|
Name |
Accession |
Description |
Interval |
E-value |
| DIX |
pfam00778 |
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ... |
390-465 |
9.82e-38 |
|
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: 132.27 E-value: 9.82e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119587577 390 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 465
Cdd:pfam00778 2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
|
|
| DAX |
smart00021 |
Domain present in Dishevelled and axin; Domain of unknown function. |
390-466 |
4.62e-20 |
|
Domain present in Dishevelled and axin; Domain of unknown function.
Pssm-ID: 197474 Cd Length: 83 Bit Score: 84.39 E-value: 4.62e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119587577 390 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEIFHDDDAIPGWEGKIVAWVE 466
Cdd:smart00021 4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-269 |
8.09e-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: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 70 EEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLII-IQSRLDQSMEENQDLKKELLK 148
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 149 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 228
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 119587577 229 KLEEALRKLSDvsyHQVDLERELEHKDVLLAHCMKREADEA 269
Cdd:COG1196 415 RLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-253 |
3.65e-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: 49.67 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 71 EQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEqerplalcepgvnpeEQLIIIQSRLDQSMEENQDLKKELLK 148
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLeeLRLEVSELE---------------EEIEELQKELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 149 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 228
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
170 180
....*....|....*....|....*
gi 119587577 229 KLEEALRKLSDVSYHQVDLERELEH 253
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLER 411
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
67-271 |
2.79e-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: 43.57 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 67 TSWEEQLLEQQEYLEKEMEE--AKKM--------ISGLQALLlngslpeDEQERPLAlcepGVNPEeqLIIIQSRLDQSM 136
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEEltAKKMtlessertVSDLTASL-------QEKERAIE----ATNAE--ITKLRSRVDLKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 137 EENQDLKKEllkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNR 207
Cdd:pfam15921 531 QELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRL 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119587577 208 LLGEYKKELGQKDrllqqhqAKLEEALRKLSDVSYHQVDL-----ERELEHKDVllahcmKREADEATN 271
Cdd:pfam15921 605 ELQEFKILKDKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DIX |
pfam00778 |
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ... |
390-465 |
9.82e-38 |
|
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: 132.27 E-value: 9.82e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119587577 390 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 465
Cdd:pfam00778 2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
|
|
| DAX |
smart00021 |
Domain present in Dishevelled and axin; Domain of unknown function. |
390-466 |
4.62e-20 |
|
Domain present in Dishevelled and axin; Domain of unknown function.
Pssm-ID: 197474 Cd Length: 83 Bit Score: 84.39 E-value: 4.62e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119587577 390 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEIFHDDDAIPGWEGKIVAWVE 466
Cdd:smart00021 4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-269 |
8.09e-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: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 70 EEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLII-IQSRLDQSMEENQDLKKELLK 148
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 149 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 228
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 119587577 229 KLEEALRKLSDvsyHQVDLERELEHKDVLLAHCMKREADEA 269
Cdd:COG1196 415 RLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-278 |
2.22e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 71 EQLLEQQEYLEKEMEEAKKMISGLQALLlngslpedeQERplalcepgvnpEEQLIIIQSRLDQSMEENQDLKKELLKCK 150
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKL 230
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119587577 231 EEALRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEATNYNSHNSQ 278
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-239 |
2.36e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 70 EEQLLEQQEYLEKEMEEAKKMISGLQALLLngslpEDEQERplalcepgvnpeeqlIIIQSRLDQSMEENQDLKKELLKC 149
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 150 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAK 229
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
170
....*....|
gi 119587577 230 LEEALRKLSD 239
Cdd:COG1196 479 LAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-253 |
3.65e-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: 49.67 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 71 EQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEqerplalcepgvnpeEQLIIIQSRLDQSMEENQDLKKELLK 148
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLeeLRLEVSELE---------------EEIEELQKELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 149 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 228
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
170 180
....*....|....*....|....*
gi 119587577 229 KLEEALRKLSDVSYHQVDLERELEH 253
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLER 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-260 |
5.62e-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: 48.90 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 70 EEQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEQERplalcepgVNPEEQLIIIQSRLDQSMEENQDLKKELL 147
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI--------EELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 148 KCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQ 227
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190
....*....|....*....|....*....|...
gi 119587577 228 AKLEEALRKLSDVSYHQVDLERELEHKDVLLAH 260
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-252 |
7.30e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 122 EEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 191
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119587577 192 ------HNQNVDLQRKLD--------ERNRLLGEYKKE---LGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELE 252
Cdd:COG3206 284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-240 |
3.42e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 118 GVNPEEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ--DTSVLQLKQELLRANMDKDELHNQN 195
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 119587577 196 VD---LQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDV 240
Cdd:COG4913 685 DDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-252 |
9.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 137 EENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLDERNRLLGEYK-- 213
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEal 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 119587577 214 -KELGQKD--------RLLQQHQAKLEEALRKLSDVSYHQVDLERELE 252
Cdd:COG4913 368 lAALGLPLpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
67-271 |
2.79e-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: 43.57 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 67 TSWEEQLLEQQEYLEKEMEE--AKKM--------ISGLQALLlngslpeDEQERPLAlcepGVNPEeqLIIIQSRLDQSM 136
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEEltAKKMtlessertVSDLTASL-------QEKERAIE----ATNAE--ITKLRSRVDLKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 137 EENQDLKKEllkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNR 207
Cdd:pfam15921 531 QELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRL 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119587577 208 LLGEYKKELGQKDrllqqhqAKLEEALRKLSDVSYHQVDL-----ERELEHKDVllahcmKREADEATN 271
Cdd:pfam15921 605 ELQEFKILKDKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-254 |
3.70e-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: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 71 EQLLEQQEYLEKEMEEAKKMISGLQALL---------LNGSLpEDEQERPLALCEPGVNPEEQLIIIQSRLDQSMEENQD 141
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIdkllaeieeLEREI-EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 142 LKKELLKCKQEarnlqgiKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDR 221
Cdd:TIGR02169 383 TRDELKDYREK-------LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
170 180 190
....*....|....*....|....*....|...
gi 119587577 222 LLQQHQAKLEEALRKLSDVSYHQVDLERELEHK 254
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-252 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 112 LALCEPGVNPEEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDEL 191
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119587577 192 HNQNVDLQRKLDERNRLLGE-----YKkeLGQKDRL-LQQHQAKLEEALRKLSDVSYHQVDLERELE 252
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEllralYR--LGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAE 153
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
67-269 |
1.70e-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: 41.11 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 67 TSWEEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLIIIQSRLDQSMEE---NQDLK 143
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPeqdLQDVR 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 144 KELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLL 223
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119587577 224 QQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMK---READEA 269
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKelmHQARTV 755
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
71-252 |
1.72e-03 |
|
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: 40.96 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 71 EQLLEQQEYLEKEMEEAKKMISGLQALLLNgslpedeQERPLALCEPGVNPEEQliIIQSRLDQSMEENQDLKKELLKCK 150
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSN-------TDTALTTLEEALSEKER--IIERLKEQREREDRERLEELESLK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLDERNRLLGEYKK------------ 214
Cdd:pfam10174 475 KENKDLKEKVSALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahnaeeavrtnp 554
|
170 180 190
....*....|....*....|....*....|....*...
gi 119587577 215 ELGQKDRLLQQhqakleEALRKLSDVSYHQVDLERELE 252
Cdd:pfam10174 555 EINDRIRLLEQ------EVARYKEESGKAQAEVERLLG 586
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
122-269 |
2.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 122 EEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ----------------DTSVLQLkqeLLRAN 185
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgeraralyrsggSVSYLDV---LLGSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 186 mDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKRE 265
Cdd:COG3883 113 -SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
....
gi 119587577 266 ADEA 269
Cdd:COG3883 192 AAAE 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
75-269 |
3.03e-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: 39.75 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 75 EQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNP-EEQLIIIQSRLDQSMEENQDLKKELLKCKQEa 153
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 154 rnLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEA 233
Cdd:COG4942 99 --LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 119587577 234 LRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEA 269
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
72-237 |
3.58e-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: 39.36 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 72 QLLEQQEYLEKEMEEAKKMISGLQALLlngslpeDEQERPLA-----LCEPGVNPEEQLIIIQSRLDQSMEENQDLKKEL 146
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAEL-------EAQKEELAellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 147 LKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlranmdkDELHNQNVDLQRKLDERNRLLGEYKKELGQKDR---LL 223
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALL-------AELEEERAALEALKAERQKLLARLEKELAELAAelaEL 218
|
170
....*....|....
gi 119587577 224 QQHQAKLEEALRKL 237
Cdd:COG4942 219 QQEAEELEALIARL 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
135-274 |
5.35e-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: 38.37 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 135 SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 214
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119587577 215 ELGQ--KDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEATNYNS 274
Cdd:COG1579 81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
71-249 |
5.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 71 EQLLEQQEYLEKEMEEAKKMISGLQALLLNgslpEDEQERPLALCEPGVNPEEQLIIIQSRLD---QSMEENQDLKKELL 147
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEK----LEKLLQLLPLYQELEALEAELAELPERLEeleERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 148 KCKQEARNLQGIKDALQQRLTqqdtsvLQLKQELLRANMDKDELHNQNVDLQRKLDErnrllgeykkelgqkdrlLQQHQ 227
Cdd:COG4717 167 ELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEE------------------AQEEL 222
|
170 180
....*....|....*....|..
gi 119587577 228 AKLEEALRKLSDVSYHQVDLER 249
Cdd:COG4717 223 EELEEELEQLENELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-253 |
7.78e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587577 132 LDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQ--QDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLL 209
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 119587577 210 GEYKkelgQKDRLLQQHQAKLEEALRKLSDVSYHQV-DLERELEH 253
Cdd:COG4717 163 EELE----ELEAELAELQEELEELLEQLSLATEEELqDLAEELEE 203
|
|
| |
