|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-412 |
2.59e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 122 YDEMRQKIRQLTQDLSVSHAQQdyLDSHIQAQASALDSFNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRHLQQTYEA 201
Cdd:TIGR02168 215 YKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 202 SMDKLREKQRQLEAAQMENQllkmRVESSQEANAEVMREMTRKLysqyeEKLQEAQRKHSAEKEVLLEETNSFLKAIEEA 281
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLA----NLERQLEELEAQLEELESKL-----DELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 282 NKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSgemaDSDKNRYQQLEEASASLRERIRHLDDMVH 361
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE----RLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 85701616 362 CQQKKVKQM----VEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRLDYL 412
Cdd:TIGR02168 440 AELEELEEEleelQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-409 |
2.75e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 174 LQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVEssQEANAEVMREMTRKLYSQYEEKL 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 254 QEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEmsgemAD 333
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-----AA 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85701616 334 SDKNRYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRL 409
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-401 |
1.44e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 96 QLKEEMNyIKDVRATLEKVRKRMyGDYDEMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALdsfnamnAALASDSVGLQ 175
Cdd:COG1196 217 ELKEELK-ELEAELLLLKLRELE-AELEELEAELEELEAELEELEAELAELEAELEELRLEL-------EELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 176 KTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQE--ANAEVMREMTRKLYSQYEEKL 253
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEelEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 254 QEAQRKHSAEkevlLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEmsgemAD 333
Cdd:COG1196 368 LEAEAELAEA----EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE-----EE 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85701616 334 SDKNRYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGE 401
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-425 |
3.47e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 93 STNQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAMNAALASDSV 172
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 173 GLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEaNAEVMREMTRKLYSQYEEk 252
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEE- 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 253 LQEAQRKHSAEKEVLLEETNSFLKAIEEANKKME--------------AAELSLEEKDQKIGELDRLIERMEKERHQLQL 318
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEelseelreleskrsELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 319 QLLEHEtEMSGEMAdsdKNRYQQLEEASASLRERIRHLddmvhcqQKKVKQM-------VEEIESLKkkvqqkqllilql 391
Cdd:TIGR02168 944 RLSEEY-SLTLEEA---EALENKIEDDEEEARRRLKRL-------ENKIKELgpvnlaaIEEYEELK------------- 999
|
330 340 350
....*....|....*....|....*....|....
gi 85701616 392 lEKISFLEGENNELQSRLDYLTETQPKTEVETRE 425
Cdd:TIGR02168 1000 -ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-426 |
3.68e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 192 IRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEAnaevMREMTRKLYSQYE--EKLQEAQRKHSAEKEVLLE 269
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKdlARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 270 ETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMS--GEMADSDKNRYQQLEEASA 347
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85701616 348 SLRERIRHLddmvhcqQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQPKTEVETREI 426
Cdd:TIGR02168 835 ATERRLEDL-------EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-426 |
1.61e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 95 NQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAMNAALASDSVGL 174
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 175 QKTLVDVTLENSHIKDQIRHLQ-QTYEASMDKLREKQRQLEAaqmenqllkmrveSSQEANAEVMREMTRKLYSqyEEKL 253
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEA-------------RLREIEQKLNRLTLEKEYL--EKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 254 QEAQRkhsaEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQL--LEHETEMSGEM 331
Cdd:TIGR02169 836 QELQE----QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLreLERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 332 ADSDKNRYQQLEEASASLRERIRHLDDMVHcQQKKVKQMVEEIESLKKKVqqkqlliLQLLEKISFLEGENN-------E 404
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEEELSLEDVQAEL-------QRVEEEIRALEPVNMlaiqeyeE 983
|
330 340
....*....|....*....|..
gi 85701616 405 LQSRLDYLTETQPKTEVETREI 426
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-426 |
5.09e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 276 KAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMADSDK---------NRYQQLEEAS 346
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaeveqleERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 347 ASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQPKTEVETREI 426
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
189-379 |
5.60e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 189 KDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMR-EMTRKLYSQYEEKLQEAqrkhsaekEVL 267
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREI--------EKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 268 LEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEK------ERHQLQLQLLEHETEMSGEMADSDKNRYQQ 341
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRLTGLTPEKLEKELEE 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 85701616 342 LEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKK 379
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-427 |
1.85e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 204 DKLREKQRQLEAAQMENQLLKMRvesSQEANAEVMREMTRKLYSQYEEKLQEaQRKHSAEKEVLLEETNSFLKA------ 277
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKDlgeeeq 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 278 ------IEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMADSDK--NRYQQLEEASASL 349
Cdd:TIGR02169 290 lrvkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKltEEYAELKEELEDL 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85701616 350 RERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQPKTEVETREIG 427
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-380 |
2.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 182 TLENSH-----IKDQIRHLQ------QTYEASMDKLREKQRQLEA-----AQMENQLLKMRVESSQEANAEVMREMTRkl 245
Cdd:COG4913 236 DLERAHealedAREQIELLEpirelaERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELER-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 246 ysqyeekLQEAQRKHSAEKEVLLEE-TNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIErmekerhQLQLQLLEHE 324
Cdd:COG4913 314 -------LEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLA-------ALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 85701616 325 TEMSgEMADSDKNRYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKK 380
Cdd:COG4913 380 EEFA-ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
96-414 |
2.19e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 96 QLKEEMNYIKDVRATLEKVRKRMygdyDEMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAMNAALASDSVGLQ 175
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKA----NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 176 KTLVDVTLENSHIKDQ-----------IRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVessQEANAEvMREMTrK 244
Cdd:pfam05483 324 KTICQLTEEKEAQMEElnkakaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL---QKKSSE-LEEMT-K 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 245 LYSQYEEKLQEAqRKHSAEKEVLLEETNSFLKAIEEankkmeaaelsLEEKDQkigELDRLIERMEKERHQLQLQLLEHE 324
Cdd:pfam05483 399 FKNNKEVELEEL-KKILAEDEKLLDEKKQFEKIAEE-----------LKGKEQ---ELIFLLQAREKEIHDLEIQLTAIK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 325 TemsgemadSDKNRYQQLEEASASL-RERIRHLDDMVHC-----QQKKVKQ----MVEEIESLKKKVQQKQLLILQLLEK 394
Cdd:pfam05483 464 T--------SEEHYLKEVEDLKTELeKEKLKNIELTAHCdklllENKELTQeasdMTLELKKHQEDIINCKKQEERMLKQ 535
|
330 340
....*....|....*....|
gi 85701616 395 ISFLEGENNELQSRLDYLTE 414
Cdd:pfam05483 536 IENLEEKEMNLRDELESVRE 555
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-313 |
2.67e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 95 NQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVSHAQQDYLDSHIqaqasaldsfnamnAALASDSVGL 174
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--------------AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 175 QKTLVDVTLEnshIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKmRVESSQEANAEVMREMTRKLYSQYEE--- 251
Cdd:COG4942 96 RAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAElea 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85701616 252 ---KLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKER 313
Cdd:COG4942 172 eraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
204-381 |
4.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 204 DKLREKQRQLEAAQMENQLLKMRVESSQEAnaevMREMTRKL--------YSQYEEKLQEAQRKHSAEKEVL--LEETNS 273
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE----LDALQERRealqrlaeYSWDEIDVASAEREIAELEAELerLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 274 FLKAIEEankKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMADSDKNRYQQLEEASASLRERi 353
Cdd:COG4913 686 DLAALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD- 761
|
170 180
....*....|....*....|....*...
gi 85701616 354 RHLDDMVHCQQKKVKQMVEEIESLKKKV 381
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
143-401 |
4.91e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.79 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 143 QDYLDSHIQAQASALDSFNAMNAALAS---------DSVGLQKTLVD-------VTLENSHIKDQIRH-LQQTYEASMDK 205
Cdd:pfam05667 191 LPPVTAQPSSRASVVPSLLERNAAELAaaqeweeewNSQGLASRLTPeeyrkrkRTKLLKRIAEQLRSaALAGTEATSGA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 206 LREKQ---RQLEAAQMEN----QLLKM----RVESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAEKEVLLEETNSF 274
Cdd:pfam05667 271 SRSAQdlaELLSSFSGSSttdtGLTKGsrftHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESS 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 275 LKAIEEANKKMEAaelSLEEKDQKIGELDRLIERMEKE---RHQLQLQLLEHETEMS--GEMADSDKNRYQQL----EEA 345
Cdd:pfam05667 351 IQELEKEIKKLES---SIKQVEEELEELKEQNEELEKQykvKKKTLDLLPDAEENIAklQALVDASAQRLVELagqwEKH 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 85701616 346 SASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGE 401
Cdd:pfam05667 428 RVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAE 483
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
244-414 |
5.96e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 244 KLYSQYEEKLQEAQRKHSAE----------------KEVLLEETNSFLKAIEEANKKM-EAAELSLEEKDQKIGELDRLI 306
Cdd:COG2433 343 KAYDAYKNKFERVEKKVPPDvdrdevkarvirglsiEEALEELIEKELPEEEPEAEREkEHEERELTEEEEEIRRLEEQV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 307 ERMEKERHQLQLQLLEHETEMSgemadsdknRYQ-QLEEASASLRERIRhlddmvhcQQKKVKQMVEEIESLKKKVQQkq 385
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIE---------RLErELSEARSEERREIR--------KDREISRLDREIERLERELEE-- 483
|
170 180
....*....|....*....|....*....
gi 85701616 386 llilqllekisfLEGENNELQSRLDYLTE 414
Cdd:COG2433 484 ------------ERERIEELKRKLERLKE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-360 |
6.84e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 205 KLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEANKK 284
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 285 MEAAELSLEEKDQKIGELDRLIERMEKERHQL----QLQLLEHE------TEMSGEMADsdknryqqLEEASASLRERIR 354
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEALgpvnLLAIEEYEeleeryDFLSEQRED--------LEEARETLEEAIE 819
|
....*.
gi 85701616 355 HLDDMV 360
Cdd:COG1196 820 EIDRET 825
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-359 |
7.85e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVSHAQQ-----DYLDSHIQAQASALDSFNAMNAALASD 170
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 171 SVGLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQME-NQLLKMRVESSQEanaevmREMTRKLYSQY 249
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlRDLESRLGDLKKE------RDELEAQLREL 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 250 EEKLQEAQ------RKHSAEKEVLLEETNSFLKAIEEANKKME---AAELSLEEKDQKIGELDRLIERMEKERhqlqlQL 320
Cdd:TIGR02169 902 ERKIEELEaqiekkRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALEPVN-----ML 976
|
250 260 270
....*....|....*....|....*....|....*....
gi 85701616 321 LEHETEMSGEMADSDKNRYQQLEEASASLRERIRHLDDM 359
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-410 |
9.96e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 95 NQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVshaqqdyLDSHIQAQ---ASALDSFNAMNAALASDS 171
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN-------LKKKIQKNkslESQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 172 VGLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAA-----QMENQLLKMRVESS---QEANAEVMREMTR 243
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikELEKQLNQLKSEISdlnNQKEQDWNKELKS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 244 KLYSQyEEKLQEAQRKHSAEKEV---LLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQL 320
Cdd:TIGR04523 315 ELKNQ-EKKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 321 --LEHETEMSGEMADSDKNRYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFL 398
Cdd:TIGR04523 394 ndLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
330
....*....|..
gi 85701616 399 EGENNELQSRLD 410
Cdd:TIGR04523 474 SRSINKIKQNLE 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-359 |
4.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 89 VYGWST----NQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVSHAQQDyldshIQAQASALDSFNAMN 164
Cdd:COG4913 603 VLGFDNraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 165 AALASDSVGLQKtlvdvtlenshIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRK 244
Cdd:COG4913 678 ERLDASSDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 245 LYSQYEEKLQEA-------------QRKHSAEKEVLLEETNSFLKAIEEANK--KMEAAEL--SLEEKDQKIGELDRLI- 306
Cdd:COG4913 747 LRALLEERFAAAlgdaverelrenlEERIDALRARLNRAEEELERAMRAFNRewPAETADLdaDLESLPEYLALLDRLEe 826
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 85701616 307 ERMEKERHQLQLQLLEHETEMSGEMAdsdknryQQLEEASASLRERIRHLDDM 359
Cdd:COG4913 827 DGLPEYEERFKELLNENSIEFVADLL-------SKLRRAIREIKERIDPLNDS 872
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
146-301 |
4.81e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 146 LDSHIQAQASALDSFNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRHLQ---QTYEASMDKLREKQ------RQLEAA 216
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLgnvrnnKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 217 QMENQLLKMRVESSQEANAEVMREMTRKlysqyEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKD 296
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEEL-----EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
....*
gi 85701616 297 QKIGE 301
Cdd:COG1579 170 AKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
178-357 |
4.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 178 LVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEaaQMENQLLKMRVESSQEANAEVMREMTRKLY---SQYEEKLQ 254
Cdd:COG3206 207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA--ALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 255 EAQRKHSAEKEVL--LEETNSFLKaiEEANKKMEAAELSLEEKDQKIGELDRLIERMEKE-----RHQLQLQLLEHETEM 327
Cdd:COG3206 285 RYTPNHPDVIALRaqIAALRAQLQ--QEAQRILASLEAELEALQAREASLQAQLAQLEARlaelpELEAELRRLEREVEV 362
|
170 180 190
....*....|....*....|....*....|
gi 85701616 328 SGEMADSDKNRYQQLEEASASLRERIRHLD 357
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-415 |
5.49e-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: 42.06 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 201 ASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTrklysQYEEKLQEAQRKHSAekevLLEETNSFLKAIEE 280
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIRA----LEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 281 ANKKMEAAELSLEEKDQKIGELDRLIERMEKER------HQLQLQLLEHETEMSGEMADSDKNRYQQLEEASASLRERIR 354
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85701616 355 HLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRLDYLTET 415
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
174-411 |
5.60e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 174 LQKTLVDVTLENSHIKDQirhlqqtyeasmdkLREKQRQLEAAQMENQLLKMRVES--SQEANAEVMREMTRKLYSQYEE 251
Cdd:TIGR04523 347 LKKELTNSESENSEKQRE--------------LEEKQNEIEKLKKENQSYKQEIKNleSQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 252 KLQEAQRkhsaEKEVLLEETNSFLKAIEEANKKMEaaelSLEEKDQkigELDRLIERMEKERHQLQLQLLEHETEMSGEM 331
Cdd:TIGR04523 413 QIKKLQQ----EKELLEKEIERLKETIIKNNSEIK----DLTNQDS---VKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 332 ADSDKNRyQQLEEASASLRERIRHLDDMvhcqQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSRLDY 411
Cdd:TIGR04523 482 QNLEQKQ-KELKSKEKELKKLNEEKKEL----EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-356 |
5.64e-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: 42.06 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 151 QAQASALDSFNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRV--- 227
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIael 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 228 ESSQEANAEVMREMTRKLY-----SQYEEKLQEAQRKHSAEKEVLLEETNSFLKA-IEEANKKMEAAELSLEEKDQKIGE 301
Cdd:COG4942 96 RAELEAQKEELAELLRALYrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 85701616 302 LDRLIERMEKERHQLQLQLLEHETEMSG--EMADSDKNRYQQLEEASASLRERIRHL 356
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARL 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-426 |
5.73e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 246 YSQYEEKLQEAQRKHSA-EKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHE 324
Cdd:COG1196 215 YRELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 325 TEMsgemadsdknryQQLEEASASLRERIRHLddmvhcqQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNE 404
Cdd:COG1196 295 AEL------------ARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180
....*....|....*....|..
gi 85701616 405 LQSRLDYLTETQPKTEVETREI 426
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-352 |
1.11e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 127 QKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKL 206
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 207 REKQ----RQLEAAQMENQLLKMRV-ESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEA 281
Cdd:COG4942 100 EAQKeelaELLRALYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85701616 282 NKKMEAAELSLEekdQKIGELDRLIERMEKERHQLQLQLLEHETEmsgemADSDKNRYQQLEEASASLRER 352
Cdd:COG4942 180 LAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQE-----AEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-426 |
1.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 230 SQEANAEVMREMTR-KLYSQYEEKLQEAQRKHSAEKEVLleetNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIER 308
Cdd:PRK03918 143 SDESREKVVRQILGlDDYENAYKNLGEVIKEIKRRIERL----EKFIKRTENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 309 MEKERHQLQLQLLEHEtemsgemadSDKNRYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLI 388
Cdd:PRK03918 219 LREELEKLEKEVKELE---------ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
|
170 180 190
....*....|....*....|....*....|....*...
gi 85701616 389 LQLLEKISfLEGENNELQSRLDYLTETQPKTEVETREI 426
Cdd:PRK03918 290 EKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
188-426 |
1.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 188 IKDQIRHLQQTYEAS-------MDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKlySQYEEKLQ--EAQR 258
Cdd:PRK03918 191 IEELIKEKEKELEEVlreineiSSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK--RKLEEKIRelEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 259 KHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQL--LEHETEMSGEMADSDK 336
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 337 ---NRYQQLEEaSASLRERIRHLDDMVHCQQKKVK-----QMVEEIESLKKKVQQKQLLILQLLEKISFLEGENNELQSR 408
Cdd:PRK03918 349 eleKRLEELEE-RHELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250
....*....|....*...
gi 85701616 409 LDYLTETQPKTEVETREI 426
Cdd:PRK03918 428 IEELKKAKGKCPVCGREL 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-380 |
1.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 95 NQLKEEMNYIKDVRATLEKVRKRmYGDYDEMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAMNAALASDSVGL 174
Cdd:PRK03918 207 REINEISSELPELREELEKLEKE-VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 175 Q--KTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTR-----KLYS 247
Cdd:PRK03918 286 KelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 248 QYEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEK----DQKIGELDRLIERMEKERHQLQL---QL 320
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEELKKAKGKCPVcgrEL 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85701616 321 LEHE-----TEMSGEMADSDKnRYQQLEEASASLRERIRHLDDMVHCQQK--KVKQMVEEIESLKKK 380
Cdd:PRK03918 446 TEEHrkellEEYTAELKRIEK-ELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEK 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
206-353 |
1.84e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 206 LREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKLysqyEEKLQEAQRKHSAEKEVLLEetnsfLKAIEEAnkkm 285
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAEL----EEELEALKARWEAEKELIEE-----IQELKEE---- 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 286 eaaelsLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETE---------MSG----EMADSDKNRYQQLEEAsasLRER 352
Cdd:COG0542 480 ------LEQRYGKIPELEKELAELEEELAELAPLLREEVTEediaevvsrWTGipvgKLLEGEREKLLNLEEE---LHER 550
|
.
gi 85701616 353 I 353
Cdd:COG0542 551 V 551
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
157-420 |
1.89e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 157 LDSFNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESsqeanae 236
Cdd:PTZ00108 1026 LVITNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWS------- 1098
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 237 VMREMTRKLYSQYEEKLQEAQR-KHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQ----KIGELDRLIERMEK 311
Cdd:PTZ00108 1099 LTKEKVEKLNAELEKKEKELEKlKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSktkgKASKLRKPKLKKKE 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 312 ERHQLQLQLLEHETEMSGEMADSDKNRYQQLEEAS---ASLRERIRHLDDMVHCQQKKVKQMVEEiESLKKKVQQKQLLI 388
Cdd:PTZ00108 1179 KKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPdnkKSNSSGSDQEDDEEQKTKPKKSSVKRL-KSKKNNSSKSSEDN 1257
|
250 260 270
....*....|....*....|....*....|..
gi 85701616 389 LQLLEKISFLEGENNELQSRLDYLTETQPKTE 420
Cdd:PTZ00108 1258 DEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPS 1289
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-398 |
2.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 200 EASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREmtRKLYSQYEEKLQEAQRKHSAEKEvlleetnsflkaIE 279
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE--LEKLEKLLQLLPLYQELEALEAE------------LA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 280 EANKKMEAaelsLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMadsdKNRYQQLEEASASLRERIRHLDDM 359
Cdd:COG4717 143 ELPERLEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT----EEELQDLAEELEELQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 85701616 360 VHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFL 398
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
189-381 |
2.26e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 189 KDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMR-------EMTRKLYSQYEEKLQEAQRKhs 261
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKK-- 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 262 aEKEVLLEETNSFLKAIEEANK----KMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMADSDKN 337
Cdd:PTZ00121 1649 -AEELKKAEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 85701616 338 RYQQLEEASASLRERIRHLDDMV--HCQQKKVKQMVEEIESLKKKV 381
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-380 |
3.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 203 MDKLREKQRQLEAAQMENQLLKMRVESSQEANAEvmREMTRKLYSQYEEKLQEAQRKHSAEKevLLEETNSFLKAIEEAN 282
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEE--LEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 283 KKMEAaelsLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMAD---SDKNRYQQLEEASASLRERIRHLDDM 359
Cdd:COG4717 146 ERLEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|.
gi 85701616 360 VHCQQKKVKQMVEEIESLKKK 380
Cdd:COG4717 222 LEELEEELEQLENELEAAALE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-289 |
4.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 95 NQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAMNAALASDS--V 172
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 173 GLQKTLVDVTLEN-------------SHIKDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMR 239
Cdd:COG3883 99 GGSVSYLDVLLGSesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 85701616 240 EMtRKLYSQYEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAE 289
Cdd:COG3883 179 EQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
147-348 |
4.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 147 DSHIQAQASALDSFNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRHLQQTYEASMDKLREKQRQLEAAQmenQLLKMR 226
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 227 VESSQEANAEVM-----------------REMTRKLYSQYEEKLQEAQrkhsAEKEVLLEETNSFLKAIEEANKKMEAAE 289
Cdd:COG3883 92 ARALYRSGGSVSyldvllgsesfsdfldrLSALSKIADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 85701616 290 LSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMADSDKNRYQQLEEASAS 348
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
124-381 |
4.92e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 38.91 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 124 EMRQKIRQLTQDLSVSHAQQDYLDSHIQAQASALDSFNAmnaalasdsvGLQKTLVDVtlenshiKDQIRHLQQTYEASM 203
Cdd:pfam04108 14 ELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVRE----------GLEKVLNEL-------KKDFKQLLKDLDAAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 204 DKLREKQRQLEAAQMENQLLKMRVESSQ------EANAEVMREMTRKLYSQYEEKLQEAQRkhsaekevLLEETNSFLKA 277
Cdd:pfam04108 77 ERLEETLDKLRNTPVEPALPPGEEKQKTlldfidEDSVEILRDALKELIDELQAAQESLDS--------DLKRFDDDLRD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 278 IEEANKKMEAAELSLEEKDQKIGELDRLIERMEK-----ERH-QLQLQLLEHETEMSGEMADSDKNRYQQLEEASASLRE 351
Cdd:pfam04108 149 LQKELESLSSPSESISLIPTLLKELESLEEEMASlleslTNHyDQCVTAVKLTEGGRAEMLEVLENDARELDDVVPELQD 228
|
250 260 270
....*....|....*....|....*....|
gi 85701616 352 RIRHLDDmvhcQQKKVKQMVEEIESLKKKV 381
Cdd:pfam04108 229 RLDEMEN----NYERLQKLLEQKNSLIDEL 254
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
203-323 |
5.04e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 37.96 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 203 MDKLREKQRQLEAAQMENQLLKM----------RVESSQEANAEVMREMT------RKLYSQYEEKLQEAQRKHSaEKEV 266
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRlqkrqekalgKYEGTESELPQLIARHNeevrvlRERLRRLQEKERDLERKLK-EKEA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 267 LLEETNSFLKA------------IEEANKKMEAAELSLEEKDQKIGELDRLIERMEKE-RHQLQLQLLEH 323
Cdd:pfam15619 96 ELLRLRDQLKRleklsedknlaeREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSfRRQLAAEKKKH 165
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
160-433 |
5.48e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 160 FNAMNAALASDSVGLQKTLVDVTLENSHIKDQIRhlqqTYEASMDKLREKQRQleaaqmenqllkmrvessqeaNAEVMR 239
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIK----TYNKNIEEQRKKNGE---------------------NIARKQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 240 EMtrklysqYEEKLQEAqRKHSAEKEVLLEEtnsflkaIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQ-- 317
Cdd:PHA02562 220 NK-------YDELVEEA-KTIKAEIEELTDE-------LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 318 ------LQLLEHETEMSGEMADSDKNRYQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQL 391
Cdd:PHA02562 285 gvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTA-IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV 363
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 85701616 392 LEKISFLEGEN-------NELQSRLDYLTETQPKTEVETREIGVGCDLL 433
Cdd:PHA02562 364 KAAIEELQAEFvdnaeelAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
206-380 |
5.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 206 LREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAEKEVLleETNSFLKAIEEANKKM 285
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL--ELKDAEKELEREEKEL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 286 EAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEmsgemadSDKNRYQQLEEASASLRERIRHLDDMVHCQQK 365
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-------ELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
170
....*....|....*
gi 85701616 366 KVKQMVEEIESLKKK 380
Cdd:PRK03918 695 TLEKLKEELEEREKA 709
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-376 |
5.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 200 EASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAEKEVLLEEtnsflkAIE 279
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE------LEQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 280 EANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEMSGEMADSD----KNRYQQLEEASASLRERIRH 355
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeelEEELEELEEELEELEEELEE 450
|
170 180
....*....|....*....|.
gi 85701616 356 LDDmvhcQQKKVKQMVEEIES 376
Cdd:COG4717 451 LRE----ELAELEAELEQLEE 467
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
208-426 |
6.09e-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: 38.95 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 208 EKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKLYSQYEEKLQEA----QRKHSAEKEVLLEETNSFLKAIEEANK 283
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAemdrQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 284 KMEAAELSLEE---KDQKIGELDRL-IER-------------------MEKERHQLQLQLLEHETEMSGEMADSDKNRYQ 340
Cdd:pfam17380 359 KRELERIRQEEiamEISRMRELERLqMERqqknervrqeleaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 341 QLEEASASLRERIRhLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKISFLEGEnNELQSRLDYLTETQPKTE 420
Cdd:pfam17380 439 RLEEERAREMERVR-LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE-KELEERKQAMIEEERKRK 516
|
....*.
gi 85701616 421 VETREI 426
Cdd:pfam17380 517 LLEKEM 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
258-396 |
6.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 258 RKHSAEKEVLLEEtNSFLKAIEEANKKMEAA--ELSLEEKDqkigELDRLIERMEKERHQLQLQLLEHETEMsgemadsd 335
Cdd:PRK12704 25 RKKIAEAKIKEAE-EEAKRILEEAKKEAEAIkkEALLEAKE----EIHKLRNEFEKELRERRNELQKLEKRL-------- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85701616 336 KNRYQQLEEASASLRERIRHLDDmvhcQQKKVKQMVEEIESLKKKVQQKQLLILQLLEKIS 396
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEK----KEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
193-379 |
6.76e-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: 38.95 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 193 RHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAE--------- 263
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVErlrqqeeer 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 264 --KEVLLEETNSFLKAIEEANKKMeaAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETEmsgEMADSDKNRYQQ 341
Cdd:pfam17380 473 krKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR---REAEEERRKQQE 547
|
170 180 190
....*....|....*....|....*....|....*...
gi 85701616 342 LEEasaslRERIRHLDDMVHCQQKKVKQMVEEIESLKK 379
Cdd:pfam17380 548 MEE-----RRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
252-381 |
7.02e-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: 37.98 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 252 KLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQL----QLQLLEHETEm 327
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEYEALQKEIE- 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 85701616 328 sgemadSDKNRYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKV 381
Cdd:COG1579 100 ------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-394 |
7.92e-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: 38.95 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 110 TLEKVRKRMyGDYDEMRQKIRQLTQDL-SVSHAQQDYLDSHIQAQASALDSFNAMNAALASDSVGLQKTLVDVTLEnshi 188
Cdd:pfam15921 413 TIDHLRREL-DDRNMEVQRLEALLKAMkSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK---- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 189 KDQIRHLQQTYEASMDKLREKQRQLEAAQMENQLLKMRVE----------------SSQEANAEVMR-EMTRK-----LY 246
Cdd:pfam15921 488 KMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelqhlknegdhlRNVQTECEALKlQMAEKdkvieIL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 247 SQYEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERhqlqLQLLEHETE 326
Cdd:pfam15921 568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK----VKLVNAGSE 643
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85701616 327 MSGEMADSDKNRYQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEEIESLKKKVQQKQLLILQLLEK 394
Cdd:pfam15921 644 RLRAVKDIKQERDQLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
189-326 |
8.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 189 KDQIRHLQQTYEASMDKLREKQRQLEAAQM------ENQLLKMRVESSQEANAEVMREMT--RKLYSQYEEKLQEAQRKH 260
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELPERLEELEERLEelRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85701616 261 SAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGELDRLIERMEKERHQLQLQLLEHETE 326
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
222-380 |
8.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 222 LLKMRVESSQEANAEVMREMTRKLYSQYEEKLQEAQRKHSAEKEVLLEETNSFLKAIEEANKKMEAAELSLEEKDQKIGE 301
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701616 302 LDRLIERMEKERHQLQLQLLEHETEMSgEMADSDKNRYQQL-----EEASASLRERIRhlDDMVHCQQKKVKQMVEEIES 376
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELE-ELIEEQLQELERIsgltaEEAKEILLEKVE--EEARHEAAVLIKEIEEEAKE 184
|
....
gi 85701616 377 LKKK 380
Cdd:PRK12704 185 EADK 188
|
|
| |
