|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-426 |
9.92e-13 |
|
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: 71.98 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 150 DISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALE 229
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 230 ESRAQAEQALSEKESQIETLVTSLLKMK-DWAAVLGEADDGNLDLDMKSglENTAALDNQPKgALKKLIyaAKLNASLKA 308
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKqNLEQKQKELKSKEKELKKLN--EEKKELEEKVK-DLTKKI--SSLKEKIEK 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 309 LEGERNQVYTQLS----EVDQVKEDLT------------EHIKSLESKQASLQSEKTEFEsesQKLQQKLKVITELYQEN 372
Cdd:TIGR04523 529 LESEKKEKESKISdledELNKDDFELKkenlekeideknKEIEELKQTQKSLKKKQEEKQ---ELIDQKEKEKKDLIKEI 605
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720372425 373 EMKLHRKLTVEENYRLEKEE--KLSKVDEKISHATEELEtcrQRAKDLEEELERTI 426
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKEneKLSSIIKNIKSKKNKLK---QEVKQIKETIKEIR 658
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
70-480 |
1.33e-12 |
|
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: 71.20 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 70 YVGREKKLALELSALIEEKCKLLDKVSIVQKEFVEGSQISEATYENLEQSKSKLEDEILLLEekleeerAKHSEQDElma 149
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS-------EKQKELEQ--- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 150 dISKRIQSLEDESKSLKSQVAEAKTtfrifEINEERLKGAIKDALNENSQLQESQKQLLQETEM---MKEQVNDLDKQKV 226
Cdd:TIGR04523 279 -NNKKIKELEKQLNQLKSEISDLNN-----QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 227 ALEESRAQAEQALSEKESQIETLvtslLKMKDwaavlgEADDGNLDLDM-KSGLENTaaLDNQPKgalkkliYAAKLNAS 305
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKL----KKENQ------SYKQEIKNLESqINDLESK--IQNQEK-------LNQQKDEQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 306 LKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHRK------ 379
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelks 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 380 ---------------------LTVEENYRLEKEEKLS----KVDEKISHATEELETCRQRAKdlEEELERTIHSYQgQVI 434
Cdd:TIGR04523 494 kekelkklneekkeleekvkdLTKKISSLKEKIEKLEsekkEKESKISDLEDELNKDDFELK--KENLEKEIDEKN-KEI 570
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1720372425 435 SHEKKAHDNWLAART--------LERNLNDLRKENAHNRQKLTETEFKFELLEK 480
Cdd:TIGR04523 571 EELKQTQKSLKKKQEekqelidqKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-422 |
2.11e-12 |
|
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: 70.86 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 146 ELMADISKRIQSLEDESKSLKSQVAEAKTTfrifeinEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQK 225
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKE-------LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 226 VALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEADDgnlDLDMKSGLENTAALDNQPKgalkkliyaaklnas 305
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD---ELRAELTLLNEEAANLRER--------------- 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 306 LKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITE---LYQENEMKLHRKLTV 382
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalaLLRSELEELSEELRE 905
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720372425 383 EENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEEL 422
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-411 |
1.15e-10 |
|
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: 65.46 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 73 REKKLALELSALIEEKCKLLDKVSIVQ-KEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADI 151
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 152 SKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEES 231
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 232 RAQAEQALSEKESQIETLVTSLLKMKDWAAVLgEADDGNLDLDMKSGLENTAALDNQPKGALKKLiyaakLNASLKALEG 311
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASL-NNEIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 312 ERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELyQENEMKLHRKLTVEENYRLEKE 391
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEGVKALLKNQSGLS 519
|
330 340
....*....|....*....|
gi 1720372425 392 EKLSKVDEKIShATEELETC 411
Cdd:TIGR02168 520 GILGVLSELIS-VDEGYEAA 538
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
184-426 |
2.49e-10 |
|
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: 63.24 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 184 ERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVL 263
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 264 geaddgnLDLDMKSGLENTAAL---DNQPKGALKKLIYAAKLNASLKAlegernqvytQLSEVDQVKEDLTEHIKSLESK 340
Cdd:COG4942 110 -------LRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 341 QASLQSEKTEFESESQKLQQKLKvitelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETCRQRAKDLEE 420
Cdd:COG4942 173 RAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
....*.
gi 1720372425 421 ELERTI 426
Cdd:COG4942 228 LIARLE 233
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-367 |
2.54e-10 |
|
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: 63.89 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 80 ELSALIEEKCKLLDKVSIVQKEfvegSQISEATYENLEQSKSKledeillleekleeeraKHSEQDELMADISKR---IQ 156
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKL----NQQKDEQIKKLQQEKEL-----------------LEKEIERLKETIIKNnseIK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 157 SLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKdalNENSQLQESQKQLLQETEMMK----------EQVNDLDKQKV 226
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSKEKELKklneekkeleEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 227 ALEESRAQAEQALSEKESQIETLVTSLLKMKD---WAAVLGEADDGNLDLDmKSGLENTAALDNQPKgaLKKLIyaakln 303
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIE-ELKQTQKSLKKKQEE--KQELI------ 591
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720372425 304 aslKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITE 367
Cdd:TIGR04523 592 ---DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-421 |
2.62e-10 |
|
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: 64.32 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 73 REKKLALELSALIEEKCK-----LLDKVSIVQKEFVEG-SQISEATyENLEQSKSKLEDeillleekleeeRAKHSEQDE 146
Cdd:TIGR02169 205 REREKAERYQALLKEKREyegyeLLKEKEALERQKEAIeRQLASLE-EELEKLTEEISE------------LEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 147 -LMADISKRIQSL-EDESKSLKSQVAEakttfriFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQ 224
Cdd:TIGR02169 272 qLLEELNKKIKDLgEEEQLRVKEKIGE-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 225 KVALEESRAQAEQALSEKESQIETLVtsllkmkdwaAVLGEADdgnldldmksglENTAALDNQPKGALKKLiyaAKLNA 304
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLR----------AELEEVD------------KEFAETRDELKDYREKL---EKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 305 SLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHRkltvee 384
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD------ 473
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720372425 385 nyrleKEEKLSKVDEKISHATEELETCRQRAKDLEEE 421
Cdd:TIGR02169 474 -----LKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-468 |
3.45e-10 |
|
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: 63.92 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 138 RAKHSEQDELMADIS-KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAI---KDALNENSQLQESQKQLLQETem 213
Cdd:TIGR02168 216 KELKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelRLEVSELEEEIEELQKELYAL-- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 214 mKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKdwaavlgeaddgnldldmksglENTAALDNQPKGAL 293
Cdd:TIGR02168 294 -ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----------------------EELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 294 KKLiyaAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENE 373
Cdd:TIGR02168 351 EEL---ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 374 MKLhrkltvEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLE---EELERTIHSYQGQVISHEKKAHdnwlAARTL 450
Cdd:TIGR02168 428 KKL------EEAELKELQAELEELEEELEELQEELERLEEALEELReelEEAEQALDAAERELAQLQARLD----SLERL 497
|
330 340
....*....|....*....|.
gi 1720372425 451 ERNLNDLR---KENAHNRQKL 468
Cdd:TIGR02168 498 QENLEGFSegvKALLKNQSGL 518
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
184-373 |
1.99e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 184 ERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTsllKMKDWAAVL 263
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 264 GEADDGNLDLDMKSGLENTA-ALDNQpkGALKKLiyAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQA 342
Cdd:COG3883 96 YRSGGSVSYLDVLLGSESFSdFLDRL--SALSKI--ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|.
gi 1720372425 343 SLQSEKTEFESESQKLQQKLKVITELYQENE 373
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-470 |
5.25e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 145 DELMADISKRIQSLEDEskslksqvAEAKTTFRIFEINEERLKGAIkdALNENSQLQESQKQLLQETEMMKEQVNDLDKQ 224
Cdd:COG1196 192 EDILGELERQLEPLERQ--------AEKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 225 KVALEESRAQAEQALSEKESQIETLVTSLLkmkdwaavLGEADDGNLDLDMKSGLENTAALDNQpkgalkkliyAAKLNA 304
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEY--------ELLAELARLEQDIARLEERRRELEER----------LEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 305 SLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEmklhRKLTVEE 384
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL----RAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 385 NYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEKKAhdnwLAARTLERNLNDLRKENAHN 464
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE----EEEEALLELLAELLEEAALL 475
|
....*.
gi 1720372425 465 RQKLTE 470
Cdd:COG1196 476 EAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-424 |
2.30e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 80 ELSALIEEKCKLLDKVSIVQKEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEErakhSEQDELMADISKRIQSLE 159
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL----TELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 160 DESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQAL 239
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 240 SEKESQIETLVTSLlkmkdwaavlgeaddgnldldmksglentaaldnqpkgalkkliyaAKLNASLKALEGERNQVYTQ 319
Cdd:TIGR02168 855 ESLAAEIEELEELI----------------------------------------------EELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 320 LSEVDQVKEDLTEHIKSLESKqaslqseKTEFESESQKLQQKLKVITELYQENEMKLHRKL-TVEENYRLEKEEklskVD 398
Cdd:TIGR02168 889 LALLRSELEELSEELRELESK-------RSELRRELEELREKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEE----AE 957
|
330 340
....*....|....*....|....*.
gi 1720372425 399 EKISHATEELETCRQRAKDLEEELER 424
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
73-484 |
3.60e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 73 REKKLALELSALIEEKCKLLDKVSIVQKEFVEGSQISEATY---ENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMA 149
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 150 DI---SKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMmkeqvnDLDKQKV 226
Cdd:pfam05483 318 DLqiaTKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM------ELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 227 ALEEsraqAEQALSEKESQIETLVTSLlkmkdwaavlgeADDGNLdLDMKSGLENTAaldNQPKGALKKLIYAaklnasL 306
Cdd:pfam05483 392 ELEE----MTKFKNNKEVELEELKKIL------------AEDEKL-LDEKKQFEKIA---EELKGKEQELIFL------L 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 307 KALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITElyQENEMKLHRKLTVEENY 386
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ--EASDMTLELKKHQEDII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 387 RLEKEE-----KLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKEN 461
Cdd:pfam05483 524 NCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
410 420
....*....|....*....|...
gi 1720372425 462 AHNRQKLTETEFKFELLEKDPYA 484
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSA 626
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-384 |
3.89e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 113 YENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKD 192
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 193 ALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLkmkDWAAVLGEADDGNLD 272
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 273 LdmksgLENTAALDNQPKGALKKLiyaAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFE 352
Cdd:COG1196 391 A-----LRAAAELAAQLEELEEAE---EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270
....*....|....*....|....*....|..
gi 1720372425 353 SESQKLQQKLKVITELYQENEMKLHRKLTVEE 384
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
155-460 |
4.06e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 155 IQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVND----LDKQKVALEE 230
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDmtleLKKHQEDIIN 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 231 SRAQAEQALSekesQIETLVTSLLKMKDwaavlgEADDGNLDLDMKsGLENTAALDNQPKGALKKLIYAAKLNASLKALE 310
Cdd:pfam05483 525 CKKQEERMLK----QIENLEEKEMNLRD------ELESVREEFIQK-GDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 311 GERNQVYTQLSEVDQVKEDLTEHIKSL------ESKQAS---LQSEKTEFESESQKlqQKLKVITELYQEnemKLHRKLT 381
Cdd:pfam05483 594 NKCNNLKKQIENKNKNIEELHQENKALkkkgsaENKQLNayeIKVNKLELELASAK--QKFEEIIDNYQK---EIEDKKI 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 382 VEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSY-------QGQVISHEKKAHDNWLAARTLERNL 454
Cdd:pfam05483 669 SEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdkiieerDSELGLYKNKEQEQSSAKAALEIEL 748
|
....*.
gi 1720372425 455 NDLRKE 460
Cdd:pfam05483 749 SNIKAE 754
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
63-367 |
8.34e-08 |
|
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: 56.21 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 63 RSIRSRFYVGREKKLALELSALI--------EEKCKLLDKVSIVQKEFVEGSQISEATYE----NLEQSKSKLEdeilll 130
Cdd:TIGR01612 662 KSELSKIYEDDIDALYNELSSIVkenaidntEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsNIENKKNELL------ 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 131 eekleeerakhseqdELMADISKRIQSleDESKSLKSQVAEakttfriFEINEERLKGAIKDALNENSQLQESQKQLLQE 210
Cdd:TIGR01612 736 ---------------DIIVEIKKHIHG--EINKDLNKILED-------FKNKEKELSNKINDYAKEKDELNKYKSKISEI 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 211 TEMMKEQVNdLDKQKValEESRAQAEQA------LSEKESQIETLVTSLLKMKDwaAVLGEAD-----DGNLDLDMKSGL 279
Cdd:TIGR01612 792 KNHYNDQIN-IDNIKD--EDAKQNYDKSkeyiktISIKEDEIFKIINEMKFMKD--DFLNKVDkfinfENNCKEKIDSEH 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 280 ENTAALDNQPKGAL--KKL-IYAAKLNAS-------LKALEGERNQVYTqLSEVD---QVKEDLTEHIKSLESKQASLQs 346
Cdd:TIGR01612 867 EQFAELTNKIKAEIsdDKLnDYEKKFNDSkslineiNKSIEEEYQNINT-LKKVDeyiKICENTKESIEKFHNKQNILK- 944
|
330 340
....*....|....*....|.
gi 1720372425 347 ektefesesQKLQQKLKVITE 367
Cdd:TIGR01612 945 ---------EILNKNIDTIKE 956
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-423 |
1.64e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 150 DISKRIQSLEDESKSLKSQVAEAKTtfrifeineerlkgAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALE 229
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRV--------------AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 230 ESRAQAEQALSEKESQIETLVTSLlkmKDWAAVLGEADDGNLDLdmksgLENTAALDNQpkgalkkliyAAKLNASLKAL 309
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERF---GDAPVDLGNAEDFLEEL-----REERDELRER----------EAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 310 EGERNQVYT---------------------QLSEVDQVKEDLTEHIKSLESKQASLQS------EKTEFESESQKLQQKL 362
Cdd:PRK02224 439 RERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERR 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720372425 363 KVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHAT---EELETCRQRAKDLEEELE 423
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeEEAEEAREEVAELNSKLA 582
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-480 |
2.14e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 75 KKLALELSALIEEKCKLLDKVSIVQKEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEER---AKHSEQDELMADI 151
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 152 SKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGA--IKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALE 229
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 230 ------ESRAQAEQALSEKESQIETLVTSL--LKMKDWAAVLGEADdgnldldmKSGLENTAALDN--QPKGALKKLIya 299
Cdd:PRK03918 352 krleelEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELE--------KAKEEIEEEISKitARIGELKKEI-- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 300 AKLNASLKALEGERNQVYTQLSEVDQvkEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVItELYQENEMKLHRK 379
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 380 LTVEENYRlEKEEKLSKVD-EKISHATEELETCRQRAKDLEEELERtihsyqgqVISHEKKAHDNWLAARTLERNLNDLR 458
Cdd:PRK03918 499 KELAEQLK-ELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKS--------LKKELEKLEELKKKLAELEKKLDELE 569
|
410 420
....*....|....*....|...
gi 1720372425 459 KENAHNRQKLTETEFK-FELLEK 480
Cdd:PRK03918 570 EELAELLKELEELGFEsVEELEE 592
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-430 |
5.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 215 KEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLkmkDWAAVLGEADDgnlDLDMKSGLENTAALDNQpkgaLK 294
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE---ALQRLAEYSWD---EIDVASAEREIAELEAE----LE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 295 KLIyaaKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEktefesesqklQQKLKVITELYQENEM 374
Cdd:COG4913 679 RLD---ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-----------LDELQDRLEAAEDLAR 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720372425 375 KLHRKLTVEENYRLEKEEKLSKVDEKIshaTEELETCRQRAKDLEEELERTIHSYQ 430
Cdd:COG4913 745 LELRALLEERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERAMRAFN 797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-423 |
1.22e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 145 DELMADISKRIQSLEDESKSLKSQVAEAKTTFRifEINEerlkgaIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQ 224
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLR--EINE------ISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 225 KVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEaddgnldldMKSGLENTAALDNQPKGALKKLiyaAKLNA 304
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE---------LKEKAEEYIKLSEFYEEYLDEL---REIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 305 SLKALEGERNQVYTQLSEVDQVK---EDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHRKLT 381
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720372425 382 VEENYRLEKEEKLSKVDEKIShateELETCRQRAKDLEEELE 423
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
138-466 |
1.68e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 138 RAKHSEQDELMADISKRIQSLedeskslKSQVAEAKTTFRIFEINEERLKgaikdalNENSQLQES-QKQLLQETEMMKE 216
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKA-------SREETFARTALKNARLDLRRLF-------DEKQSEKDKkNKALAERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 217 QVNDLDKQKVALEEsraQAEQALSEKESQIETLVTSllKMKDWAAVLGEADD--GNLDLDMKSGLENTAA----LDNQPK 290
Cdd:pfam12128 683 RLNSLEAQLKQLDK---KHQAWLEEQKEQKREARTE--KQAYWQVVEGALDAqlALLKAAIAARRSGAKAelkaLETWYK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 291 GALKKL----IYAAKLNASLKALEGERNQVYTQLSEVDQVkEDLTEHIKSLESKQasLQSEKTEFESESQKLQQKLKVIT 366
Cdd:pfam12128 758 RDLASLgvdpDVIAKLKREIRTLERKIERIAVRRQEVLRY-FDWYQETWLQRRPR--LATQLSNIERAISELQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 367 ELYQENEMKLHRKLTVEENYRLEKEEKLSKV-------------------DEKISHATEELETCRQRAKDLEEELERTIH 427
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQVRLSENLRGLrcemsklatlkedanseqaQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720372425 428 SYQGQVISHEKKAHD-NWLAARTLERNLNDLRKENAHNRQ 466
Cdd:pfam12128 915 HFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-472 |
2.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 299 AAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITEL---YQENEMK 375
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrreLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 376 LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTihsyQGQVISHEKKAHDNWLAARTLERNLN 455
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAA 396
|
170
....*....|....*..
gi 1720372425 456 DLRKENAHNRQKLTETE 472
Cdd:COG1196 397 ELAAQLEELEEAEEALL 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-481 |
3.62e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 138 RAKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQE----TEM 213
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlSLA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 214 MKEQVNDLDKQKVALEESRAQAEQALSEKESQIETL---VTSLLKMKDWAAVLGEADDGNLDLDMKSGLENTAALDNQPK 290
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 291 GALKKLIYAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQK--LQQKLKVITEL 368
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeeLLELLDRIEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 369 YQENE--MKLHRKLTVEEnYRLEKEEKLSKVDekishaTEELETCRQRAKDLEE--ELERTIHSYQGQVISHEKKAHDNW 444
Cdd:COG4717 350 QELLReaEELEEELQLEE-LEQEIAALLAEAG------VEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELL 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720372425 445 LAA---------RTLERNLNDLRKENAHNRQKLTETEFKFELLEKD 481
Cdd:COG4717 423 EALdeeeleeelEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
307-424 |
4.30e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 307 KALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFEsesQKLQQKLKVITELyqENEMKLHRKltvEENY 386
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE---AELEEKDERIERL--ERELSEARS---EERR 459
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720372425 387 RLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELER 424
Cdd:COG2433 460 EIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
80-474 |
6.82e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 80 ELSALIEEKCKLLDKVSIVqKEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEqdELMADISK---RIQ 156
Cdd:PRK03918 339 RLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKE--EIEEEISKitaRIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 157 SLEDESKSLKSQVAEAKTTFRIF-----EINEE-------RLKGAIKDALNENSQLQESQKQL---LQETEMMKEQVNDL 221
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCpvcgrELTEEhrkelleEYTAELKRIEKELKEIEEKERKLrkeLRELEKVLKKESEL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 222 DKQKVALEESRAQAE-------QALSEKESQIETLVTSLLKMKdwaavlGEADDGNLDLDMKSGLEntaaldnqpkgalK 294
Cdd:PRK03918 496 IKLKELAEQLKELEEklkkynlEELEKKAEEYEKLKEKLIKLK------GEIKSLKKELEKLEELK-------------K 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 295 KLiyaAKLNASLKALEGERNQVYTQLSE-----VDQVKEDLTE-------------HIKSLESKQASLQSEKTEFESESQ 356
Cdd:PRK03918 557 KL---AELEKKLDELEEELAELLKELEElgfesVEELEERLKElepfyneylelkdAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 357 KLQQKLKVITELyqENEMKLHRKLTVEENYRlEKEEKLSKVDEKISHATEELEtcrqRAKDLEEELERTIHSYQGQVISH 436
Cdd:PRK03918 634 ELAETEKRLEEL--RKELEELEKKYSEEEYE-ELREEYLELSRELAGLRAELE----ELEKRREEIKKTLEKLKEELEER 706
|
410 420 430
....*....|....*....|....*....|....*...
gi 1720372425 437 EKKAHDNWLAARTLERnLNDLRKENAHNRQKLTETEFK 474
Cdd:PRK03918 707 EKAKKELEKLEKALER-VEELREKVKKYKALLKERALS 743
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-481 |
1.01e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 153 KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDalnENSQLQESQKQLLQetemMKEQVNDLDKQKVALEESR 232
Cdd:TIGR04523 54 KELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK---NKDKINKLNSDLSK----INSEIKNDKEQKNKLEVEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 233 AQAEQALSEKESQIETLVTSLLKMKDWAAVLGEADDgnlDLD-MKSGLENTaaldnqpKGALKKLIyaAKLNASLKALEG 311
Cdd:TIGR04523 127 NKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN---DLKkQKEELENE-------LNLLEKEK--LNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 312 ERNQVYTQLSevdqVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLhrKLTVEENYRL--- 388
Cdd:TIGR04523 195 KLLKLELLLS----NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL--NQLKDEQNKIkkq 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 389 --EKEEKLSKVDEKISHATEELETCR--------QRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLR 458
Cdd:TIGR04523 269 lsEKQKELEQNNKKIKELEKQLNQLKseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
330 340 350
....*....|....*....|....*....|
gi 1720372425 459 KE-------NAHNRQKLTETEFKFELLEKD 481
Cdd:TIGR04523 349 KEltnseseNSEKQRELEEKQNEIEKLKKE 378
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
139-438 |
1.03e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.80 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 139 AKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEE--------RLKGAIKDALNE-NSQLQESQKQLLQ 209
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESleeqlaaaEAEQELEESKREtETGIQNLTAEIEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 210 ETEMMKEQVNDLDKQK--VALEESRAQAEQALSEKESQIETLVTSLL-KMKDWAAVLGEADDgNLDLDMKSGLENTAALD 286
Cdd:COG5185 348 GQESLTENLEAIKEEIenIVGEVELSKSSEELDSFKDTIESTKESLDeIPQNQRGYAQEILA-TLEDTLKAADRQIEELQ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 287 NQPKGALKKLIYAAKLnasLKALEGERNQVYTQLSevDQVKEDLTEHIKSLESkqaSLQSEKTEFESESQKLQQKLKVIT 366
Cdd:COG5185 427 RQIEQATSSNEEVSKL---LNELISELNKVMREAD--EESQSRLEEAYDEINR---SVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720372425 367 ELYQENEMKLHRKL--TVEENYRLEKEEKLSKVDEKISHATEElETCRQRAKDLEEELERTIhSYQGQVISHEK 438
Cdd:COG5185 499 ATLEKLRAKLERQLegVRSKLDQVAESLKDFMRARGYAHILAL-ENLIPASELIQASNAKTD-GQAANLRTAVI 570
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
138-480 |
1.08e-05 |
|
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: 49.02 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 138 RAKHSEQDELMADISKRiqSLEDESKSLKSQVAEAKTtfRIFEI------NEERLKGAIKDALNENSQLQESQKQLLQET 211
Cdd:pfam01576 195 RLKKEEKGRQELEKAKR--KLEGESTDLQEQIAELQA--QIAELraqlakKEEELQAALARLEEETAQKNNALKKIRELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 212 EMMKEQVNDLDKQKVAleesRAQAEQALSEKESQIETLVTSLLKMKDWAAV---LGEADDGNLDLDMKSGLENTAALDNQ 288
Cdd:pfam01576 271 AQISELQEDLESERAA----RNKAEKQRRDLGEELEALKTELEDTLDTTAAqqeLRSKREQEVTELKKALEEETRSHEAQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 289 PKGALKKLIYA---------------AKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQS------- 346
Cdd:pfam01576 347 LQEMRQKHTQAleelteqleqakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQArlseser 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 347 EKTEFESESQKLQQKLKVITELYQENEMKLHrkltveenyRLEKEekLSKVDEKIsHATEEL--ETCRQ------RAKDL 418
Cdd:pfam01576 427 QRAELAEKLSKLQSELESVSSLLNEAEGKNI---------KLSKD--VSSLESQL-QDTQELlqEETRQklnlstRLRQL 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372425 419 EEE-----------------LERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEK 480
Cdd:pfam01576 495 EDErnslqeqleeeeeakrnVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
181-481 |
1.10e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 181 INEERLKGaikdaLNENSQLQESQKQLLQEtemmkeqvnDLDKQKVALEESRAQAEQALSEKESQIETLVTsllKMKDWA 260
Cdd:PHA02562 171 LNKDKIRE-----LNQQIQTLDMKIDHIQQ---------QIKTYNKNIEEQRKKNGENIARKQNKYDELVE---EAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 261 AVLGEADDGNLDLDMKSGlentaaldnQPKGALKKL-IYAAKLNASLKALEGERNqVYTQLSEVDQVKEDLTEHIKSLES 339
Cdd:PHA02562 234 AEIEELTDELLNLVMDIE---------DPSAALNKLnTAAAKIKSKIEQFQKVIK-MYEKGGVCPTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 340 KQASLQSEKTEFESESQKlQQKLKVITELYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTCRQRAKDLE 419
Cdd:PHA02562 304 IKDKLKELQHSLEKLDTA-IDELEEIMDEFNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVK 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720372425 420 EELERTihsyQGQVISHEKkahdnwlAARTLERNLNDLRKENAHNRQKLTETEFKFELLeKD 481
Cdd:PHA02562 365 AAIEEL----QAEFVDNAE-------ELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL-KD 414
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
153-470 |
1.38e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 153 KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENS---------------------------------- 198
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkeqakkaleyyqlkekleleeeyllyldyl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 199 QLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEADDGNLDLDMKSG 278
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 279 LENTAALDNQPKGALKKLIYAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKL 358
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 359 QQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEK 438
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350
....*....|....*....|....*....|..
gi 1720372425 439 KAHDNWLAARTLERNLNDLRKENAHNRQKLTE 470
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
153-460 |
2.02e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 153 KRIQSLEDESKSLKSQVAEAKTTFrifeinEERLKGAIKDALNENSQLQESQKqllqETEMMKEQVNDLDKQKVALEESR 232
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMY------EDKIEELEKQLVLANSELTEART----ERDQFSQESGNLDDQLQKLLADL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 233 AQAEQALSEKESQIETLvtsllkmkdWAAVLG----------EADDGNLDLDMKSGLenTAALDNQPKGALKKLIYAAK- 301
Cdd:pfam15921 387 HKREKELSLEKEQNKRL---------WDRDTGnsitidhlrrELDDRNMEVQRLEAL--LKAMKSECQGQMERQMAAIQg 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 302 LNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLhrklt 381
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL----- 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 382 vEENYRLEKEEklskvdEKISHATEELETCRQRAKDLE---EELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLR 458
Cdd:pfam15921 531 -QELQHLKNEG------DHLRNVQTECEALKLQMAEKDkviEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
..
gi 1720372425 459 KE 460
Cdd:pfam15921 604 LE 605
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
142-513 |
2.03e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 142 SEQDELMADISKRIQSLEDESKslksqvaeAKTTFRIFEINEERLKGA-IKDALNENSQLQESQKQLLQETEMMKEQVND 220
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIK--------REKKLRETEEVEFSLKAEvLIQKFGRSLKAKKRFSLLKKETIYLQSAQRV 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 221 LDKQKVALE-----ESRAQAEQALSEKESQIETLV----TSLLK--------MKDWAAVLGEADDGNlDLDMKSGLENTA 283
Cdd:COG5022 878 ELAERQLQElkidvKSISSLKLVNLELESEIIELKkslsSDLIEnlefktelIARLKKLLNNIDLEE-GPSIEYVKLPEL 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 284 ALDNQPKGALKKLiyAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLqSEKTEFESESQKLQQKLK 363
Cdd:COG5022 957 NKLHEVESKLKET--SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQEST-KQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 364 VI----TELYQENEM-KLHRKLTVEENYrLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEK 438
Cdd:COG5022 1034 IIssesTELSILKPLqKLKGLLLLENNQ-LQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPA 1112
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720372425 439 KAHDNWLAARTlerNLNDLRKENAHNRQKLTETEFKFELLEKDPYALDVPNTAFGREHSPYGPSPLGRPPSETRA 513
Cdd:COG5022 1113 NVLQFIVAQMI---KLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQ 1184
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-371 |
2.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 148 MADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINeerlkgaikdalNENSQLQESQKQLLQETEMMKEQVNDLDKQKVA 227
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 228 LEESRAQAEQALSEKESQIETLVTSllkmkdwaAVLGEADDGNLDLDMKSGLENTAALDNQPKgalkkliyaaklnasLK 307
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQS--------PVIQQLRAQLAELEAELAELSARYTPNHPD---------------VI 294
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720372425 308 ALEGERNQVYTQL-SEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQE 371
Cdd:COG3206 295 ALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
151-255 |
2.64e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 151 ISKRIQSLEDESKSLKSQV---AEAKTTFRIFEINEE--RLKGAIKDALNE-NSQLQESQKQLLQETEMMKEQVNDLDKQ 224
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAkkeAEAIKKEALLEAKEEihKLRNEFEKELRErRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110
....*....|....*....|....*....|....
gi 1720372425 225 KVALEESR---AQAEQALSEKESQIETLVTSLLK 255
Cdd:PRK12704 109 EEELEKKEkelEQKQQELEKKEEELEELIEEQLQ 142
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
300-425 |
3.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 300 AKLNASLKALEGERNQVYTQLSEVDQVK---------EDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQ 370
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720372425 371 ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERT 425
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
73-476 |
5.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 73 REKKLALELSALIEEKcklldKVSIVQKEFVEGSQISEATyENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADIS 152
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKK-----KADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 153 KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGaikDALNENSQLQESQKQLLQETEMMKEQVNDLDKQkvalEESR 232
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 233 AQAEQALSEKEsqietlvtsllkmKDWAAVLGEADDGNLDLDMKSGLENTAALDNQPKGALKKLIYAAKLNASLKAlEGE 312
Cdd:PTZ00121 1510 KKADEAKKAEE-------------AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EED 1575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 313 RNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKvitelYQENEMKLHRKLTVEENYRLEKEE 392
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEEEKKKVEQLKKKEAEEKKKAE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 393 KLSKVDEKISHATEEL----ETCRQRAKDL--EEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQ 466
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEakkaEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
410
....*....|
gi 1720372425 467 KLTETEFKFE 476
Cdd:PTZ00121 1731 KAEEAKKEAE 1740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-363 |
7.66e-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: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 138 RAKHSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQE 210
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 211 TEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLlkmkdwAAVLGEADDgnLDLDMKSGLENTAALDNQPK 290
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL------EALEEELSE--IEDPKGEDEEIPEEELSLED 955
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720372425 291 GALKKLiyaaKLNASLKALEGERNQVytqLSEVDQVKEDLTEhiksLESKQASLQSEKTEFESESQKLQQKLK 363
Cdd:TIGR02169 956 VQAELQ----RVEEEIRALEPVNMLA---IQEYEEVLKRLDE----LKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
153-250 |
8.19e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 44.49 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 153 KRIQSLEDESKSLKS---QVAEAKTTFRIFEINEE--RLKGAIKDALNE-NSQLQESQKQLLQETEMMKEQVNDLDKQKV 226
Cdd:pfam12072 27 AKIGSAEELAKRIIEeakKEAETKKKEALLEAKEEihKLRAEAERELKErRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100
....*....|....*....|....*..
gi 1720372425 227 AL---EESRAQAEQALSEKESQIETLV 250
Cdd:pfam12072 107 SLekkEKELEAQQQQLEEKEEELEELI 133
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
145-432 |
9.14e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 145 DELMADIS------KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQV 218
Cdd:PRK01156 176 DMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 219 NDLDKQkvaleESRAQAEQALSEKESQIETLVTSLLKMKDWAA---VLGEADDGNLDLDMKSGLENTAALDNQPKGALKK 295
Cdd:PRK01156 256 SEIKTA-----ESDLSMELEKNNYYKELEERHMKIINDPVYKNrnyINDYFKYKNDIENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 296 LiyaaklnaslKALEGERNQVYTQLSEvdqvKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMK 375
Cdd:PRK01156 331 L----------SVLQKDYNDYIKKKSR----YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 376 LHRKLTVEENYRLEKEEKLSKVDE---KISHATEELETCRQRakdlEEELERTIHSYQGQ 432
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIRALREN----LDELSRNMEMLNGQ 452
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
306-486 |
1.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 306 LKALEGERNQVYTQLSEVDQvkedLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVItELYQENEmKLHRKLTvEEN 385
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELE-ALEAELA-ELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 386 YRLEK-EEKLskvdEKISHATEELETCRQRAKDLEEELERTIHSYQgqvISHEKKAHDNWLAARTLERNLNDLRKENAHN 464
Cdd:COG4717 146 ERLEElEERL----EELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180
....*....|....*....|..
gi 1720372425 465 RQKLTETEFKFELLEKDPYALD 486
Cdd:COG4717 219 QEELEELEEELEQLENELEAAA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-325 |
1.36e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 107 QISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERL 186
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 187 KGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLvtsLLKMKDWAAVLGEA 266
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL---EEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372425 267 DDGNLDLDmksgLENTAALDNQPKGALKKLIYAAKLNASLKALEGERNQVYTQLSEVDQ 325
Cdd:COG1196 448 AEEEAELE----EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-442 |
1.60e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 149 ADISKRIQSLEDESKSLKSQvaeaKTTFRIFEINEERLKGAIKDALNENSQLQESQK------QLLQET----------- 211
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQ----RKAIQELQFENEKVSLKLEEEIQENKDLIKENNatrhlcNLLKETcarsaektkky 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 212 EMMKEQV--------NDLDKQKVALEESRAQAEQA-------------------------LSEKESQIETLVTSLL---- 254
Cdd:pfam05483 175 EYEREETrqvymdlnNNIEKMILAFEELRVQAENArlemhfklkedhekiqhleeeykkeINDKEKQVSLLLIQITeken 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 255 KMKDWAAVLGEADDGNLDLDMKSGL--ENTAALdNQPKGALKKLIYAAKLN-----ASLKALEgERNQVYTQlsEVDQVK 327
Cdd:pfam05483 255 KMKDLTFLLEESRDKANQLEEKTKLqdENLKEL-IEKKDHLTKELEDIKMSlqrsmSTQKALE-EDLQIATK--TICQLT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 328 EDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLhRKLTVEENYRLEKEEKLSKVDEKISHATEE 407
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1720372425 408 LETC----------RQRAKDLEEELERTIHSYQGQVISHEKKAHD 442
Cdd:pfam05483 410 LKKIlaedeklldeKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
138-474 |
2.37e-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: 44.81 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 138 RAKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFrifEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQ 217
Cdd:pfam10174 351 RLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 218 VNDLDKQKVALeesrAQAEQALSEKESQIETLVTSllKMKDWAAVLGEADDGNLDL-DMKSGL--------ENTAALDNQ 288
Cdd:pfam10174 428 QTDSSNTDTAL----TTLEEALSEKERIIERLKEQ--REREDRERLEELESLKKENkDLKEKVsalqpeltEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 289 PKGALKKLIYAAKLNASLKALEGE-----------RNQVYT--QLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESES 355
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAveqkkeecsklENQLKKahNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 356 QKLQQKLKvitelyqenEMklhrkltveENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTihsyQGQVIS 435
Cdd:pfam10174 582 ERLLGILR---------EV---------ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK----GAQLLE 639
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720372425 436 HEKKAHDNwLAARTLERNLNDLRKENAHNRQKLTETEFK 474
Cdd:pfam10174 640 EARRREDN-LADNSQQLQLEELMGALEKTRQELDATKAR 677
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
189-481 |
2.42e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 189 AIKDALNENSQLQESQKQLLQETEMMKEQVNDLDkqKVALEEsraQAEQALSEKE---SQIETLVTSLLKMkdwAAVLGE 265
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLEELE--AAALQP---GEEEELEEERrrlSNAEKLREALQEA---LEALSG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 266 ADDGNLDLdmksglentaaLDNqpkgALKKLIYAAKLNASLKALEGERNQVYTQLSEVdqvkedltehiksleskQASLQ 345
Cdd:COG0497 238 GEGGALDL-----------LGQ----ALRALERLAEYDPSLAELAERLESALIELEEA-----------------ASELR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 346 SEKTEFESESQKLQQKLKVITELYQenemkLHRK--LTVEE--NYRLEKEEKLskvdEKISHATEELETCRQRAKDLEEE 421
Cdd:COG0497 286 RYLDSLEFDPERLEEVEERLALLRR-----LARKygVTVEEllAYAEELRAEL----AELENSDERLEELEAELAEAEAE 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720372425 422 LERtihsyQGQVISHEKKAhdnwlAARTLE----RNLNDLRKENAhnrqkltetEFKFELLEKD 481
Cdd:COG0497 357 LLE-----AAEKLSAARKK-----AAKKLEkavtAELADLGMPNA---------RFEVEVTPLE 401
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
152-251 |
2.43e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 42.60 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 152 SKRIQSLEDESKSLKSQVAEAKTTFrifeinEERLKGAIKDALNENSQLQESQKQllQETEMMKEQVNDLDKQKvalEES 231
Cdd:PRK14473 41 TRRIEESLRDAEKVREQLANAKRDY------EAELAKARQEAAKIVAQAQERARA--QEAEIIAQARREAEKIK---EEA 109
|
90 100
....*....|....*....|....
gi 1720372425 232 RAQAEQ----ALSEKESQIETLVT 251
Cdd:PRK14473 110 RAQAEQerqrMLSELKSQIADLVT 133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-480 |
2.48e-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: 44.67 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 72 GREKKLALELSALIEEKCKLLDKVSIVQKEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDEL---M 148
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 149 ADISKRIQSLEDESKSLKSQVAEAkttfrifEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDKQKVAL 228
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQ-------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 229 EE---SRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEADDGNL--------DLDMKSGLE---------------NT 282
Cdd:TIGR02169 503 EErvrGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvvedDAVAKEAIEllkrrkagratflplNK 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 283 AALDNQPKGALKK---LIYAAKL--------------------------------NASLKALEGE--------------- 312
Cdd:TIGR02169 583 MRDERRDLSILSEdgvIGFAVDLvefdpkyepafkyvfgdtlvvedieaarrlmgKYRMVTLEGElfeksgamtggsrap 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 313 RNQVYTQLSEVDQVKEdLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHRKLTVEENYRlekeE 392
Cdd:TIGR02169 663 RGGILFSRSEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----E 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 393 KLSKVDEKISHATEELETCRQRAKDLE---EELERTIHSYQGQVisHEKKAHDNWLAARTLERNLNDLRKENAHNR---- 465
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEariEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEarlr 815
|
490
....*....|....*...
gi 1720372425 466 ---QKLTETEFKFELLEK 480
Cdd:TIGR02169 816 eieQKLNRLTLEKEYLEK 833
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
145-429 |
2.62e-04 |
|
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: 44.66 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 145 DELMADISKRiQSLEDESKSLKSQVAEAKTTFRIFE---------INEERLKGAIKDALNENSQL----QESQKQLLQET 211
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKkdvtellnkYSALAIKNKFAKTKKDSEIIikeiKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 212 EMMKEQVNDLDKQKVALEESRA---QAEQALSEKESQIETLVTSLLKMKDwaavlgeaddgnldldmksglentaaldnq 288
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAkndKSNKAAIDIQLSLENFENKFLKISD------------------------------ 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 289 pkgaLKKliyaaKLNASLKALEGERNQVY--------TQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFEsesqKLQQ 360
Cdd:TIGR01612 1615 ----IKK-----KINDCLKETESIEKKISsfsidsqdTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDS 1681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372425 361 KLKVItelyqENEMKLHRKltveeNYRLEKEEklsKVDEKISHATEELETCRQRakdLEEELERTIHSY 429
Cdd:TIGR01612 1682 EIEKI-----EIDVDQHKK-----NYEIGIIE---KIKEIAIANKEEIESIKEL---IEPTIENLISSF 1734
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
300-447 |
2.64e-04 |
|
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: 43.37 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 300 AKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFES---------ESQKLQQKLKvitelYQ 370
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIE-----SL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720372425 371 ENEMKLHRKLTVEENYRLE-KEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAA 447
Cdd:COG1579 102 KRRISDLEDEILELMERIEeLEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
148-479 |
3.15e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 148 MADISKRIQSLEDESKSLKsqVAEAKTtfrifEIN--EERLKGA---IKDALNENSQLQESQKQLLQETEMMKEQVNDLD 222
Cdd:PRK04778 81 LPDIEEQLFEAEELNDKFR--FRKAKH-----EINeiESLLDLIeedIEQILEELQELLESEEKNREEVEQLKDLYRELR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 223 KQkvaLEESRAQAEQALSEKESQIETLVTSLLKMKDwaavlgEADDGN--------LDLDMKsglenTAALDNQ----PK 290
Cdd:PRK04778 154 KS---LLANRFSFGPALDELEKQLENLEEEFSQFVE------LTESGDyveareilDQLEEE-----LAALEQImeeiPE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 291 GaLKKLiyAAKLNASLKALEgernQVYTQLSE---------VDQVKEDLTEHIKSLESKQASLqsEKTEFESESQKLQQK 361
Cdd:PRK04778 220 L-LKEL--QTELPDQLQELK----AGYRELVEegyhldhldIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQER 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 362 lkvITELYQ--ENEMKLHRKLtveenyrlekEEKLSKVDEKISHATEEletcrqrAKDLEEELERTIHSYQgqvISHEKK 439
Cdd:PRK04778 291 ---IDQLYDilEREVKARKYV----------EKNSDTLPDFLEHAKEQ-------NKELKEEIDRVKQSYT---LNESEL 347
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720372425 440 AHdnwlaARTLERNLNDLRKENAHNRQKLTETEFKFELLE 479
Cdd:PRK04778 348 ES-----VRQLEKQLESLEKQYDEITERIAEQEIAYSELQ 382
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
143-481 |
3.69e-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: 44.04 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 143 EQDELMADISKRIQSLEDESkslkSQVAEAKTTFrifeinEERL--KGAIKDALNEnsQLQESQKQLLQETEMMKEQVND 220
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDS----SNTDTALTTL------EEALseKERIIERLKE--QREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 221 LDKQKVALEESRAQAEQALSEKESQIETLVTSLLKmKDwaavlgeADDGNLDLDMKSGLENTAALDNQPKGALKKLIYA- 299
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLK-KD-------SKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVr 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 300 --AKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESES--QKLQQKLKVITELYQENEMK 375
Cdd:pfam10174 552 tnPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTlrQMKEQNKKVANIKHGQQEMK 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 376 LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTihsyqgQVISHEKKAHdnwlaartlernLN 455
Cdd:pfam10174 632 KKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSST------QQSLAEKDGH------------LT 693
|
330 340 350
....*....|....*....|....*....|..
gi 1720372425 456 DLRKEnahNRQKLTET-EFKFELL-----EKD 481
Cdd:pfam10174 694 NLRAE---RRKQLEEIlEMKQEALlaaisEKD 722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-424 |
4.52e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 150 DISKRIQSLEDESKSLKSQVAEAKTTFRifeineerlkgAIKDALNENSQLQESQK-----QLLQETEMMkEQVNDLDKQ 224
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLR-----------TARERVEEAEALLEAGKcpecgQPVEGSPHV-ETIEEDRER 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 225 KVALEESRAQAEQALSEKESQIETLvTSLLKMKDWAAVLGEADDGNLDL--DMKSGLENTA-ALDNQPKGALKKLIYAAK 301
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELiaERRETIEEKReRAEELRERAAELEAEAEE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 302 LNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLEsKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKL----H 377
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekrE 634
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720372425 378 RKLTVEENY---RLEK--------EEKLSKVDEKISHATE-----------------ELETCRQRAKDLEEELER 424
Cdd:PRK02224 635 RKRELEAEFdeaRIEEaredkeraEEYLEQVEEKLDELREerddlqaeigaveneleELEELRERREALENRVEA 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-460 |
5.28e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 73 REKKLALELSALIEEKCKLLDKVSIVQKEFVEgsqiSEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADIS 152
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLE----AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 153 KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQLLQETEMMKEQVNDLDkQKVALEESR 232
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL-EELAEAAAR 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 233 AQAEQALSEKESQIETLVTSLLKMKDW---------------------AAVLGEADDGNLDLDMKSGLENTAALDNQPKG 291
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 292 ALKKL--------------------IYAAKLNASLKALEGERNQVYTQLSEVDQ-------------VKEDLTEHIKSLE 338
Cdd:COG1196 573 RATFLpldkiraraalaaalargaiGAAVDLVASDLREADARYYVLGDTLLGRTlvaarleaalrraVTLAGRLREVTLE 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 339 SKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHRKLTVEENYRL-EKEEKLSKVDEKISHATEELETCRQRAKD 417
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEeEEERELAEAEEERLEEELEEEALEEQLEA 732
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1720372425 418 LEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKE 460
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
146-341 |
5.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 146 ELMADISKRIQSLEdESKSLKSQVAEAKTTFRIFEINEERL---KGAIKDALNEN--SQLQESQKQLLQETEMMKEQVND 220
Cdd:COG4913 242 EALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALrlwFAQRRLELLEAelEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 221 LDKQKVALEESRAQA--------EQALSEKESQIETLVTSLLKMKDWAAVLGEAddgnLDLDMKSGLENTAALDNQpkga 292
Cdd:COG4913 321 LREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLP----LPASAEEFAALRAEAAAL---- 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720372425 293 lkkliyAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQ 341
Cdd:COG4913 393 ------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
155-373 |
5.78e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 155 IQSLEDESKSLKSQVAEAKTTFRIFEiNEERLKGAIKDALNENSQLQesqKQLLQETEMMKEQVNDLDKQKVALEESRAQ 234
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDKLVQQDLE-QTLALLDKIDRQKEETEQLK---QQLAQAPAKLRQAQAELEALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 235 AEQALS--EKESQIETLVTSLlkmKDWAAVLGEAddgNLDL------------DMKSGLENTAALDNQPKG--ALKKLIY 298
Cdd:PRK11281 117 TLSTLSlrQLESRLAQTLDQL---QNAQNDLAEY---NSQLvslqtqperaqaALYANSQRLQQIRNLLKGgkVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 299 A---AKLNASLKALEGE----RN--QVYTQLSEVDQVKEDL-TEHIKSLESKQASLQ----------SEKTEFESESQKL 358
Cdd:PRK11281 191 PsqrVLLQAEQALLNAQndlqRKslEGNTQLQDLLQKQRDYlTARIQRLEHQLQLLQeainskrltlSEKTVQEAQSQDE 270
|
250
....*....|....*
gi 1720372425 359 QQKLKVITELYQENE 373
Cdd:PRK11281 271 AARIQANPLVAQELE 285
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
293-439 |
6.24e-04 |
|
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: 42.22 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 293 LKKLIYAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITEL---- 368
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372425 369 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQGQVISHEKK 439
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
199-480 |
6.89e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 199 QLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVlgEADDGNLDLDMKSG 278
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE--ESDLERLKEEIEKS 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 279 LENTAALdnqpkgALKKLIYAAKLNASLkalegERNQVYTQLSEVD-QVKEDLTEHIKSLESKQASLQSEKTEFESESQK 357
Cdd:TIGR00606 652 SKQRAML------AGATAVYSQFITQLT-----DENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 358 LQQKLKVITELY--QENEMKLHRKLTVEENYRLEK-EEKLSKVDEKISHATEELETC---RQRAKDLEEELErTIHSYQG 431
Cdd:TIGR00606 721 KEKRRDEMLGLApgRQSIIDLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVT-IMERFQM 799
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720372425 432 QVISHEKKAHDnwLAART----LERNLNDLRKENAHNRQKLTETEFKFELLEK 480
Cdd:TIGR00606 800 ELKDVERKIAQ--QAAKLqgsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
312-403 |
8.17e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 312 ERNQVYTQLSE-VDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKLHR--KLTVEEnyrl 388
Cdd:PRK12704 79 ERRNELQKLEKrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEE---- 154
|
90
....*....|....*
gi 1720372425 389 EKEEKLSKVDEKISH 403
Cdd:PRK12704 155 AKEILLEKVEEEARH 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-481 |
9.85e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 74 EKKLALELSALIEEKckllDKVSIVQKEFVEGSQISEAtyenleqsKSKLEDEILLLEEKLEEERAKHSEQDELMADISK 153
Cdd:PTZ00121 1416 AKKKADEAKKKAEEK----KKADEAKKKAEEAKKADEA--------KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 154 RIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNENSQLQESQKQllqETEMMKEQVNDLDKQKVALEESRA 233
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA---DEAKKAEEKKKADELKKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 234 QAEQALSEKESQIETLVTSLLKmkdwAAVLGEADDGNLDLDMKSGLENTAALDNQPKGALKKLIYAAKLnaslKALEGER 313
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRK----AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL----KKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 314 NQVytqlsevDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMKlhRKltVEENYRLEKEEK 393
Cdd:PTZ00121 1633 KKV-------EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KK--AAEALKKEAEEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 394 lsKVDEKISHATEELETCRQRAKDLEEelERTIHSYQGQVISHEKKAHDNWLAARTLERN----LNDLRKENAHNRQKLT 469
Cdd:PTZ00121 1702 --KKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiahLKKEEEKKAEEIRKEK 1777
|
410
....*....|..
gi 1720372425 470 ETEFKFELLEKD 481
Cdd:PTZ00121 1778 EAVIEEELDEED 1789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-241 |
1.34e-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: 42.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 72 GREKKLALELSALIEEKCKLLDKVSIVQKEFVEGSQISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADI 151
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 152 SKRIQSLEDESKSLKSQVAE-AKTTFRIFEINEERLKGAIKDALNENSQLQESQKQL-------LQETEMMKEQVNDLDK 223
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTA 1007
|
170
....*....|....*...
gi 1720372425 224 QKVALEESRAQAEQALSE 241
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAIEE 1025
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
301-424 |
1.71e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 301 KLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKV-ITELYQENEMKLhRK 379
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEkLKKLLQEIMIKV-KK 226
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720372425 380 LTveenyrlEKEEKLSKVDEKISHATEELETCRQRAKDLEEELER 424
Cdd:smart00787 227 LE-------ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
104-470 |
3.81e-03 |
|
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: 40.93 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 104 EGSQISEATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINE 183
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 184 ERLKGAIKDaLNENSQLQESQKQLLQ---------------ETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIET 248
Cdd:pfam01576 99 KKMQQHIQD-LEEQLDEEEAARQKLQlekvtteakikkleeDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 249 LvtSLLKMKDWAavlgeaddgnldldMKSGLENTaaLDNQPKGALkkliyaaKLNASLKALEGERNQVYTQLSEVDQVKE 328
Cdd:pfam01576 178 L--SKLKNKHEA--------------MISDLEER--LKKEEKGRQ-------ELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 329 DLTehiKSLESKQASLQSEKTEFESESQKLQQKLKVITELyQENEMKLHRKLTVEENYRlEKEEKLSKvdekisHATEEL 408
Cdd:pfam01576 233 ELR---AQLAKKEEELQAALARLEEETAQKNNALKKIREL-EAQISELQEDLESERAAR-NKAEKQRR------DLGEEL 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720372425 409 ETCRqraKDLEEELERT-----IHSYQGQVISHEKKAHDNwlAARTLERNLNDLRKENAHNRQKLTE 470
Cdd:pfam01576 302 EALK---TELEDTLDTTaaqqeLRSKREQEVTELKKALEE--ETRSHEAQLQEMRQKHTQALEELTE 363
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
186-432 |
4.12e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 186 LKGAIKDALNENSQLQESQKQ---LLQETEMMKEQVNDLDKQKVALEesrAQAEQALSEKESQIETlVTSLLKmkdwaaV 262
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEiraLVQERGEQDKRLQALEEELEKVE---AKLNAAVREKTSLSAS-VASLEK------Q 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 263 LGEADDGNLDLDMKSGLENTAALDNQPKGALKKLiyAAKLNASLKALEGERNQVYTQLSEVDQVKEDLTEHIKSLESKQA 342
Cdd:pfam15905 131 LLELTRVNELLKAKFSEDGTQKKMSSLSMELMKL--RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 343 SLQSEKTEFESESQKLqqkLKVITELYQENE--MKLHRKLTVEENYRLEKEEKL----SKVDEKISHATEELETCRQRAK 416
Cdd:pfam15905 209 STEKEKIEEKSETEKL---LEYITELSCVSEqvEKYKLDIAQLEELLKEKNDEIeslkQSLEEKEQELSKQIKDLNEKCK 285
|
250
....*....|....*.
gi 1720372425 417 DLEEELERTIHSYQGQ 432
Cdd:pfam15905 286 LLESEKEELLREYEEK 301
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
300-430 |
4.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 300 AKLNASLKALEGERNQVYTQL----SEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQENEMK 375
Cdd:COG4372 48 EQLREELEQAREELEQLEEELeqarSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720372425 376 lhrkltveENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIHSYQ 430
Cdd:COG4372 128 --------EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
81-258 |
5.35e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 81 LSALIEEKCKLLDKVSIVQKEFVEGSQISE----ATYENLEQSKSKLEDEILLLEEKLEEERAKHSEQDELMADIsKRIQ 156
Cdd:pfam15905 154 MSSLSMELMKLRNKLEAKMKEVMAKQEGMEgklqVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYI-TELS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 157 SLEDESKSLKSQVAEAKttfrifEINEERlkgaikdalneNSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRaqaE 236
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLE------ELLKEK-----------NDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---E 292
|
170 180
....*....|....*....|..
gi 1720372425 237 QALSEKESQIETLVTSLLKMKD 258
Cdd:pfam15905 293 ELLREYEEKEQTLNAELEELKE 314
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
142-384 |
6.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 142 SEQDELMADiskRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALNEN----SQLQESQKQLLQETEMMKEQ 217
Cdd:PHA02562 166 SEMDKLNKD---KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKqnkyDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 218 VNDLDKQKVALEESRAQAEQALSEKESQIETLvTSLLKM--------------KDWAAVLGEADDGNLDLDMKSGLENTA 283
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF-QKVIKMyekggvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 284 ALDNQpkgalKKLIYAAKLNASLKALEGERNQVYTQLS-EVDQvkedltehIKSLESKQASLQSEKTEFESESQKLQQKL 362
Cdd:PHA02562 322 IDELE-----EIMDEFNEQSKKLLELKNKISTNKQSLItLVDK--------AKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
250 260
....*....|....*....|..
gi 1720372425 363 KVITELYQENEMKLHRKLTVEE 384
Cdd:PHA02562 389 DKIVKTKSELVKEKYHRGIVTD 410
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
328-439 |
6.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 328 EDLTEHIksLESKQASLQSEKTEFESESQKLQQKLKviTELYQENEMKLhRKLTVEENYRLEKEEKLSKVDEKISHATEE 407
Cdd:PRK12704 37 EEEAKRI--LEEAKKEAEAIKKEALLEAKEEIHKLR--NEFEKELRERR-NELQKLEKRLLQKEENLDRKLELLEKREEE 111
|
90 100 110
....*....|....*....|....*....|..
gi 1720372425 408 LETCRQRAKDLEEELERTIHSYQGQVISHEKK 439
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
141-471 |
6.64e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.20 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 141 HSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKDALnENSQLQESQKQLLQETEMMKEQVND 220
Cdd:PTZ00440 438 NLEIIEIKKKYDEKINELKKSINQLKTLISIMKSFYDLIISEKDSMDSKEKKES-SDSNYQEKVDELLQIINSIKEKNNI 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 221 LDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAavlgeaDDGNLDLDMKSGLENtaaldnqpkgalkKLIYAa 300
Cdd:PTZ00440 517 VNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLI------KDEKLKRSMKNDIKN-------------KIKYI- 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 301 klnaslkalegerNQVYTQLSEVDQVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLK-VITELYQENEMKLHRK 379
Cdd:PTZ00440 577 -------------EENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKyILNKFYKGDLQELLDE 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 380 LT--VEENYRLEKEeklskvdekiSHATEELETCRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAAR--TLERNLN 455
Cdd:PTZ00440 644 LShfLDDHKYLYHE----------AKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKenIIKKQLN 713
|
330
....*....|....*.
gi 1720372425 456 DLRKENAHNRQKLTET 471
Cdd:PTZ00440 714 NIEQDISNSLNQYTIK 729
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
299-463 |
6.65e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 299 AAKLNASLKALEGERNQVYTQLSEVD-QVKEDLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITElyqenemKLH 377
Cdd:pfam08614 16 TALLEAENAKLQSEPESVLPSTSSSKlSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNE-------ELQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 378 rkltveenyrlEKEEKLSKVDEKISHATEELETCRQRAKDLEEEL---ERTIHSYQGQVISHekkahdnWLAARTLERNL 454
Cdd:pfam08614 89 -----------ELEKKLREDERRLAALEAERAQLEEKLKDREEELrekRKLNQDLQDELVAL-------QLQLNMAEEKL 150
|
....*....
gi 1720372425 455 NDLRKENAH 463
Cdd:pfam08614 151 RKLEKENRE 159
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
148-424 |
6.90e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 148 MADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLKGAIKD---ALNENSQLQESQKQLLQETEmmkEQVNDLDKQ 224
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELE---ARVSDLELE 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 225 KVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEaDDGNLDLDMKSGLENTAALDNQPKGALKKLIYA-AKLN 303
Cdd:pfam15921 634 KVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSElEQTR 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 304 ASLKALEGE-----------RNQVYTQLSEVDQvkedLTEHIKSLESKQASLQSEKTEFESESQKLQQKLKVITElyQEN 372
Cdd:pfam15921 713 NTLKSMEGSdghamkvamgmQKQITAKRGQIDA----LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT--EKN 786
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720372425 373 EMKLHRKLTVEENYRLekEEKLSKVDEKISHATEELETCRQRAKDLEEELER 424
Cdd:pfam15921 787 KMAGELEVLRSQERRL--KEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
194-472 |
7.58e-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: 39.95 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 194 LNENSQLQESQKQLLQETEMMKEQVNDLDKQKVALEESRAQAEQALSEKESQIETLVTSLLKMKDWAAVLGEADDGNLDL 273
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 274 DMKSGLENTAALDNQPKGALKKLIyAAKLNASLKALEGErnqvytqlsEVDQVKEDLTEHIKSLESKQASLQSEKTEFES 353
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQC-SQELALKLTALHAL---------QLTLTQERVREHALSIRVLPKELLASRQLALQ 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 354 ESQKLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETCRQRAKDLEEELERTIhsyQGQV 433
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL---KART 760
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720372425 434 ISHEKKAHDNWLAART------LERNLNDLRKENAHNRQKLTETE 472
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTgaelshLAAEIQFFNRLREEDTHLLKTLE 805
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
334-424 |
7.90e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 37.23 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 334 IKSLESKQASLQSEKTEFESESQKLQQKLKVITELYQ------ENEMKLH----RKLTVEENYRLEKEEKLSKVDEKISH 403
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAReaqqnyERELVLHaediKALQALREELNELKAEIAELKAEAES 82
|
90 100
....*....|....*....|.
gi 1720372425 404 ATEELETCRQRAKDLEEELER 424
Cdd:pfam07926 83 AKAELEESEESWEEQKKELEK 103
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
321-424 |
8.79e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 321 SEVDQVKEDLTE----HIkslESKQASLQSEKT-EFESESQKLQQKLKVITELYQENEMKLHRKLTVEENyRLEK----- 390
Cdd:PRK05771 16 SYKDEVLEALHElgvvHI---EDLKEELSNERLrKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVK-SLEElikdv 91
|
90 100 110
....*....|....*....|....*....|....
gi 1720372425 391 EEKLSKVDEKISHATEELETCRQRAKDLEEELER 424
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELENEIKELEQEIER 125
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
331-471 |
9.81e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.57 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372425 331 TEHIKSLESKQASLQSEKTEFESESQKLQQKLKV-----------ITELYQENEMkLHRKLTVEENYRLEKEEKLSKVDE 399
Cdd:pfam17078 2 TKVIESLHDQIDALTKTNLQLTVQSQNLLSKLEIaqqkeskflenLASLKHENDN-LSSMLNRKERRLKDLEDQLSELKN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372425 400 KISHATEE-------LETCRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTET 471
Cdd:pfam17078 81 SYEELTESnkqlkkrLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQR 159
|
|
| |
