|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-489 |
1.63e-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: 74.29 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 136 QKEyEGLESSLKE--ASFEKESTEAQSlefvegsQIS--EAAYENLERSKSKLEDEILLLEKKLEEERVKHSEQDELMAD 211
Cdd:TIGR04523 303 QKE-QDWNKELKSelKNQEKKLEEIQN-------QISqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 212 ISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEE 291
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 292 SRAQAEQVLSEKETQIESLIKSLLKMKdwaavlgdDTADDGNLDLDMK----SGL-EDTASLDNQPKgALKKLIyaAKLN 366
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIK--------QNLEQKQKELKSKekelKKLnEEKKELEEKVK-DLTKKI--SSLK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 367 ASLKALEGERNQIYTQLS----EVDQIKEDLT------------EHIKSLESKQASLQSENTEFEsesQRLQQKLKVITE 430
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISdledELNKDDFELKkenlekeideknKEIEELKQTQKSLKKKQEEKQ---ELIDQKEKEKKD 600
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958781444 431 LYQENEMKLHRKLTVEENYRLEKEEKlSKVDERISHAAEELETYRQRAKDLEEELERTI 489
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKEN-EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
211-543 |
1.59e-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: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 211 DISKRIQSLEDESKSLKSQVAEAKTTfrIFEINEERLRGAIKdaLNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLE 290
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKN--IDKIKNKLLKLELL--LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 291 ESRAQAEQVLSEKETQIESLIKSLLKMKdwaavlgdDTADDGNLDLD---------------MKSGLEDtasLDNQPKGA 355
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIK--------KQLSEKQKELEqnnkkikelekqlnqLKSEISD---LNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 356 LKKliyaaKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESEsqrLQQKLKVITELYQEN 435
Cdd:TIGR04523 308 WNK-----ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 436 EMKLhrkltvEENYRLEKEeklskvderishaAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKaHDNWLAARTLER 515
Cdd:TIGR04523 380 QSYK------QEIKNLESQ-------------INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE-IERLKETIIKNN 439
|
330 340
....*....|....*....|....*....
gi 1958781444 516 N-LNDLRKENAHNRQKLTETEFKFELLEK 543
Cdd:TIGR04523 440 SeIKDLTNQDSVKELIIKNLDNTRESLET 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-484 |
1.09e-11 |
|
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: 68.94 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVsfvQKEYEGLESsLKEASFEKESTEAQslEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLE 196
Cdd:TIGR02169 188 RLDLIIDEKRQQLERL---RREREKAER-YQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 EERVKHSEQDELMADISKRIQSL-EDESKSLKSQVAEakttfriFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIM 275
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGE-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 276 KEQVSDLDKQkvtLEESRAQAEQVLSEketqiesliksllkMKDWAAVLGDDTADDGNLDLDMKSGLEDTASLDnqpkga 355
Cdd:TIGR02169 335 LAEIEELERE---IEEERKRRDKLTEE--------------YAELKEELEDLRAELEEVDKEFAETRDELKDYR------ 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 356 lKKLiyaAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQEN 435
Cdd:TIGR02169 392 -EKL---EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958781444 436 EMKLHRKltveenyrlekEEKLSKVDERISHAAEELETYRQRAKDLEEE 484
Cdd:TIGR02169 468 EQELYDL-----------KEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
107-543 |
2.15e-11 |
|
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: 67.35 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 107 YVGREKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFE-----------KESTEAQSLEFVEGSQISEAAYE 175
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqlkdeqnkiKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 176 NLERSKSKLEDeilllekkleeerVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTfrIFEINEE--RLRGAIKD 253
Cdd:TIGR04523 289 QLNQLKSEISD-------------LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI--ISQLNEQisQLKKELTN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 254 ALNENS----QLQESQKQ---LLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESL----------IKSLLK 316
Cdd:TIGR04523 354 SESENSekqrELEEKQNEiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLqqekellekeIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 317 MK-DWAAVLGDDTADDGNLDLDMKSgLEDTASLDNQPKGALKKLIYAAKLNasLKALEGERNQIYTQLSEVDQIKEDLTE 395
Cdd:TIGR04523 434 TIiKNNSEIKDLTNQDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQN--LEQKQKELKSKEKELKKLNEEKKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 396 HIKSLESKQASLQSENTEFESESQRLQQKLKVItelyqENEMKlhrKLTVEENYRLEKEEKLSKvDERIS---HAAEELE 472
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDL-----EDELN---KDDFELKKENLEKEIDEK-NKEIEelkQTQKSLK 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958781444 473 TYRQRAKDLEEELERTIHSYQGQVISHEKKAhdnwlaaRTLERNLNDLRKENAHNRQKLTETEFKFELLEK 543
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-486 |
9.56e-11 |
|
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: 65.85 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 108 VGREKKLAlELSALIEEkckLLEKVSFVQKEYEGLESSLKEAsfEKESTEAQSLEFVEGSQISEAA--YENLERSKSKLE 185
Cdd:TIGR02168 673 LERRREIE-ELEEKIEE---LEEKIAELEKALAELRKELEEL--EEELEQLRKELEELSRQISALRkdLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 186 DEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFrifeineERLRGAIKDALNENSQLQESQ 265
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-------KALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 266 KQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDwaavlgddtaddgnldlDMKSGLEDT 345
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-----------------ELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 346 ASLDNQPKGALKKLiyaAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKL 425
Cdd:TIGR02168 883 ASLEEALALLRSEL---EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958781444 426 KVITELYqenEMKLHRKLTveenyRLEKE-EKLSKVDERishAAEELETYRQRAKDLEEELE 486
Cdd:TIGR02168 960 ENKIEDD---EEEARRRLK-----RLENKiKELGPVNLA---AIEEYEELKERYDFLTAQKE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-523 |
1.50e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 172 AAYENLERSKSKLEDEILLLEKkleeervKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAI 251
Cdd:COG1196 232 LKLRELEAELEELEAELEELEA-------ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 252 KDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLkmkdwaavlgDDTADD 331
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL----------EAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 332 GNLDLDMKSGLEDTASLDNQpkgalkKLIYAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSEN 411
Cdd:COG1196 375 AEAEEELEELAEELLEALRA------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 412 TEFESESQRLQQKLKVITELYQENEmklhrKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHS 491
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAA-----LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350
....*....|....*....|....*....|..
gi 1958781444 492 YQGQVISHEKKAHDNWLAARTLERNLNDLRKE 523
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
245-489 |
7.96e-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: 61.70 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 245 ERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAVL 324
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 325 gddtaddgnLDLDMKSGLEDTASL---DNQPKGALKKLIYAAKLNASLKAlegernqiytQLSEVDQIKEDLTEHIKSLE 401
Cdd:COG4942 110 ---------LRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 402 SKQASLQSENTEFESESQRLQQKLKvitelyqenemklhrkltveenyrlEKEEKLSKVDERISHAAEELETYRQRAKDL 481
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 1958781444 482 EEELERTI 489
Cdd:COG4942 226 EALIARLE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
103-522 |
1.00e-09 |
|
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: 62.30 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 103 RSRFYVGREKKLAlelsALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKS 182
Cdd:pfam02463 164 GSRLKRKKKEALK----KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 183 KLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQ 262
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 263 ESQKQLLQEAEIMKEQVSDLDKQKvtLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDldmkSGL 342
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKE--LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA----KLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 343 EDTASLDNQPKGALKKLIYAAKLNASLkaLEGERNQIYTQLSEVDQIKEDLTEHI---KSLESKQASLQSENTEFESESQ 419
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDL--LKEEKKEELEILEEEEESIELKQGKLteeKEELEKQELKLLKDELELKKSE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 420 RLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERI-SHAAEELETYRQRAKDLEEELERTIHSYQGQVIS 498
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIkDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
|
410 420
....*....|....*....|....
gi 1958781444 499 HEKKAHDNWLAARTLERNLNDLRK 522
Cdd:pfam02463 552 EVSATADEVEERQKLVRALTELPL 575
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
110-479 |
1.06e-09 |
|
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: 62.30 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSfvQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEIL 189
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILR--RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLL 269
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 270 QEAEIMKEQVSDLDKQKvtLEESRAQAEQVLSEKETQIESLIKSLLKMKDwaavlgddtaDDGNLDLDMKSGLEDTASLD 349
Cdd:pfam02463 831 KEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELLLKEEE----------LEEQKLKDELESKEEKEKEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 350 NQPKGALKKLIYAaklnasLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESesQRLQQKLKVIT 429
Cdd:pfam02463 899 KKELEEESQKLNL------LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNKRLLLAKE 970
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958781444 430 ELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAK 479
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-473 |
1.26e-09 |
|
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: 62.00 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 122 IEEKCKLLEKVSFVQKEYEGLESSLKEAsfEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLEEERVK 201
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 202 HSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSD 281
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 282 LDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAVLgddTADDGNLDLDMKSGLEDTASLDNQPKGALKKLiy 361
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARLERLEDRRERLQQEIEELLKKL-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 362 aakLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELyQENEMKLHR 441
Cdd:TIGR02168 431 ---EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSE 506
|
330 340 350
....*....|....*....|....*....|..
gi 1958781444 442 KLTVEENYRLEKEEKLSKVDERIShAAEELET 473
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELIS-VDEGYEA 537
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-544 |
5.19e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 137 KEYEGLESSLKEAsfekESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKleeerVKHSEQDELMADISKRI 216
Cdd:COG4717 71 KELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 217 QSLEDESKSLKSQVAEAKTTFRifeiNEERLRGAIKDALNE-NSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQ 295
Cdd:COG4717 142 AELPERLEELEERLEELRELEE----ELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 296 AEQVLSEKETQIESLIKSLLKMKDwaavlgDDTADDGNLDLDMKSGLEDTASLDNQPKGALKKLIYAAKLNASLKALEGE 375
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAAL------EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 376 RNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQ--RLQQKLKVITELYQENE--MKLHRKLTVEEnYRL 451
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeELLELLDRIEELQELLReaEELEEELQLEE-LEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 452 EKEEKLSKVDerishaAEELETYRQRAKDLEE--ELERTIHSYQGQVISHEKKAHDNWLAA---------RTLERNLNDL 520
Cdd:COG4717 371 EIAALLAEAG------VEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEEL 444
|
410 420
....*....|....*....|....
gi 1958781444 521 RKENAHNRQKLTETEFKFELLEKD 544
Cdd:COG4717 445 EEELEELREELAELEAELEQLEED 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-402 |
8.28e-09 |
|
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: 59.30 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFvegsqisEAAYENLERSKSKLEDEIL 189
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-------KEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLL 269
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 270 QEAEIMKEQVSDLDKQKVTLE-------ESRAQAEQVLSEKETQIESLIKSLlkmkdwaavlgddtADDGNLDLDMKSGL 342
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRreleelrEKLAQLELRLEGLEVRIDNLQERL--------------SEEYSLTLEEAEAL 959
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958781444 343 EDTASLDnqpkgalkkliyAAKLNASLKALEGERNQI----------YTQLSE----VDQIKEDLTEHIKSLES 402
Cdd:TIGR02168 960 ENKIEDD------------EEEARRRLKRLENKIKELgpvnlaaieeYEELKErydfLTAQKEDLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-419 |
1.06e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 138 EYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLEEERVKHSEQDELMADISKRIQ 217
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 218 SLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAE 297
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 298 QVLSEKETQIESLIKSLlkmkdwAAVLGDDTADDGNLDLDMKSGLEDTASLDNQPKGALKKLIYAAKLNASLKALEGERN 377
Cdd:COG1196 393 RAAAELAAQLEELEEAE------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958781444 378 QIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQ 419
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-487 |
1.89e-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: 58.14 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 201 KHSEQDELMADIS-KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAI---KDALNENSQLQESQKQLLQEAeimK 276
Cdd:TIGR02168 218 LKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelRLEVSELEEEIEELQKELYAL---A 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 277 EQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKdwaavlgddtaddgnldldmksglEDTASLDNQPKGAL 356
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA------------------------EELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 357 KKLiyaAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSEnteFESESQRLQQKLKVITELYQENE 436
Cdd:TIGR02168 351 EEL---ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE---IERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958781444 437 mKLHRKLtvEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELER 487
Cdd:TIGR02168 425 -ELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-539 |
3.21e-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: 57.37 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 362 AAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLEskqASLQSENTEFESESQRLQQKLKVITELyQENEMKLHR 441
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALR---KDLARLEAEVEQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 442 KLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERT---IHSYQGQVISHEKKAHDNWLAARTLERNLN 518
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....
gi 1958781444 519 DLRKE---NAHNRQKLTETEFKFE 539
Cdd:TIGR02168 849 ELSEDiesLAAEIEELEELIEELE 872
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-544 |
3.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLE---SSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLED------E 187
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 188 ILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKD--ALNENSQLQESQ 265
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 266 KQLLQEAEIMKEQVSD------------LDKQKVTLEESRAQAEQVLSEKETQIESL---IKSLLKMKDWAAVLGDDTAD 330
Cdd:PRK03918 368 KAKKEELERLKKRLTGltpeklekeleeLEKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 331 DGNLDLdMKSGLEDTASLDNQPKGALKKLiyaAKLNASLKALEGERN---QIYTQLSEVDQIKEdLTEHIKSLESKQasL 407
Cdd:PRK03918 448 EHRKEL-LEEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKkesELIKLKELAEQLKE-LEEKLKKYNLEE--L 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 408 QSENTEFE---SESQRLQQKLKVI-TELYQENEMKlhRKLTVEENYRLEKEEKLSKVDERIshaaeeletyRQRAKDLEE 483
Cdd:PRK03918 521 EKKAEEYEklkEKLIKLKGEIKSLkKELEKLEELK--KKLAELEKKLDELEEELAELLKEL----------EELGFESVE 588
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958781444 484 ELERTIHSYqgqvisheKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEKD 544
Cdd:PRK03918 589 ELEERLKEL--------EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-378 |
4.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEAsfEKESTEAQSLEFVEGSQISEaayenLERSKSKLEDEIL 189
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL--ELELEEAQAEEYELLAELAR-----LEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLL 269
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 270 QEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDW----AAVLGDDTADDGNLDLDMKSGLEDT 345
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAleeaAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270
....*....|....*....|....*....|...
gi 1958781444 346 ASLDNQPKGALKKLIYAAKLNASLKALEGERNQ 378
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-523 |
5.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEIL 189
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLL 269
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 270 QEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESlIKSLLKMKDWAAVLGD-----------DTADDGNLDLDM 338
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG-VKAALLLAGLRGLAGAvavligveaayEAALEAALAAAL 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 339 KSGLEDTASLDNQPKGALKK----------------------------LIYAAKLNASLKALEGERNQIYTQLSEVDQI- 389
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAakagratflpldkiraraalaaalargaIGAAVDLVASDLREADARYYVLGDTLLGRTLv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 390 ------------KEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLHRKLTVEENYRL-EKEEK 456
Cdd:COG1196 629 aarleaalrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEeEEERE 708
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 457 LSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKE 523
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-483 |
8.29e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLE 196
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 EERV---KHSEQDELM----ADISKRIQSLEDESKSLKSQVAEAKTTFR-----IFEINEE--RLRGAIKDALNENSQLQ 262
Cdd:PRK02224 332 ECRVaaqAHNEEAESLredaDDLEERAEELREEAAELESELEEAREAVEdrreeIEELEEEieELRERFGDAPVDLGNAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 263 ESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSE-KETQIESLIKSllkmKDWAAVLGDDTADDGNLDLDMKSG 341
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAgKCPECGQPVEG----SPHVETIEEDRERVEELEAELEDL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 342 LEDTASLDNQpkgalkklIYAAKlnaSLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESqrl 421
Cdd:PRK02224 488 EEEVEEVEER--------LERAE---DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA--- 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 422 QQKLKVITELYQENEMKLHRKLTVEE-----NYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEE 483
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSklaelKERIESLERIRTLLAAIADAEDEIERLREKREALAE 620
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
109-537 |
1.71e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 109 GREKKLALELSALiEEKCKLLEKVSFVQKEYEGLESSLKEASFEKesteaqslefvegsqiSEAAYENLERSKSKLEDEI 188
Cdd:PRK03918 345 KKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEK----------------LEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 189 LllekkleeervkhseqdelmaDISKRIQSLEDESKSLKSQVAEAKTTFRIF-----EINEE-------RLRGAIKDALN 256
Cdd:PRK03918 408 S---------------------KITARIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEhrkelleEYTAELKRIEK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 257 ENSQLQESQKQL---LQEAEIMKEQVSDLDKQKVTLEESRAQAEQV-------LSEKETQIESLIKSLLKMKDWAAVLGD 326
Cdd:PRK03918 467 ELKEIEEKERKLrkeLRELEKVLKKESELIKLKELAEQLKELEEKLkkynleeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 327 DtaddgnldLDMKSGLEdtasldnqpkgalKKLiyaAKLNASLKALEGERNQIYTQLSEVD-QIKEDLTEHIKSLES--- 402
Cdd:PRK03918 547 E--------LEKLEELK-------------KKL---AELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPfyn 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 403 --------------KQASLQSENTEFESESQRLQQKLKVITELyqENEMKLHRKLTVEENYRlEKEEKLSKVDERISHAA 468
Cdd:PRK03918 603 eylelkdaekelerEEKELKKLEEELDKAFEELAETEKRLEEL--RKELEELEKKYSEEEYE-ELREEYLELSRELAGLR 679
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958781444 469 EELEtyrqRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERnLNDLRKENAHNRQKLTETEFK 537
Cdd:PRK03918 680 AELE----ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKALLKERALS 743
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
141-486 |
1.76e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 141 GLESSLKEASFEKESTEAQSLEFVEgsqISEAAYENLERSKSKLEdEILLLEKKLEEERVKHSEQDELMADISKRIQSLE 220
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARE---TRDEADEVLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 221 DESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQE-------SQKQLLQEAEIMKEQVSDLDKQKVTLEESR 293
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleecrvAAQAHNEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 294 AQ-------AEQVLSEKETQIESL---IKSLLKMKDWAAVLGDDTADDGNLDLDMKSGL-EDTASLDNQPKGALKKLIYA 362
Cdd:PRK02224 366 AEleseleeAREAVEDRREEIEELeeeIEELRERFGDAPVDLGNAEDFLEELREERDELrEREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 363 AKLNASLKALEG----ERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENT------EFESESQRLQQKLKVITELY 432
Cdd:PRK02224 446 EALLEAGKCPECgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELI 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 433 QENEMKLHRKLTVEENYRLEKEEKLSKVDE---RISHAAEELETYRQRAKDLEEELE 486
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEkreAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
200-567 |
1.78e-07 |
|
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: 55.07 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 200 VKHSEQDELmADISKRIQSLEDESKSLKSQVAEAKTtfRIFEineerLRGAIKDALNENSQLQESQKQLLQEAEIMKEQV 279
Cdd:TIGR02169 668 FSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIEN--RLDE-----LSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 280 SDLDKQKVTLEESRAQAEQvlseketqiesliksllKMKDWAAVLGDDTADDGNLDLDMKSgLEdtASLDNQPkgalkkl 359
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKS-----------------ELKELEARIEELEEDLHKLEEALND-LE--ARLSHSR------- 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 360 iyAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLkvitelyqenemkl 439
Cdd:TIGR02169 793 --IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-------------- 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 440 hrkltveENYRLEKEEKlskvderishaAEELETYRQRAKDLEEELERtihsyqgqvISHEKKAHDNWLaaRTLERNLND 519
Cdd:TIGR02169 857 -------ENLNGKKEEL-----------EEELEELEAALRDLESRLGD---------LKKERDELEAQL--RELERKIEE 907
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958781444 520 LRKENAHNRQKLTETEFKFELLEKDPYALDVPntaFGRGSRGPENLLD 567
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDP---KGEDEEIPEEELS 952
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-488 |
2.19e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESteaqslefvegsqISEAAYEnLERSKSKLEDEILLlekkle 196
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAEIEDLRETIAETEREREE-------------LAEEVRD-LRERLEELEEERDD------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 eeRVKHSEQDELMAD-ISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLlqeaeim 275
Cdd:PRK02224 298 --LLAEAGLDDADAEaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 276 keqVSDLDKQKVTLEESRAQaeqvLSEKETQIESLIKSLlkmkDWAAVLGDDTADDGNLDLDMKSGL-EDTASLDNQPKG 354
Cdd:PRK02224 369 ---ESELEEAREAVEDRREE----IEELEEEIEELRERF----GDAPVDLGNAEDFLEELREERDELrEREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 355 ALKKLIYAAKLNASLKALEG----ERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENT------EFESESQRLQQK 424
Cdd:PRK02224 438 ARERVEEAEALLEAGKCPECgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEER 517
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958781444 425 LKVITELYQEnemklhRKLTVEEnyrleKEEKLSKVDERISHAAEELETYRQRAKDLEEELERT 488
Cdd:PRK02224 518 REDLEELIAE------RRETIEE-----KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
128-487 |
2.83e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 128 LLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLEEERVKHSEQDE 207
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 208 LMADISKRIQSLE---DESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQK-----QLLQEAEIMkEQV 279
Cdd:PRK02224 392 EIEELRERFGDAPvdlGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHV-ETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 280 SDLDKQKVTLEESRAQAEQVLSEKETQIESLiKSLLKMKDWAAVLGDDTADDGNLDLDMKSGLEDT----ASLDNQpKGA 355
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKreraEELRER-AAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 356 LKKLIYAAKLNASLKALEGERNQIytQLSEVDQIKEDLTEHIKSLEsKQASLQSENTEFESESQRLQQKLKVITELYQEN 435
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEARE--EVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDER 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 436 EMKL----HRKLTVEENY---RLEK--------EEKLSKVDERISHAAE-----------------ELETYRQRAKDLEE 483
Cdd:PRK02224 626 RERLaekrERKRELEAEFdeaRIEEaredkeraEEYLEQVEEKLDELREerddlqaeigaveneleELEELRERREALEN 705
|
....
gi 1958781444 484 ELER 487
Cdd:PRK02224 706 RVEA 709
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
199-537 |
3.05e-07 |
|
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: 54.06 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 199 RVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFrifEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQ 278
Cdd:pfam10174 351 RLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 279 VSD---LDKQKVTLEESRAQAEQVLS-----------EKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKsglED 344
Cdd:pfam10174 428 QTDssnTDTALTTLEEALSEKERIIErlkeqreredrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK---EH 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 345 TASLDNQPkgaLKKLIYAAKLNASLKALEGERNQIYTQL------SEVDQIKEDLTEHIKSLESKQASLQSENTEFESES 418
Cdd:pfam10174 505 ASSLASSG---LKKDSKLKSLEIAVEQKKEECSKLENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 419 QRLQQKLKvitelyqenEMklhrkltveENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTihsyQGQVIS 498
Cdd:pfam10174 582 ERLLGILR---------EV---------ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK----GAQLLE 639
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958781444 499 HEKKAHDNwLAARTLERNLNDLRKENAHNRQKLTETEFK 537
Cdd:pfam10174 640 EARRREDN-LADNSQQLQLEELMGALEKTRQELDATKAR 677
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
113-543 |
7.28e-07 |
|
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: 53.05 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 113 KLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLE 192
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 193 KKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEA 272
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 273 EIMKEQVSDLDKQKVTLEESRAQAEQVL-------SEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKSGLEDT 345
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSrqkleerSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 346 ASLDNQPKGALKKLIYAA----KLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRL 421
Cdd:pfam02463 544 AISTAVIVEVSATADEVEerqkLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 422 QQKLKVITELYQENEMKLHRKLTVEEN--YRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISH 499
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKgvSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958781444 500 -EKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEK 543
Cdd:pfam02463 704 kEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE 748
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
245-436 |
7.42e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 245 ERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKsllKMKDWAAVL 324
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 325 GDDTADDGNLDLDMKSglEDTAS-LDNQpkGALKKLiyAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESK 403
Cdd:COG3883 96 YRSGGSVSYLDVLLGS--ESFSDfLDRL--SALSKI--ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|...
gi 1958781444 404 QASLQSENTEFESESQRLQQKLKVITELYQENE 436
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-312 |
7.65e-07 |
|
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: 53.14 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEY-------EGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKS 182
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 183 KLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAkttfrifEINEERLRGAIKDALNENSQLQ 262
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL-------ELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958781444 263 ESQKQLLQEAE--IMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIK 312
Cdd:TIGR02168 414 DRRERLQQEIEelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-539 |
1.00e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 111 EKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILL 190
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 191 LEKKLEEER--------VKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRG------AIKDALN 256
Cdd:PTZ00121 1380 ADAAKKKAEekkkadeaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeakkkAEEAKKA 1459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 257 ENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQV--LSEKETQIESLIKSLLKMKDWAAvlgdDTADDGNL 334
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEA----KKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 335 DLDMKSGLEDTASLDNQPKGALKKLIYAAKLNASLKAlEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEF 414
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 415 ESESQRLQQKLKvitelYQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEEL----ETYRQRAKDL--EEELERT 488
Cdd:PTZ00121 1615 AEEAKIKAEELK-----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkaEEDKKKAEEAkkAEEDEKK 1689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958781444 489 IHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKFE 539
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
180-529 |
1.18e-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: 52.53 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 180 SKSKLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLedeskslKSQVAEAKTTFRIFEINEERLRG---AIKDALN 256
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA-------SREETFARTALKNARLDLRRLFDekqSEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 257 EN------------SQLQESQKQLLQEAEIMKEQVSD---------LDKQKVTLEESRAQAEQVLSEKETQIESLIKSLL 315
Cdd:pfam12128 671 KAlaerkdsanerlNSLEAQLKQLDKKHQAWLEEQKEqkreartekQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 316 KMKDWAAVLGDDTADDGNLDLDMKSGLED-TASLDNQPKGALKKLIYAAKLNASLKAlegERNQIYTQLSEVDQIKEDLT 394
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREIRTlERKIERIAVRRQEVLRYFDWYQETWLQ---RRPRLATQLSNIERAISELQ 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 395 EHIKSLeskQASLQSENTEFESESQRLQQKLKVITElyqenemkLHRKLTVEENY--RLEKEEKLSKVDERISHAAEELE 472
Cdd:pfam12128 828 QQLARL---IADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLE 896
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958781444 473 TYRQRAKDLEEELERTIHSYQGQVISHEKKAHD-NWLAARTLERNLNDLRKENAHNRQ 529
Cdd:pfam12128 897 DLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
174-547 |
1.22e-06 |
|
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: 52.03 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 174 YENLERSKSKLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKD 253
Cdd:pfam05483 221 HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 254 ALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVT-LEES---RAQAEQVLSEKETQIESLiKSLLKMKDWAAVLGDDTA 329
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAqMEELnkaKAAHSFVVTEFEATTCSL-EELLRTEQQRLEKNEDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 330 DDGNLDLDMKSG-LEDTASLDNQPK----------GALKKLIYAAK---------------LNASLKALEGERNQIYTQL 383
Cdd:pfam05483 380 KIITMELQKKSSeLEEMTKFKNNKEveleelkkilAEDEKLLDEKKqfekiaeelkgkeqeLIFLLQAREKEIHDLEIQL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 384 SEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITElyQENEMKLHRKLTVEENYRLEKEE-----KLS 458
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ--EASDMTLELKKHQEDIINCKKQEermlkQIE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 459 KVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKF 538
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
....*....
gi 1958781444 539 ELLEKDPYA 547
Cdd:pfam05483 618 KALKKKGSA 626
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-533 |
1.48e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 112 KKLALELSALIEEKCKLLEkvsfVQKEYEglESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLL 191
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAE----AAKAEA--EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 192 EKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGaikdalnENSQLQESQKQLLQE 271
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA-------EEAKKKAEEAKKADE 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 272 AEIMKEQVSDLDKQKVTLEESRAQAEQV--LSEKETQIESLIKSLLKMKDWAAvlgdDTADDGNLDLDMKSGLEDTASLD 349
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEA----KKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 350 NQPKGALKKLIYAAKLNASLKAlEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVIT 429
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 430 EL---------YQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEEL----ETYRQRAKDL--EEELERTIHSYQG 494
Cdd:PTZ00121 1630 EEkkkveqlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEALkkEAEEAKKAEELKK 1709
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958781444 495 QVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTE 533
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
234-548 |
1.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 234 KTTFRIFEINEERLRgaIKDALNE-NSQLQ--ESQKQLLQEAEIMKEQVSDLDK-----QKVTLEESRAQAEQVLSEKET 305
Cdd:TIGR02168 176 ETERKLERTRENLDR--LEDILNElERQLKslERQAEKAERYKELKAELRELELallvlRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 306 QIESLiKSLLKMKDwAAVlgdDTADDGNLDLDMKSGLEDTASLD-NQPKGALKKLIyaAKLNASLKALEGERNQIYTQLS 384
Cdd:TIGR02168 254 ELEEL-TAELQELE-EKL---EELRLEVSELEEEIEELQKELYAlANEISRLEQQK--QILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 385 EVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLhrkltveenyrLEKEEKLSKVDERI 464
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-----------ETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 465 SHAAEELETYRQRAKDLEEELERTihsyQGQVISHEKKAHDNWLAA-----RTLERNLNDLRKENAHNRQKLTETEFKFE 539
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERL----QQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELE 471
|
....*....
gi 1958781444 540 LLEKDPYAL 548
Cdd:TIGR02168 472 EAEQALDAA 480
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-426 |
2.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 231 AEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESL 310
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 311 IKSLLK----MKDWAAVLGDDTADDgnlDLDMKSGLEDTASLDNQPKGALKKLIyaAKLNASLKALEGERNQIYTQLSEV 386
Cdd:COG3883 92 ARALYRsggsVSYLDVLLGSESFSD---FLDRLSALSKIADADADLLEELKADK--AELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958781444 387 DQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLK 426
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
242-485 |
3.04e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 242 INEERLRGaikdaLNENSQLQESQKQLLQEaeimkeqvsDLDKQKVTLEESRAQAEQVLSEKETQIESLIKsllKMKDWA 321
Cdd:PHA02562 171 LNKDKIRE-----LNQQIQTLDMKIDHIQQ---------QIKTYNKNIEEQRKKNGENIARKQNKYDELVE---EAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 322 AVLGDDTADDGNLDLDMKSgledtasldnqPKGALKKL-IYAAKLNASLKALEGERNqIYT----------QLSEVDQIK 390
Cdd:PHA02562 234 AEIEELTDELLNLVMDIED-----------PSAALNKLnTAAAKIKSKIEQFQKVIK-MYEkggvcptctqQISEGPDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 391 EDLTEHIKSLeskQASLQSENTEFESESQR---LQQKLKVITELyqENEMKLHR---KLTVEENYRLEKE-EKLSkvDER 463
Cdd:PHA02562 302 TKIKDKLKEL---QHSLEKLDTAIDELEEImdeFNEQSKKLLEL--KNKISTNKqslITLVDKAKKVKAAiEELQ--AEF 374
|
250 260
....*....|....*....|..
gi 1958781444 464 ISHaAEELETYRQRAKDLEEEL 485
Cdd:PHA02562 375 VDN-AEELAKLQDELDKIVKTK 395
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
363-487 |
3.94e-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: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 363 AKLNASLKALEGERNQIYTQLSEVDQikEDLTEHIKSLESKQASLQSENTEFEsesQRLQQKLKVITELyqENEMKLHRK 442
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEEREL--TEEEEEIRRLEEQVERLEAEVEELE---AELEEKDERIERL--ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958781444 443 ltvEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELER 487
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-304 |
4.55e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQisEAAYENLERSKSKLEDEILLLEKKLE 196
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI--EARLREIEQKLNRLTLEKEYLEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 EERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMK 276
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
170 180
....*....|....*....|....*...
gi 1958781444 277 EQVSDLDKQKVTLEESRAQAEQVLSEKE 304
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-302 |
4.84e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLkeasfEKESTEAQSLEFVEGSQisEAAYENLERSKSKLEDEILLLEKKLE 196
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELI-----EELESELEALLNERASL--EEALALLRSELEELSEELRELESKRS 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 EERVKHSEQDELMADISKRIQSLEDESKSLKSQVAE-AKTTFRIFEINEERLRGAIKDALNENSQLQESQKQL------- 268
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaa 991
|
170 180 190
....*....|....*....|....*....|....
gi 1958781444 269 LQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSE 302
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-487 |
1.27e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEIL 189
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLL 269
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 270 QEAEIMKEQVSDLDKQKVT----------------LEESRAQAEQVLSEKETQIESLIKSLLK----------------- 316
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAgavavligveaayeaaLEAALAAALQNIVVEDDEVAAAAIEYLKaakagratflpldkira 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 317 -------------MKDWAAVLGDDTADDGNLDLDMKSGLEDTASLDNQPKG----------ALKKLIYAAKLNASLKALE 373
Cdd:COG1196 585 raalaaalargaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAlrravtlagrLREVTLEGEGGSAGGSLTG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 374 GERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLHRKLTVEENYRLEK 453
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
410 420 430
....*....|....*....|....*....|....
gi 1958781444 454 EEKLSKVDERISHAAEELETYRQRAKDLEEELER 487
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
206-523 |
1.84e-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: 48.58 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 206 DELMADISKRIQSLEDESKSLKSQVAEAKTTFrifEINEERLRGAIKDALNENSQLQESQKQL---LQEAEIMKE-QVSD 281
Cdd:pfam15921 270 EQLISEHEVEITGLTEKASSARSQANSIQSQL---EIIQEQARNQNSMYMRQLSDLESTVSQLrseLREAKRMYEdKIEE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 282 LDKQKV----TLEESRAQAEQVLSEK---ETQIESLIKSLLKMKD------------WAAVLGDDTA--------DDGNL 334
Cdd:pfam15921 347 LEKQLVlansELTEARTERDQFSQESgnlDDQLQKLLADLHKREKelslekeqnkrlWDRDTGNSITidhlrrelDDRNM 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 335 DLDMKSGLedTASLDNQPKGALKKLIYAAK-LNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTE 413
Cdd:pfam15921 427 EVQRLEAL--LKAMKSECQGQMERQMAAIQgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 414 FESESQRLQQKLKVITELYQENEMKLhrkltvEENYRLEKEEklskvdERISHAAEELETYRQRAKDLE---EELERTIH 490
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKL------QELQHLKNEG------DHLRNVQTECEALKLQMAEKDkviEILRQQIE 572
|
330 340 350
....*....|....*....|....*....|...
gi 1958781444 491 SYQGQVISHEKKAHDNWLAARTLERNLNDLRKE 523
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
212-316 |
3.98e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 212 ISKRIQSLEDESKSLKSQV---AEAKTTFRIFEINEE--RLRGAIKDALNE-NSQLQESQKQLLQEAEIMKEQVSDLDKQ 285
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAkkeAEAIKKEALLEAKEEihKLRNEFEKELRErRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110
....*....|....*....|....*....|....
gi 1958781444 286 KVTLEESR---AQAEQVLSEKETQIESLIKSLLK 316
Cdd:PRK12704 109 EEELEKKEkelEQKQQELEKKEEELEELIEEQLQ 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-535 |
4.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 299 VLSEKETQIESL------------IKSLLKMKD-WAAVLGDDTADDgnldldmksgledtasldnqpkgalkkliYAAKL 365
Cdd:COG1196 194 ILGELERQLEPLerqaekaeryreLKEELKELEaELLLLKLRELEA-----------------------------ELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 366 NASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLHRKLTV 445
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 446 EEnyrlEKEEKLSKVDERISHAAEELETYRQRAKDLEEEL---ERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRK 522
Cdd:COG1196 325 LA----ELEEELEELEEELEELEEELEEAEEELEEAEAELaeaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250
....*....|...
gi 1958781444 523 ENAHNRQKLTETE 535
Cdd:COG1196 401 QLEELEEAEEALL 413
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
206-533 |
4.74e-05 |
|
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: 47.35 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 206 DELMADISKRiQSLEDESKSLKSQVAEAKTTFRIFE---------INEERLRGAIKDALNENSQL----QESQKQLLQEA 272
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKkdvtellnkYSALAIKNKFAKTKKDSEIIikeiKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 273 EIMKEQVSDLDKQKVTLEESRA---QAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKsgledTASLD 349
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAkndKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIS-----SFSID 1639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 350 NQPKGALKKLIYAAKLNASLKALEGERNQIYTQLSEVDQ-------IKEDLTEHIKS-----LESKQASLQSENTEFESE 417
Cdd:TIGR01612 1640 SQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDEldseiekIEIDVDQHKKNyeigiIEKIKEIAIANKEEIESI 1719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 418 SQRLQQKLKVITELYQENEMKlhrkltveenyRLEKEEKLSKVDERISHAAEE-LETYRQRAKDLE---------EELER 487
Cdd:TIGR01612 1720 KELIEPTIENLISSFNTNDLE-----------GIDPNEKLEEYNTEIGDIYEEfIELYNIIAGCLEtvskepityDEIKN 1788
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958781444 488 TIHSYQGQ---VISHEKKAH---DNwLAARTLERNLNDLRKENAHNRQKLTE 533
Cdd:TIGR01612 1789 TRINAQNEflkIIEIEKKSKsylDD-IEAKEFDRIINHFKKKLDHVNDKFTK 1839
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
165-533 |
4.86e-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: 47.09 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 165 EGSQISEAAYENLERSKSKLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINE 244
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 245 ERLRGAIKDaLNENSQLQESQKQLLQ------EAEI--MKEQVSDLDKQKVTLEESRAQAEQVLSEKETQI---ESLIKS 313
Cdd:pfam01576 99 KKMQQHIQD-LEEQLDEEEAARQKLQlekvttEAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeEEKAKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 314 LLKMKdwaavlgddtaddgNLDLDMKSGLEDTASLDNQPKGALKKLiyaaklnasLKALEGERNQIYTQLSEVDQIKEDL 393
Cdd:pfam01576 178 LSKLK--------------NKHEAMISDLEERLKKEEKGRQELEKA---------KRKLEGESTDLQEQIAELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 394 TehiKSLESKQASLQSENTEFESESQRLQQKLKVITELyQENEMKLHRKLTVEENYRlekeeklSKVDERISHAAEELET 473
Cdd:pfam01576 235 R---AQLAKKEEELQAALARLEEETAQKNNALKKIREL-EAQISELQEDLESERAAR-------NKAEKQRRDLGEELEA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958781444 474 YRqraKDLEEELERT-----IHSYQGQVISHEKKAHDNwlAARTLERNLNDLRKENAHNRQKLTE 533
Cdd:pfam01576 304 LK---TELEDTLDTTaaqqeLRSKREQEVTELKKALEE--ETRSHEAQLQEMRQKHTQALEELTE 363
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
96-533 |
5.62e-05 |
|
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: 46.96 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 96 WRGFRSIRSRF-YVGREKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVE------GSQ 168
Cdd:TIGR00606 556 SRHSDELTSLLgYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQ 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 169 ISEAAYENLERskskledeilllekkleeeRVKHSEQDELM-----ADISKRIQSLEDESKS---LKSQVAEAKTtfrif 240
Cdd:TIGR00606 636 DEESDLERLKE-------------------EIEKSSKQRAMlagatAVYSQFITQLTDENQSccpVCQRVFQTEA----- 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 241 EINE--ERLRGAIKDALNENSQLQESQKQLLQEAEIM----KEQVSDLDKQKVTLEESRAQAEQV----------LSEKE 304
Cdd:TIGR00606 692 ELQEfiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQSIIDLKEKEIPELRNKLQKVnrdiqrlkndIEEQE 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 305 TQIESLIKSLlkmkDWAAVLGDDTADDGNLDLDMKSGLEDTASLDNQPKGALKKLIYaAKLNASLKALEGERNQIYTQLS 384
Cdd:TIGR00606 772 TLLGTIMPEE----ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTV-QQVNQEKQEKQHELDTVVSKIE 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 385 EVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQ-------KLKVITELYQENEMKLHRKLTVEENyrleKEEKL 457
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeqlveLSTEVQSLIREIKDAKEQDSPLETF----LEKDQ 922
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 458 SKVDERISHAAEELETYRQRAKDLEEELERtIHSYQGQVISHEKKAHDNWLAARTLERN-LNDLRKENAHNRQKLTE 533
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVNDIKEKVKN-IHGYMKDIENKIQDGKDDYLKQKETELNtVNAQLEECEKHQEKINE 998
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
68-456 |
6.32e-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: 46.49 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 68 ADFNPNGFSLELAICVLTVGLLAIVLFLWRGFRSIRSRFyvgrekklALELSALIEEKCKLLEKVSFVQKEYEGLESSLK 147
Cdd:COG5185 147 ADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLT--------LGLLKGISELKKAEPSGTVNSIKESETGNLGSE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 148 EASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLEEervKHSEQDELMADISKRIQSLEDESKSLK 227
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE---KLGENAESSKRLNENANNLIKQFENTK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 228 SQVAEAKTTFRIFEINEE--------RLRGAIKDALNE-NSQLQESQKQLLQEAEIMKEQVSDLDKQK--VTLEESRAQA 296
Cdd:COG5185 296 EKIAEYTKSIDIKKATESleeqlaaaEAEQELEESKREtETGIQNLTAEIEQGQESLTENLEAIKEEIenIVGEVELSKS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 297 EQVLSEKETQIESLIKSLL-KMKDWAAVLGDDTAddgNLDLDMKSGLEDTASLDNQPKGALKKLIYAAK--------LNA 367
Cdd:COG5185 376 SEELDSFKDTIESTKESLDeIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSSNEEVSKllneliseLNK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 368 SLKALEGERNQIYTQ-----LSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRlqQKLKVITELYQENEMKLHRK 442
Cdd:COG5185 453 VMREADEESQSRLEEaydeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER--QLEGVRSKLDQVAESLKDFM 530
|
410
....*....|....
gi 1958781444 443 LTVEENYRLEKEEK 456
Cdd:COG5185 531 RARGYAHILALENL 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
110-543 |
7.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALiEEKCKLLEKVSFVQKEYEGLE---SSLKEASFEKESTEAQSLEFVEG--SQISEAayENLERSKSKL 184
Cdd:PRK03918 267 RIEELKKEIEEL-EEKVKELKELKEKAEEYIKLSefyEEYLDELREIEKRLSRLEEEINGieERIKEL--EEKEERLEEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 185 EDEILLLEKKLEEERVKHSEQDELMA------DISKRIQSLE-DESKSLKSQVAEAKTTFR--IFEINEER--LRGAIKD 253
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAkkeeleRLKKRLTGLTpEKLEKELEELEKAKEEIEeeISKITARIgeLKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 254 ALNENSQLQESQ------KQLLQE---AEIMKE---QVSDLDKQKVTLEESRAQAEQVLSEKETQI--ESLIKSLLKMKD 319
Cdd:PRK03918 424 LKKAIEELKKAKgkcpvcGRELTEehrKELLEEytaELKRIEKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 320 WAAVLGDDTADDGNLDLDMKSGL-----EDTASLDNQPKGALKKLIYAAKLNASLKALEGERNQIYTQLSEV-DQIKEDL 393
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEyeklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELG 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 394 TEHIKSLESKQASLQSENTEF------ESESQRLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDErisha 467
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE----- 658
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958781444 468 aeelETYRqRAKDLEEELERTIHSYQGQVISHEKKahdnwlaARTLERNLNDLRKEnahnRQKLTETEFKFELLEK 543
Cdd:PRK03918 659 ----EEYE-ELREEYLELSRELAGLRAELEELEKR-------REEIKKTLEKLKEE----LEEREKAKKELEKLEK 718
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
110-535 |
8.85e-05 |
|
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: 46.12 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEIL 189
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKleeeRVKHSEQDELMADISKRIQSLEDESKSLKSQVAE---AKTTFRIFEINEERLRGAIkdalNENSQLQESQK 266
Cdd:TIGR00618 474 QLQTK----EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpnpARQDIDNPGPLTRRMQRGE----QTYAQLETSEE 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 267 QLLQEAEIMKEQVSDLDKQkvtlEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGnldlDMKSGLEDTA 346
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE----DMLACEQHAL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 347 SLDNQPKGALKKLI-YAAKLNASLKALEGERNQIYTQLSevdqiKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKL 425
Cdd:TIGR00618 618 LRKLQPEQDLQDVRlHLQQCSQELALKLTALHALQLTLT-----QERVREHALSIRVLPKELLASRQLALQKMQSEKEQL 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 426 KVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIhsyQGQVISHEKKAHD 505
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL---KARTEAHFNNNEE 769
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958781444 506 NWLAART------LERNLNDLRKENAHNRQKLTETE 535
Cdd:TIGR00618 770 VTAALQTgaelshLAAEIQFFNRLREEDTHLLKTLE 805
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
214-544 |
9.26e-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: 46.17 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 214 KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEqvsdldkQKVTLEESR 293
Cdd:TIGR04523 54 KELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE-------QKNKLEVEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 294 AQAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKSGL----EDTASLDNQPKGALKKLIYAAKLNASL 369
Cdd:TIGR04523 127 NKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKLELLLSNL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 370 KALEGERNQIYTQLSEVDQIKEDLTehiKSLESKQASLQSENTEFesesQRLQQKLKVITELYQENEMKLHRK-LTVEEN 448
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLK---DNIEKKQQEINEKTTEI----SNTQTQLNQLKDEQNKIKKQLSEKqKELEQN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 449 YRL--EKEEKLSKVDERIShaaeELEtyRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKE--- 523
Cdd:TIGR04523 280 NKKikELEKQLNQLKSEIS----DLN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltn 353
|
330 340
....*....|....*....|....*
gi 1958781444 524 ----NAHNRQKLTETEFKFELLEKD 544
Cdd:TIGR04523 354 seseNSEKQRELEEKQNEIEKLKKE 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-427 |
1.15e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALElsALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLER---------- 179
Cdd:pfam15921 506 QEKERAIE--ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmtqlvgqhgr 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 180 -------SKSKLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIK 252
Cdd:pfam15921 584 tagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVK 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 253 DALNENSQLQES----QKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAavlgddT 328
Cdd:pfam15921 664 TSRNELNSLSEDyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI------T 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 329 ADDGNLD-LDMK-SGLEDTASLDNQPKGALKKliYAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLES--KQ 404
Cdd:pfam15921 738 AKRGQIDaLQSKiQFLEEAMTNANKEKHFLKE--EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValDK 815
|
330 340 350
....*....|....*....|....*....|
gi 1958781444 405 ASLQ-------SENTEFESESQRLQQKLKV 427
Cdd:pfam15921 816 ASLQfaecqdiIQRQEQESVRLKLQHTLDV 845
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-499 |
1.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 109 GREKKLALELSALIEEKCKLLEKVsfvQKEYEGLESSLKEASFEKESTEAQslefvegsqiseaaYENLERSKSKLEDEI 188
Cdd:COG4717 63 GRKPELNLKELKELEEELKEAEEK---EEEYAELQEELEELEEELEELEAE--------------LEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 189 LLLEKKLEEERVKH------SEQDELMADIsKRIQSLEDESKSLKSQVAEAKTTF-RIFEINEERLRGAIKDALNENSQL 261
Cdd:COG4717 126 QLLPLYQELEALEAelaelpERLEELEERL-EELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 262 QESQKQLLQEAEIMKEQVSDLDKQKVTLEES--RAQAEQVLSE------------------------------------- 302
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEarlllliaaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 303 --------------------KETQIESLIKSL--LKMKDWAAVLGDDTADDGNLDLDMKSGLEDTASLDNQPKGALKKL- 359
Cdd:COG4717 285 llallflllarekaslgkeaEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELq 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 360 ----------IYAAKLNASLKALE--GERNQIYTQL-SEVDQIKEDLTEHIKSLESKQASLQSEntEFESESQRLQQKLK 426
Cdd:COG4717 365 leeleqeiaaLLAEAGVEDEEELRaaLEQAEEYQELkEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958781444 427 VITELYQENEMKL----HRKLTVEENYRL-EKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISH 499
Cdd:COG4717 443 ELEEELEELREELaeleAELEQLEEDGELaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
214-312 |
1.40e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 214 KRIQSLEDESKSLKS---QVAEAKTTFRIFEINEE--RLRGAIKDALNE-NSQLQESQKQLLQEAEIMKEQVSDLDKQKV 287
Cdd:pfam12072 27 AKIGSAEELAKRIIEeakKEAETKKKEALLEAKEEihKLRAEAERELKErRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100
....*....|....*....|....*...
gi 1958781444 288 TL---EESRAQAEQVLSEKETQIESLIK 312
Cdd:pfam12072 107 SLekkEKELEAQQQQLEEKEEELEELIE 134
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
209-434 |
1.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 209 MADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINeerlrgaikdalNENSQLQESQKQLLQeaeimkeQVSDLDKQKVT 288
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 289 LEESRAQAEQVLSEKETQIESLIKSLlkmkdwAAVLGDDTADDGNLDLDMKSGLEDTASLDNQPKgalkkliyaaklNAS 368
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDAL------PELLQSPVIQQLRAQLAELEAELAELSARYTPN------------HPD 292
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 369 LKALEGERNQIYTQL-SEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQE 434
Cdd:COG3206 293 VIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-486 |
1.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 174 YENLERSKSKLEDEIlllekkleeervkhseqDELMADISKRIQSLEDESKSLKSQVAEAKTTFRifEINEerlrgaIKD 253
Cdd:PRK03918 160 YENAYKNLGEVIKEI-----------------KRRIERLEKFIKRTENIEELIKEKEKELEEVLR--EINE------ISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 254 ALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAvlgddtaddgn 333
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK----------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 334 lDLDMKSGLEDTASLDNQPKGALKKLIYaaKLNASLKALEGERNQIYTQLSEVDQIK---EDLTEHIKSLESKQASLQSE 410
Cdd:PRK03918 284 -ELKELKEKAEEYIKLSEFYEEYLDELR--EIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEER 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958781444 411 NTEFESESQRLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERIShaaeELETYRQRAKDLEEELE 486
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-326 |
1.72e-04 |
|
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: 44.75 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 136 QKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLEEERVK----HSEQDELMAD 211
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 212 ISKRIQSL-----EDESKSLKSQ--VAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQEAEIMKEQVSDLDK 284
Cdd:COG4942 106 LAELLRALyrlgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958781444 285 QKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAVLGD 326
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
117-320 |
1.82e-04 |
|
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: 45.01 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKE--STEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKK 194
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKekESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 195 LEEERVKHSEQDELmadiskrIQSLEDESKSLKSQVAEAKTTfrIFEINEErlrgaIKDALNENSQLQESQKQLLQEAEI 274
Cdd:TIGR04523 577 QKSLKKKQEEKQEL-------IDQKEKEKKDLIKEIEEKEKK--ISSLEKE-----LEKAKKENEKLSSIIKNIKSKKNK 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958781444 275 MKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSllkMKDW 320
Cdd:TIGR04523 643 LKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIEL---MKDW 685
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
110-550 |
2.02e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLaLELSALIEEKCKLLEKVSFVQKEYEGlESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEIL 189
Cdd:COG5022 932 RLKKL-LNNIDLEEGPSIEYVKLPELNKLHEV-ESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 LLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEE--RLRGAIKDALNENSQL--QESQ 265
Cdd:COG5022 1010 ALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARykALKLRRENSLLDDKQLyqLEST 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 266 KQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSL---LKMKDwAAVLGDDTADDGNLDLDMKSGL 342
Cdd:COG5022 1090 ENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLvntLEPVF-QKLSVLQLELDGLFWEANLEAL 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 343 EDTASLDNQPKgalKKLIYAAKLNASLKALEgernqiytqlSEVDQIKEDLTEHiksleskqASLQSENTEFESESQRLQ 422
Cdd:COG5022 1169 PSPPPFAALSE---KRLYQSALYDEKSKLSS----------SEVNDLKNELIAL--------FSKIFSGWPRGDKLKKLI 1227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 423 QKLKVITELYQenemklhrKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSY-------QGQ 495
Cdd:COG5022 1228 SEGWVPTEYST--------SLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLlqyinvgLFN 1299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958781444 496 VISHEKKAHdNWLAARTLERNLNDL-----RKENAH---NRQKLTETEFKFELLEKDPYALDV 550
Cdd:COG5022 1300 ALRTKASSL-RWKSATEVNYNSEELddwcrEFEISDvdeELEELIQAVKVLQLLKDDLNKLDE 1361
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-543 |
2.28e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 119 SALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLLEKKLEEE 198
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 199 RVK-------HSEQDELMADISKRIQ--------------SLEDESKSLKSQVAEAKTtfRIFEI------NEERLRGAI 251
Cdd:pfam01576 172 EEKakslsklKNKHEAMISDLEERLKkeekgrqelekakrKLEGESTDLQEQIAELQA--QIAELraqlakKEEELQAAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 252 KDALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVtleeSRAQAEQVLSEKETQIESLIKSLlkmkdwaavlgDDTADD 331
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERA----ARNKAEKQRRDLGEELEALKTEL-----------EDTLDT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 332 GNLDLDMKSGLEdtasldnQPKGALKkliyaaklnaslKALEGERNQIYTQLSEVDQIK----EDLTEHIKSLESKQASL 407
Cdd:pfam01576 315 TAAQQELRSKRE-------QEVTELK------------KALEEETRSHEAQLQEMRQKHtqalEELTEQLEQAKRNKANL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 408 QSENTEFESESQRLQQKLKVITELYQENEMK----------LHRKLTVEENYRLEKEEKLSKVD---ERISHAAEELET- 473
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKrkklegqlqeLQARLSESERQRAELAEKLSKLQselESVSSLLNEAEGk 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 474 -------------------------------YRQRAKDLEEE-----------------LERTIHSYQGQVISHEKKAHD 505
Cdd:pfam01576 456 niklskdvsslesqlqdtqellqeetrqklnLSTRLRQLEDErnslqeqleeeeeakrnVERQLSTLQAQLSDMKKKLEE 535
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958781444 506 NWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEK 543
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
213-311 |
2.77e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 42.22 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 213 SKRIQSLEDESKSLKSQVAEAKTTFrifeinEERLRGAIKDALNENSQLQESQKQllQEAEIMKEQVSDLDKQKvtlEES 292
Cdd:PRK14473 41 TRRIEESLRDAEKVREQLANAKRDY------EAELAKARQEAAKIVAQAQERARA--QEAEIIAQARREAEKIK---EEA 109
|
90 100
....*....|....*....|...
gi 1958781444 293 RAQAEQ----VLSEKETQIESLI 311
Cdd:PRK14473 110 RAQAEQerqrMLSELKSQIADLV 132
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
117-545 |
2.97e-04 |
|
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: 44.44 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKE-----ASFEKESTEAQSLEFVEGSQISEAAYENLErskskledeilll 191
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEqnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALE------------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 192 ekklEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQLLQE 271
Cdd:pfam12128 422 ----SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 272 AEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLK-MKDWAAVLGD--DTADDGNLDLdmksgleDTASL 348
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKeAPDWEQSIGKviSPELLHRTDL-------DPEVW 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 349 DNQPKGALKklIYAAKLNasLKALEGERNQIYTQL--SEVDQIKEDLtehiKSLESKQASLQSENTEFESESQRLQQKLK 426
Cdd:pfam12128 571 DGSVGGELN--LYGVKLD--LKRIDVPEWAASEEElrERLDKAEEAL----QSAREKQAAAEEQLVQANGELEKASREET 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 427 VITELYQENEMKLHRKLTVEENYRLEKEEKLSkvdERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDN 506
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEKQSEKDKKNKALA---ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY 719
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958781444 507 WLAARTLERNLNDL-------RKENAHNRQKLTETEFKFELLEKDP 545
Cdd:pfam12128 720 WQVVEGALDAQLALlkaaiaaRRSGAKAELKALETWYKRDLASLGV 765
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
118-543 |
3.23e-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: 44.27 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 118 LSALIEEKCKLLEK----VSFVQKEYEGLESSLKEAsfekesteaqsLEFVEGSQISEAAYENLERSKS---KLEDEILL 190
Cdd:TIGR00606 438 LGRTIELKKEILEKkqeeLKFVIKELQQLEGSSDRI-----------LELDQELRKAERELSKAEKNSLtetLKKEVKSL 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 191 LEKKLEEERVKHSEqDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNEnSQLQESQKQLLQ 270
Cdd:TIGR00606 507 QNEKADLDRKLRKL-DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 271 EAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKmkdwAAVLGDDTADDGNLDLDMKSGLEDTASLdn 350
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD----VCGSQDEESDLERLKEEIEKSSKQRAML-- 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 351 qpkgALKKLIYAAKLNASLkalegERNQIYTQLSEVD-QIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVIT 429
Cdd:TIGR00606 659 ----AGATAVYSQFITQLT-----DENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 430 ELY--QENEMKLHRKLTVEENYRLEK-EEKLSKVDERISHAAEELETY---RQRAKDLEEELErTIHSYQGQVISHEKKA 503
Cdd:TIGR00606 730 GLApgRQSIIDLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVT-IMERFQMELKDVERKI 808
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958781444 504 HD--NWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEK 543
Cdd:TIGR00606 809 AQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-543 |
3.27e-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: 44.29 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSlefvegsqisEAAYENLERSKSKLEDEilllekkle 196
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI----------KKQEWKLEQLAADLSKY--------- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 eervkhseQDELMaDISKRIQSLEDESKSLKSQVAEAKTTFRIFEiNEERLRGAIKDALNEN--------SQLQESQKQL 268
Cdd:TIGR02169 468 --------EQELY-DLKEEYDRVEKELSKLQRELAEAEAQARASE-ERVRGGRAVEEVLKASiqgvhgtvAQLGSVGERY 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 269 LQEAEIMKEqvSDLDKQKVTLEESRAQAEQVLSEKETQIESLIkSLLKMKDwAAVLGDDTADDGNLDLDMksgleDTASL 348
Cdd:TIGR02169 538 ATAIEVAAG--NRLNNVVVEDDAVAKEAIELLKRRKAGRATFL-PLNKMRD-ERRDLSILSEDGVIGFAV-----DLVEF 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 349 DNQPKGALKKL---------IYAAK---LNASLKALEGE---------------RNQIYTQLSEVDQIKEdLTEHIKSLE 401
Cdd:TIGR02169 609 DPKYEPAFKYVfgdtlvvedIEAARrlmGKYRMVTLEGElfeksgamtggsrapRGGILFSRSEPAELQR-LRERLEGLK 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 402 SKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLHRKLTVEENYRlekeEKLSKVDERISHAAEELETYRQRAKDL 481
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----ERLEELEEDLSSLEQEIENVKSELKEL 763
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958781444 482 E---EELERTIHSYQGQVisHEKKAHDNWLAARTLERNLNDLRKENAHNR-------QKLTETEFKFELLEK 543
Cdd:TIGR02169 764 EariEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEarlreieQKLNRLTLEKEYLEK 833
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
214-533 |
6.10e-04 |
|
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: 43.42 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 214 KRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENS---------------------------------- 259
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkeqakkaleyyqlkekleleeeyllyldyl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 260 QLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKdwAAVLGDDTADDGNLDLDMK 339
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL--AKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 340 SGLEDTASLDNQPKGALKKLIYAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQ 419
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 420 RLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISH 499
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350
....*....|....*....|....*....|....
gi 1958781444 500 EKKAHDNWLAARTLERNLNDLRKENAHNRQKLTE 533
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
109-481 |
7.99e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 109 GREKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQslefvegsqiseaayenLERSKSKLEDei 188
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE-----------------LEQARSELEQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 189 llLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQL 268
Cdd:COG4372 78 --LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 269 LQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKSGLEDTASL 348
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 349 DNQ-----PKGALKKLIYAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQ 423
Cdd:COG4372 236 SALldaleLEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958781444 424 KLKvitELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDL 481
Cdd:COG4372 316 ALL---AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
363-510 |
8.13e-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: 41.83 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 363 AKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFES---------ESQRLQQKLKvitelYQ 433
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIE-----SL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958781444 434 ENEMKLHRKLTVEENYRLE-KEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAA 510
Cdd:COG1579 102 KRRISDLEDEILELMERIEeLEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
375-479 |
9.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 375 ERNQIYTQLSE-VDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLHR--KLTVEEnyrl 451
Cdd:PRK12704 79 ERRNELQKLEKrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEE---- 154
|
90 100
....*....|....*....|....*....
gi 1958781444 452 EKEEKLSKVDERISH-AAEELETYRQRAK 479
Cdd:PRK12704 155 AKEILLEKVEEEARHeAAVLIKEIEEEAK 183
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-316 |
1.03e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 112 KKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEILLL 191
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 192 EKKLEEERV---KHSEQDELM--------ADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQ 260
Cdd:COG4942 103 KEELAELLRalyRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958781444 261 LQESQKQLLQEAEIMKEQVSDLDKQkvtlEESRAQAEQVLSEKETQIESLIKSLLK 316
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEELEALIARLEA 234
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
586-796 |
1.03e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 586 PRAPSDRSLSPPweqERRMTAHPPPGQPYSDPVPQR--QDRFYSNSGRLSGP-AELRSYNMPSLDKVDGPVSSEMES-SR 661
Cdd:PHA03247 2628 PPSPSPAANEPD---PHPPPTVPPPERPRDDPAPGRvsRPRRARRLGRAAQAsSPPQRPRRRAARPTVGSLTSLADPpPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 662 NDTKDNLGNSNVPDSPHPTESEAAGRGFIPPPFPPV-----RAPLFPVDPRSQFMRRGPSFPPPPpgniyTAPRDYF--P 734
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAppavpAGPATPGGPARPARPPTTAGPPAP-----APPAAPAagP 2779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958781444 735 PRDFPGPPLPPFPGRTVYAPRGFPPFLPPRAGFFPPPPHHENRSELPPDMSPPSKEPAADPP 796
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
117-310 |
1.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 117 ELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQslefvegsqiseaaYENLERSKSKLEDEILLlekkle 196
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE--------------LEALQAEIDKLQAEIAE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 197 eervKHSEQDELMADISKRIQSL--EDESKSLKSQVAEAK--TTF--RIFEINeeRLRGAIKDALNENSQLQESQKQLLQ 270
Cdd:COG3883 77 ----AEAEIEERREELGERARALyrSGGSVSYLDVLLGSEsfSDFldRLSALS--KIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958781444 271 EAEimkEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESL 310
Cdd:COG3883 151 ELE---AKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
394-534 |
1.64e-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: 40.88 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 394 TEHIKSLESKQASLQSENTEFESESQRLQQKLKV-----------ITELYQENEMkLHRKLTVEENYRLEKEEKLSKVDE 462
Cdd:pfam17078 2 TKVIESLHDQIDALTKTNLQLTVQSQNLLSKLEIaqqkeskflenLASLKHENDN-LSSMLNRKERRLKDLEDQLSELKN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958781444 463 RISHAAEE-------LETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTET 534
Cdd:pfam17078 81 SYEELTESnkqlkkrLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQR 159
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
343-550 |
1.73e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 343 EDTASLDNQPKGALKKLIYAAKLNASLKALEGERNQ----IYTQL--------SEVDQIKEDLTEHIKSLESKQASLQSE 410
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIArkqnKYDELveeaktikAEIEELTDELLNLVMDIEDPSAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 411 NTEfesesqrlQQKLKVITELYQEnEMKLHRKLTV---------EENYRLEK--------EEKLSKVDERISHAAEELET 473
Cdd:PHA02562 261 NTA--------AAKIKSKIEQFQK-VIKMYEKGGVcptctqqisEGPDRITKikdklkelQHSLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 474 YRQRAKDLeEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNRQKLTETEFKFELLEKDPYALDV 550
Cdd:PHA02562 332 FNEQSKKL-LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
200-320 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 200 VKHSEQ-DELMADISKRIQSLEDESKSLKSQVAEakttfriFEINEERLRGAIKDALnensqlqesqKQLLQEAEIMKEQ 278
Cdd:smart00787 164 MKELELlNSIKPKLRDRKDALEEELRQLKQLEDE-------LEDCDPTELDRAKEKL----------KKLLQEIMIKVKK 226
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958781444 279 VSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKDW 320
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF 268
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
212-487 |
1.83e-03 |
|
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: 42.13 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 212 ISKRIQSLEDESKSLKSQVAEAKTtfrifeineerLRGAIKDALNENSQLQESQKQLLQEaeiMKEQVSDLDKQkvtLEE 291
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSH-----------LHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQ---WKE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 292 SRAQAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKSGLEDTASLdnqpkgalkkliyaakLNASLKA 371
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN----------------LEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 372 LEGERNQIYTQLSEVDQ-IKEDLTEHIKSLESKQASLQSE----NTEFESESQRLQQKLKVITE--LYQENEMKLHRKLT 444
Cdd:pfam12128 366 LTGKHQDVTAKYNRRRSkIKEQNNRDIAGIKDKLAKIREArdrqLAVAEDDLQALESELREQLEagKLEFNEEEYRLKSR 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958781444 445 VEE-NYRL-----EKEEKLSKV--DERISHAAEELETYRQRAKDLEEELER 487
Cdd:pfam12128 446 LGElKLRLnqataTPELLLQLEnfDERIERAREEQEAANAEVERLQSELRQ 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-523 |
2.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 136 QKEYEGLESSLKEASFEKESTEaqslEFVEgsqiSEAAYENLERSKSKLEDEILLLEKKLEEERVKHSEQDELMADISKR 215
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLE----KFIK----RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 216 IQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQKQlLQEAEIMKEQVSDLDKQKVTLEESRAQ 295
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 296 AEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLdLDMKSGLEDTASLDNQpkgALKKLIYAAKLNASLKALEGE 375
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-EKRLEELEERHELYEE---AKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 376 RnqIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLqQKLKVITELyqenemkLHRKLTVEENYRLEKE- 454
Cdd:PRK03918 388 K--LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPV-------CGRELTEEHRKELLEEy 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 455 -EKLSKVDERISHAAEELETYRQRAKDLEEELER-----TIHSYQGQVISHEKK--------AHDNWLAARTLERNLNDL 520
Cdd:PRK03918 458 tAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKlkkynleeLEKKAEEYEKLKEKLIKL 537
|
...
gi 1958781444 521 RKE 523
Cdd:PRK03918 538 KGE 540
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
373-544 |
2.44e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 373 EGERNQIYTQLSEVDQIKEdltEHIKSLESKQASLQSENTEFESESQRLQQKLKVITE---LYQENEMKLHRKLTVEENY 449
Cdd:pfam17380 349 ELERIRQEERKRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 450 RLEKEEKLSKVDERISHA-AEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLNDLRKENAHNR 528
Cdd:pfam17380 426 RAEQEEARQREVRRLEEErAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
170
....*....|....*.
gi 1958781444 529 QKLTETEFKFELLEKD 544
Cdd:pfam17380 506 QAMIEEERKRKLLEKE 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-487 |
2.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 111 EKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSlefvegsQISEAayENLERSKSKLEDEILL 190
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-------KAEEA--KKADEAKKKAEEAKKA 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 191 LEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQLQESQK-QLL 269
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKaDEA 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 270 QEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLLKMKdwaavlgddtADDGNLDLDMKSGLEDTASLD 349
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK----------AEEARIEEVMKLYEEEKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 350 NQPKGALKKLIYAAKLNaslKALEGERNQIYTQLSEVDQIKEdlTEHIKSLESKQASLQSENTEFESESQRLQQKLKVIT 429
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKK--AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 430 ELYQENEMKLHRKL----TVEENYRLEKEEK-----LSKVDERISHAAEELETYRQRAKDLEEELER 487
Cdd:PTZ00121 1685 EDEKKAAEALKKEAeeakKAEELKKKEAEEKkkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
100-491 |
2.53e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 100 RSIRSRFYVGREKKLALELSALI--------EEKCKLLEKVSFVQKEYEGLESslkeasFEKESTEAQslefvegsqise 171
Cdd:TIGR01612 662 KSELSKIYEDDIDALYNELSSIVkenaidntEDKAKLDDLKSKIDKEYDKIQN------METATVELH------------ 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 172 aaYENLERSKSKLEDEILllekkleeeRVKHSEQDELMADISKRIQSLEDESKSLKSQV---AEAKTTFRIFEINEERLR 248
Cdd:TIGR01612 724 --LSNIENKKNELLDIIV---------EIKKHIHGEINKDLNKILEDFKNKEKELSNKIndyAKEKDELNKYKSKISEIK 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 249 GAIKDALN-ENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQI--------------ESLIKS 313
Cdd:TIGR01612 793 NHYNDQINiDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFInfennckekidsehEQFAEL 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 314 LLKMKdwaAVLGDDTADDgnldldMKSGLEDTASLDNQPKGALKK----LIYAAKLNASLKALEGERNQIYTQLSEVDQI 389
Cdd:TIGR01612 873 TNKIK---AEISDDKLND------YEKKFNDSKSLINEINKSIEEeyqnINTLKKVDEYIKICENTKESIEKFHNKQNIL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 390 KEDLTEHIKSLESKQASLQSENTEFESE-SQRLQQKLKVITEL----YQENEMKLHRKLT-VEENYRLEKEEKL-SKVDE 462
Cdd:TIGR01612 944 KEILNKNIDTIKESNLIEKSYKDKFDNTlIDKINELDKAFKDAslndYEAKNNELIKYFNdLKANLGKNKENMLyHQFDE 1023
|
410 420
....*....|....*....|....*....
gi 1958781444 463 RiSHAAEELETYRQRAKDLEEELERTIHS 491
Cdd:TIGR01612 1024 K-EKATNDIEQKIEDANKNIPNIEIAIHT 1051
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
171-368 |
2.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 171 EAAYENLERSKSKLEDEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKTTFRifeineERLRGA 250
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA------ELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 251 IK-----------------DALNENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKS 313
Cdd:COG4942 114 YRlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958781444 314 LLKMKDWAAVLGDDTADDGNLDLDMKsglEDTASLDNQPKGALKKLIYAAKLNAS 368
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQ---QEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
206-542 |
2.68e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 206 DELMADISKRIQSLEDESKSLKSQvaeakttfrifeinEERLRGAIKDALNensQLQESQKQLLQEAEIMKEQVSDLDKQ 285
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLES--------------EEKNREEVEQLKD---LYRELRKSLLANRFSFGPALDELEKQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 286 KVTLEESRAQAEQvLSEKETQIESLiKSLLKMKDWAAVLGDDTADdgnldldMKSGLEDtasLDNQPKGALKKLIYAakl 365
Cdd:PRK04778 174 LENLEEEFSQFVE-LTESGDYVEAR-EILDQLEEELAALEQIMEE-------IPELLKE---LQTELPDQLQELKAG--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 366 naslkalegernqiYTQLSE---------VDQIKEDLTEHIKSLESKQASLqsENTEFESESQRLQQKlkvITELYQ--E 434
Cdd:PRK04778 239 --------------YRELVEegyhldhldIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQER---IDQLYDilE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 435 NEMKLHRKLtveenyrlekEEKLSKVDERISHAAEEletyrqrAKDLEEELERTIHSYQgqvISHEKKAHdnwlaARTLE 514
Cdd:PRK04778 300 REVKARKYV----------EKNSDTLPDFLEHAKEQ-------NKELKEEIDRVKQSYT---LNESELES-----VRQLE 354
|
330 340
....*....|....*....|....*...
gi 1958781444 515 RNLNDLRKENAHNRQKLTETEFKFELLE 542
Cdd:PRK04778 355 KQLESLEKQYDEITERIAEQEIAYSELQ 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
356-502 |
3.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 356 LKKLIYAAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITEL---- 431
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958781444 432 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKK 502
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
111-459 |
4.13e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 40.70 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 111 EKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLED---E 187
Cdd:pfam15818 66 KKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKyyaT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 188 ILLLEKKLEEERVK--HSEQDEL-----MADISKR----IQSLEDESKSLKSQVAEAKTTFRiFEINEERLRGAIKDaln 256
Cdd:pfam15818 146 ITGQFGLVKENHGKleQNVQEAIqlnkrLSALNKKqeseICSLKKELKKVTSDLIKSKVTCQ-YKMGEENINLTIKE--- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 257 enSQLQESQKQLLQEAEIMK---EQVSDLDKQKVTLEESRAQAEQVLsEKETQIESLIKSLLKmkdwaaVLGDDTAD--- 330
Cdd:pfam15818 222 --QKFQELQERLNMELELNKkinEEITHIQEEKQDIIISFQHMQQLL-QQQTQANTEMEAELK------ALKENNQTler 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 331 DGNLDLD-MKSGLEDTASLDNQPKGALKkliyaaKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQASlqs 409
Cdd:pfam15818 293 DNELQREkVKENEEKFLNLQNEHEKALG------TWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKF--- 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958781444 410 entefeSESQRLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSK 459
Cdd:pfam15818 364 ------EEDKKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQEIREENTK 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-487 |
5.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 266 KQLLQEAEIMKEQVSDLD----------KQKVTLEESRAQAEQvLSEKETQIESLIKSLLKMKDWAAVLGDDTADDgnld 335
Cdd:COG4913 221 PDTFEAADALVEHFDDLErahealedarEQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA---- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 336 lDMKSGLEDTASLDNQpkgalkkliyAAKLNASLKALEGERNQIYTQLSEVDqikedlTEHIKSLESKQASLQSENTEFE 415
Cdd:COG4913 296 -ELEELRAELARLEAE----------LERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958781444 416 SESQRLQQKLKVITELYQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELER 487
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
110-308 |
5.45e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 110 REKKLALELSALIEEKCKLLEKVSFVQKEYEGLESSLKEASFEKESTEAQSLEFVEGSQISEAAYENLERSKSKLEDEil 189
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 190 lleKKLEEERVKHSEQDElmadiSKRIQSLEDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALNENSQ--LQESQKQ 267
Cdd:pfam17380 444 ---RAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamIEEERKR 515
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958781444 268 LLQEAEIMKEQVSdldkqkVTLEESRAQAEQvlsEKETQIE 308
Cdd:pfam17380 516 KLLEKEMEERQKA------IYEEERRREAEE---ERRKQQE 547
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-335 |
6.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 100 RSIRSRFYVGR--EKKLAlelsALIEEKCKLLEKVSFVQKEYEGLESSLKEAsfEKESTEAQSLEFVEGSQIS----EAA 173
Cdd:COG4913 596 RRIRSRYVLGFdnRAKLA----ALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDvasaERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 174 YENLERSKSKLE---DEILLLEKKLEEERVKHSEQDELMADISKRIQSLEDESKSLKSQVAEAkttfrifeinEERLRGA 250
Cdd:COG4913 670 IAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL----------QDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 251 IKDA-LNENSQLQESQKQLLQEaeimkEQVSDLDKQkvtLEESRAQAEQVLSEKETQIESLIKSLLkmKDWAAVLGDDTA 329
Cdd:COG4913 740 EDLArLELRALLEERFAAALGD-----AVERELREN---LEERIDALRARLNRAEEELERAMRAFN--REWPAETADLDA 809
|
....*.
gi 1958781444 330 DDGNLD 335
Cdd:COG4913 810 DLESLP 815
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
207-404 |
8.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 207 ELMADISKRIQSLEdESKSLKSQVAEAKTTFRIFEINEERLR---GAIKDALNEN--SQLQESQKQLLQEAEIMKEQVSD 281
Cdd:COG4913 242 EALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRlwfAQRRLELLEAelEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 282 LDKQKVTLEESRAQAE-QVLSEKETQIESLIKSLLKMKDWAAVLGDDTADdgnLDLDMKSGLEDTASLDNQPKGALkkli 360
Cdd:COG4913 321 LREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA---LGLPLPASAEEFAALRAEAAALL---- 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958781444 361 yaAKLNASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLESKQ 404
Cdd:COG4913 394 --EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
141-523 |
9.00e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 39.50 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 141 GLESSLKEASfEKESTEAQSLEfvEGSQISEAAyeNLERSKSKLEDEilllEKKLEEERVKHSEQDELMADISKRIQSLE 220
Cdd:pfam15964 318 SVRSSLAEAQ-QRESSAYEQVK--QAVQMTEEA--NFEKTKALIQCE----QLKSELERQKERLEKELASQQEKRAQEKE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 221 DESKSLKSQVAEAKTTFRIFEINEERLRGAI----KDALNENSQLQESQKQL-LQEAEIMK---EQVSDLDKQKVTLEES 292
Cdd:pfam15964 389 ALRKEMKKEREELGATMLALSQNVAQLEAQVekvtREKNSLVSQLEEAQKQLaSQEMDVTKvcgEMRYQLNQTKMKKDEA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 293 -------RAQAEQVLSEKETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKSGL---EDTASLDNQPKGALKKLIYA 362
Cdd:pfam15964 469 ekehreyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLgesEHQLHLTRLEKESIQQSFSN 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 363 AKLNASLKALegERNQIYTQlsevdQIKEDLTEHIKSLESKQASLQSENT---EFESESQRLQQKLKVITELYQeNEMKl 439
Cdd:pfam15964 549 EAKAQALQAQ--QREQELTQ-----KMQQMEAQHDKTVNEQYSLLTSQNTfiaKLKEECCTLAKKLEEITQKSR-SEVE- 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 440 hrKLTVEENYRLEKEEKLSKVDERISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAARTLERNLND 519
Cdd:pfam15964 620 --QLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQS 697
|
....
gi 1958781444 520 LRKE 523
Cdd:pfam15964 698 LRSQ 701
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
111-486 |
9.13e-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: 39.77 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 111 EKKLALELSALIEEKCKLLEKVSFVqkeyEGLESSLKEASFEKESTEAQSLEfvegsqiSEAAYENLERSKSKLEDEILL 190
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTL----EALEEGKKRLQRELEALTQQLEE-------KAAAYDKLEKTKNRLQQELDD 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 191 LEkkleeerVKHSEQDELMADISKRIQSLED---ESKSLKSQVAE----AKTTFRIFEINEERLRGAIKDALNENSQLQE 263
Cdd:pfam01576 585 LL-------VDLDHQRQLVSNLEKKQKKFDQmlaEEKAISARYAEerdrAEAEAREKETRALSLARALEEALEAKEELER 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 264 SQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQVLSEKETQIESLIKSLlkmkdwaavlgdDTADDGNLDLD-----M 338
Cdd:pfam01576 658 TNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL------------QATEDAKLRLEvnmqaL 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 339 KSGLE-DTASLDNQPKGALKKLI-----YAAKLN----------ASLKALEGERNQIYTQLSEVDQIKEDLTEHIKSLES 402
Cdd:pfam01576 726 KAQFErDLQARDEQGEEKRRQLVkqvreLEAELEderkqraqavAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQA 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 403 KQASLQSE-------NTEFESESQRLQQKLKVItelyQENEMKLHRKLTVEENYRLEKEEKLSKVDERISHAA------- 468
Cdd:pfam01576 806 QMKDLQREleearasRDEILAQSKESEKKLKNL----EAELLQLQEDLAASERARRQAQQERDELADEIASGAsgksalq 881
|
410
....*....|....*...
gi 1958781444 469 EELETYRQRAKDLEEELE 486
Cdd:pfam01576 882 DEKRRLEARIAQLEEELE 899
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
140-534 |
9.53e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 39.81 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 140 EGLESSLKEASFEKESTEAQSlefvEGSQISEAAYENLERSKSKLEDeilllekkleEERVKHSEQDELMADISKRIQSL 219
Cdd:PTZ00440 390 EKIETLLDSEYFISKYTNIIS----LSEHTLKAAEDVLKENSQKIAD----------YALYSNLEIIEIKKKYDEKINEL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 220 EDESKSLKSQVAEAKTTFRIFEINEERLRGAIKDALnENSQLQESQKQLLQEAEIMKEQVSDLDKQKVTLEESRAQAEQV 299
Cdd:PTZ00440 456 KKSINQLKTLISIMKSFYDLIISEKDSMDSKEKKES-SDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 300 lsekETQIESLIKSLLKMKDWAAVLGDDTADDGNLDLDMKsgledtasldnqpkgalKKLIYAaklnaslkalegerNQI 379
Cdd:PTZ00440 535 ----KNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIK-----------------NKIKYI--------------EEN 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781444 380 YTQLSEVDQIKEDLTEHIKSLESKQASLQSENTEFESESQRLQQKLKVITELYQENEMKLhrkLTVEENYRLEKEEKLSk 459
Cdd:PTZ00440 580 VDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQE---LLDELSHFLDDHKYLY- 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958781444 460 vdeRISHAAEELETYRQRAKDLEEELERTIHSYQGQVISHEKKAHDNWLAAR--TLERNLNDLRKENAHNRQKLTET 534
Cdd:PTZ00440 656 ---HEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKenIIKKQLNNIEQDISNSLNQYTIK 729
|
|
| |
