|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
56-318 |
1.92e-97 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 297.50 E-value: 1.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 56 LTSCEAELQELMKQIDIMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYK 135
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 136 EELMKLQEELSRLKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 215
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 216 AEQSEIIQA-----QLANRKQKLEsvelSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKE 290
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 348605202 291 EKLRESEKLLEALQEEQKELKASLQAQE 318
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-395 |
7.70e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 95 RDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQemalEYKEELMKLQEELSRLKRSYEKLQKkqlrEFRGNTKSLREDR 174
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 175 SEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELssqsEIQHLSSKLERA 254
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 255 KDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKmQEKLQTKL 334
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-EALEEAAE 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348605202 335 KAVDTKHSVERSLEDCQVERKYSSSGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESV 395
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-402 |
3.24e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 97 RELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYkEELMKLQEELSrlkrsyEKLQKKQLREFRGNTKSLREDRSE 176
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL-EEIEQLLEELN------KKIKDLGEEEQLRVKEKIGELEAE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 177 IERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLANRKQKLESVELSSQSEIQHLSSKLER 253
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 254 AKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKMQ-EKLQT 332
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKlEQLAA 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 333 KLKAVDTKHSVERSLEDcQVERKYSSSgQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQL 402
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYD-RVEKELSKL-QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-437 |
1.10e-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: 64.69 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 118 QQIEEQEKTKQEMALEYKE---ELMKLQEELSRLKRSYEKLQKK---QLREFRGNTKSLREDRSEIERLTGKIEEFRQKS 191
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAElekALAELRKELEELEEELEQLRKEleeLSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 192 LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQS----------EIQHLSSKLERAKDTICAN 261
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 262 ELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQES--FILDAKMQE------KLQTK 333
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSelEELSEELREleskrsELRRE 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 334 LKAVDTK-HSVERSLEDCQVERKY-----SSSGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTtckqLSQELM 407
Cdd:TIGR02168 917 LEELREKlAQLELRLEGLEVRIDNlqerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP----VNLAAI 992
|
330 340 350
....*....|....*....|....*....|
gi 348605202 408 EKYEELKRMEGHNNEYRTEIKKLKEQILQA 437
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-455 |
2.51e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 119 QIEEQEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQR 198
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 199 liyQQQVSSLEAQRKALAEQSEIIqaqlanrKQKLESVELSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGT 278
Cdd:TIGR02169 261 ---SELEKRLEEIEQLLEELNKKI-------KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 279 NVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAqesfiLDAKMQEKLQTKLKAVDTKHSVERSLEDCQVERkysS 358
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED-----LRAELEEVDKEFAETRDELKDYREKLEKLKREI---N 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 359 SGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQIlqad 438
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY---- 478
|
330
....*....|....*..
gi 348605202 439 QTYSSALEGMKTEISQL 455
Cdd:TIGR02169 479 DRVEKELSKLQRELAEA 495
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-552 |
3.20e-10 |
|
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: 63.21 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 38 AMEALLEGIQTRGHSGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGIL 116
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 117 HQQIEEqektkqemaleYKEELMKLQEELSRLKRSYEKLQKKQLrefrGNTKSLREDRSEIERLTGKIEEFRQ--KSLDW 194
Cdd:pfam15921 376 DDQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSITIDHLRRELDDRNMEVQRLEAllKAMKS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 195 EKQRLIYQQ------------QVSSLEAQRKALAEQSEIIQAQLANRKQKLESvelsSQSEIQHLSSKLERAKDTICANE 262
Cdd:pfam15921 441 ECQGQMERQmaaiqgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 263 LEIERLNIRVkDLmgtNVTILQEQRQKEEKLRESEKLLEALQ-------------EEQKELKASLQAQESFILDAKMQEK 329
Cdd:pfam15921 517 AEITKLRSRV-DL---KLQELQHLKNEGDHLRNVQTECEALKlqmaekdkvieilRQQIENMTQLVGQHGRTAGAMQVEK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 330 LQTKLKAVDTKHSVE--RSLEDcQVERKYSSSGQGVLDNVLSQLDISHSSEELLQA--EVTRLEGSLESVSTTCKQLSQE 405
Cdd:pfam15921 593 AQLEKEINDRRLELQefKILKD-KKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkDIKQERDQLLNEVKTSRNELNS 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 406 LMEKYEELKR--------MEGHNNEYRTEIKKLKEQILQADQTYSS----------ALEGMKTEISQLTRELH--QRDIT 465
Cdd:pfam15921 672 LSEDYEVLKRnfrnkseeMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkVAMGMQKQITAKRGQIDalQSKIQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 466 IASAKCSSSDMERQ-LKAEMQKAEEK----AVEHKEILSQLESLRLENRRLSETVMKLELGLHECSMPVSPLGLIATRFL 540
Cdd:pfam15921 752 FLEEAMTNANKEKHfLKEEKNKLSQElstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQE 831
|
570
....*....|...
gi 348605202 541 EEE-ELRSHHILE 552
Cdd:pfam15921 832 QESvRLKLQHTLD 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-501 |
1.83e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 174 RSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqSEIQHLSSKLER 253
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 254 AKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAqesfiLDAKMQEKLQTK 333
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-----LNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 334 LKAVDTKHSVERSLEDCQvERKYSSSGQgVLDNVLSQLDISHSSEElLQAEVTRLEGSLESVSTTCKQLSQELMEKYEEL 413
Cdd:TIGR02168 827 ESLERRIAATERRLEDLE-EQIEELSED-IESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 414 KRMEGHNNEYRTEIKKLKEQILQADQtyssALEGMKTEISQLT---RELHQRDITIASAKcsssdmERQLKAEMQKAEEK 490
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLEL----RLEGLEVRIDNLQerlSEEYSLTLEEAEAL------ENKIEDDEEEARRR 973
|
330
....*....|.
gi 348605202 491 AVEHKEILSQL 501
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-415 |
2.01e-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: 60.47 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 73 MVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILH---QQIEEQEKTKQEMALEYKEELMKLQEELSRLK 149
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 150 RSYEKLqkkqlrefrgntkslredRSEIERLTGKIEEFRQKSLDWEkqRLIYQQQVSSLEAQRKALAEQSEIIQAQLANR 229
Cdd:TIGR02169 758 SELKEL------------------EARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 230 KQKLESVELSSQ---SEIQHLSSKLERAKDTICANELEIERLNIRVKDLmgtnvtiLQEQRQKEEKLRESEKLLEALQEE 306
Cdd:TIGR02169 818 EQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 307 QKELKASLQAQESFILDAKMQ-EKLQTKLKAVDTKHSV----ERSLEDCQVERKYSSSGQGVLDNVLSQL---------- 371
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQiEKKRKRLSELKAKLEAleeeLSEIEDPKGEDEEIPEEELSLEDVQAELqrveeeiral 970
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 348605202 372 -DISHSSEELLQAEVTR---LEGSLESVSTTCKQLsQELMEKYEELKR 415
Cdd:TIGR02169 971 ePVNMLAIQEYEEVLKRldeLKEKRAKLEEERKAI-LERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-337 |
1.30e-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: 54.68 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 56 LTSCEAELQELMKQIDiMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEmaleYK 135
Cdd:TIGR02168 234 LEELREELEELQEELK-EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI----LR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 136 EELMKLQEELSRLKRSYEKLQKKQLR---EFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 212
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDElaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 213 KALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAKdticanELEIERLNIRVKDLMGTNVTILQEQRQKEEK 292
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 348605202 293 LRESEKLLEALQEEQKELKASL-QAQESFILDAKMQEKLQTKLKAV 337
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELaQLQARLDSLERLQENLEGFSEGV 508
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-517 |
3.53e-07 |
|
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: 53.30 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 197 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnRKQKLESVELSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDL- 275
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 276 MGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESfILDAKMQEKLQTKLKAVDTK-HSVERSLEDCQVER 354
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEGALDAQlALLKAAIAARRSGA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 355 KYSSSG-QGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESvsttCKQLSQELMEKYEELK-RMEGHNNEYRTEIKKLKE 432
Cdd:pfam12128 746 KAELKAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIER 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 433 QILQADQTYSSALEGMKTEISQLTRELHQRDitiaSAKCSSSDMERQLKAEMQK---------AEEKAVEHKEILSQLES 503
Cdd:pfam12128 822 AISELQQQLARLIADTKLRRAKLEMERKASE----KQQVRLSENLRGLRCEMSKlatlkedanSEQAQGSIGERLAQLED 897
|
330
....*....|....
gi 348605202 504 LRLENRRLSETVMK 517
Cdd:pfam12128 898 LKLKRDYLSESVKK 911
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-349 |
1.22e-06 |
|
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: 50.92 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 136 EELMKLQEELSRLKRSYEKLQKKqlrefrgntksLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 215
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKE-----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 216 AEQSEIIQAQLANRKQKLESV-----ELSSQSEIQHLSSKlERAKDTICANELeIERLNIRVKDLMGTNVTILQEQRQKE 290
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELlralyRLGRQPPLALLLSP-EDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348605202 291 EKLRESEKLLEALQEEQKELKASLQAQ--ESFILDAKMQEKLQTKLKAVDTKHSVERSLED 349
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALkaERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-561 |
3.11e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 95 RDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKEELMKLQEELSRLKRsyeklqkkqlrefrgntkSLREDR 174
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------------------ALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 175 SEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERA 254
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 255 KDTicanELEIERLNIRVKDLmgtnVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKMQEKLQTKL 334
Cdd:COG1196 452 AEL----EEEEEALLELLAEL----LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 335 KAVDTKHSVERSLEDCQVERKYSSSGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELK 414
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 415 RMEghNNEYRTEIKKLKEQILQADQTYSSALEGMKTEISQLTRELHQRDITIASAKCSSSDMERQLKAEMQKAEEKAVEH 494
Cdd:COG1196 604 VAS--DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348605202 495 KEILSQLESLRLENRRLSETVMKLELGLHECSMPVSPLGLIATRFLEEEELRSHHILERLDAHIEEL 561
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
66-189 |
3.32e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 66 LMKQIDIMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKE------ELM 139
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEarseerREI 461
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 348605202 140 KLQEELSRLKRSYEKLQKKqlrefrgntksLREDRSEIERLTGKIEEFRQ 189
Cdd:COG2433 462 RKDREISRLDREIERLERE-----------LEEERERIEELKRKLERLKE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
123-571 |
1.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 123 QEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRliyQ 202
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA---A 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 203 QQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQS--EIQHLSSKLERAKDticANEL----EIERLNIRVKDLM 276
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKK---ADEAkkkaEEAKKADEAKKKA 1492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 277 GTNVTILQEQRQKEEKLRESEKLLEAlqEEQKELKASLQAQESFILDAKMQEKLQTKLKAVDTKHSVERSLEDCQVERKY 356
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 357 SSSGQgvldnvlsQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELME------KYEELKRMEGHNNEYRTEIKKL 430
Cdd:PTZ00121 1571 KAEED--------KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeakiKAEELKKAEEEKKKVEQLKKKE 1642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 431 KEQILQADQTySSALEGMKTEISQLTRELHQRDITIASAKCSSSDMERQLKAEMQKAEE-KAVEHKEILSQLESLRLENR 509
Cdd:PTZ00121 1643 AEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEaKKAEELKKKEAEEKKKAEEL 1721
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348605202 510 RLSETVMKLELGLHECSMPVSPLGLIATRFLEEEELRSHHILERLDAHIEELKRESEKTVRQ 571
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
60-255 |
1.70e-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: 47.45 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 60 EAELQELMKQIDIM------VAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALE 133
Cdd:COG4942 26 EAELEQLQQEIAELekelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 134 YKEELMKLQ--------------EELSRLKRSYEKLqKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRL 199
Cdd:COG4942 106 LAELLRALYrlgrqpplalllspEDFLDAVRRLQYL-KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 348605202 200 IYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAK 255
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-331 |
1.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 145 LSRLKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKsldwEKQRLIYQQQVSSLEAQRKALAEQSEIIQA 224
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 225 QLANRKQKLESVELSSQ---------------SEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTNVTILQEQRQK 289
Cdd:COG4717 124 LLQLLPLYQELEALEAElaelperleeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 348605202 290 -EEKLRESEKLLEALQEEQKELKASLQAQESFILDAKMQEKLQ 331
Cdd:COG4717 204 lQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
101-524 |
3.45e-05 |
|
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: 47.02 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 101 ALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKEELMKLQEELSRlkrsyEKLQKKQLREFRGNTKSLREDRSEIERL 180
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQE-----NKDLIKENNATRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 181 TGKIEEFRqksldwEKQRLIYQQQVSSLEAQRKALAEqseiIQAQLANRKQKLESVELSSQSEIQHLSsklERAKDTICA 260
Cdd:pfam05483 171 TKKYEYER------EETRQVYMDLNNNIEKMILAFEE----LRVQAENARLEMHFKLKEDHEKIQHLE---EEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 261 NELEIERLNIRV---KDLMGTNVTILQEQRQKEEKLRESEKL----LEALQEEQKELKASLQ-----AQESFILDAKMQE 328
Cdd:pfam05483 238 KEKQVSLLLIQItekENKMKDLTFLLEESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmsLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 329 KLQTKLKavdtkhSVERSLEDCQVERKYSSSGQGVLDNVLSQLDISHSS-EELLQAEVTRLEGSLESVsttcKQLSQELM 407
Cdd:pfam05483 318 DLQIATK------TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSlEELLRTEQQRLEKNEDQL----KIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 408 EKYEELKRMEGHNNEYRTEIKKLK------EQILQADQTYSSALEGMKTEISQLT-------RELHQRDITIASAKCSSS 474
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKkilaedEKLLDEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEE 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 348605202 475 DMERQLKAEMQKAEEKAVEHKEILSQLESLRLENRRLSETV--MKLELGLHE 524
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQ 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-336 |
4.04e-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: 45.91 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 167 TKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQH 246
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 247 LSSKLERAKDTI---------------------CANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQE 305
Cdd:COG4942 95 LRAELEAQKEELaellralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190
....*....|....*....|....*....|..
gi 348605202 306 EQKELKASLQAQESFILDAK-MQEKLQTKLKA 336
Cdd:COG4942 175 ELEALLAELEEERAALEALKaERQKLLARLEK 206
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-570 |
4.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 97 RELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMA------LEYKEELMKLQEELSRLKRSYEKLQK--KQLREFRGNTK 168
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEelekelESLEGSKRKLEEKIRELEERIEELKKeiEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 169 SLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlanRKQKLESVELSSQSEIQHLS 248
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE--------RLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 249 SKlERAKDTICANELEIERLNIRVKDLmgtnvtilqEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKmqe 328
Cdd:PRK03918 359 ER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 329 KLQTKLKAVDTKHSVERSLEDCQVERKYSSSGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLS----- 403
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeql 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 404 ------------QELMEKYEELKRMEGHNNEYRTEIKKLKEQiLQADQTYSSALEGMKTEISQLTRELHQRDITIASAKC 471
Cdd:PRK03918 506 keleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 472 SSSDMERQLKAEMQKAEEKAVE----HKEILSQLESLRLENRRLSETVMKLELGLHECSMPVSPLGLIATRFLEEE--EL 545
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYLElkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeEL 664
|
490 500 510
....*....|....*....|....*....|
gi 348605202 546 RSHHI-----LERLDAHIEELKRESEKTVR 570
Cdd:PRK03918 665 REEYLelsreLAGLRAELEELEKRREEIKK 694
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-459 |
4.87e-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: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 133 EYKEELMKLQEELSRLKRSYEKLQKkqlrEFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 212
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKD----NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 213 KALAEQSEIIQAQLAN-RKQKLESVELSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEE 291
Cdd:TIGR04523 284 KELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 292 KLRESEKLLEALQEEQKELKASLQAQESFILDAKMQ--------EKLQTKLKAVDT-KHSVERSLEDCQVERKYSSSGQG 362
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnqeklnQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 363 VLDNVLSQLDIS----HSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI---L 435
Cdd:TIGR04523 444 DLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslK 523
|
330 340
....*....|....*....|....
gi 348605202 436 QADQTYSSALEGMKTEISQLTREL 459
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDEL 547
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
62-522 |
6.80e-05 |
|
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: 45.98 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 62 ELQELMKQIDIMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKEELMKL 141
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 142 QEELSRLKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLdwEKQRLIYQQQVSSL----EAQRKALAE 217
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL--AVAEDDLQALESELreqlEAGKLEFNE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 218 QSEIIQAQLANRKQKLESVELSSQ--SEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGtnvtilqEQRQKEEKLRE 295
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPEllLQLENFDERIERAREEQEAANAEVERLQSELRQARK-------RRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 296 SEKLLEALQEEQKELKASLQAQESFILDAKMQEklqtklkAVDTKHSVERSLEDCQVER--------KYSSSGQGVLDNV 367
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAGTLLHFLRKE-------APDWEQSIGKVISPELLHRtdldpevwDGSVGGELNLYGV 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 368 ---LSQLDI--SHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKklkeqilQADQTYS 442
Cdd:pfam12128 584 kldLKRIDVpeWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK-------NARLDLR 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 443 SALEGMKTEISQLTRELHQRditIASAKCSSSDMERQLKAEMQKAEEKAVEHKEILSQLESLRLENRRLSETVMKLELGL 522
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAER---KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAL 733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
116-513 |
8.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 116 LHQQIEEQEKTKQEMAL-EYKEELMKLQEELSRlkrsYEKlQKKQLREFRGNTKSL----REDRSEIERLTGKIEEFRQK 190
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLnGLESELAELDEEIER----YEE-QREQARETRDEADEVleehEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 191 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSS---QSEIQHLSSKLERAKDTICANELEIER 267
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARReelEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 268 LNIRVKDLmgtnvtilqEQRQKEeklreseklleaLQEEQKELKASLQAQESFIldakmqEKLQTKLKAVDTK-HSVERS 346
Cdd:PRK02224 347 LREDADDL---------EERAEE------------LREEAAELESELEEAREAV------EDRREEIEELEEEiEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 347 LEDCQVERKYSSSgqgVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVST--------TCKQLSQE------LMEKYEE 412
Cdd:PRK02224 400 FGDAPVDLGNAED---FLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 413 LKRMEGHNNEYRTEIKKLKEQILQADQTYSSA--LEGMKTEISQLTRELHQRDITIA--SAKCSSSDMERQ-LKAEMQKA 487
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEERREDLEELIAERRETIEekRERAEELRERAAeLEAEAEEK 556
|
410 420
....*....|....*....|....*..
gi 348605202 488 EEKAVE-HKEILSQLESLRLENRRLSE 513
Cdd:PRK02224 557 REAAAEaEEEAEEAREEVAELNSKLAE 583
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-417 |
9.75e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 124 EKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQ----------LREFRGNTKSLREDRSEIERL-------TGKIEE 186
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELrrienrldelSQELSDASRKIGEIEKEIEQLeqeeeklKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 187 FRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLesvelsSQSEIQHLSSKLERAKDTICANELEIE 266
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL------SHSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 267 RLNIRVKDLmgtnvtiLQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFIldAKMQEKLQTKLKAVDTkhsVERS 346
Cdd:TIGR02169 816 EIEQKLNRL-------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK--EELEEELEELEAALRD---LESR 883
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348605202 347 LEDCQVERkysssgqgvlDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRME 417
Cdd:TIGR02169 884 LGDLKKER----------DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-533 |
1.20e-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: 45.05 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 205 VSSLEAQRKALAEQSEIIQaQLANRKQKLESVELSSQS-EIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTNVTIL 283
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAE-RYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 284 QEQRQKEEKLRESEKLLEALQEEQKELKASLQaqesfILDAKMQEkLQTKLKAVDTKHSVERSLEDCQVERKYSssgqgv 363
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQ-----ILRERLAN-LERQLEELEAQLEELESKLDELAEELAE------ 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 364 LDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI--------- 434
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrrerlqq 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 435 ---LQADQTYSSALEGMKTEISQLTRELHQ---RDITIASAKCSSSDMERQLKAEMQKAEEKAVEHKEILSQLESLRLEN 508
Cdd:TIGR02168 422 eieELLKKLEEAELKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340
....*....|....*....|....*
gi 348605202 509 RRLSETVMKLELGLHECSMPVSPLG 533
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLS 526
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-519 |
1.54e-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: 44.63 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 120 IEEQEKTKQEMALEYKEELMKLQEElsrlKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRL 199
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQ----KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 200 IYQQQVSSLEAQRKALAEQSEIIQAQlaNRKQKlesvelSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTN 279
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKK--IQKNK------SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 280 VTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKMQeklqtklKAVDTKHSVERSLEDCQVErkysss 359
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ-------KEQDWNKELKSELKNQEKK------ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 360 gqgvLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKL--------- 430
Cdd:TIGR04523 323 ----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesqindles 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 431 ----------------------KEQILQADQTYSSALEGMKTEISQLTRELHQRDITIASAKCSSSDMERQLKA------ 482
Cdd:TIGR04523 399 kiqnqeklnqqkdeqikklqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrsin 478
|
410 420 430
....*....|....*....|....*....|....*...
gi 348605202 483 -EMQKAEEKAVEHKEILSQLESLRLENRRLSETVMKLE 519
Cdd:TIGR04523 479 kIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-336 |
1.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 87 ALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKtkqemaleykeELMKLQEELSRLKRSYEKLQKKqlrefrgn 166
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------RIAALARRIRALEQELAALEAE-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 167 tksLREDRSEIERLTGKIEEFRQksldwEKQRLIYQQQVSSLEAQRKALAEQSEIiqAQLANRKQKLESVELSSQSEIQH 246
Cdd:COG4942 85 ---LAELEKEIAELRAELEAQKE-----ELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 247 LSSKLERAKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKM 326
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|
gi 348605202 327 QEKLQTKLKA 336
Cdd:COG4942 235 EAAAAAERTP 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
56-355 |
1.98e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 56 LTSCEAELQELMKQIDIMVahkkseweGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYK 135
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEML--------GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 136 EE---------LMKLQEELSRLKRSYEKLQKKQ-----LREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIY 201
Cdd:TIGR00606 783 SAkvcltdvtiMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 202 QQQVSSLEAQRKALAEQseiiqaqlANRKQKLESVELSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTNVT 281
Cdd:TIGR00606 863 KSKTNELKSEKLQIGTN--------LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 282 -----------ILQEQRQKEEKLRESEKLLEALQEEQKELKAS------LQAQESFILDAKMQEKLQTKLKAVDTKHSVE 344
Cdd:TIGR00606 935 snkkaqdkvndIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntvnAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
330
....*....|.
gi 348605202 345 RSLEDCQVERK 355
Cdd:TIGR00606 1015 RWLQDNLTLRK 1025
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
65-312 |
2.02e-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: 44.34 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 65 ELMKQIDIMVAHKKSEWEGQTHAletclDMRDRELKALRSQLDMKHKEVGiLHQQIEEQEKTKQ--------------EM 130
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQE-----KFEKMEQERLRQEKEEKAREVE-RRRKLEEAEKARQaemdrqaaiyaeqeRM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 131 ALEYKEELMKLQEElsRLKRSYEKLQKKQLREFRGNTKSLR----EDRSEIERLTGKIEEFR-QKSLDWEKQRLIYQQQV 205
Cdd:pfam17380 343 AMERERELERIRQE--ERKRELERIRQEEIAMEISRMRELErlqmERQQKNERVRQELEAARkVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 206 SSLE---AQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHL--------SSKLERAKDTICANELEIERLNIRVKD 274
Cdd:pfam17380 421 EMEQiraEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250 260 270
....*....|....*....|....*....|....*...
gi 348605202 275 LMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKA 312
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
97-236 |
3.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 97 RELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKEELMKLQEELSR-LKRSYEKLQKKQlrefrgntkslredrs 175
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKeLRERRNELQKLE---------------- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348605202 176 eiERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESV 236
Cdd:PRK12704 89 --KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
183-336 |
4.17e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 183 KIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLSSKLERAKDTI---- 258
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 259 --------CANELE-----------IERLNIrVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQES 319
Cdd:COG3883 93 ralyrsggSVSYLDvllgsesfsdfLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170
....*....|....*...
gi 348605202 320 FILDAKM-QEKLQTKLKA 336
Cdd:COG3883 172 ELEAQQAeQEALLAQLSA 189
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
119-555 |
5.90e-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: 42.79 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 119 QIEEQEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQlrefrgntKSLREDRSEIERLTGKIEEFRQKSLD-WEKQ 197
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ--------KALEEDLQIATKTICQLTEEKEAQMEeLNKA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 198 RLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELssqsEIQHLSSKLERAKDTICANELEIERLnirvKDLMG 277
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEEMTKFKNNKEVELEEL----KKILA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 278 TNVTILQEQRQkeeklreSEKLLEALQEEQKELKASLQAQESFILDAKMQEKLQTKlkavdTKHSVERSLEDCQVERKYS 357
Cdd:pfam05483 416 EDEKLLDEKKQ-------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT-----SEEHYLKEVEDLKTELEKE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 358 SSGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEghnNEYRTEIKKLKEQILQA 437
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKE---MNLRDELESVREEFIQK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 438 DQTYSSALEGMKTEISQLTRELHQRDITIASAKCSSSDMERQLKAEMQKAEEKAVEHKEILSQLESLRLENRRLSETVMK 517
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK 640
|
410 420 430
....*....|....*....|....*....|....*...
gi 348605202 518 LELGLHECSMPVSPLGLIATRFLEEEELRSHHILERLD 555
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVE 678
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-346 |
7.15e-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: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 166 NTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI--IQAQLANRKQKLESVELSSqSE 243
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASS-DD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 244 IQHLSSKLERAkdticanELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQK-----ELKASLQAQE 318
Cdd:COG4913 687 LAALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAAL 759
|
170 180
....*....|....*....|....*...
gi 348605202 319 SFILDAKMQEKLQTKLKAVDTKHSVERS 346
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEE 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-293 |
8.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 97 RELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMAleykeelmKLQEELSRLKRSYEKLqkKQLREFRGNTKSLREDRSE 176
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE--------ELEAELEELREELEKL--EKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 177 IERLTGKIEEFRQKSLDWekqrliyQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAKD 256
Cdd:COG4717 141 LAELPERLEELEERLEEL-------RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190
....*....|....*....|....*....|....*..
gi 348605202 257 TICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKL 293
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
118-331 |
9.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 118 QQIEEQEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKqlrefrgntksLREDRSEIERLTGKIEEFRQKsldwekq 197
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-----------LEALQAEIDKLQAEIAEAEAE------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 198 rliyqqqvssLEAQRKALAEQseIIQAQLANRKQKLESVELSSQS------EIQHLSSKLERAKDTIcaneLEIERLNIR 271
Cdd:COG3883 81 ----------IEERREELGER--ARALYRSGGSVSYLDVLLGSESfsdfldRLSALSKIADADADLL----EELKADKAE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 272 VKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKMQEKLQ 331
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
95-343 |
9.98e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 95 RDRELKALRsqldmkhkEVGILHqqIEE-QEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQLREFRGNTKSLRED 173
Cdd:PRK05771 18 KDEVLEALH--------ELGVVH--IEDlKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 174 RSEIERLTGKIEEfRQKSLDWEKQRLiyQQQVSSLEAQRKAL------------AEQSEIIQAQLANRkqKLESVELSSQ 241
Cdd:PRK05771 88 IKDVEEELEKIEK-EIKELEEEISEL--ENEIKELEQEIERLepwgnfdldlslLLGFKYVSVFVGTV--PEDKLEELKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 242 SEIQHLSSKLERAKDT-----ICANEL------EIERLNIRVKDLmGTNVTILQEQRQKEEKLRESEKLLEALQEEQKEL 310
Cdd:PRK05771 163 ESDVENVEYISTDKGYvyvvvVVLKELsdeveeELKKLGFERLEL-EEEGTPSELIREIKEELEEIEKERESLLEELKEL 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 348605202 311 KASLqaqESFILDAKMQ-----EKLQTKLKAVDTKHSV 343
Cdd:PRK05771 242 AKKY---LEELLALYEYleielERAEALSKFLKTDKTF 276
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-316 |
1.12e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 88 LETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEY----------KEELMKLQEELSRLKRSYEKLQK 157
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeelkalREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 158 KQlrefRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVE 237
Cdd:TIGR02168 825 RL----ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 238 ---LSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGT-NVTILQEQRQKEEKLRESEKLLEALQEEQKELKAS 313
Cdd:TIGR02168 901 eelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
...
gi 348605202 314 LQA 316
Cdd:TIGR02168 981 IKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-519 |
1.25e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 95 RDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEmALEYKEELMKLQE-ELSRLKRSYEKLQKK--QLREFRGNTKSLR 171
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADEaKKAEEKKKADEAKKKaeEAKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 172 EDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLEsvELSSQSEIQHLSSKL 251
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 252 ERAKDTICANELEIERLNIRVKDlmGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDaKMQEKLQ 331
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 332 TKLKAVDTKHSVERSLEDCQVERKYSSSGQGVLDnvLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKqlsQELMEKYE 411
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE--AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK---ADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 412 ELKRMEghnneyrtEIKKLkEQILQADQTYSSALEgmKTEISQLTRELHQRDITIASAKCSSSDMERQLKAEMQ--KAEE 489
Cdd:PTZ00121 1556 ELKKAE--------EKKKA-EEAKKAEEDKNMALR--KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkiKAEE 1624
|
410 420 430
....*....|....*....|....*....|..
gi 348605202 490 --KAVEHKEILSQLESLRLENRRLSETVMKLE 519
Cdd:PTZ00121 1625 lkKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-268 |
1.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 97 RELKALRSQLDMKHKEVGILHQQIEEQEktkqemALEYKEELMKLQEELSRLKRSYEKLQKkQLREFRGNTKSLREDRSE 176
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRR------LELLEAELEELRAELARLEAELERLEA-RLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 177 -----IERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQ----RKALAEQSEIIQAQLANRKQKLESVElSSQSEIQHL 247
Cdd:COG4913 335 nggdrLEQLEREIERLERELEERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALE-EALAEAEAA 413
|
170 180
....*....|....*....|.
gi 348605202 248 SSKLERAKDTIcanELEIERL 268
Cdd:COG4913 414 LRDLRRELREL---EAEIASL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-311 |
1.39e-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: 41.59 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 56 LTSCEAELQELMKQIDIMVAhKKSEWEGQTHALETCLDM-RDRELKALRSQLDMKHKEVGILHQQIEeQEKTKQEMALEY 134
Cdd:TIGR02169 753 IENVKSELKELEARIEELEE-DLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIE-QKLNRLTLEKEY 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 135 KEELMKLQEELSRLKRSYEKLQKKQLREFRGNtksLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKA 214
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGK---KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 215 LAEQSEIIQAQLANRKQKLESVElSSQSEIQHLSSKLERAKDTICANE---LEIERLNIRVKDLMGTNVTILQEQRQKEE 291
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALE-EELSEIEDPKGEDEEIPEEELSLEdvqAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
250 260
....*....|....*....|
gi 348605202 292 KLRESEKLLEALQEEQKELK 311
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAIL 1006
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-444 |
1.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 60 EAELQELMKQIDiMVAHKKSEWEGQTHALETCLDMRD--RELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMAlEYKEE 137
Cdd:COG4717 94 QEELEELEEELE-ELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 138 LMKLQEELSRLKRSYEKLQKKQLREFRGNTKSLRED-----------RSEIERLTGKIEEFRQKSLDWEKQRLIYQQQ-- 204
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRlaeleeeleeaQEELEELEEELEQLENELEAAALEERLKEARll 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 205 ------VSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGT 278
Cdd:COG4717 252 lliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 279 NVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFIL----DAKMQEKLQTKLKAVDTKHSVERSLEdcQVER 354
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELE--ELEE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 355 KYSSSGQGVLDnvlsqlDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNN--EYRTEIKKLKE 432
Cdd:COG4717 410 QLEELLGELEE------LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKA 483
|
410
....*....|..
gi 348605202 433 QILQADQTYSSA 444
Cdd:COG4717 484 ELRELAEEWAAL 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
95-434 |
1.85e-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: 41.50 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 95 RDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQE-MALEYKEELMKLQEELSRLK-RSYEKLQKKQLREFRGNTKSLRE 172
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAkKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 173 DRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLE 252
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 253 RAKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFIL-----DAKMQ 327
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 328 EKLQTKLKAVDTKHSVERSLEDCQVERKYSSSGQGVLDNVlsQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELM 407
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE--ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340
....*....|....*....|....*..
gi 348605202 408 EKYEELKRMEGHNNEYRTEIKKLKEQI 434
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLALI 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-575 |
1.89e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 372 DISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTY---SSALEGM 448
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 449 KTEISQLTRELHQRDITIASAKCSSSDMERQLKAEMQKAEEKAVEHKEILSQLESLRLENRRLSETVMKLELGLHECSMP 528
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 348605202 529 VSPL-GLIATRFLEEEELRSHhiLERLDAHIEELKRESEKTVRQFTAL 575
Cdd:TIGR02168 381 LETLrSKVAQLELQIASLNNE--IERLEARLERLEDRRERLQQEIEEL 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
120-319 |
1.93e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 120 IEEQEKTKQEMALE----YKEELMKLQEELSRLKRSYEKLQKKQ------------LREFRGNTKSLREDRSEIERLTGK 183
Cdd:COG3206 162 LEQNLELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNglvdlseeakllLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 184 IEEFRQ--KSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANR-------KQKLESVELSSQSEIQHLSSKLERA 254
Cdd:COG3206 242 LAALRAqlGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348605202 255 KDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQES 319
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVG 386
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
56-301 |
2.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 56 LTSCEAELQELMKQID------IMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKevgiLHQQIEEQEKTKQe 129
Cdd:PRK01156 192 LKSSNLELENIKKQIAddekshSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNR----YESEIKTAESDLS- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 130 MALEYKEELMKLQEELSRLKRSYEKLQKKQLREF---RGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQR---LIYQQ 203
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIINDPVYKNRNYINDYfkyKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYndyIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 204 QVSSLEAQRKALAEQSEIIQAQL---ANRKQKLESVELSSQSEIQHLSSKLERAKdtICANELEIERLNIRVK-DLMGTN 279
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKIQE--IDPDAIKKELNEINVKlQDISSK 424
|
250 260
....*....|....*....|....*.
gi 348605202 280 VTILQEQ----RQKEEKLRESEKLLE 301
Cdd:PRK01156 425 VSSLNQRiralRENLDELSRNMEMLN 450
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
60-234 |
2.25e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 60 EAELQELMKQIDIMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMalEYKEELM 139
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDR 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 140 KLQEELSR--LKRSYEKLQKKQLREFRGNT---KSLREDRSEI--ERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 212
Cdd:pfam17380 487 KRAEEQRRkiLEKELEERKQAMIEEERKRKlleKEMEERQKAIyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
170 180
....*....|....*....|....
gi 348605202 213 K--ALAEQSEIIQAQLANRKQKLE 234
Cdd:pfam17380 567 RleAMEREREMMRQIVESEKARAE 590
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
102-197 |
3.63e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 102 LRSQLDMKHKEVGILHQQIE----EQEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQLREfRGNTKSLREDRSEI 177
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEqleiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAE-KELIEEIQELKEEL 480
|
90 100
....*....|....*....|
gi 348605202 178 ERLTGKIEEFRQKSLDWEKQ 197
Cdd:COG0542 481 EQRYGKIPELEKELAELEEE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
170-321 |
5.31e-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: 38.75 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 170 LREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelSSQSEIQHLSS 249
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348605202 250 KLERAKDTICANELEIERLNIRV----KDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFI 321
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIeeleEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
277-477 |
6.16e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 39.55 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 277 GTNVTILQEQRQKEEKLRES-EKLLEALQEEQKELKASLQAQESFILDAKMQEK--LQTKLKAVDTKHSVERSLEDCQVE 353
Cdd:pfam07902 132 GIATRISEDTDKKLALINETiSGIRREYQDADRQLSSSYQAGIEGLKATMASDKigLQAEIQASAQGLSQRYDNEIRKLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 354 RKYSSSGQGVLDNVLSQLD-----ISHSSEELLQAEVTRLEGSLESVSTTCKQLSQelmekyeELKRMEGHNNEYRTEIK 428
Cdd:pfam07902 212 AKITTTSSGTTEAYESKLDdlraeFTRSNQGMRTELESKISGLQSTQQSTAYQISQ-------EISNREGAVSRVQQDLD 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 348605202 429 KLKEQILQADQTYSS---ALEGMKTEISQLTRELHQRDITIA---SAKCSSSDME 477
Cdd:pfam07902 285 SYQRRLQDAEKNYSSltqTVKGLQSTVSDPNSKLESRITQLAgliEQKVTRGDVE 339
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-433 |
8.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 95 RDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKK---QLREFRGNTKSLR 171
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKitaRIGELKKEIKELK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 172 EDRSEIERLTGKIEEFRQKSLDWEKQRLI--YQQQVSSLEAQRKALAEQSEiiqaQLANRKQKLESVeLSSQSEIQHLSS 249
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELTEEHRKELLeeYTAELKRIEKELKEIEEKER----KLRKELRELEKV-LKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 250 KLERAKDT-----------ICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQE 318
Cdd:PRK03918 501 LAEQLKELeeklkkynleeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 319 SF------ILDAKMQE------KLQTKLKAVDTKHSVERSLEDCQVERKYSSSGQGVLDNVLSQLdishsSEELLQAEVT 386
Cdd:PRK03918 581 ELgfesveELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL-----RKELEELEKK 655
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 348605202 387 RLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 433
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
98-439 |
9.43e-03 |
|
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: 39.03 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 98 ELKALRSQLDMKHKEVGILHQQIE---EQEKTKQEMALEYKEELMKLQ--------------EELSRLKRSYEKLQKKQL 160
Cdd:pfam10174 381 EIRDLKDMLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLKERVKSLQtdssntdtalttleEALSEKERIIERLKEQRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 161 REFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAqrKALAEQSEIIQAQLANRKQKLESVELSS 240
Cdd:pfam10174 461 REDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLAS--SGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 241 QSEIQHLSSKLERAKdticaneleiERLNIRVKDLMgtnvtiLQEQRQKEEKLR---ESEKLLEALQEEQKELKASLQAQ 317
Cdd:pfam10174 539 QLKKAHNAEEAVRTN----------PEINDRIRLLE------QEVARYKEESGKaqaEVERLLGILREVENEKNDKDKKI 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605202 318 ESFILDAKMQEKLQTKlKAVDTKHSVersledcQVERKyssSGQGVLDNVLSQLDISHSSEELLQAEvtRLEGSLESVST 397
Cdd:pfam10174 603 AELESLTLRQMKEQNK-KVANIKHGQ-------QEMKK---KGAQLLEEARRREDNLADNSQQLQLE--ELMGALEKTRQ 669
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 348605202 398 TCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQ 439
Cdd:pfam10174 670 ELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQ 711
|
|
| |
