|
Name |
Accession |
Description |
Interval |
E-value |
| DIX |
pfam00778 |
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ... |
392-467 |
3.57e-37 |
|
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.
Pssm-ID: 459936 Cd Length: 77 Bit Score: 130.72 E-value: 3.57e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672062112 392 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 467
Cdd:pfam00778 2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
|
|
| DAX |
smart00021 |
Domain present in Dishevelled and axin; Domain of unknown function. |
392-468 |
2.04e-19 |
|
Domain present in Dishevelled and axin; Domain of unknown function.
Pssm-ID: 197474 Cd Length: 83 Bit Score: 82.46 E-value: 2.04e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672062112 392 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGsHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 468
Cdd:smart00021 4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTKKN-YKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-264 |
6.86e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 70 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 149
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 150 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 229
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 672062112 230 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 264
Cdd:COG1196 479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-253 |
1.31e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 70 EEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLII-IRSRLDQSMEENQDLKKELLK 148
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 149 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQA 228
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180
....*....|....*....|....*
gi 672062112 229 KLEDALRKLSDASYQQVDLERELEQ 253
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-260 |
7.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 71 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCK 150
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKL 230
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190
....*....|....*....|....*....|
gi 672062112 231 EDALRKLSDASYQQVDLERELEQKDVLLAH 260
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-260 |
2.40e-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: 50.44 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 70 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELL 147
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 148 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLDERNRLLGEYKKDLGQKDRLLQQ 225
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891
|
170 180 190
....*....|....*....|....*....|....*
gi 672062112 226 QQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 260
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-252 |
2.50e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 122 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 191
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672062112 192 ------HNQNVDLQRKLD--------ERNRLLGEYKKD---LGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELE 252
Cdd:COG3206 284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-254 |
2.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 71 EQLLEQQEHL---EKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD--QSMEENQDLKKE 145
Cdd:COG4913 228 DALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARER-----------LAELEYLRAALRlwFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 146 LLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLDERNRLLGEYKKDLGQKD---- 220
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGlplp 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 672062112 221 ----------RLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 254
Cdd:COG4913 377 asaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
74-271 |
3.16e-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: 49.73 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 74 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSMEENQDLKKE 145
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 146 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNRLLGEYKKDL 216
Cdd:pfam15921 540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 672062112 217 GQKDRLLQQQQAKLED---ALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEVTN 271
Cdd:pfam15921 614 DKKDAKIRELEARVSDlelEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-253 |
3.18e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 80 LEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGI 159
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEA--------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 160 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSD 239
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170
....*....|....
gi 672062112 240 ASYQQVDLERELEQ 253
Cdd:TIGR02168 370 LESRLEELEEQLET 383
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-254 |
3.34e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 70 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLpEDEQERPVALCEPGVNPEEQLIIIRSRLDQ-------SMEENQ 140
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIeeLEREI-EEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaeTRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 141 DLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDErnrllgeykkdlgqKD 220
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK--------------QE 454
|
170 180 190
....*....|....*....|....*....|....
gi 672062112 221 RLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 254
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
71-289 |
4.55e-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: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 71 EQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLK 148
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLaaLERRIAALARRIRAL--------EQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 149 CKQEARNL------QGIKDALQQRLTQQDTS------------VLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLG 210
Cdd:COG4942 102 QKEELAELlralyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 211 EYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH--RVKGDTDEVTNYNSHSSQRNGFVLPVAG 288
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAAGFAALKGKLPWPVSG 261
|
.
gi 672062112 289 R 289
Cdd:COG4942 262 R 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
112-259 |
2.17e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 112 VALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD---- 187
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 188 KDELHNQNVDLQRK-----------------------------LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLS 238
Cdd:COG3883 85 REELGERARALYRSggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180
....*....|....*....|.
gi 672062112 239 DASYQQVDLERELEQKDVLLA 259
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLA 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-271 |
3.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 118 GVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSV---------LQLKQEL--LRANM 186
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELerLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 187 DK--------DELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDA-------LRKLSDASYQQVDLEREL 251
Cdd:COG4913 685 DDlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarleLRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|
gi 672062112 252 EQKDVLLAHRVKGDTDEVTN 271
Cdd:COG4913 765 RELRENLEERIDALRARLNR 784
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-245 |
5.33e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 71 EQLLEQQEHLEKEMEEAKKMISGLQAlllngSLPEDEQERPVALCEPGVNpEEQLIIIRSRLDQSMEENQDLKKELLKCK 150
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEE-----LIEELESELEALLNERASL-EEALALLRSELEELSEELRELESKRSELR 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVDLQRKLDERNRLLGEYKKDLG--------- 217
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiee 994
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 672062112 218 ---QKDRL--LQQQQAKLEDALRKLSDA--------------SYQQV 245
Cdd:TIGR02168 995 yeeLKERYdfLTAQKEDLTEAKETLEEAieeidrearerfkdTFDQV 1041
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
71-252 |
6.85e-04 |
|
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: 42.12 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 71 EQLLEQQEHLEKEMEEAKKMISGLQALLLN-----GSLPE--DEQERPValcepgvnpeEQLIIIRSRLDQS-MEENQDL 142
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalTTLEEalSEKERII----------ERLKEQREREDRErLEELESL 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 143 KKELLKCKQEArnlqgikDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLDERNRLLGEYKK---- 214
Cdd:pfam10174 474 KKENKDLKEKV-------SALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahna 546
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 672062112 215 --------DLGQKDRLLQQQQAkledalRKLSDASYQQVDLERELE 252
Cdd:pfam10174 547 eeavrtnpEINDRIRLLEQEVA------RYKEESGKAQAEVERLLG 586
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-241 |
9.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 61 PGTYLEATWE-EQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD---QSM 136
Cdd:COG4717 87 EEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----------EAELAELPERLEeleERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 137 EENQDLKKELLKCKQEARNLQGIKDALQQRLTqqdtsvLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDL 216
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|....*..
gi 672062112 217 GQ--KDRLLQQQQAKLEDALRKLSDAS 241
Cdd:COG4717 230 EQleNELEAAALEERLKEARLLLLIAA 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-259 |
1.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 129 RSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRL 208
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672062112 209 LGE-----YK-------------KDLGQKDR-------LLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLA 259
Cdd:COG4942 106 LAEllralYRlgrqpplalllspEDFLDAVRrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
122-253 |
1.51e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 122 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 201
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 672062112 202 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQ 253
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-240 |
1.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 71 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpeDEQERPVALCEPGVNPEEQLIIIRS-------------RLDQSME 137
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRLAEYSWDEIDVASaereiaeleaeleRLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 138 ENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDEL-HNQNVDLQRKLDERNRLLGEYKKdL 216
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAV-E 764
|
170 180
....*....|....*....|....
gi 672062112 217 GQKDRLLQQQQAKLEDALRKLSDA 240
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEE 788
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
66-263 |
2.72e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 66 EATWEEQLLEQQEHLEKEMEEAKKMISGLQAL---------LLNGSLPEDEQERPvaLCEPGVNPEEQLIIIRSRLDQSM 136
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskeDIPNLQNITVRLQD--LTEKLSEAEDMLACEQHALLRKL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 137 EE---NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYK 213
Cdd:TIGR00618 622 QPeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 672062112 214 KDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAHRVK 263
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
70-253 |
3.14e-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: 40.32 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 70 EEQLLEQQEHLEKEMEEAKKMISGL----QALllngslpeDEQ--------------ERPVALCE-PGVNPE---EQLII 127
Cdd:COG3096 374 AEQLAEAEARLEAAEEEVDSLKSQLadyqQAL--------DVQqtraiqyqqavqalEKARALCGlPDLTPEnaeDYLAA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 128 IRSRLDQSMEENQDLKKEL---------------LKCK-----------QEARNLqgIKDALQQRLTQQDTSvlQLKQEL 181
Cdd:COG3096 446 FRAKEQQATEEVLELEQKLsvadaarrqfekayeLVCKiageversqawQTAREL--LRRYRSQQALAQRLQ--QLRAQL 521
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672062112 182 LRAnmdKDELHNQNvDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQ 253
Cdd:COG3096 522 AEL---EQRLRQQQ-NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
135-259 |
4.32e-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: 38.75 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 135 SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 214
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 672062112 215 DLGQ--KDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLA 259
Cdd:COG1579 81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-269 |
4.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 65 LEATWEE--QLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSMEENQDL 142
Cdd:COG4913 257 IRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL--------EAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 143 KKELLK--------CKQEARNLQGIKDALQQRLTQQDTSVLQLKqelLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 214
Cdd:COG4913 329 EAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 672062112 215 DLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEV 269
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
78-253 |
5.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 78 EHLEKEMEEAKKmISGLQALLLNGSLPEDEQERPVALCEpgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQ 157
Cdd:COG4717 49 ERLEKEADELFK-PQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 158 GIKDALQQRLTQQdtsvlQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQ----QQAKLEDA 233
Cdd:COG4717 123 KLLQLLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDL 197
|
170 180
....*....|....*....|
gi 672062112 234 LRKLSDASYQQVDLERELEQ 253
Cdd:COG4717 198 AEELEELQQRLAELEEELEE 217
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
69-244 |
7.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.35 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 69 WEEQLLEQQEHLEKEMEEAKKMISGlqalllngslpedeqerpvalcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLK 148
Cdd:COG1340 134 EEKELVEKIKELEKELEKAKKALEK----------------------------NEKLKELRAELKELRKEAEEIHKKIKE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062112 149 CKQEArnlQGIKDALQQRLTQQDtsvlQLKQELlranmdkDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQA 228
Cdd:COG1340 186 LAEEA---QELHEEMIELYKEAD----ELRKEA-------DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRK 251
|
170
....*....|....*.
gi 672062112 229 KLEDALRKLSDASYQQ 244
Cdd:COG1340 252 KQRALKREKEKEELEE 267
|
|
| |
