|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-462 |
2.64e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 166 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 241
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 242 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEAS--LSE 319
Cdd:TIGR02168 751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 320 IKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLEQ 385
Cdd:TIGR02168 829 LERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348626 386 ELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 462
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-479 |
5.65e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 193 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 261
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 262 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 341
Cdd:COG1196 306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 342 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 417
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348626 418 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 479
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-477 |
4.76e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 187 IQHLLSEREEALKqHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklr 266
Cdd:TIGR02168 202 LKSLERQAEKAER-YKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK---------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 267 dtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEK-KSLEDLLSEKQESLEKQ 345
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEElESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 346 INDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVdnnTALVDKL 425
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEE------LEEQLETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRR 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 50348626 426 KRFQQENEELKARMDKH--MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 477
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-465 |
5.15e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 190 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 260
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 261 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLE-D 333
Cdd:TIGR02168 324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEiE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 334 LLSEKQESLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEK 413
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKL-EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 50348626 414 LVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESK 465
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
223-477 |
3.42e-09 |
|
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: 59.70 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKYKMQLQEqfdnlnaahetsKLEIEA 300
Cdd:TIGR02169 170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYQALLKE------------KREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 301 ShseklELL--KKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLK--SEEQKRRAREKanlk 376
Cdd:TIGR02169 226 Y-----ELLkeKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKdlGEEEQLRVKEK---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 377 npqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQE--------NEELKARMDKHMAISRQ 448
Cdd:TIGR02169 296 ---IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDLRAE 372
|
250 260
....*....|....*....|....*....
gi 50348626 449 LSTEQAVLQESLEKESKVNKRLSMENEEL 477
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
241-478 |
9.17e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 241 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEAS 316
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 317 LSEIKKGHEIEkksledLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEI 396
Cdd:COG1196 295 AELARLEQDIA------RLEERRRELEERLEELEEELAELEEELEELEEELEELEE------ELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 397 KNEKLHQQDIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSM 472
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
....*.
gi 50348626 473 ENEELL 478
Cdd:COG1196 443 ALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
181-406 |
7.33e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 181 EALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQaektERENRLKEFYTR 260
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 261 EYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 340
Cdd:COG1196 388 LLEALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----AAEEEAELEEEEEA 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348626 341 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDI 406
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
223-475 |
1.20e-07 |
|
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: 54.59 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 302
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 303 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 382
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 383 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 462
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
250
....*....|...
gi 50348626 463 ESKVNKRLSMENE 475
Cdd:TIGR00618 344 RRLLQTLHSQEIH 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
190-477 |
1.24e-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: 54.69 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 190 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKE---FYTREYEKLR 266
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 267 DTY------IEEAEKYKMQLQEQFDNLNAAHETSKLEIE------ASHSEKLELLKKAYEASLSEIKkghEIEKKSLEdl 334
Cdd:TIGR02169 308 RSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EVDKEFAE-- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 335 LSEKQESLEKQINDLKSENDAL--NEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKme 412
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELkrELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-- 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50348626 413 klvdnntaLVDKLKRFQQENEELKarmdkhmaisrqlsteqavlqeslEKESKVNKRLSMENEEL 477
Cdd:TIGR02169 460 --------LAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-389 |
3.33e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 187 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfVQQHQAEKTERENRLKefytREYEKLR 266
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAE----AELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 267 DTYIEEAEKYKMQLQEQFDNLNA-AHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQ 345
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348626 346 INDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELES 389
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
226-474 |
3.54e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 226 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKL-----EIEA 300
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAALEEFRQKNGLVDLSEEAKLLlqqlsELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 301 SHSEkLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ-ESLEKQINDLKSENDALNEKLKSEeqkrrarekanlkNPQ 379
Cdd:COG3206 227 QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTPN-------------HPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 380 IMYLEQELESLKAvlEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQES 459
Cdd:COG3206 293 VIALRAQIAALRA--QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|....*..
gi 50348626 460 LEK--ESKVNKRLSMEN 474
Cdd:COG3206 371 LQRleEARLAEALTVGN 387
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-476 |
4.95e-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: 52.76 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 163 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 239
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 240 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 319
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 320 IKKghEIEKKSLED--LLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANL 375
Cdd:TIGR02169 817 IEQ--KLNRLTLEKeyLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 376 KNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEELkarmdkhmAISRQLSTEQAV 455
Cdd:TIGR02169 895 EA-QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE--------LSLEDVQAELQR 962
|
330 340
....*....|....*....|.
gi 50348626 456 LQESLEKESKVNKRLSMENEE 476
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEE 983
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
186-506 |
5.64e-07 |
|
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: 52.43 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 186 VIQH--LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KE 256
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 257 FYTREYEKLRD-------TYIEEAEKYKMQLQEQFD----NLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKKGHE 325
Cdd:pfam17380 357 ERKRELERIRQeeiameiSRMRELERLQMERQQKNErvrqELEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 326 IEKKSLED-----LLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKNE 399
Cdd:pfam17380 435 REVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 400 KlhqqdiKLMKMEkLVDNNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAVLQESLEKESKVNKRLsMENEE 476
Cdd:pfam17380 515 R------KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
|
330 340 350
....*....|....*....|....*....|
gi 50348626 477 LLWKLhngdlcsPKRSPTSSAIPLQSPRNS 506
Cdd:pfam17380 587 ARAEY-------EATTPITTIKPIYRPRIS 609
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
147-469 |
1.60e-06 |
|
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: 51.13 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 147 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVNLRGELVTAsttcEKL 225
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEK----EEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 226 EKARNELQTVYEAFVQQHQAEKTERENRLKEfytREYEKLRdTYIEEAEKYKMQLQEQFDNL-NAAHETSKLEIEASHSE 304
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL---KAQEEEL-RALEEELKEEAELLEEEQLLiEQEEKIKEEELEELALE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 305 KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQinDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 384
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 385 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES 464
Cdd:pfam02463 920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
....*
gi 50348626 465 KVNKR 469
Cdd:pfam02463 1000 LEEEK 1004
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
281-431 |
1.99e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.96 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 281 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 358
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348626 359 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 431
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
338-463 |
3.32e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 338 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMK------ 410
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 411 ---------------------------MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE 463
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
195-477 |
8.19e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 195 EEALKQHKTLSQELVNLRGELVTASTTC-EKLEKARNELQtvYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtYIEEA 273
Cdd:pfam05557 44 DRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKK--YLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 274 EKYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLsEKQESLEKQINDLKSEN 353
Cdd:pfam05557 121 QRAELELQSTNSELEELQE--RLDLLKAKASEAEQLRQNLEKQQSSLAE-AEQRIKELEFEI-QSQEQDSEIVKNSKSEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 354 DALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-------------AVLEIKNEKLHQqdiKLMKMEKLVDNNT- 419
Cdd:pfam05557 197 ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyreeaATLELEKEKLEQ---ELQSWVKLAQDTGl 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348626 420 ------ALVDKLKRFQQENEELKARMD------KHMAIS-RQLSTEQAVLQESLEKESKVNKRLSMENEEL 477
Cdd:pfam05557 274 nlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-395 |
8.29e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 151 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 230
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 231 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 307
Cdd:TIGR02168 863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 308 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRRAREKANlknpQIMYL 383
Cdd:TIGR02168 941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKERYDFLTA----QKEDL 1012
|
250
....*....|..
gi 50348626 384 EQELESLKAVLE 395
Cdd:TIGR02168 1013 TEAKETLEEAIE 1024
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-373 |
1.01e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 162 QSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ 241
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 242 QHQAEKTERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKL 306
Cdd:COG4942 98 ELEAQKEELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50348626 307 ELLK--KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 373
Cdd:COG4942 178 ALLAelEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
270-430 |
1.39e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.98 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 270 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 349
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 350 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 404
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
|
170 180
....*....|....*....|....*.
gi 50348626 405 DIKLMKMEKLVDNNTALVDKLKRFQQ 430
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
193-473 |
1.86e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 193 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF---------YTR 260
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 261 EYEKLRDTYIEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEKQE 340
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 341 SLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNT 419
Cdd:pfam07888 217 TLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADASL 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 50348626 420 ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSME 473
Cdd:pfam07888 294 ALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
270-512 |
2.07e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 270 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 349
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 350 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 417
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 418 NTALVDKLKRFQQENEE----LKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDLCSPKRSP 493
Cdd:COG4942 169 LEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAAAERTP 244
|
250
....*....|....*....
gi 50348626 494 TSSAiplqsPRNSGSFPSP 512
Cdd:COG4942 245 AAGF-----AALKGKLPWP 258
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
271-476 |
3.26e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 271 EEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEdLLSEKQESLEKQINDLK 350
Cdd:COG1196 210 EKAERYR-ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 351 SENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEIKNEKL--HQQDIKLMKMEKLVDNNTALVDKLKRF 428
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELAELEEELeeLEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50348626 429 QQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEE 476
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
147-483 |
4.52e-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: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 147 EKTLELTQYKTKCENQSGFILQLK-QLLACGNTKFEALTVVIQHLLSEREEALKQHKT-----------LSQELVNLRGE 214
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkiisqLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 215 LVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREN--------RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDN 286
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 287 LNAAHETSKLEIEASHSE---------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------KQESLEKQINDLKS 351
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 352 ENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVL---EIKNEKLH-QQDIKLMKMEK--LVDNNTALVDK 424
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEkKEKESKISDLEDELNKDDFELkkeNLEKEIDEkNKEIEELKQTQksLKKKQEEKQEL 590
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50348626 425 LKRFQQENEELKARMDKHMAISRQLSTEqavlqesLEKESKVNKRLSMENEELLWKLHN 483
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKE-------LEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
266-477 |
6.55e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 266 RDTYIEEA---EKYKMQLQEQFDNLNAA-----------HETSK----LEIEASHSEKLellkKAYEASLSEIKKG-HEI 326
Cdd:TIGR02168 157 RRAIFEEAagiSKYKERRKETERKLERTrenldrledilNELERqlksLERQAEKAERY----KELKAELRELELAlLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 327 EKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESL-KAVLEIKNEklhQQD 405
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELqKELYALANE---ISR 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348626 406 IKLMKMEkLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 477
Cdd:TIGR02168 300 LEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
187-348 |
7.74e-05 |
|
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: 44.15 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 187 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRLKEFYT-REY 262
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRNnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 263 EKLR------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKghEIEKksledlLS 336
Cdd:COG1579 92 EALQkeieslKRRISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------LE 162
|
170
....*....|..
gi 50348626 337 EKQESLEKQIND 348
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
259-397 |
7.87e-05 |
|
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: 44.62 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 259 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLELLK----KAYEASLSEIKKGHEIEKKSLEDL 334
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEDCDptelDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348626 335 LSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 397
Cdd:smart00787 231 EEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-434 |
1.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 187 IQHLLSEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQHQAEKT--ERENRLKEFYTReyek 264
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSlkKELEKLEELKKK---- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 265 lrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQ 339
Cdd:PRK03918 558 -----LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAF 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 340 ESLEKQINDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIK 407
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKE 712
|
250 260
....*....|....*....|....*..
gi 50348626 408 LMKMEKLVDNNTALVDKLKRFQQENEE 434
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKE 739
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
185-482 |
1.39e-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: 44.96 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 185 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEK 264
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 265 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK 344
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 345 QINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMK-----MEKLV 415
Cdd:pfam02463 322 EKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKlkeeeLELKS 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348626 416 DNNTALVDKLKRFQQENEELKARMDKhmaISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 482
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKE---ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
186-435 |
1.69e-04 |
|
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: 44.57 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 186 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 264
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 265 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 342
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 343 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 417
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
250
....*....|....*...
gi 50348626 418 NTALVDKLKRFQQENEEL 435
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
280-369 |
2.21e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 280 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 348
Cdd:PRK05771 25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104
|
90 100
....*....|....*....|.
gi 50348626 349 LKSENDALNEKLKSEEQKRRA 369
Cdd:PRK05771 105 LEEEISELENEIKELEQEIER 125
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-440 |
2.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 202 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 279
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 280 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 347
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 348 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 419
Cdd:COG4913 770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849
|
250 260
....*....|....*....|.
gi 50348626 420 ALVDKLKRfqqENEELKARMD 440
Cdd:COG4913 850 DLLSKLRR---AIREIKERID 867
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
150-432 |
2.30e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 150 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKA- 228
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQi 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 229 ----------RNELQTVYEAFVQQH-----QAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHET 293
Cdd:pfam05483 537 enleekemnlRDELESVREEFIQKGdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 294 SKLEIEASHSE------------KLEL----LKKAYEASLSEIKKGHEIEKKSLEDLLSEK-------------QESLEK 344
Cdd:pfam05483 617 NKALKKKGSAEnkqlnayeikvnKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVekakaiadeavklQKEIDK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 345 QINDLKSENDALNEKLKSEEQK---RRAREKANLKNPqimylEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTAL 421
Cdd:pfam05483 697 RCQHKIAEMVALMEKHKHQYDKiieERDSELGLYKNK-----EQEQSSAKAALEIELSNIKAE---LLSLKKQLEIEKEE 768
|
330
....*....|.
gi 50348626 422 VDKLKRFQQEN 432
Cdd:pfam05483 769 KEKLKMEAKEN 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-367 |
2.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 195 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 274
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 275 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 354
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|...
gi 50348626 355 ALNEKLKSEEQKR 367
Cdd:COG4913 423 ELEAEIASLERRK 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
191-371 |
2.53e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 191 LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA-----EKTERENRLKEFyTREYEKL 265
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL-PERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 266 RDTY--IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKgheiekksledlLSEKQESLE 343
Cdd:COG4717 152 EERLeeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE------------LEEELEEAQ 219
|
170 180
....*....|....*....|....*...
gi 50348626 344 KQINDLKSENDALNEKLKSEEQKRRARE 371
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKE 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-482 |
2.70e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 187 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEkterenrLKEFYTREYEKLR 266
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE-------LLEEYTAELKRIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 267 DTyIEEAEKYKMQLQEqfdnlnaahETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEdllSEKQESLEK 344
Cdd:PRK03918 466 KE-LKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNLEELEKK---AEEYEKLKE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 345 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKN-EKLHQQDIKLMKMEKLVDNNTALVD 423
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 50348626 424 KLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 482
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
147-462 |
2.90e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 147 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 226
Cdd:pfam10174 363 KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 227 KARNELQTVYEAFvqQHQAEKTERENRlkefytreyeklrdtyiEEAEKYKMQLQEQFDNLNAAHeTSKLEIEAShseKL 306
Cdd:pfam10174 443 EALSEKERIIERL--KEQREREDRERL-----------------EELESLKKENKDLKEKVSALQ-PELTEKESS---LI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 307 ELLKKAYEASLSEIKKGHEIekKSLEDLLSEKQESLEKQINDL-KSENDALNEKLKSE--EQKRRAREKANLKNPQIMYL 383
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKL--KSLEIAVEQKKEECSKLENQLkKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 384 EQELESLKAVL-EIKNEKlHQQDIKLMKMEKL----VDNNTALVDKLKRFQQEN--------EELKARMDKHMAISRQLS 450
Cdd:pfam10174 578 QAEVERLLGILrEVENEK-NDKDKKIAELESLtlrqMKEQNKKVANIKHGQQEMkkkgaqllEEARRREDNLADNSQQLQ 656
|
330
....*....|..
gi 50348626 451 TEQavLQESLEK 462
Cdd:pfam10174 657 LEE--LMGALEK 666
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
223-481 |
3.28e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVyeafvqqhQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASh 302
Cdd:TIGR02169 681 ERLEGLKRELSSL--------QSELRRIENRLDELSQE---------LSDASRKIGEIEKEIEQLEQEEEKLKERLEEL- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 303 seklellkkayEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMY 382
Cdd:TIGR02169 743 -----------EEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 383 LEQELESLKAVLeikNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR-------MDKHMAISRQLSTEQAV 455
Cdd:TIGR02169 810 IEARLREIEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGD 886
|
250 260
....*....|....*....|....*.
gi 50348626 456 LQESLEKESKVNKRLSMENEELLWKL 481
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQI 912
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
260-454 |
3.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 260 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 339
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 340 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 416
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348626 417 NNTAlvDKLKRFQQENEELKARMDKH------MAISRqLSTEQA 454
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHV 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
174-476 |
4.06e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 174 ACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAFVQQHQaektereNR 253
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKIELLLQQHQ-------DR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 254 LKEFYTrEYEKLRDTYIEEAEKYKMQ----------LQEQFDNLNAAHETSKLEIEASHSE---KLELLKKAYEASLSEI 320
Cdd:pfam15921 269 IEQLIS-EHEVEITGLTEKASSARSQansiqsqleiIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYEDKIEEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 321 KK------GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE-EQKRRAREKANLKNPQIMYLEQELESlkav 393
Cdd:pfam15921 348 EKqlvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEkEQNKRLWDRDTGNSITIDHLRRELDD---- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 394 leiKNEKLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEELkarmDKHMAISRQLSTEQAVLQESLEKESKvnKRLSME 473
Cdd:pfam15921 424 ---RNMEVQRLEALLKAMKS--ECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTA--KKMTLE 492
|
...
gi 50348626 474 NEE 476
Cdd:pfam15921 493 SSE 495
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
178-441 |
4.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 178 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKARNELQTVyeafvqqhQAEKTERENRLKEF 257
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------EELEERHELYEEA--------KAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 258 YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAahETSKLEIEASHSEK-LELLKKAYE------ASLSEIKKGHEIEKKS 330
Cdd:PRK03918 382 TGLTPEKLEKE-LEELEKAKEEIEEEISKITA--RIGELKKEIKELKKaIEELKKAKGkcpvcgRELTEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 331 LE--DLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANlknpQIMYLEQELESLKA-VLEIKNEKLHQQDIK 407
Cdd:PRK03918 459 AElkRIEKELKE-IEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLeELEKKAEEYEKLKEK 533
|
250 260 270
....*....|....*....|....*....|....
gi 50348626 408 LMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 441
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
188-461 |
4.09e-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: 43.24 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 188 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqqhqAEKTERENRLKEFYTREYEKLRD 267
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA-----------ARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 268 TYIEEAEKYKMQ-----LQEQFDNLNAAHEtsKLEIEASHSE----KLELLKKAYEASLSEIKKgheiEKKSLEDLLSE- 337
Cdd:pfam01576 91 SQQLQNEKKKMQqhiqdLEEQLDEEEAARQ--KLQLEKVTTEakikKLEEDILLLEDQNSKLSK----ERKLLEERISEf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 338 -----KQESLEKQINDLKSENDA----LNEKLKSEEQKRRAREKANLK--------NPQIMYLEQELESLKAVLEIKNEK 400
Cdd:pfam01576 165 tsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348626 401 LHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLE 461
Cdd:pfam01576 245 LQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
160-483 |
4.35e-04 |
|
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: 43.02 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 160 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 239
Cdd:COG5185 160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 240 VQQhqaEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLSE 319
Cdd:COG5185 236 KGF---QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDIKKAT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 320 IKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 399
Cdd:COG5185 312 ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 400 KLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 479
Cdd:COG5185 392 SLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469
|
....
gi 50348626 480 KLHN 483
Cdd:COG5185 470 DEIN 473
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
188-413 |
5.04e-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: 42.70 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 188 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEklrd 267
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 268 tyIEEAEKYKMQLQEQFDNLNAahetsklEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLE------DLLSEKQES 341
Cdd:TIGR04523 276 --LEQNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiiSQLNEQISQ 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348626 342 LEKQINDLKSENDALNEKLKSEEQKRRAREKANL-KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEK 413
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
326-465 |
5.19e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 326 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE------EQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 399
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEakeeihKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348626 400 KLHQQDIKLMKMEKLVDNNTALVDKLKrfqQENEELKARMDKHMAISRQLSTEQA--VLQESLEKESK 465
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
223-407 |
5.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVYEAFVQQHQAE--KTERENRLKEFYTREYEKLRDTY-----IEEAEKYK---MQLQEQFDNLNAAHE 292
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKaeeLKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 293 TSKLEIEASHSEKL------------ELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDLKSENDalNEK 359
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAE--EDK 1743
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50348626 360 LKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK 407
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
118-349 |
5.67e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 118 ALNAVEKSRQknprsLCIQPQTAPDALPPEktleLTQYKTKCENQSGFILQLKQLLACGN---TKFEALTVVIQHLLSE- 193
Cdd:COG3096 418 AVQALEKARA-----LCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEv 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 194 -REEA-------LKQH---KTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENrLKEFYTREY 262
Cdd:COG3096 489 eRSQAwqtarelLRRYrsqQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 263 EKLRD--TYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIEASH----SEKLELLKKAYEASL---SEIKKG------HEIE 327
Cdd:COG3096 564 AQLEEleEQAAEAVEQRSELRQQLEQLRARIK--ELAARAPAwlaaQDALERLREQSGEALadsQEVTAAmqqlleRERE 641
|
250 260
....*....|....*....|..
gi 50348626 328 KKSLEDLLSEKQESLEKQINDL 349
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
226-469 |
6.20e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 226 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 305
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 306 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRARE-KANLKNPQI 380
Cdd:PTZ00121 1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 381 MYLEQELESLKAVLEIKN--EKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQE 458
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250
....*....|.
gi 50348626 459 SLEKESKVNKR 469
Cdd:PTZ00121 1461 EAKKKAEEAKK 1471
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-478 |
7.85e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 149 TLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLR---GELVTASTTCEKL 225
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilAEDEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 226 EKARNELQTVYEAFVQQHQAEKTEREN---------RLKEFYTREYEKLRdTYIEEAEKYKMQLQEQFD-----NLNAAH 291
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDleiqltaikTSEEHYLKEVEDLK-TELEKEKLKNIELTAHCDkllleNKELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 292 ETSKLEIE-ASHSEKLELLKKAYEASLSEIKKGHEIEKKsLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAR 370
Cdd:pfam05483 507 EASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 371 EKA---------NL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNTALVDKLKRFQQENEE 434
Cdd:pfam05483 586 EKQmkilenkcnNLkkqienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIED 665
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 50348626 435 LKARMDKHMAisrQLSTEQAVLQESLEKESKVNKRLSMENEELL 478
Cdd:pfam05483 666 KKISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
266-478 |
8.86e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 266 RDTYIEEAEKYKMQLQEQFDNLNAAHEtsklEIEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDLlSEKQESLEKQ 345
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQL-RKELEELSRQISALRKDLARL-EAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 346 INDLKSENDALNEKLKSEEQKRrarEKANlknPQIMYLEQELESLKAV--------------LEIKNEKLHQQDIKLMKM 411
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERL---EEAE---EELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348626 412 EKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELL 478
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
237-471 |
9.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 237 EAFVQQHQAEKTERENRLKEFYTREYEKLRDTY-------IEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEKLEL 308
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 309 LKKAYEASLSEIKKGHEIEKKSLEdlLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkanlknpqimyLEQELE 388
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----------LEEELE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 389 SLKAVLEIKNEKLHQQDIKLMKMEklvdNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQE-SLEKESKVN 467
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEyREERLPPVL 518
|
....
gi 50348626 468 KRLS 471
Cdd:COG4717 519 ERAS 522
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
295-404 |
9.72e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 295 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 370
Cdd:COG0542 403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
|
90 100 110
....*....|....*....|....*....|....
gi 50348626 371 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQ 404
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
246-366 |
1.09e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 246 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 320
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50348626 321 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 366
Cdd:PRK00409 599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
270-392 |
1.22e-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: 40.68 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 270 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEA--SHSEKLELLKKAYEASLSEIKK-------GHEIE-----KKSLEDLL 335
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRleLEIEEVEARIKKYEEQLGNVRNnkeyealQKEIEslkrrISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 336 SE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKAnlknpqimyLEQELESLKA 392
Cdd:COG1579 113 LElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAE---------LEAELEELEA 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
179-462 |
1.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 179 KFEALTVVIQHLLSERE----EALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqQHQAEKTERENRL 254
Cdd:PRK03918 183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIE--------ELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 255 KefytREYEKLRDT--YIEEAEKYKMQLQEQfdnlnaAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIekksle 332
Cdd:PRK03918 255 R----KLEEKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 333 dlLSEKQESLEKQINDLKSENDALNEKLKSEEqkrrarekanlknpqimyleqELESLKAVLEIKNEKLHQQDIKLMKME 412
Cdd:PRK03918 319 --LEEEINGIEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50348626 413 KLVDNNTA-----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 462
Cdd:PRK03918 376 RLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
157-408 |
2.03e-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: 40.98 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 157 TKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQhktLSQELVNLRGELVtasttcEKLEKARNELQTVY 236
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 237 EAfVQQHQAEKTERENRLKEFYTREYEKLR---------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 307
Cdd:pfam12128 315 AA-VAKDRSELEALEDQHGAFLDADIETAAadqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 308 LLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE--------------EQKR------ 367
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLEnfderi 473
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 50348626 368 -RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKL 408
Cdd:pfam12128 474 eRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-409 |
2.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVYEAFvQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE-AS 301
Cdd:COG4717 74 KELEEELKEAEEKEEEY-AELQEELEELEEELEELEAE---------LEELREELEKLEKLLQLLPLYQELEALEAElAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 302 HSEKLELLKKAYEA------SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanl 375
Cdd:COG4717 144 LPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--- 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 50348626 376 knpQIMYLEQELESLKAVLEI--KNEKLHQQDIKLM 409
Cdd:COG4717 221 ---ELEELEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-471 |
2.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 193 EREEALKQHKtlsQELVNLRGELVTASttcEKLEKARNELQTVYEAFVQQhqaEKTERENRLKEFYTREYEKLRDTYIEE 272
Cdd:PRK03918 449 HRKELLEEYT---AELKRIEKELKEIE---EKERKLRKELRELEKVLKKE---SELIKLKELAEQLKELEEKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 273 AEKYKmqlqEQFDNLNAAHETSKLEIE--ASHSEKLELLKKAYEASLSEIKKGHEiEKKSLEDLLSEK----QESLEKQI 346
Cdd:PRK03918 520 LEKKA----EEYEKLKEKLIKLKGEIKslKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELgfesVEELEERL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 347 NDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLM--KMEKLVDNNTALVDK 424
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEELREEYLELSRE 674
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 50348626 425 LKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 471
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
270-413 |
2.41e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 270 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 349
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348626 350 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 413
Cdd:PRK00409 572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-462 |
2.63e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 193 EREEALKQHKTLSQELVNLRG-------ELVTASTTCEKLEKARNELQTVYEAfVQQHQAEKTERENRLKEFYTREyEKL 265
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAqlakkeeELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKA-EKQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 266 RDTYIEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEK-LELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE--- 340
Cdd:pfam01576 294 RRDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRnka 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 341 SLEKQINDLKSENDALNEKL------KSEEQKRRAREKANLKNPQIMY----------------LEQELESLKAVL---E 395
Cdd:pfam01576 374 NLEKAKQALESENAELQAELrtlqqaKQDSEHKRKKLEGQLQELQARLseserqraelaeklskLQSELESVSSLLneaE 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50348626 396 IKNEKLHQQ----DIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHM----AISRQLSTEQAVLQESLEK 462
Cdd:pfam01576 454 GKNIKLSKDvsslESQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEeakrNVERQLSTLQAQLSDMKKK 532
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-481 |
3.32e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 331 LEDLLSEkqesLEKQINDLKSE-NDALN-EKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKL 408
Cdd:COG1196 191 LEDILGE----LERQLEPLERQaEKAERyRELKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348626 409 MKMEKLVDNNTAlvdKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKL 481
Cdd:COG1196 263 AELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
304-470 |
3.83e-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: 39.14 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 304 EKLELLKK--AYEASLSEIK---KGHEIEKKSLEDLLSEKQESLEK---QINDLKSENDALNEKLKSEEQKR-RAREK-A 373
Cdd:COG1579 4 EDLRALLDlqELDSELDRLEhrlKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkKYEEQlG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 374 NLKNP-QIMYLEQELESLKAVLEIKNEKLHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKhmAISRQLSTE 452
Cdd:COG1579 84 NVRNNkEYEALQKEIESLKRRISDLEDEILE---LMERIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAEL 158
|
170
....*....|....*...
gi 50348626 453 QAVLQESLEKESKVNKRL 470
Cdd:COG1579 159 EELEAEREELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
191-463 |
4.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 191 LSEREEALKQHKTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYI 270
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKA----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 271 EEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLK 350
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE-EAKKAEEDKKKAEEAK 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 351 SENDalNEKLKSEEQKRRAREKANLKNPQimylEQELESLKAVLEIKNEKlHQQDIKLMKMEKLVDNNTALVDKLKRFQQ 430
Cdd:PTZ00121 1682 KAEE--DEKKAAEALKKEAEEAKKAEELK----KKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
250 260 270
....*....|....*....|....*....|....
gi 50348626 431 ENEELKARMDKHMAISRQLSTE-QAVLQESLEKE 463
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEkEAVIEEELDEE 1788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-403 |
4.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVY--EAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLnaAHETSKLEIEA 300
Cdd:COG4717 49 ERLEKEADELFKPQgrKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEEL--REELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 301 SHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEK--LKSEEQKRRAREKANLK 376
Cdd:COG4717 126 QLLPLYQELEAL-EAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEEL 204
|
170 180
....*....|....*....|....*..
gi 50348626 377 NPQIMYLEQELESLKAVLEIKNEKLHQ 403
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
224-477 |
4.64e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 224 KLEKARNELQTVYEAFVQQHQAEKTERENR---LKEFYTREYEKLRDTYIEEaeKYKMQLQEQFDNLNAAHETSKLEIEA 300
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKaevLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 301 SHSEKLELLKKAYEASLSEIKKgheiekkSLEDLLSEKqeslekqiNDLKSENDALNEKLKSEEQKRRAREKANLKNPQI 380
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKK-------SLSSDLIEN--------LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 381 MYLEQELESLKAVLEIKNEKLHQQDI-------KLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK---HMAISRQLS 450
Cdd:COG5022 957 NKLHEVESKLKETSEEYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaeLQSASKIIS 1036
|
250 260
....*....|....*....|....*..
gi 50348626 451 TEQAVLQeSLEKESKVNKRLSMENEEL 477
Cdd:COG5022 1037 SESTELS-ILKPLQKLKGLLLLENNQL 1062
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
309-477 |
5.22e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 309 LKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE--SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLE- 384
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 385 -QELESLKAVLEIKNEKLHQQDIKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMAiSRQLSTEQAvLQESLEKE 463
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELR-------ELEEELEELEAELAELQEELEELLE-QLSLATEEE-LQDLAEEL 201
|
170
....*....|....
gi 50348626 464 SKVNKRLSMENEEL 477
Cdd:COG4717 202 EELQQRLAELEEEL 215
|
|
| Snf7 |
pfam03357 |
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ... |
332-481 |
5.27e-03 |
|
Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.
Pssm-ID: 460896 [Multi-domain] Cd Length: 168 Bit Score: 37.99 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 332 EDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLE-IKNEKLHQQDIKLMK 410
Cdd:pfam03357 10 IRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEK-QLDQLDGQLSNLEQQRMaIENAKSNQEVLNAMK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 411 --------MEKLVDnntalVDKLKRFQQENEELKARMD-KHMAISRQLSTEQAVLQESLEKEskVNKRLSMENEELLWKL 481
Cdd:pfam03357 89 qgakamkaMNKLMD-----IDKIDKLMDEIEDQMEKADeISEMLSDPLDDADEEDEEELDAE--LDALLDEIGDEESVEL 161
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
316-403 |
5.40e-03 |
|
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13); Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain.
Pssm-ID: 381623 Cd Length: 290 Bit Score: 38.86 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 316 SLSEIKK-GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK--A 392
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 50348626 393 VLEIKNEKLHQ 403
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
223-470 |
5.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 223 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASH 302
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 303 SEklELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRA---REKANLKNPQ 379
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 380 IMYLEQELESLKAVLEIKNEKLHQQD--IKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHmaisrqlSTEQAVLQ 457
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-------AEEAKIKA 1622
|
250
....*....|...
gi 50348626 458 ESLEKESKVNKRL 470
Cdd:PTZ00121 1623 EELKKAEEEKKKV 1635
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
225-391 |
6.56e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 38.75 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 225 LEKARNELQTVYEAFVQQHQAEkterENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHET----------- 293
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAE----PSRLYSLYEKEIEDLRRQ-LDTLTVERARLQLELDNLRLAAEDfrqkyedelnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 294 --------------------SKLEIEA---SHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLK 350
Cdd:pfam00038 98 rtsaendlvglrkdldeatlARVDLEAkieSLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLD-LTSALAEIR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348626 351 SENDALNEKLKSE--------------------EQKRRAREKANLKNPQIMYLEQELESLK 391
Cdd:pfam00038 177 AQYEEIAAKNREEaeewyqskleelqqaaarngDALRSAKEEITELRRTIQSLEIELQSLK 237
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
239-404 |
6.75e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.18 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 239 FVQQHQAEKTERENrLKEFYTREYEKLRDTyieeaEKYKMQLQEQFDNLNAAHETSKLE------IEASHSEKLELLKKA 312
Cdd:pfam17078 43 FLENLASLKHENDN-LSSMLNRKERRLKDL-----EDQLSELKNSYEELTESNKQLKKRlenssaSETTLEAELERLQIQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348626 313 YEASLSEIK--KGH---EIE--KKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkaNLKNPQIMYLEQ 385
Cdd:pfam17078 117 YDALVDSQNeyKDHyqqEINtlQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLD--NIYVNKNNKLLT 194
|
170 180
....*....|....*....|
gi 50348626 386 ELESLKAVLEIKN-EKLHQQ 404
Cdd:pfam17078 195 KLDSLAQLLDLPSwLNLYPE 214
|
|
| |
