|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-388 |
3.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 65 SEKALELAQYKSKcTKQSGIILQLKQLLSLgNTKFEALTVVAQHLLSEREEALKQNKTLSQELVNLRGELvtvsttcEKL 144
Cdd:TIGR02168 209 AEKAERYKELKAE-LRELELALLVLRLEEL-REELEELQEELKEAEEELEELTAELQELEEKLEELRLEV-------SEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 145 EKARNELQIAYEGFVQKLN------QQHQTDLTELENRLKEfYTGECEKLQNiYIEEAEKYKTQLQEQFDNLNATHETSK 218
Cdd:TIGR02168 280 EEEIEELQKELYALANEISrleqqkQILRERLANLERQLEE-LEAQLEELES-KLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 219 LKIEASHSEKIEL---LKKAYENSLSEIKKSHEMEKKslEDLLYEKQESLEKQISDLKSENDTLNEKLKSEEQKRISREK 295
Cdd:TIGR02168 358 AELEELEAELEELesrLEELEEQLETLRSKVAQLELQ--IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 296 ANL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQENEELKARMDKHMAIS 369
Cdd:TIGR02168 436 KELqaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
330
....*....|....*....
gi 122133619 370 RQLSTEQAVLQESLEKESK 388
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-400 |
3.64e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 115 EALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYegfVQKLNQQHQTDLTELENRLKEFytgeceklqNIYIE 194
Cdd:TIGR02168 210 EKAERYKELKAELRELELALLVLRLEELREELEELQEELKE---AEEELEELTAELQELEEKLEEL---------RLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 195 EAEKYKTQLQEQFDNLNATHETSKLKIEAsHSEKIELLkkayENSLSEIKKSHEMEKKSLEDLLYEKQEsLEKQISDLKS 274
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQI-LRERLANL----ERQLEELEAQLEELESKLDELAEELAE-LEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 275 ENDTLNEKLKSEEQKRISREKANLKnpqimyLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVdsnTALVDRLKRFQQE 354
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEE------LEEQLETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRRERLQQE 422
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 122133619 355 NEELKARMDKH--MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 400
Cdd:TIGR02168 423 IEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-400 |
4.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 112 EREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEgfvqKLNQQHQTDLTELENRLKEFY--TGECEKLQ 189
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYelLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 190 NIYIEEAEKyKTQLQEQFDNLNATHETSKLKIEASHSEKIELlkkayENSLSEIKKSHEMEKKSLEDLLYEKQESLEKQI 269
Cdd:COG1196 302 QDIARLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 270 SDLKSENDTLNEKLksEEQKRISREKANLKNPQimylEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLK 349
Cdd:COG1196 376 EAEEELEELAEELL--EALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 122133619 350 RFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 400
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-400 |
1.89e-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: 53.92 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 107 QHLLSEREEA-----LKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEGFVQKLNQ--------------QHQ 167
Cdd:TIGR02169 214 QALLKEKREYegyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlgeeeqlRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 168 TDLTELENRLKEFYTGECEKLQNIyiEEAEKYKTQLQEQFDNLNATHETSKLKIEASHSEKIEL------LKKAYENSLS 241
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKEREL--EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyaeLKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 242 EIKkshEMEKKSLEdlLYEKQESLEKQISDLKSENDTL--NEKLKSEEQKRISREKANLKNpQIMYLEQELESLKAVLEI 319
Cdd:TIGR02169 372 ELE---EVDKEFAE--TRDELKDYREKLEKLKREINELkrELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 320 KNEKLHQQDVKLMKmeklvdsntalvdrlkrfqqeneelkarmdkhmaISRQLSTEQAVLQESLEKESKVNKRLSMENEE 399
Cdd:TIGR02169 446 KALEIKKQEWKLEQ----------------------------------LAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
.
gi 122133619 400 L 400
Cdd:TIGR02169 492 L 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-409 |
4.49e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 194 EEAEKYKtQLQEQFDNLNATHETSKLKIEASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQEsLEKQISDLK 273
Cdd:TIGR02168 210 EKAERYK-ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 274 SENDTLNEKL-KSEEQKRISREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSntaLVDRLKRFQ 352
Cdd:TIGR02168 288 KELYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES---LEAELEELE 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122133619 353 QENEELKARMDKHMAISRQLSTEQAVLQESLEK--------ESKVN------KRLSMENEELLWKLHNGNL 409
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASlnneierlEARLErledrrERLQQEIEELLKKLEEAEL 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-402 |
5.92e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 65 SEKALELAQYKSKcTKQSGIILQLKQLLSLgNTKFEALTVVAQHLLSEREEALKQNKTLSQELVNLRGELvtvsttcEKL 144
Cdd:COG1196 209 AEKAERYRELKEE-LKELEAELLLLKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLEL-------EEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 145 EKARNELQIAYegfvqklnQQHQTDLTELENRLKEfytgECEKLQNIY--IEEAEKYKTQLQEQFDNLNATHETSKLKIE 222
Cdd:COG1196 280 ELELEEAQAEE--------YELLAELARLEQDIAR----LEERRRELEerLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 223 ASHSEKIELLKKAYENSLSEIKKSHEM-EKKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSEEQKRISREKAnlknp 301
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE----- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 302 QIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAVLQE 381
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340
....*....|....*....|.
gi 122133619 382 SLEKESKVNKRLSMENEELLW 402
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-400 |
1.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 142 EKLEKARNELQiayegfvqklnqqhqtdltELENRLKEFYTGECEKLQNIYIEEAEKYKtqlQEQFDNLNATHETSKLKI 221
Cdd:TIGR02169 170 RKKEKALEELE-------------------EVEENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 222 EASHSEKIELLKKAYENSLSEIkkshEMEKKSLEDLLYEKQESLEKQISDLKSENDTLnEKLKSEEQKRISREkanlknp 301
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLEEIEQLLEELNKKI-KDLGEEEQLRVKEK------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 302 qIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQE--------NEELKARMDKHMAISRQLS 373
Cdd:TIGR02169 296 -IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDLRAELE 374
|
250 260
....*....|....*....|....*..
gi 122133619 374 TEQAVLQESLEKESKVNKRLSMENEEL 400
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-401 |
2.21e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 110 LSEREEALKQNK-TLSQELVNLRGEL----VTVSTTCEKLEKARNELQI--AYEGFVQKLNQQHQTDLTELENRLKEfYT 182
Cdd:TIGR02169 679 LRERLEGLKRELsSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQleQEEEKLKERLEELEEDLSSLEQEIEN-VK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 183 GECEKLqNIYIEEAEKYKTQLQEQFDNLNATHETSKLKIEASHSEKIELLKKAYENSLSEIkkshemeKKSLEDLLYEKq 262
Cdd:TIGR02169 758 SELKEL-EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-------EQKLNRLTLEK- 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 263 ESLEKQISDLKSENDTLNEKLKSEEQkrisrekanlknpQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSnt 342
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEK-------------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-- 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 122133619 343 aLVDRLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELL 401
Cdd:TIGR02169 894 -LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-358 |
6.12e-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: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 85 ILQLKQLLSLGNTKFEALTVVAQHLLSEREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEGFVQKLNQ 164
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 165 QHQtDLTELENRLKEF-------------YTGECEKLQNIyIEEAEKYKTQLQEQFDNLNATHETSKLKIEASHSEKIEL 231
Cdd:TIGR02168 766 LEE-RLEEAEEELAEAeaeieeleaqieqLKEELKALREA-LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 232 LKKAYENSLSEIKKSHEMEK------------KSLEDLLYEKQESLEKQISDLKSENDTLNEKlksEEQKRISREKANLK 299
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEEleelieeleselEALLNERASLEEALALLRSELEELSEELREL---ESKRSELRRELEEL 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122133619 300 NPQIMYLEQELESLKAVLEIKNEKLHQQ-----DVKLMKMEKLVDSNTALVDRLKRFQQENEEL 358
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEysltlEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
261-386 |
2.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 261 KQESLEKQISDLKSENDTLNEKLKS--EEQKRISREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDVKLMK----- 333
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAlqAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGEraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 334 ----------------------------MEKLVDSNTALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 385
Cdd:COG3883 96 yrsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
.
gi 122133619 386 E 386
Cdd:COG3883 176 Q 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-394 |
3.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 112 EREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEgfvqklnqqhqtdLTELENRLKEFYTGECEKlqni 191
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-------------LKELEEKLKKYNLEELEK---- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 192 yieEAEKYKTqLQEQFDNLNAthETSKLKIEASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQESLEKQISD 271
Cdd:PRK03918 523 ---KAEEYEK-LKEKLIKLKG--EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 272 LKSENDTLNEKLKSEEQKRISREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLM--KMEKLVDSNTALVDRLK 349
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEELREEYLELSRELA 676
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 122133619 350 RFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 394
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-400 |
3.76e-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: 46.20 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 124 SQELVNLRGELVTVSTTCEKLEKARNELqiayegfvqklnqqhQTDLTELENRLKEFYTGECEKLQNIyieeaekykTQL 203
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAEL---------------RKELEELEEELEQLRKELEELSRQI---------SAL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 204 QEQFDNLNATHETSKLKIEASHSEKIELlkKAYENSLSEIKKSHEMEKKSLEdllyEKQESLEKQISDLKSENDTLNEKL 283
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAE----AEIEELEAQIEQLKEELKALREAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 284 kSEEQKRISREKANLKNPQIMYleQELESLKAVLEIKNEKLHQQ-DVKLMKMEKLVDSNTALVDRLKRFQQENEELKARM 362
Cdd:TIGR02168 806 -DELRAELTLLNEEAANLRERL--ESLERRIAATERRLEDLEEQiEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270
....*....|....*....|....*....|....*...
gi 122133619 363 DKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 400
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
63-392 |
4.05e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 63 LSSEKALELAQYKSKCTKQSGIILQLKQLLSLGNTKFEALTVVAQHLLSEREEALKQNKT-LSQELVNLRGELVT--VST 139
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEkeEEK 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 140 TCEKLEKARNELQIAYEGfVQKLNQQHQTDLTELENRLKEfytgeceklqniyIEEAEKYKTQLQEQFDNL-NATHETSK 218
Cdd:pfam02463 767 SELSLKEKELAEEREKTE-KLKVEEEKEEKLKAQEEELRA-------------LEEELKEEAELLEEEQLLiEQEEKIKE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 219 LKIEASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQESLEKQisDLKSENDTLNEKLKSEEQKRISREKANL 298
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 299 KNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAV 378
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
330
....*....|....
gi 122133619 379 LQESLEKESKVNKR 392
Cdd:pfam02463 991 NKDELEKERLEEEK 1004
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
63-320 |
7.03e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 63 LSSEKALELAQYKSKCtkqSGIILQLKQLLSLGNTKFEALTVVAqhlLSEREEALKQnktLSQELVNLRGELvtvsttcE 142
Cdd:PRK05771 40 LSNERLRKLRSLLTKL---SEALDKLRSYLPKLNPLREEKKKVS---VKSLEELIKD---VEEELEKIEKEI-------K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 143 KLEKARNELQiayegfvqklnqqhqTDLTELENRLKEfytgeCEKLQNIYIEEAEKYKTQL---------QEQFDNLNAT 213
Cdd:PRK05771 104 ELEEEISELE---------------NEIKELEQEIER-----LEPWGNFDLDLSLLLGFKYvsvfvgtvpEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 214 HETSKLKIEASHSEKIEL----LKKAYENSLSEIKKsHEMEKKSLED--LLYEKQESLEKQISDLKSENDTLNEKLKSee 287
Cdd:PRK05771 164 SDVENVEYISTDKGYVYVvvvvLKELSDEVEEELKK-LGFERLELEEegTPSELIREIKEELEEIEKERESLLEELKE-- 240
|
250 260 270
....*....|....*....|....*....|...
gi 122133619 288 qkrISREKANLKNPQIMYLEQELESLKAVLEIK 320
Cdd:PRK05771 241 ---LAKKYLEELLALYEYLEIELERAEALSKFL 270
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-364 |
9.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 112 EREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAyegfvQKLNQQHQTDLTELENRLKEFytgecEKlqni 191
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL-----EKELESLEGSKRKLEEKIREL-----EE---- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 192 YIEEAEKYKTQLQEQFDNLNathetsKLKIEASHSEKIELLKKAYENSLSEIKKshemEKKSLEDLLyekqESLEKQISD 271
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELK------ELKEKAEEYIKLSEFYEEYLDELREIEK----RLSRLEEEI----NGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 272 LKSENDTLNE--KLKSEEQKRISR-EKANLKNPQIMYLEQELESLKAVLEIKN-EKLHQQDVKLMKM-EKLVDSNTALVD 346
Cdd:PRK03918 333 LEEKEERLEElkKKLKELEKRLEElEERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAkEEIEEEISKITA 412
|
250
....*....|....*...
gi 122133619 347 RLKRFQQENEELKARMDK 364
Cdd:PRK03918 413 RIGELKKEIKELKKAIEE 430
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
89-401 |
1.63e-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: 44.33 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 89 KQLLSLGNTKFEALTVVAQHLLSEREE--ALKQNKTLS-QELVNLRGELVTVSTTCEKLEKARNELQiAYEGFVQKLNQQ 165
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELK-GKEQELIFLLQA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 166 HQTDLTELENRLKEFYTGEceklqNIYIEEAEKYKTQLQEQ---------------FDNLNATHETSKLKIE-ASHSEKI 229
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSE-----EHYLKEVEDLKTELEKEklknieltahcdkllLENKELTQEASDMTLElKKHQEDI 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 230 ELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQEsLEKQISDLKSENDTLNEKLKSEEQKRISREKANL----------- 298
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREE-FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenkcnnlkk 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 299 ----KNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKME-KLVDSNTALVDRLKRFQQENEELKARMDKHMAisrQLS 373
Cdd:pfam05483 602 qienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKISEEKLLE---EVE 678
|
330 340
....*....|....*....|....*...
gi 122133619 374 TEQAVLQESLEKESKVNKRLSMENEELL 401
Cdd:pfam05483 679 KAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
217-329 |
3.21e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 217 SKLKIEASHS-EKIELLKKAyensLSEIKKSHEMEKKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSE----EQKRI 291
Cdd:COG0542 400 ARVRMEIDSKpEELDELERR----LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQE 475
|
90 100 110
....*....|....*....|....*....|....*...
gi 122133619 292 SREKANLKNPQIMYLEQELESLKAVLEiKNEKLHQQDV 329
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELA-ELAPLLREEV 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
144-439 |
3.23e-04 |
|
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: 43.19 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 144 LEKARNELQIAYEGFVQKLNQQHQTDLTELENRLKEFYTGECEKLQN-----IYIEEAEKYKTQLQE-QFDNLNATHETS 217
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKnervrQELEAARKVKILEEErQRKIQQQKVEME 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 218 KLKIEASHSEKIELLKKayenslsEIKKSHEMEKKSLEDLlyEKQESLEKQISDlksENDTLNEKLKSEEQKRisrEKAN 297
Cdd:pfam17380 424 QIRAEQEEARQREVRRL-------EEERAREMERVRLEEQ--ERQQQVERLRQQ---EEERKRKKLELEKEKR---DRKR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 298 LKNPQIMYLEQELESLK-AVLEIKNEKlhqqdvKLMKMEkLVDSNTALVDRLKRFQQENEELKAR-MDKHMAISRQL--S 373
Cdd:pfam17380 489 AEEQRRKILEKELEERKqAMIEEERKR------KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkA 561
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122133619 374 TEQAVLQESLEKESKVNKRLsMENEELLWKLhngnlcsPKRSPTSPAAPFQSPRNSGSFPSPSISH 439
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQI-VESEKARAEY-------EATTPITTIKPIYRPRISEYQPPDVESH 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-329 |
3.52e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 65 SEKALELAQYKSKCTKQSGIILQLKQLLSLGNTKFEALTVVAQHLLSEREEALKQNKTLSQELVNLRGELVTVSTTCEKL 144
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 145 EKARNELQIAYEGFVQKLNQQHQTDLTELENRLKEFytgecEKLQNIYIEEAEKYKTQLQE--QFDNLNATHETSKLKIE 222
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-----EELEELAEELLEALRAAAELaaQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 223 ASHSEKIELLKKAYENSLSEIK-KSHEMEKKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSEEQKRIS-REKANLKN 300
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLLL 497
|
250 260
....*....|....*....|....*....
gi 122133619 301 PQIMYLEQELESLKAVLEIKNEKLHQQDV 329
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
145-289 |
5.57e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 145 EKARNElqiaYEGFVQKLNQQHQtDLTELENRLKEFYTgECEKLqniyIEEAEKYKTQLQEQFDNLNATHETSKLKIEAS 224
Cdd:PRK00409 505 EEAKKL----IGEDKEKLNELIA-SLEELERELEQKAE-EAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122133619 225 HSEKIELLKKAYENSLSEIKKSHEMEKKSLED--------LLYEKQESLEKQISDLKSENDTLNE----KLKSEEQK 289
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVKAheliearkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-384 |
6.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 202 QLQEQFDNLNATHETSK---------LKIEASHSEKIELLKKAyeNSLSEIKKSHEMEKKSLE-DLLYEKQESLEKQISD 271
Cdd:COG4913 229 ALVEHFDDLERAHEALEdareqiellEPIRELAERYAAARERL--AELEYLRAALRLWFAQRRlELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 272 LKSENDTLNEKLKSEEQKR--ISREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKM--------EKLVDSN 341
Cdd:COG4913 307 LEAELERLEARLDALREELdeLEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaEEFAALR 386
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 122133619 342 TALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLE 384
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
112-396 |
8.94e-04 |
|
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: 41.80 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 112 EREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEGFVQ------KLNQQHQTDLTELENRLKEFYTGEC 185
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEekdallAQRAAHEARIRELEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 186 EKLQNI--YIEEAEKYKTQLQEQfdnlNATHETSKLKIEASHSEKIELLKKayensLSEIKKSHEMEKKSLEDLlyekQE 263
Cdd:pfam07888 147 ERETELerMKERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKE-----FQELRNSLAQRDTQVLQL----QD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 264 SLEKQISDLKSENDTLNEKLKSEEQKRISREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKME-KLVDSNT 342
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADASL 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 122133619 343 ALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSME 396
Cdd:pfam07888 294 ALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
239-326 |
1.02e-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: 40.78 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 239 SLSEIKK-SHEMEKKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSEEQKRISREKANLKNPQIMYLEQELESLK--A 315
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 122133619 316 VLEIKNEKLHQ 326
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
85-364 |
2.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 85 ILQLKQLLSLGNTKFEALTVVAQHLLSEREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARnelqiayegfvqklnq 164
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK---------------- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 165 QHQTDLTELENRLKEFYTGECEKLqniyIEEAEKYKTQLQEQFDNLNAthETSKLKIEASHSEK-IELLKKAYE------ 237
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKE----LEELEKAKEEIEEEISKITA--RIGELKKEIKELKKaIEELKKAKGkcpvcg 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 238 NSLSEIKKSHEMEKKSLE--DLLYEKQEsLEKQISDLKSENDTLNEKLKSEeqKRISREKANLKnpQIMYLEQELESLKA 315
Cdd:PRK03918 443 RELTEEHRKELLEEYTAElkRIEKELKE-IEEKERKLRKELRELEKVLKKE--SELIKLKELAE--QLKELEEKLKKYNL 517
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 122133619 316 -VLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQENEELKARMDK 364
Cdd:PRK03918 518 eELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
204-354 |
2.15e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 204 QEQFDNLNA--THETSKLKIEASHSEKIELLKKAYENSLSeikkSHEMEKKSLEDLLYEkqesLEKQISDLKSENDTLNE 281
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLS----AAEAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 282 KLKSEEQkrISREKAN---LKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKM-EKLvdsNTALVDR---LKRFQQE 354
Cdd:PRK09039 124 ELDSEKQ--VSARALAqveLLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
112-405 |
2.38e-03 |
|
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: 40.73 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 112 EREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEGFVQKLNQQHQTDLTELENRLKEFYTgECEKLQNI 191
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID-LLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 192 YIEEAEKYKTQLQEQFDNLNATHETSKLKIEASHSEKIELLKKAYENSLSEIKKSH-EMEKKSLEDLLYEKQESLEKQIS 270
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKlERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 271 DLKSENDTLNEKLKSEEQKRISREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQ------DVKLMKMEKLVDSNTAL 344
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlssaakLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122133619 345 vDRLKRFQQENEELKARMDKhmaISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 405
Cdd:pfam02463 409 -LLLELARQLEDLLKEEKKE---ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
223-393 |
2.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 223 ASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLlyekqESLEKQISDLKSENDTLNEKLKSEEQK--RISREKANLKN 300
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-----AALERRIAALARRIRALEQELAALEAElaELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 301 pQIMYLEQELESLKAVLEIKNEK------LHQQDVK-----LMKMEKLVDSNTALVDRLKRFQQENEELKARMDKHMAIS 369
Cdd:COG4942 98 -ELEAQKEELAELLRALYRLGRQpplallLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180
....*....|....*....|....
gi 122133619 370 RQLSTEQAVLQESLEKESKVNKRL 393
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKL 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
87-282 |
2.47e-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: 39.52 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 87 QLKQLLSLgntkfealtvvaQHLLSEREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYegfvqklnQQH 166
Cdd:COG1579 5 DLRALLDL------------QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------KRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 167 QTDLTELENRLKefytgeceklqniyieeaeKYKTQLQEQFDN--LNA-THETSKLKIEASHSEKIELLKKAYENSLSEI 243
Cdd:COG1579 65 ELEIEEVEARIK-------------------KYEEQLGNVRNNkeYEAlQKEIESLKRRISDLEDEILELMERIEELEEE 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 122133619 244 KKSHEMEKKSLEDLLYEKQESLEKQISDLKSENDTLNEK 282
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-398 |
2.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 193 IEEAEKYKTQLQEQFDNLNATHetSKLKIEASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQESLEKqisdL 272
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----L 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 273 KSENDTLNEKLKSEEQKRISREKanlknpqimylEQELESLKAVLEIKNEKLHQQdvklMKMEKLVDSNTALVDRLKRFQ 352
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 122133619 353 QENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENE 398
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
237-404 |
2.81e-03 |
|
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: 40.44 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 237 ENSLSEIKKSHEMEKKSLEDLLyEKQESLEKQISDLKSENDTLNEKL------KSEEQKRISREKANLKNPQIMYLEQEL 310
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELKELEARIeeleedLHKLEEALNDLEARLSHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 311 ESLKAV----------LEIKNEKLHQQDVKLMK-MEKLVDSNTALVDRLKRFQQENEELKAR-------MDKHMAISRQL 372
Cdd:TIGR02169 801 SKLEEEvsriearlreIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDL 880
|
170 180 190
....*....|....*....|....*....|..
gi 122133619 373 STEQAVLQESLEKESKVNKRLSMENEELLWKL 404
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
110-400 |
2.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 110 LSEREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEgfvqklnqqhqtDLTELENRLKEFyTGECEKLQ 189
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK------------ELEEKEERLEEL-KKKLKELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 190 NIYIEEAEKYKT-----QLQEQFDNLNATHE-TSKLKIEashsEKIELLKKAYENSLSEIKKSHEMeKKSLEdllyEKQE 263
Cdd:PRK03918 352 KRLEELEERHELyeeakAKKEELERLKKRLTgLTPEKLE----KELEELEKAKEEIEEEISKITAR-IGELK----KEIK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 264 SLEKQISDLKS---ENDTLNEKLKSEEQKRISRE-KANLKN--PQIMYLEQELESLKAVLEiKNEKLHQQDVKLMKMEKL 337
Cdd:PRK03918 423 ELKKAIEELKKakgKCPVCGRELTEEHRKELLEEyTAELKRieKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKEL 501
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122133619 338 VDSNTALVDRLKRFQQENEELKAR-MDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 400
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
201-290 |
3.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 201 TQLQE----QFDNLNATHETSKLKIEASH----SEKIELLKKAYENSLSEIKKSHEMEKKSLEDLL---YEKQESLEKQI 269
Cdd:PRK05771 23 EALHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIkdvEEELEKIEKEI 102
|
90 100
....*....|....*....|.
gi 122133619 270 SDLKSENDTLNEKLKSEEQKR 290
Cdd:PRK05771 103 KELEEEISELENEIKELEQEI 123
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
251-388 |
3.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 251 KKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSEEQKRISREKA------NLKNPQIMYLEQELESLKAVLEIKNEKL 324
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNefekelRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122133619 325 HQQDVKLMKMEKlvdSNTALVDRLKRFQQENEELKARMDKHMAISRQLSTEQA--VLQESLEKESK 388
Cdd:PRK12704 106 EKREEELEKKEK---ELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
144-422 |
4.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 144 LEKARNELQIAYEgFVQKLNQQHQTDLTELENRLKEFytgeceKLQNIYIEEAEKyKTQLQEQFDNLNAthetsklKIEA 223
Cdd:COG3206 166 LELRREEARKALE-FLEEQLPELRKELEEAEAALEEF------RQKNGLVDLSEE-AKLLLQQLSELES-------QLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 224 SHSEKIELlkkayENSLSEIKKSHEMEKKSLEDLLYEKQ-ESLEKQISDLKSENDTLNEKLKSEeqkrisrekanlkNPQ 302
Cdd:COG3206 231 ARAELAEA-----EARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTPN-------------HPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 303 IMYLEQELESLKAvlEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAVLQES 382
Cdd:COG3206 293 VIALRAQIAALRA--QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 122133619 383 LEK--ESKVNKRLSMENEELLwklhngnlcSPKRSPTSPAAP 422
Cdd:COG3206 371 LQRleEARLAEALTVGNVRVI---------DPAVVPLKPVSP 403
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
193-336 |
4.68e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 193 IEEAEKYKTQLQEQFDNLnathetsklkIEASHSEKIELLKKAYEnsLSEIKKSHEMEKKSLEDLLYEKQESLEKQISDL 272
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEE--AEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122133619 273 KSENDTLNEKLKSEEQKRISREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEK 336
Cdd:PRK00409 572 EKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
83-406 |
5.39e-03 |
|
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: 39.17 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 83 GIILQLKQLLSLGNTKFEALTVVAQHLLSEREEALKQNKTLSQELVNLRGELVTVSTTCEKLEKARNELQIAYEGFVQKL 162
Cdd:COG5185 128 SEIVALKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 163 NQ----QHQTDLTELENRLKEFYTGECEKLQNIYIEEAEKYKT------QLQEQFDNLNATHETSKLKIEASHSEKIELL 232
Cdd:COG5185 208 KEsetgNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQtsdkleKLVEQNTDLRLEKLGENAESSKRLNENANNL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 233 KKAYEN---SLSEIKKSHEMEKKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSE-------EQKRISREKANLKN-- 300
Cdd:COG5185 288 IKQFENtkeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEieqgqesLTENLEAIKEEIENiv 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 301 --PQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKlvDSNTALVDRLKRFQQENEELKARMDKHMAISRQLSTEQAV 378
Cdd:COG5185 368 geVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
330 340
....*....|....*....|....*...
gi 122133619 379 LQESLEKESKVNKRLSMENEELLWKLHN 406
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEIN 473
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-394 |
5.54e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 147 ARNELQIAYEGFVQKLNQQHQTDLTELENRL--KEFYTGECEKLQNIYIEEAEKYKTQLQEQFDNLNATHE-TSKLKIEA 223
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLesERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElRSKREQEV 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 224 SHSEK-IELLKKAYENSLSEIKKSHEMEKKSLEDLL---------YEK-QESLEKQISDLKSENDTLNEKLKSEEQKRIS 292
Cdd:pfam01576 330 TELKKaLEEETRSHEAQLQEMRQKHTQALEELTEQLeqakrnkanLEKaKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 293 RE--------KANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDVKLMKMEKLVDSNTALVDRLKRFQQENEELKARMDK 364
Cdd:pfam01576 410 LEgqlqelqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLST 489
|
250 260 270
....*....|....*....|....*....|
gi 122133619 365 HMaisRQLSTEQAVLQESLEKESKVNKRLS 394
Cdd:pfam01576 490 RL---RQLEDERNSLQEQLEEEEEAKRNVE 516
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
54-300 |
5.73e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.26 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 54 IQTQTSPDVLSSeKALELAQYKSK---CTKQSGIILQLKQLLSLgNTKFEALTVVAQHLLSERE--EALKQNKtlsQELV 128
Cdd:TIGR01612 1596 IDIQLSLENFEN-KFLKISDIKKKindCLKETESIEKKISSFSI-DSQDTELKENGDNLNSLQEflESLKDQK---KNIE 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 129 NLRGELVTVSTTCEKLEKARNELQIAYE-GFVQKLNQQHQTDLTELE-----------NRLKEFYTGECEKLQNIyiEEA 196
Cdd:TIGR01612 1671 DKKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIEsikelieptieNLISSFNTNDLEGIDPN--EKL 1748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 197 EKYKTQLQEQFDNLNATHE--TSKLKIEASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQESLEKQISDLKS 274
Cdd:TIGR01612 1749 EEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAKEFDRIINHFKK 1828
|
250 260 270
....*....|....*....|....*....|..
gi 122133619 275 ENDTLNEKLKSEEQK------RISREKANLKN 300
Cdd:TIGR01612 1829 KLDHVNDKFTKEYSKinegfdDISKSIENVKN 1860
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
142-286 |
7.05e-03 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 39.10 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 142 EKLEKARNELQIAYEGFVQKLNQQHQTDLTELENRLKEFYTGECEKLQNIYIEEAEKY-----------KTQLQEQFDNL 210
Cdd:pfam20435 624 EGLGRAVALFAMALQNFERKLKSAAEKKSSEIIASVSEEIHLELENIKSHIITEAGKTsnlaktkrkhaETRLQEQEEKM 703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122133619 211 NATHEtsKLKIEASHS-EKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQESLEKQISDLKSENDTLNEKLKSE 286
Cdd:pfam20435 704 RMIHE--KFKDDVSHHlEDFKSTIEELEANQSELKGSIKKQRTSHQKLIAHFEGGIETKLDDATKRIDSVNKSARGK 778
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
192-320 |
8.97e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122133619 192 YIEEAEKYKTQLQEQFDNLNATHETSKlKIEASHSEKIELLKKAYENSLSEIKKSHEMEKKSLEDLLYEKQEsLEKQISD 271
Cdd:smart00787 166 ELELLNSIKPKLRDRKDALEEELRQLK-QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQE-LESKIED 243
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 122133619 272 LKSENDTLNEKLKSEEQKRISREKANLKnpQIMYLEQELESLKAVLEIK 320
Cdd:smart00787 244 LTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
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