 123
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL------ALE---KGREDLAREALERKAELEAQAEALEAQL 107
|
90 100
....*....|....*....|....*
gi 528485282 124 HRLKEQVKELRQEVIRQEDQQREVR 148
Cdd:COG1842 108 AQLEEQVEKLKEALRQLESKLEELK 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-235 |
9.68e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 54 KRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHRLKEQVKEl 133
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485282 134 RQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQ----SLLENRNADSVVQHVDL 209
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkEAEEKKKAEELKKAEEE 1727
|
170 180
....*....|....*....|....*.
gi 528485282 210 DLDQSNKRKEKEDTAERHTVAARRND 235
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
|
| |
