|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
76-297 |
5.03e-79 |
|
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: 253.59 E-value: 5.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 76 LTSCEAELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYK 155
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 156 E-----------------------------------------ELLKLQEEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 194
Cdd:pfam17045 81 QqlqklqeelsklkrsyeklqrkqlkeareeaksreedrselSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 195 AEQSEIIQA-----QLANRKQKLEsvelSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKE 269
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 1907198326 270 EKLRESEKLLEALQEEQKELKASLQSQE 297
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-413 |
4.74e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 115 RDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMA------------MEYKEELLKLQEEEFRQKSLDWEKQRLIYQQ 182
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 183 QVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTIL 262
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 263 QDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFIleAKMQEKLQTTLKAVgtqQSVERPLEDCQKERKYSSPGQGV 342
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESELEALLNER---ASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907198326 343 LDNVLSQLDFSHsseELLQAEVTRLEGSLESVSATCKQLSQELMEKYE-ELKRMEGHNNEYRTEIKKLKEQI 413
Cdd:TIGR02168 906 LESKRSELRREL---EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-438 |
6.26e-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: 65.86 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 117 RELKALRSQLDMKHKEVGILHQQIEEHEKTKqEMAMEYKEELLKLQEEEFRQKSLDW---EKQRLIYQQQVSSLEAQRKA 193
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEGYELLKEKealERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 194 LAEQSEIIQAQLANRKQKLESVE-----------LSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTIL 262
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNkkikdlgeeeqLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 263 QDHRQKEEKLRESEKLLEALQEEQKELKASLQsqetfILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERkysSPGQGV 342
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELE-----DLRAELEEVDKEFAETRDELKDYREKLEKLKREI---NELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 343 LDNVLSQLDFSHSSEELLQAEVTRLEGSLesvsatcKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSS 422
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330
....*....|....*.
gi 1907198326 423 alegMKMEISQLTREL 438
Cdd:TIGR02169 481 ----VEKELSKLQREL 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-513 |
3.26e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 182 QQVSSLEAQR------KALAEQSEIIQAQLA---------------NRKQKLESVELSSQSEIQHLNSKLERAKDTICAN 240
Cdd:COG1196 200 RQLEPLERQAekaeryRELKEELKELEAELLllklreleaeleeleAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 241 ELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLkavgtqq 320
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 321 sverpLEDCQKERKysspgqgvldnvlsqldfshSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNN 400
Cdd:COG1196 353 -----LEEAEAELA--------------------EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 401 EyRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQL 480
Cdd:COG1196 408 A-EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350
....*....|....*....|....*....|...
gi 1907198326 481 ESLKLENHRLSETVMKLELGLHEAKEISLADLQ 513
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
121-551 |
2.17e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 121 ALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEEEFRQKSLDWEKQ------RLIYQQQVSSLEAQRKAL 194
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNatrhlcNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 195 AEQSEIIQA--QLANRKQKLESV--ELSSQSEIQHLNSKLERAKDTICANELEiERLNIRVNDLMGTNMTILQDHRQKEE 270
Cdd:pfam05483 176 YEREETRQVymDLNNNIEKMILAfeELRVQAENARLEMHFKLKEDHEKIQHLE-EEYKKEINDKEKQVSLLLIQITEKEN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 271 KLRESEKLLEALQEE--QKELKASLQSQETFILEAKMQ------EKLQTTL-KAVGTQQSVERPL-----------EDCQ 330
Cdd:pfam05483 255 KMKDLTFLLEESRDKanQLEEKTKLQDENLKELIEKKDhltkelEDIKMSLqRSMSTQKALEEDLqiatkticqltEEKE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 331 KERKYSSPGQGVLDNVLSQLDFSHSS-EELLQAEVTRLEGSLESVsatcKQLSQELMEKYEELKRMEGHNNEYRTEIKKL 409
Cdd:pfam05483 335 AQMEELNKAKAAHSFVVTEFEATTCSlEELLRTEQQRLEKNEDQL----KIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 410 KeQILQADQTY----------SSALEGMKMEISQL----TRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKE 475
Cdd:pfam05483 411 K-KILAEDEKLldekkqfekiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198326 476 ILSQLESLKLENHRLSETV--MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKK 551
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-413 |
2.18e-08 |
|
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: 57.77 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 55 EDLEMEALLEGIQNRghsggfLTSCEAELQELMKQIDIMVAhKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVG 134
Cdd:TIGR02169 675 ELQRLRERLEGLKRE------LSSLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 135 ILHQQIEEHEKTKQEMAMEYKEELLKLQEEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAqLANRKQKLES 214
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE-IEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 215 VELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLmgtnmtiLQDHRQKEEKLRESEKLLEALQEEQKELKASLQ 294
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 295 SQETFILEAKMQ----EKLQTTLKA-VGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDfshsseellqaEVTRLEG 369
Cdd:TIGR02169 900 ELERKIEELEAQiekkRKRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ-----------RVEEEIR 968
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907198326 370 SLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI 413
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-533 |
4.37e-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: 56.99 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 180 YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVEL---SSQSEIQHLNSKLERAKDTICANELEIERLNIR----VN 252
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERlanlER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 253 DLMGTNMTILQDHRQKEEKlresEKLLEALQEEQKELKASLQSqetfiLEAKMQEKlqttlkaVGTQQSVERPLEDCQKE 332
Cdd:TIGR02168 317 QLEELEAQLEELESKLDEL----AEELAELEEKLEELKEELES-----LEAELEEL-------EAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 333 rkysspgqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYR-TEIKKLKE 411
Cdd:TIGR02168 381 ----------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 412 QILQADQTYSSALEGMKMEISQLTRELHQ--RDITIASAKCSSsdmekqLKAEMQKAEEKAVEHKEILSQLESLKLENHR 489
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAaeRELAQLQARLDS------LERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907198326 490 LSEtVMKLELGLHEAKEISLAdlqenyiEALNKLVSENQQLQKD 533
Cdd:TIGR02168 525 LSE-LISVDEGYEAAIEAALG-------GRLQAVVVENLNAAKK 560
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-543 |
4.63e-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: 56.60 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 183 QVSSLEAQRKAlAEQSEIIQAQL--------ANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRvndl 254
Cdd:TIGR02168 201 QLKSLERQAEK-AERYKELKAELrelelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE---- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 255 mgtnmtilqdHRQKEEKLRESEKLLEALQEEQKELKASLQsqetfILEAKMQEkLQTTLKAVGTQqsverpledcqkerk 334
Cdd:TIGR02168 276 ----------VSELEEEIEELQKELYALANEISRLEQQKQ-----ILRERLAN-LERQLEELEAQ--------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 335 ysspgqgvLDNVLSQLDfshsseeLLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIkklkeqil 414
Cdd:TIGR02168 325 --------LEELESKLD-------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 415 qadQTYSSALEGMKMEISQLTRELHQRDITIAsakcSSSDMEKQLKAEMQKAEEKAVEH--KEILSQLESLKLENHRLSE 492
Cdd:TIGR02168 382 ---ETLRSKVAQLELQIASLNNEIERLEARLE----RLEDRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQE 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907198326 493 tvmklELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEH 543
Cdd:TIGR02168 455 -----ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
82-376 |
6.47e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 82 ELQELMKQIDIMVAHKKSEW-EGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLK 160
Cdd:COG1196 217 ELKEELKELEAELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 161 LQEEefrQKSLDWEKQRLI-YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTIcA 239
Cdd:COG1196 297 LARL---EQDIARLEERRReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE-A 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 240 NELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESE----KLLEALQEEQKELKASLQSQETFILEAKM--QEKLQTTL 313
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeallERLERLEEELEELEEALAELEEEEEEEEEalEEAAEEEA 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907198326 314 KAVGTQQSVERPLEDCQKERKYsspGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSA 376
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAAL---LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
80-555 |
7.10e-08 |
|
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: 56.28 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 80 EAELQELMKQIDIMVAHKKSEWEGQ----------THALETCLDIRDRELKALRSQLDMkhkevgiLHQQIEEHEKTKQE 149
Cdd:pfam15921 116 QTKLQEMQMERDAMADIRRRESQSQedlrnqlqntVHELEAAKCLKEDMLEDSNTQIEQ-------LRKMMLSHEGVLQE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 150 MAMEYKEELLKLQEEEFRQKSLdwekQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHL-NS 228
Cdd:pfam15921 189 IRSILVDFEEASGKKIYEHDSM----STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLlQQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 229 KLERAKDTICANELEIERLNIRVN------DLMGTNMTILQDH--RQKEEKLRESEKLLEALQEEQKELKASLQSQETFI 300
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASsarsqaNSIQSQLEIIQEQarNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKI 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 301 LEAKMQEKLQTTlkavgtqqsverPLEDCQKERKYSSPGQGVLDNVLSQL--DFSHSSEEL-LQAEVT-RLEGSLESVSA 376
Cdd:pfam15921 345 EELEKQLVLANS------------ELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKELsLEKEQNkRLWDRDTGNSI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 377 TCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQ----------TYSSALEGMKMEISQLTRELHQRDITIA 446
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 447 SAKCSSSDMEKQLKAEMQKAEEKAVEHKEI-------LSQLESLKLENHRLSETVMKLE-LGLHEAKEISLADLQENYIE 518
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHLRNVQTECEaLKLQMAEKDKVIEILRQQIE 572
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1907198326 519 ALNKLVS-----------ENQQLQKDLMSTKSELEHATNMCKKKDGEI 555
Cdd:pfam15921 573 NMTQLVGqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
80-381 |
7.98e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 80 EAELQELMKQIDIMVAhKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQI-----EEHEKTKQEMAMEY 154
Cdd:TIGR02169 222 EYEGYELLKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 155 KEELLKLQEEEFRQKSL-DWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLANRKQKLESVELSSQSEIQHLNSKL 230
Cdd:TIGR02169 301 AEIASLERSIAEKERELeDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 231 ERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLqsqETFILEAKMQE-KL 309
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK---EDKALEIKKQEwKL 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907198326 310 QTTLKAVGT-QQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQL 381
Cdd:TIGR02169 458 EQLAADLSKyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-423 |
1.30e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 174 EKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLNSKLERAKDTICANELEIERLNIRVND 253
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 254 LMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKmQEKLQTTLKAVGTQQSVERPLEDCQKER 333
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE-AELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 334 KYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI 413
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250
....*....|
gi 1907198326 414 LQADQTYSSA 423
Cdd:COG1196 480 AELLEELAEA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-353 |
3.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 97 KKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEEEFRQKSLD---- 172
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqle 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 173 --------WEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQS---EIQHLNSKLERAKDTICANE 241
Cdd:TIGR02168 320 eleaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 242 LEIERLNIRVNDLMGTNMTILQDHRQKEEKLRES------------EKLLEALQEEQKELKASLQSQETFILEAkmQEKL 309
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEA--EQAL 477
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907198326 310 QTTLKAVGTQQSVERPLEDCQkeRKYSSPGQGVLDNVLSQLDFS 353
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQ--ENLEGFSEGVKALLKNQSGLS 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
114-546 |
4.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 114 IRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAmeykEELLKLQEEEFRQKSLDWEKQRLIYQQQVSSLEAQRKA 193
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 194 LAEQSEIIQAQLANRKQKLESVElSSQSEIQHLNSKLERAKDTIC-ANELEIERLNIRVNDLmgtnmtilqdhrqkEEKL 272
Cdd:COG4717 144 LPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL--------------QQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 273 RESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTT--LKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQL 350
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 351 DFSHSSEELLQAEVTRLEGSLEsvsATCKQLSQELMEKYeeLKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKmE 430
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQAL---PALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-E 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 431 IsQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELglheakEISLA 510
Cdd:COG4717 363 L-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL------EEELE 435
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907198326 511 DLQEnyieALNKLVSENQQLQKDLMSTKSELEHATN 546
Cdd:COG4717 436 ELEE----ELEELEEELEELREELAELEAELEQLEE 467
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
176-496 |
9.85e-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: 52.53 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 176 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDL- 254
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 255 MGTNMTILQDHRQKEEKLRESEKLLEALQeeqKELKASLQSQETFILEAKMQeKLQTTLKAVGT---------------Q 319
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLD---KKHQAWLEEQKEQKREARTE-KQAYWQVVEGAldaqlallkaaiaarR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 320 QSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfshsseellQAEVTRLEGSLESvsatCKQLSQELMEKYEELK-RMEGH 398
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVDPDVIAKL----------KREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 399 NNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDitiaSAKCSSSDMEKQLKAEMQK---------AEEK 469
Cdd:pfam12128 809 RPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE----KQQVRLSENLRGLRCEMSKlatlkedanSEQA 884
|
330 340
....*....|....*....|....*..
gi 1907198326 470 AVEHKEILSQLESLKLENHRLSETVMK 496
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
41-605 |
1.05e-06 |
|
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: 52.43 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 41 KSRSSRTQSCcqnkedlEMEALLEGIQNRGHSGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDREL 119
Cdd:pfam15921 286 KASSARSQAN-------SIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 120 KALRSQLDMKHKEVGILHQQIE----EHEKTKQEMAMEYKEELLKLQEEEFRQKSLD----------WEKQRL------- 178
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQkllaDLHKREKELSLEKEQNKRLWDRDTGNSITIDhlrrelddrnMEVQRLeallkam 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 179 ------IYQQQVSSLEAQRKALaEQSEIIQAQLANRKQKLESV--EL--------SSQSEIQHLNSKLERAKDTICANEL 242
Cdd:pfam15921 439 ksecqgQMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVveELtakkmtleSSERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 243 EIERLNIRVNdlmgTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQsqetfILEAKMQEKLQ------TTLKAV 316
Cdd:pfam15921 518 EITKLRSRVD----LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE-----ILRQQIENMTQlvgqhgRTAGAM 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 317 GTQQS-VERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELlqAEVTRLEGSLESVSATcKQLSQELMEKYEELKRM 395
Cdd:pfam15921 589 QVEKAqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL--EKVKLVNAGSERLRAV-KDIKQERDQLLNEVKTS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 396 EGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSSD-------MEKQLKAE------ 462
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKrgqida 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 463 -----------MQKA--------EEK----------AVEHKEILSQLESLKLENHRLSETVMKLELGLHEAkEISLADLQ 513
Cdd:pfam15921 746 lqskiqfleeaMTNAnkekhflkEEKnklsqelstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA-SLQFAECQ 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 514 EnyiealnkLVSENQQlqkdlMSTKSELEHATNMckkkdGEIFNPAHSRAAGFKNAELKPIHGQHRHDGIKTEQYKT--- 590
Cdd:pfam15921 825 D--------IIQRQEQ-----ESVRLKLQHTLDV-----KELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTAsfl 886
|
650
....*....|....*
gi 1907198326 591 GHHSPRGQTLDSiDP 605
Cdd:pfam15921 887 SHHSRKTNALKE-DP 900
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-555 |
1.84e-06 |
|
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: 51.17 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 118 ELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEEEfrQKSLDWEKQRLIYQQQVSSLEAQRKALAEQ 197
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLN--NKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 198 SEIIQAQLANRKQKLESVELSSQ------SEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEK 271
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 272 LRESEKLLEALQEEQKELKASLQSQETFILEAKmQEKLQTTLKAVGTQqsverpLEDCQKErkysspgqgvLDNVLSQLD 351
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLN-NQKEQDWNKELKSE------LKNQEKK----------LEEIQNQIS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 352 FSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQIlqadqtysSALEGMKMEI 431
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI--------NDLESKIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 432 SQLTRELhqrditiasakcsssdmEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEAKeiSLAD 511
Cdd:TIGR04523 404 EKLNQQK-----------------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD--NTRE 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907198326 512 LQENYIEAL----NKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 555
Cdd:TIGR04523 465 SLETQLKVLsrsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-557 |
1.93e-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: 51.61 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 228 SKLERAKdticaNELEIERLNIRVNDLmgtnmtILQDHRQKEEKLR-ESEKLlealqEEQKELKASLQSQETFILeAKMQ 306
Cdd:TIGR02169 170 RKKEKAL-----EELEEVEENIERLDL------IIDEKRQQLERLRrEREKA-----ERYQALLKEKREYEGYEL-LKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 307 EKLQTTLKAVGTQ-QSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfSHSSEELLQAEVTRLEGSLESVSATCKQLSQEL 385
Cdd:TIGR02169 233 EALERQKEAIERQlASLEEELEKLTEEISELEKRLEEIEQLLEEL--NKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 386 MEKYEELKRMEGHNNEYRTEIKKLKEQILQADQtyssALEGMKMEISQLTRELhqrditiasakcssSDMEKQLKAEMQK 465
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELER----EIEEERKRRDKLTEEY--------------AELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 466 AEEKAVEHKE--------------ILSQLESLKLENHRLSETVMKLELGLHEAKEiSLADLqenyIEALNKLVSENQQLQ 531
Cdd:TIGR02169 373 LEEVDKEFAEtrdelkdyreklekLKREINELKRELDRLQEELQRLSEELADLNA-AIAGI----EAKINELEEEKEDKA 447
|
330 340
....*....|....*....|....*.
gi 1907198326 532 KDLMSTKSELEHATNMCKKKDGEIFN 557
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYD 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
192-551 |
2.28e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 192 KALAEQSEIIQAQLANRKQKLESVeLSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEK 271
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEV-LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 272 LRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVGTQ---------------QSVERPLEDCQKERKYS 336
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekrlsrleeeiNGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 337 SPGQGVLDNVLSQLDFSHSSEELLQaEVTRLEGSLESVSATCKQLSQELMEKyeELKRMEGHNNEYRTEIKKLKEQILQA 416
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 417 DQTYSS------ALEGMKMEISQLTREL--HQRDITIASAKCSSSDMEKqlkaEMQKAEEKAVEHKEILSQLESLKLENH 488
Cdd:PRK03918 418 KKEIKElkkaieELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEK----ELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198326 489 RLS---ETVMKLELGLHEAKEISLADLQENYiEALNKLVSENQQLQKDLMSTKSELEHATNMCKKK 551
Cdd:PRK03918 494 ELIklkELAEQLKELEEKLKKYNLEELEKKA-EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-557 |
3.21e-06 |
|
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: 50.40 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 181 QQQVSSLEAQRKALAEQSEIIQAQLAN-RKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNM 259
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 260 TILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFI--LEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSS 337
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 338 PGQGVLDNVLSQLDFSHSSEEL-----------LQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEI 406
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELiiknldntresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 407 KKLKEQI---LQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSSDMEK-----QLKAEMQKAEEKAVEHKEILS 478
Cdd:TIGR04523 513 KDLTKKIsslKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 479 QLESLKLE-NHRLSETVMKL-----ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDL---MSTKSELEHATNMCK 549
Cdd:TIGR04523 593 QKEKEKKDlIKEIEEKEKKIsslekELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIkeiRNKWPEIIKKIKESK 672
|
....*...
gi 1907198326 550 KKDGEIFN 557
Cdd:TIGR04523 673 TKIDDIIE 680
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-555 |
8.45e-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: 49.28 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 257 TNMTILqdHRQKEekLRESEKLLEALQEEQKELKASLQSqetfiLEAKMQEKLQTTLKAVGTQQSVERPLEDCQKerkys 336
Cdd:TIGR02168 668 TNSSIL--ERRRE--IEELEEKIEELEEKIAELEKALAE-----LRKELEELEEELEQLRKELEELSRQISALRK----- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 337 spgqgvldnvlsQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQA 416
Cdd:TIGR02168 734 ------------DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 417 DQTYSSAlegmKMEISQLTRELHQRDITIASakcsssdMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMK 496
Cdd:TIGR02168 802 REALDEL----RAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907198326 497 LELGLHEAKEISlaDLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 555
Cdd:TIGR02168 871 LESELEALLNER--ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-555 |
3.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 117 RELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAmeykeellklqeeefrqksldwEKQRliyqqQVSSLEAQRKALAE 196
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIE----------------------ELEK-----ELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 197 QSEIIQAQLANRKQKLESVE-----LSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEK 271
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 272 LRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVgTQQSVERPLEDCQKERKYSspgQGVLDNVLSQLD 351
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEI---EEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 352 FSHSSEELLQAEVTRLEGSlESVSATCKQL-----SQELMEKY-EELKRMEGHNNEYRTEIKKLKEQILQADQTYS---- 421
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKA-KGKCPVCGRElteehRKELLEEYtAELKRIEKELKEIEEKERKLRKELRELEKVLKkese 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 422 -SALEGMKMEISQLTRELHQRDITIASAKcsSSDMEK------QLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETV 494
Cdd:PRK03918 495 lIKLKELAEQLKELEEKLKKYNLEELEKK--AEEYEKlkekliKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL 572
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907198326 495 MKL-----ELGLHEAKEI-----SLADLQENYIEALNkLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 555
Cdd:PRK03918 573 AELlkeleELGFESVEELeerlkELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
180-351 |
5.27e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.88 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 180 YQQQVSSLEAQRKALAEQSEIIQAQLaNRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNdlmgtNM 259
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAEL-DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA-----RR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 260 TIL--QDHRQKeEKLRESEKLLEALQEEQKELKASL--------QSQETFILEAKmQEKLQTTLKAVGTQQSVERPLEDC 329
Cdd:pfam00529 130 RVLapIGGISR-ESLVTAGALVAQAQANLLATVAQLdqiyvqitQSAAENQAEVR-SELSGAQLQIAEAEAELKLAKLDL 207
|
170 180
....*....|....*....|...
gi 1907198326 330 QK-ERKysSPGQGVLDNVLSQLD 351
Cdd:pfam00529 208 ERtEIR--APVDGTVAFLSVTVD 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-563 |
5.93e-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: 46.59 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 53 NKEDLEMEALLEGIQNRGHSGGFLTS-CEAELQELMKQIDIMVAhKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHK 131
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISrLEQQKQILRERLANLER-QLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 132 EVGILHQQIEEHEKTKQEMamEYKEELLKLQEEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQK 211
Cdd:TIGR02168 352 ELESLEAELEELEAELEEL--ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 212 LESVELS-SQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELK 290
Cdd:TIGR02168 430 LEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 291 ASLQSQETF-----------------------ILEAKMQ----EKLQTTLKAVGTQ------------------------ 319
Cdd:TIGR02168 510 ALLKNQSGLsgilgvlselisvdegyeaaieaALGGRLQavvvENLNAAKKAIAFLkqnelgrvtflpldsikgteiqgn 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 320 -----QSVERPLEDCQKERKYSSPGQGVLDNVLSQ----------LDFSHSSEEL-----LQAEVTRLEGS--------- 370
Cdd:TIGR02168 590 dreilKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddldnaLELAKKLRPGyrivtLDGDLVRPGGVitggsaktn 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 371 ---------LESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQtyssALEGMKMEISQLTRELHQR 441
Cdd:TIGR02168 670 ssilerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR----QISALRKDLARLEAEVEQL 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 442 DITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEAKEIsLADLQENYIEALN 521
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRE 824
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907198326 522 KLvsenQQLQKDLMSTKSELEHATNMCKKKDGEIFNPAHSRA 563
Cdd:TIGR02168 825 RL----ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-542 |
7.96e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 240 NELEIERLNI-RVNDLMG---TNMTILQDHRQKEEKLREseklleaLQEEQKELKASLQSQETFILEAKMQEKLQTTLKA 315
Cdd:COG1196 179 RKLEATEENLeRLEDILGeleRQLEPLERQAEKAERYRE-------LKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 316 VGTQQSVERPLEDCQKERKysspgqgVLDNVLSQLDFS----HSSEELLQAEVTRLEGSLESVSATCKQLS---QELMEK 388
Cdd:COG1196 252 EAELEELEAELAELEAELE-------ELRLELEELELEleeaQAEEYELLAELARLEQDIARLEERRRELEerlEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 389 YEELkrmEGHNNEYRTEIKKLKEQILQADQTYSSALEgmkmEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEE 468
Cdd:COG1196 325 LAEL---EEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198326 469 KAVEHKEILSQLESLKLENHRLSETVMKLELGL--HEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELE 542
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALaeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
76-532 |
8.49e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 76 LTSCEAELQELMKQIDImvAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVgilhQQIEEHEKTKQEMAMEYK 155
Cdd:TIGR00618 272 LRAQEAVLEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL----MKRAAHVKQQSSIEEQRR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 156 EELLKLQEEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESV---------ELSSQSEIQ-- 224
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILqreqatidtRTSAFRDLQgq 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 225 ----HLNSKLERAKDTIC----ANELEIERLNIRVNDLMGTNM--------TILQDHRQKEEKLRESEKLLEALQEEQKE 288
Cdd:TIGR00618 426 lahaKKQQELQQRYAELCaaaiTCTAQCEKLEKIHLQESAQSLkereqqlqTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 289 LKASLQSQEtfileakmqEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLE 368
Cdd:TIGR00618 506 LCGSCIHPN---------PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 369 GSLESVSATCKQLSQELME---------KYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELH 439
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRlqdlteklsEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 440 QRDITIASAkcsSSDMEKQLKAEMQKAEEKAVEH--------KEILSQLESLKLENHRLSETVMKLELGLHEAKEISLAD 511
Cdd:TIGR00618 657 QERVREHAL---SIRVLPKELLASRQLALQKMQSekeqltywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
|
490 500
....*....|....*....|.
gi 1907198326 512 LQENyIEALNKLVSENQQLQK 532
Cdd:TIGR00618 734 LAAR-EDALNQSLKELMHQAR 753
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
181-506 |
9.12e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 181 QQQVSSLEAQRKALAEQseiiQAQLANRKQKLESVELS-SQSEIQHLNSKL----ERAKDTICANELEIERlniRVNDLM 255
Cdd:COG3096 784 EKRLEELRAERDELAEQ----YAKASFDVQKLQRLHQAfSQFVGGHLAVAFapdpEAELAALRQRRSELER---ELAQHR 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 256 GTNmtilQDHRQKEEKLRESEKLLEALQEEqkelkASLQSQETfiLEAKMQEklqttlkavgtqqsVERPLEDCQKERKY 335
Cdd:COG3096 857 AQE----QQLRQQLDQLKEQLQLLNKLLPQ-----ANLLADET--LADRLEE--------------LREELDAAQEAQAF 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 336 -SSPGQ--GVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSqELMEK-----YEELKRMEGHNNEYRTeik 407
Cdd:COG3096 912 iQQHGKalAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS-EVVQRrphfsYEDAVGLLGENSDLNE--- 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 408 KLKEQILQADQTYSSALEGMKMEISQLTrELHQRDITIASAKCSSSDMEKQLKAEMQK--------AEEKAVEHK----- 474
Cdd:COG3096 988 KLRARLEQAEEARREAREQLRQAQAQYS-QYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeAEERARIRRdelhe 1066
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907198326 475 ----------EILSQLESLKLENHRLSETVMKLELGLHEAKE 506
Cdd:COG3096 1067 elsqnrsrrsQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-334 |
1.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 181 QQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLNSKLERAKDTI------------CANELE----- 243
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELgeraralyrsggSVSYLDvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 244 ------IERLNIrVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETfILEAKMQEKLQTTLKAVG 317
Cdd:COG3883 112 esfsdfLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-ELEAQQAEQEALLAQLSA 189
|
170
....*....|....*..
gi 1907198326 318 TQQSVERPLEDCQKERK 334
Cdd:COG3883 190 EEAAAEAQLAELEAELA 206
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
123-551 |
2.51e-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: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 123 RSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEEEFRQKSLDWEKQRLIYQQQ--VSSLE----------AQ 190
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDhlTKELEdikmslqrsmST 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 191 RKALAEQSEIIQAQLANRKQKLES-VELSSQSEIQHlNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKE 269
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAH-SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 270 EKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKavGTQQSVERPLEDCQKErkysspgqgvLDNVLSQ 349
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK--GKEQELIFLLQAREKE----------IHDLEIQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 350 LDFSHSSEELLQAEVTRLEGSLES-------VSATCKQLSQELMEKYEELKRMEGHNNEYRTEI---KKLKEQILQADQT 419
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 420 YSSALEGMKMEISQLTRELHQRDITIasaKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLEl 499
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH- 614
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907198326 500 glHEAKEISLADLQENyiEALNKLVSENQQLQKDLMSTKSELEHATNMCKKK 551
Cdd:pfam05483 615 --QENKALKKKGSAEN--KQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-413 |
2.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 181 QQQVSSLEAQRKALAEQSEII----------------QAQLANRKQKLESVELSsqseiqhlNSKLERAKDTICANELEI 244
Cdd:COG4913 630 EERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELERLDAS--------SDDLAALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 245 ERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQK-----ELKASLQSQETFILEAKMQEKLQTTLKAVGTQ 319
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAVERELRENLEERIDALRAR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 320 QS-VERPLEDCQKE--RKYSSPGQGVLDNVLSQLDFshsseellQAEVTRLEGSlesvsatckqlsqELMEKYEELKRME 396
Cdd:COG4913 782 LNrAEEELERAMRAfnREWPAETADLDADLESLPEY--------LALLDRLEED-------------GLPEYEERFKELL 840
|
250 260
....*....|....*....|....*.
gi 1907198326 397 GHNN---------EYRTEIKKLKEQI 413
Cdd:COG4913 841 NENSiefvadllsKLRRAIREIKERI 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-328 |
2.84e-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: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 107 ALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEEEFRQKSLDWEKQRLiyQQQvss 186
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 187 LEAQRKALAEQseIIQAQLANRKQKLESveLSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNmtilqdhR 266
Cdd:COG4942 99 LEAQKEELAEL--LRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-------A 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907198326 267 QKEEKLRESEKLLEALQEEQKELKASLQSQETfiLEAKMQEKLQTTLKAVGTQQSVERPLED 328
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQK--LLARLEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
80-304 |
3.89e-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: 43.21 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 80 EAELQELMKQIDIM------VAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAME 153
Cdd:COG4942 26 EAELEQLQQEIAELekelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 154 YKEELLKLqeeefrQKSLDWEKQRLIYQQQvSSLEAQRKAlaeqsEIIQAQLANRKQKLESVElSSQSEIQHLNSKLERA 233
Cdd:COG4942 106 LAELLRAL------YRLGRQPPLALLLSPE-DFLDAVRRL-----QYLKYLAPARREQAEELR-ADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907198326 234 KDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESeklLEALQEEQKELKASLQSQETFILEAK 304
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
80-489 |
4.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 80 EAELQELMKQIDiMVAHKKSEWEGQTHALETCLDIRD--RELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAM--EYK 155
Cdd:COG4717 94 QEELEELEEELE-ELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEEleAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 156 EELLKLQEEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLEsvELSSQSEIQHLNSKLERAK- 234
Cdd:COG4717 173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE--QLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 235 -----DTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKL 309
Cdd:COG4717 251 llliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 310 QTTLKAVGTQQSVERPLEDCQKERKYSSpgqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLsQELMEKY 389
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEE-----LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 390 EELK-RMEGHNNEYRTEIKKL-KEQILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAE 467
Cdd:COG4717 405 EELEeQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
410 420
....*....|....*....|..
gi 1907198326 468 EKAVEHKEILSQLESLKLENHR 489
Cdd:COG4717 485 LRELAEEWAALKLALELLEEAR 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-542 |
5.84e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 320 QSVERPLEDCQKERkysSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQ-------LSQELMEKYEEL 392
Cdd:TIGR02169 684 EGLKRELSSLQSEL---RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 393 KRMEGHNNEYRTEIKKLKEQILQADQTYSSAlegmkmEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVE 472
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 473 HKEILSQLESLKLENHRLSETVMKLELGLHEAKEIsladlQENYIEALNKLVSENQQLQKDLMSTKSELE 542
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
128-430 |
1.27e-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: 42.03 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 128 MKHKEVGILHQQIEEHEKT--------KQEMAMEYKEELLKLQEEEFRQKSLDweKQRLIYQQQvssleaQRKALAEQSE 199
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMeqerlrqeKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQ------ERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 200 IIQAQLANRKQKLE-------SVELSSQSEIQHLNSKLERaKDTICANELEIERlnirvndlmgtNMTILQDHRQKeeKL 272
Cdd:pfam17380 350 LERIRQEERKRELErirqeeiAMEISRMRELERLQMERQQ-KNERVRQELEAAR-----------KVKILEEERQR--KI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 273 RESEKLLEALQEEQKELKaslQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSspgqgvLDNVLSQLDF 352
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEAR---QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKK------LELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 353 SHSSEE---LLQAEVTRLEGSLESVSATCKQLSQELMEK----YEELKRMEGHnNEYRTEI-----KKLKEQILQADQTy 420
Cdd:pfam17380 487 KRAEEQrrkILEKELEERKQAMIEEERKRKLLEKEMEERqkaiYEEERRREAE-EERRKQQemeerRRIQEQMRKATEE- 564
|
330
....*....|
gi 1907198326 421 SSALEGMKME 430
Cdd:pfam17380 565 RSRLEAMERE 574
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-365 |
2.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 166 FRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESV-----ELSSQSEIQHLNSKLERAkdtic 238
Cdd:COG3206 201 FRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQLRAQLAEL----- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 239 anELEIERLNIRVNDlmgtnmtilqDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFIL--EAKMQEKLQTTLKAV 316
Cdd:COG3206 276 --EAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQarEASLQAQLAQLEARL 343
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907198326 317 GTQQSVERPLEdcQKERKYSSpGQGVLDNVLSQLDFSHSSEELLQAEVT 365
Cdd:COG3206 344 AELPELEAELR--RLEREVEV-ARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-545 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 265 HRQKEE---KLRESEKLLEALQEEQKELKASLQSQEtfiLEAKMQEK---LQTTLKAVGTQQSVERpLEDCQKErkyssp 338
Cdd:TIGR02168 171 KERRKEterKLERTRENLDRLEDILNELERQLKSLE---RQAEKAERykeLKAELRELELALLVLR-LEELREE------ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 339 gqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLEsvsatckQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQ 418
Cdd:TIGR02168 241 ----LEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 419 TYSSALEGMKMEISQLTRELHQRDITIASAKcSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETV---- 494
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskv 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907198326 495 --MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHAT 545
Cdd:TIGR02168 389 aqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
179-448 |
3.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 179 IYQQQvsSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqseiqhlnsklerakdticaNELEIERLNIRVNDLMGTN 258
Cdd:COG3206 160 AYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAE-----------------------AALEEFRQKNGLVDLSEEA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 259 MTILQdhrqkeeKLRESEKLLEALQEEQKELKASLQSqetfiLEAKMQEKLQT--TLKAVGTQQSVERPLEDCQKE---- 332
Cdd:COG3206 215 KLLLQ-------QLSELESQLAEARAELAEAEARLAA-----LRAQLGSGPDAlpELLQSPVIQQLRAQLAELEAElael 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 333 RKYSSPGQGVLDNVLSQLDfshSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 412
Cdd:COG3206 283 SARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907198326 413 ILQADQTYSSALEgmKMEISQLTRELHQRDITIASA 448
Cdd:COG3206 360 VEVARELYESLLQ--RLEEARLAEALTVGNVRVIDP 393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
263-572 |
3.74e-03 |
|
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: 40.80 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 263 QDHRQKEEKLRESEKLLEALQEEQKELKasLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLED------CQKERKYS 336
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLFDVCGSQDEESD--LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvCQRVFQTE 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 337 SPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQA 416
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 417 DQTYSSALEGMK-----------MEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKL 485
Cdd:TIGR00606 771 ETLLGTIMPEEEsakvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 486 ENHRLSETVMKL-----ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEIFNPAH 560
Cdd:TIGR00606 851 LIQDQQEQIQHLksktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
330
....*....|..
gi 1907198326 561 SRAAGFKNAELK 572
Cdd:TIGR00606 931 SKETSNKKAQDK 942
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
256-456 |
3.97e-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: 40.32 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 256 GTNMTILQDHRQKEEKLRES-EKLLEALQEEQKELKASLQSQETFILEAKMQEK--LQTTLKAVGTQQSVERPLEDCQKE 332
Cdd:pfam07902 132 GIATRISEDTDKKLALINETiSGIRREYQDADRQLSSSYQAGIEGLKATMASDKigLQAEIQASAQGLSQRYDNEIRKLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 333 RKYSSPGQGVLDNVLSQLD-----FSHSSEELLQAEVTRLEGSLESVSATCKQLSQelmekyeELKRMEGHNNEYRTEIK 407
Cdd:pfam07902 212 AKITTTSSGTTEAYESKLDdlraeFTRSNQGMRTELESKISGLQSTQQSTAYQISQ-------EISNREGAVSRVQQDLD 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907198326 408 KLKEQILQADQTYSS---ALEGMKMEISQLTRELHQRDITIA---SAKCSSSDME 456
Cdd:pfam07902 285 SYQRRLQDAEKNYSSltqTVKGLQSTVSDPNSKLESRITQLAgliEQKVTRGDVE 339
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-542 |
4.45e-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: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 168 QKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ---LANRKQKLESVE-----LSSQSEIQHLNSKLERAKDTICA 239
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQeavLEETQERINRARkaaplAAHIKAVTQIEQQAQRIHTELQS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 240 NELEIERLnirvndlmgtnMTILQDHRQKEEKLRESEKLLEALQEEQKELkASLQSQETFILEAKMQEKlqTTLKAVGTQ 319
Cdd:TIGR00618 319 KMRSRAKL-----------LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI-RDAHEVATSIREISCQQH--TLTQHIHTL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 320 QSVERPLEDcqkERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHN 399
Cdd:TIGR00618 385 QQQKTTLTQ---KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 400 NE----YRTEIKKL--KEQILQADQTYSSALEGMKMEISQLTREL---------HQRDITIASAKCSSSDMEKQLKAEMQ 464
Cdd:TIGR00618 462 QEsaqsLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEPCPLcgscihpnpARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 465 KAEEKaVEHK--EILSQLESLKLENHRLSETVMKLELGLHEAKEIslADLQENYIEALNKLVSENQQLQKDLMSTKSELE 542
Cdd:TIGR00618 542 TSEED-VYHQltSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--IPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-416 |
5.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 180 YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTnm 259
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 260 tiLQDHRQKEEKLRESE-----KLLEALQEEQKELKASLQSQETfiLEAKMQEKLQT-TLKAVGTQQSVERpledcqker 333
Cdd:COG4913 318 --LDALREELDELEAQIrgnggDRLEQLEREIERLERELEERER--RRARLEALLAAlGLPLPASAEEFAA--------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 334 kysspgqgVLDNVLSQLDFSHSSEELLQAEVTRLEGSLEsvsatckQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI 413
Cdd:COG4913 385 --------LRAEAAALLEALEEELEALEEALAEAEAALR-------DLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
...
gi 1907198326 414 LQA 416
Cdd:COG4913 450 AEA 452
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-324 |
5.89e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 76 LTSCEAELQELMKQIDIMVAHKKSEWEGQT-----HALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEM 150
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERleerrEDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 151 AMEYKEELLKLQEEEFRQKSLDWEKQRLI-----------YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSS 219
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLErirtllaaiadAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 220 QSE-IQHLNSKLERAKDTICANELEIERLNIRVNDLmgtnmtilqdhrQKEEKLRESE-KLLEALQEEQKELKASLQSQE 297
Cdd:PRK02224 644 DEArIEEAREDKERAEEYLEQVEEKLDELREERDDL------------QAEIGAVENElEELEELRERREALENRVEALE 711
|
250 260
....*....|....*....|....*..
gi 1907198326 298 TFILEAKMQEKLQTTLKAVGTQQSVER 324
Cdd:PRK02224 712 ALYDEAEELESMYGDLRAELRQRNVET 738
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
82-550 |
5.94e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 82 ELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMA----MEYKEE 157
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 158 LLKLQEEEFRQKSLDWEKQRL---IYQQQVSSLEAQRKALAEQSEIIQAQLA---NRKQKLESvELSSQSEIQHLNSKLE 231
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRrskIKEQNNRDIAGIKDKLAKIREARDRQLAvaeDDLQALES-ELREQLEAGKLEFNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 232 RAKdticaNELEIERLNIRVNDLMGTNMTILQdhrqkeekLRESEKLLEALQEEQKELKASlqsqetfileakmQEKLQT 311
Cdd:pfam12128 439 EYR-----LKSRLGELKLRLNQATATPELLLQ--------LENFDERIERAREEQEAANAE-------------VERLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 312 TLKAVGTQQsvERPLEDCQKERKYSSPGQGVLDNVLSQLD-FSHSSEELLQAEVTRLEGSLESVSATcKQLSQELMEKYE 390
Cdd:pfam12128 493 ELRQARKRR--DQASEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISP-ELLHRTDLDPEV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 391 ELKRMEGHNNEYrteikKLKEQILQADQTYSSALEgmkmeiSQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKA 470
Cdd:pfam12128 570 WDGSVGGELNLY-----GVKLDLKRIDVPEWAASE------EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 471 VEHKEILSQLESLKLENHRLSETVMKLELGLHEAkeisLADLQENYIEALNKLVSENQQLQKDLMSTKSE-----LEHAT 545
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFDEKQSEKDKKNKA----LAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkREART 714
|
....*
gi 1907198326 546 NMCKK 550
Cdd:pfam12128 715 EKQAY 719
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-394 |
5.95e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 203 AQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVndlmgtnmtilQDHRQKEEKLRE------SE 276
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-----------EEVEARIKKYEEqlgnvrNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 277 KLLEALQEEQKELKASLQSQETFILEAKMQ-EKLQTTLKAVGTQqsverpLEDCQKErkysspgqgvLDNVLSQLDfshS 355
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERiEELEEELAELEAE------LAELEAE----------LEEKKAELD---E 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907198326 356 SEELLQAEVTRLEGSLESVSATckqLSQELMEKYEELKR 394
Cdd:COG1579 150 ELAELEAELEELEAEREELAAK---IPPELLALYERIRK 185
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
220-496 |
7.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 220 QSEIQHLNSKLERAKDTICANELEIERLNIRVNDlmgtnmtILQDHRQKEEKLREsekllealqeEQKELKASLQSQETF 299
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE-------NIARKQNKYDELVE----------EAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 300 ILEAKMQ-EKLQTTLKAVGTQQS-VERPLEDCQKERKYSSPGqGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLEsvsat 377
Cdd:PHA02562 243 LLNLVMDiEDPSAALNKLNTAAAkIKSKIEQFQKVIKMYEKG-GVCPTCTQQISEGPDRITKIKDKLKELQHSLE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 378 ckqlsqELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSalegmkmeisqltrelhqrdiTIASAKcsssdmek 457
Cdd:PHA02562 317 ------KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT---------------------LVDKAK-------- 361
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907198326 458 QLKAEMQKAEEKAVEHKEILSQL-ESLKLENHRLSETVMK 496
Cdd:PHA02562 362 KVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSELVKE 401
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
37-413 |
7.35e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 37 LQRWKSRSSRTQSCCQNkedlEMEALLEGIQNRGHSGGFLTSCEAELQ---ELMKQIDIMVAHKKSEWEGQTHAL----- 108
Cdd:pfam15921 428 VQRLEALLKAMKSECQG----QMERQMAAIQGKNESLEKVSSLTAQLEstkEMLRKVVEELTAKKMTLESSERTVsdlta 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 109 -----ETCLDIRDRELKALRSQLDMKHKEVGILHQQiEEHEKTKQemameykeellkLQEEEFRQKSLDWEKQRLIYQQQ 183
Cdd:pfam15921 504 slqekERAIEATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQ------------TECEALKLQMAEKDKVIEILRQQ 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 184 VSSL-----EAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQhlNSKLERAKDTICANELEIERLNIRVNDLMGTN 258
Cdd:pfam15921 571 IENMtqlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKK--DAKIRELEARVSDLELEKVKLVNAGSERLRAV 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 259 MTILQDHRQKEEKLRESEKLLEALQEEQKELKASL--QSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYS 336
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198326 337 SPG-QGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI 413
Cdd:pfam15921 729 AMGmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
360-481 |
9.00e-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: 38.37 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 360 LQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQAD-----QTYSSALEGMKMEISQL 434
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKEIESLKRRISDL 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907198326 435 TRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLE 481
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-321 |
9.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 117 RELKALRSQLDMKHKEVGILhQQIEEHEKTKQEMAMEYKEELLKlqeeefRQKSLDWEKQRLI--YQQQVSSLEAQRKAL 194
Cdd:COG4913 235 DDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYL------RAALRLWFAQRRLelLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 195 AEQSEIIQAQLANRKQKLESVEL----SSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLmgtNMTILQDHRQKEE 270
Cdd:COG4913 308 EAELERLEARLDALREELDELEAqirgNGGDRLEQLEREIERLERELEERERRRARLEALLAAL---GLPLPASAEEFAA 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907198326 271 KLRESEKLLEALQEEQKELKASLQSQETFILEAKMQ-EKLQTTLKAVGTQQS 321
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRElRELEAEIASLERRKS 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
174-296 |
9.94e-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: 38.37 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198326 174 EKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNd 253
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKEIESLKRRISDLEDEILELMERIE- 120
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90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907198326 254 lmgtnmtilqdhrQKEEKLRESEKLLEALQEEQKELKASLQSQ 296
Cdd:COG1579 121 -------------ELEEELAELEAELAELEAELEEKKAELDEE 150
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