|
Name |
Accession |
Description |
Interval |
E-value |
| IFT81_CH |
pfam18383 |
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in ... |
3-126 |
2.00e-67 |
|
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in IFT81 proteins. Crystal structure analysis revealed that IFT81-N adopts the fold of a calponin homology (CH) domain with structural similarity to the kinetochore complex component NDC80 with microtubule (MT)-binding properties. Functional analysis show that IFT74 and IFT81 form a tubulin-binding module required for ciliogenesis. It is suggested that IFT81-N binds the globular domain of tubulin to provide specificity, and IFT74-N recognizes the beta-tubulin tail to increase affinity.
Pssm-ID: 465736 Cd Length: 124 Bit Score: 210.57 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 3 DQIKFIMDSLNKEPFRKNYNLITFDSLEPMQLLQVLSDVLAEIDPKQLVDIREEMPEQTAKRMLSLLGILKYKPSGNATD 82
Cdd:pfam18383 1 ENLKFIVTELNKEPFNKNYNLITFDSLSPEQLLQVLNDVLAEIDPKQKVDIREESPEETAIRILEALRILKYKPPPDIDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1124872660 83 MSTFRQGLVIGSKPVIYPVLHWLLQRTNELKKRAYLARFLIKLE 126
Cdd:pfam18383 81 PSAFRQGLVRGEKLVIYPILYWLLSNVEELKKRAYLARFLVKVE 124
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-407 |
1.67e-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: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 142 KQYEELMEAFKTLHKEYEQLKISGFST--AEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQwmLKIARQLRVEKERE 219
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAelEELEAELEELEAELEELEAELAELEAELEELRLEL--EELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 220 EYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADAkpESLMKRLEEEIKFNLYMVTEKFPKELENKKKELHFLQKVV 299
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 300 SEPAMGHSDLLELESKINEINTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLEREASVK 379
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260
....*....|....*....|....*...
gi 1124872660 380 RNQTREFDGTEVLKGDERQDLTLSPRLE 407
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-398 |
9.81e-06 |
|
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: 48.14 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 134 DETVADTNKQYEELMEAFKTLHKEYEQLkiSGFSTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQWMLKIAR-QL 212
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 213 RVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQ---AAADAKPESLMKRLEEeikfnLYMVTEKFPKELENKK 289
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK-----LEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 290 KELHFLQKVVSEPAMGHSDLLELESKINEINTEINQL---IEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQEAK 366
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
250 260 270
....*....|....*....|....*....|..
gi 1124872660 367 EKLASLEREASVKRNQTREFDGTEVLKGDERQ 398
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
169-293 |
2.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 169 AEIRKDISAMEEEKDQLIKRVEHLKKRVETAqnhqwmLKIARQLR--VEKEREEyLAQQKQEQKNQLFHAVQRL-QRVQN 245
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK------AEEAEALLkeAEKLKEE-LEEKKEKLQEEEDKLLEEAeKEAQQ 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1124872660 246 QLKSMRQAAADakpesLMKRLEEEIKFNLYMVTEkfpKELENKKKELH 293
Cdd:PRK00409 578 AIKEAKKEADE-----IIKELRQLQKGGYASVKA---HELIEARKRLN 617
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IFT81_CH |
pfam18383 |
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in ... |
3-126 |
2.00e-67 |
|
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in IFT81 proteins. Crystal structure analysis revealed that IFT81-N adopts the fold of a calponin homology (CH) domain with structural similarity to the kinetochore complex component NDC80 with microtubule (MT)-binding properties. Functional analysis show that IFT74 and IFT81 form a tubulin-binding module required for ciliogenesis. It is suggested that IFT81-N binds the globular domain of tubulin to provide specificity, and IFT74-N recognizes the beta-tubulin tail to increase affinity.
Pssm-ID: 465736 Cd Length: 124 Bit Score: 210.57 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 3 DQIKFIMDSLNKEPFRKNYNLITFDSLEPMQLLQVLSDVLAEIDPKQLVDIREEMPEQTAKRMLSLLGILKYKPSGNATD 82
Cdd:pfam18383 1 ENLKFIVTELNKEPFNKNYNLITFDSLSPEQLLQVLNDVLAEIDPKQKVDIREESPEETAIRILEALRILKYKPPPDIDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1124872660 83 MSTFRQGLVIGSKPVIYPVLHWLLQRTNELKKRAYLARFLIKLE 126
Cdd:pfam18383 81 PSAFRQGLVRGEKLVIYPILYWLLSNVEELKKRAYLARFLVKVE 124
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-407 |
1.67e-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: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 142 KQYEELMEAFKTLHKEYEQLKISGFST--AEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQwmLKIARQLRVEKERE 219
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAelEELEAELEELEAELEELEAELAELEAELEELRLEL--EELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 220 EYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADAkpESLMKRLEEEIKFNLYMVTEKFPKELENKKKELHFLQKVV 299
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 300 SEPAMGHSDLLELESKINEINTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLEREASVK 379
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260
....*....|....*....|....*...
gi 1124872660 380 RNQTREFDGTEVLKGDERQDLTLSPRLE 407
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
168-382 |
6.37e-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: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 168 TAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQWMLKIARQLRVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQL 247
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 248 KSMRQAAADAKPESLMKRLEEEIkfnlymvtekfpKELENKKKELhfLQKVVSEpamgHSDLLELESKINEINTEINQLI 327
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQL------------AELEAELAEL--SARYTPN----HPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124872660 328 EKKM--MRNEpiegKLSLYRQQASIISRKKEAKAE--ELQEAKEKLASLEREASVKRNQ 382
Cdd:COG3206 312 QRILasLEAE----LEALQAREASLQAQLAQLEARlaELPELEAELRRLEREVEVAREL 366
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-398 |
9.81e-06 |
|
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: 48.14 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 134 DETVADTNKQYEELMEAFKTLHKEYEQLkiSGFSTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQWMLKIAR-QL 212
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 213 RVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQ---AAADAKPESLMKRLEEeikfnLYMVTEKFPKELENKK 289
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK-----LEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 290 KELHFLQKVVSEPAMGHSDLLELESKINEINTEINQL---IEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQEAK 366
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
250 260 270
....*....|....*....|....*....|..
gi 1124872660 367 EKLASLEREASVKRNQTREFDGTEVLKGDERQ 398
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-374 |
6.98e-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: 45.43 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 134 DETVADTNKQYEELMEAFKTLHKEYEQLkisgfstaeiRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQWMLKiARQLR 213
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEEL----------RLEVSELEEEIEELQKELYALANEISRLEQQKQILR-ERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 214 VEKEREEYLAQ-----QKQEQKNQLFHAVQ-RLQRVQNQLKSMRQAAADAKP-----ESLMKRLEEEIK------FNLYM 276
Cdd:TIGR02168 314 LERQLEELEAQleeleSKLDELAEELAELEeKLEELKEELESLEAELEELEAeleelESRLEELEEQLEtlrskvAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 277 VTEKFPKELENKKKELHFLQKVVS---------EPAMGHSDLLELESKINEINTEINQLIEkkmmRNEPIEGKLSLYRQQ 347
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRErlqqeieelLKKLEEAELKELQAELEELEEELEELQE----ELERLEEALEELREE 469
|
250 260
....*....|....*....|....*..
gi 1124872660 348 ASIISRKKEAKAEELQEAKEKLASLER 374
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLER 496
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
169-293 |
2.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 169 AEIRKDISAMEEEKDQLIKRVEHLKKRVETAqnhqwmLKIARQLR--VEKEREEyLAQQKQEQKNQLFHAVQRL-QRVQN 245
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK------AEEAEALLkeAEKLKEE-LEEKKEKLQEEEDKLLEEAeKEAQQ 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1124872660 246 QLKSMRQAAADakpesLMKRLEEEIKFNLYMVTEkfpKELENKKKELH 293
Cdd:PRK00409 578 AIKEAKKEADE-----IIKELRQLQKGGYASVKA---HELIEARKRLN 617
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
128-377 |
2.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 128 PSEFLQDETVADTNKQYEELMEAFKTLHKEYEQLKisgFSTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNhqwmlK 207
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-----E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 208 IARQLRvekereeylAQQKQEQK----NQLFHA------VQRLQRVQNQLKSMRQAAADAKpeSLMKRLEEEIkfnlymv 277
Cdd:COG3883 88 LGERAR---------ALYRSGGSvsylDVLLGSesfsdfLDRLSALSKIADADADLLEELK--ADKAELEAKK------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 278 tekfpKELENKKKELHFLQKVVSEpamghsDLLELESKINEINTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEA 357
Cdd:COG3883 150 -----AELEAKLAELEALKAELEA------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250 260
....*....|....*....|
gi 1124872660 358 KAEELQEAKEKLASLEREAS 377
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
183-400 |
3.92e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 183 DQLIKRVEHLKKRVETA---QNHQWMLKI------ARQLRVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQA 253
Cdd:COG1196 196 GELERQLEPLERQAEKAeryRELKEELKEleaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 254 AADAKpESLMKRLEEEikFNLYMVTEKFPKELENKKKELHFLQKVVSEpamGHSDLLELESKINEINTEINQLIEKKMM- 332
Cdd:COG1196 276 LEELE-LELEEAQAEE--YELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEa 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 333 --RNEPIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLEREASVKRNQTREFDGTEVLKGDERQDL 400
Cdd:COG1196 350 eeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-396 |
4.95e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 138 ADTNKQYEELMEAFKTLHKEYEQLKisgfsTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQwmLKIARQLRVEKE 217
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEE 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 218 REEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADAKPESLMKRLEEEIKfnlymVTEKFPKELENKKKELHFLQK 297
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-----KADEAKKKAEEKKKADEAKKK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 298 V--------VSEPAMGHSDLLELESKINEINT--EINQLIEKKmMRNEPIEGKLSLYRQQASIISRKKEA--KAEELQEA 365
Cdd:PTZ00121 1440 AeeakkadeAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEA-KKADEAKKKAEEAKKKADEAKKAAEAkkKADEAKKA 1518
|
250 260 270
....*....|....*....|....*....|..
gi 1124872660 366 KEKLASLE-REASVKRNQTREFDGTEVLKGDE 396
Cdd:PTZ00121 1519 EEAKKADEaKKAEEAKKADEAKKAEEKKKADE 1550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-374 |
5.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 142 KQYEELMEAFKTLHKEYEQLkisgfstaEIRKDISAMEEEKDQLIKRVEHLKKRVETAQnhqwMLKIARQLRVEKEREEY 221
Cdd:COG4913 232 EHFDDLERAHEALEDAREQI--------ELLEPIRELAERYAAARERLAELEYLRAALR----LWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 222 LAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADAKPESLmKRLEEEIKfnlymVTEKFPKELENKKKELHFLQKVVSE 301
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL-EQLEREIE-----RLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124872660 302 PAMGHSDLLEleskinEINTEINQLIEKkmmrnepIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLER 374
Cdd:COG4913 374 PLPASAEEFA------ALRAEAAALLEA-------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
170-363 |
5.44e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 170 EIRKDISAMEEEKDQLIKRVEHL-KKRVETAQNHQWMLKIARQLRVEKEREEYLAQQKQEQKNQLfhavqrlqrvQNQLK 248
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI----------KNRYK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 249 SMRQAAADAKPESLMKRLEEEIKFNLymvtEKFPKELENKKKELHFLQKVVSEPAMGHSD--------LLELESKINEIN 320
Cdd:PRK01156 557 SLKLEDLDSKRTSWLNALAVISLIDI----ETNRSRSNEIKKQLNDLESRLQEIEIGFPDdksyidksIREIENEANNLN 632
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1124872660 321 TEINQLIEKKMMRnEPIEGKLSLYRQQAS----IISRKKEAKAEELQ 363
Cdd:PRK01156 633 NKYNEIQENKILI-EKLRGKIDNYKKQIAeidsIIPDLKEITSRIND 678
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
135-325 |
5.49e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.26 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 135 ETVADTN-KQYEELMEAFKTLHKEYEQLkISGFSTAEIRKDISAMEEEKDQLIKRVEHLKKRV--ETAQNHQWMLKIAR- 210
Cdd:TIGR01612 1499 KDEADKNaKAIEKNKELFEQYKKDVTEL-LNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFilEAEKSEQKIKEIKKe 1577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 211 QLRVEKEREEYLAQQKQEQKNQLfhAVQRLQRVQNQLKSMRQAAAD--AKPESLMKRL--------EEEIKFNLYMVT-- 278
Cdd:TIGR01612 1578 KFRIEDDAAKNDKSNKAAIDIQL--SLENFENKFLKISDIKKKINDclKETESIEKKIssfsidsqDTELKENGDNLNsl 1655
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1124872660 279 EKFPKELENKKKELHFLQKvvsepamghsDLLELESKINEINTEINQ 325
Cdd:TIGR01612 1656 QEFLESLKDQKKNIEDKKK----------ELDELDSEIEKIEIDVDQ 1692
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
133-385 |
7.07e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 133 QDETVADTNKQYEELMEAFKTLHKEYEQLKISgfsTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNH------QWML 206
Cdd:PRK02224 228 QREQARETRDEADEVLEEHEERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaEAGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 207 KIARQLRVEKEREEyLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADakpeslmkrLEEEikfnlymvtekfPKELE 286
Cdd:PRK02224 305 DDADAEAVEARREE-LEDRDEELRDRLEECRVAAQAHNEEAESLREDADD---------LEER------------AEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 287 NKKKELHflqkvvSEPAMGHSDLLELESKINEINTEINQLIEKkmMRNEPIE-GKLSLYRqqasiisrkkEAKAEELQEA 365
Cdd:PRK02224 363 EEAAELE------SELEEAREAVEDRREEIEELEEEIEELRER--FGDAPVDlGNAEDFL----------EELREERDEL 424
|
250 260
....*....|....*....|
gi 1124872660 366 KEKLASLEREASVKRNQTRE 385
Cdd:PRK02224 425 REREAELEATLRTARERVEE 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-393 |
7.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 175 ISAMEEEKDQLIKRveHLKKRVETAQNHQWMLKIARQLRVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAA 254
Cdd:COG4717 48 LERLEKEADELFKP--QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 255 ADAKPESLMKRLEEEIkfnlymvtEKFPKELENKKKELHFLQKVVSEpamghsdLLELESKINEINTEINQLIEKkmmRN 334
Cdd:COG4717 126 QLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEE-------LEELEAELAELQEELEELLEQ---LS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124872660 335 EPIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLEREASVKRNQTREFDGTEVLK 393
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
110-429 |
7.90e-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: 38.80 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 110 NELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKTLHKEYEQLKISGFSTAEIRKDIS---AMEEEKDQLI 186
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 187 KRVEHLKKRVETA-QNHQWMLKIARQLRVEKEREEYLaQQKQEQKNQLFHAVQRLQRVQNQlksmrQAAADAKPESLMKR 265
Cdd:TIGR00618 277 AVLEETQERINRArKAAPLAAHIKAVTQIEQQAQRIH-TELQSKMRSRAKLLMKRAAHVKQ-----QSSIEEQRRLLQTL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 266 LEEEIKFNLYMVTEKFPKELENKKKELHFLQKVVSEPAMGHSDLLELESKINEINTEINQLIEKKMMRNEPIEGKL---- 341
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahak 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124872660 342 --------SLYRQQASIISRKKEAKAEE--LQEAKEKLASLEREASVKRNQTREFDGTEVLKGDERQDLTLSPRLECGGV 411
Cdd:TIGR00618 431 kqqelqqrYAELCAAAITCTAQCEKLEKihLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
330
....*....|....*...
gi 1124872660 412 IMAYCSLKLLGSSDPPTS 429
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTR 528
|
|
| |
