|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-409 |
7.51e-13 |
|
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: 71.24 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQL 177
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM------QVHALREDFREKNSSTNQHIIRLESL 251
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 332 L--TEERSLQSSAATSTSLLSEIEQSMEAEELEQERE-QVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRD 406
Cdd:TIGR02168 948 EysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEID 1027
|
...
gi 578824469 407 EAI 409
Cdd:TIGR02168 1028 REA 1030
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-462 |
2.50e-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: 66.23 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 164 EGRVSELESDVKQLQDELerqqihlreadreksravQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQ 243
Cdd:TIGR02168 683 EEKIEELEEKIAELEKAL------------------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 244 HIIRLESLQAEQV---LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRL 320
Cdd:TIGR02168 745 LEERIAQLSKELTeleAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 321 SCRQLQVKVEELTEE-RSLQSSAATSTSLLSEIEQSMEAEELEQE--REQVTLLSVEMTALKEERDRLR-----VTSEDK 392
Cdd:TIGR02168 825 RLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEelESELEALLNERASLEEALALLRseleeLSEELR 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 393 EPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 462
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-420 |
2.88e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 135 HKELTDKLEHLEQEKHELRRR-FENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL 213
Cdd:COG1196 215 YRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVERQLSMQvHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG1196 295 AELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 294 VLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS-LQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLS 372
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 578824469 373 VEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELA 420
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-339 |
2.23e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 103 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRF---ENREGEWEGRVSELESDVKQLQD 179
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 180 ELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmQVHALREDFREKNSSTNQHIIRLESLQAEQVLEI 259
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 260 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQ 339
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-337 |
3.71e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELT---DKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 195 KSRAVQELSEQNQRLLDQLSRASEVERQLsmqvHALREDFREKNSSTNQHIIR-LESLQAEQVLEIKMLSDRKRELEHRL 273
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824469 274 SATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-351 |
4.28e-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: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 100 LSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEwegrVSELESDVKQLQD 179
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 180 ELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVhalredfreknsstnQHIIRLESLQAEQVLEI 259
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA---------------AQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 260 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQ 339
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
250
....*....|..
gi 578824469 340 SSAATSTSLLSE 351
Cdd:COG1196 497 LEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-457 |
5.66e-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: 55.46 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 136 KELTDKLEHLEQEKH------ELRRRFENREG-EWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQR 208
Cdd:TIGR02169 194 DEKRQQLERLRREREkaeryqALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 209 LldqlsraseveRQLSMQVHALRED----FREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQ 284
Cdd:TIGR02169 274 L-----------EELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 285 GTVEELQdrvlilerqghdkdLQLHQSQLELQEVRLSCRQLQVKVEEltEERSLQSSAATSTSLLSEIEQsmeaeeleqe 364
Cdd:TIGR02169 343 REIEEER--------------KRRDKLTEEYAELKEELEDLRAELEE--VDKEFAETRDELKDYREKLEK---------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 365 reqvtlLSVEMTALKEERDRL-----RVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQ 439
Cdd:TIGR02169 397 ------LKREINELKRELDRLqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330
....*....|....*...
gi 578824469 440 KLNLSQQLEAWQDDMHRV 457
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-416 |
1.39e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESdVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA-LANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 201 ELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREknsstnqhiirLESLQAEQVLEIKMLSDRKRELEHRLsatleen 280
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELES-----------LEAELEELEAELEELESRLEELEEQL------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 281 dllqgtvEELQDRVLILERQghdkdLQLHQSQLELQEVRLScrQLQVKVEELTEERSLQSSAATSTSlLSEIEQSMEAEE 360
Cdd:TIGR02168 382 -------ETLRSKVAQLELQ-----IASLNNEIERLEARLE--RLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELE 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578824469 361 LEQEREQVTLLSVEmTALKEERDRLRvtsedkEPKEQLQKAIRDRDEAIAKKNAVE 416
Cdd:TIGR02168 447 EELEELQEELERLE-EALEELREELE------EAEQALDAAERELAQLQARLDSLE 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-332 |
2.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 129 RQYEQMHKELTDKLEHLEQEKHELRRRFENRE-GEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 208 RLLDQLSRaseverqlsmQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTV 287
Cdd:COG4913 338 DRLEQLER----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578824469 288 EELQDRVLILERQGHD-----KDLQLHQSQL--ELQEVRLS-CRQLQVKVEEL 332
Cdd:COG4913 408 AEAEAALRDLRRELREleaeiASLERRKSNIpaRLLALRDAlAEALGLDEAEL 460
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
95-448 |
5.93e-07 |
|
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: 52.42 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKEL-TDKLEHLEQEKHELRRRFENREgewegrvseLESD 173
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCDKLLLENKE---------LTQE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 174 VKQLQDELERQQihlreadreksRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQA 253
Cdd:pfam05483 508 ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELT 333
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 334 E--ERSLQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLS-----VEMTALKEERdrlrvtsedkepKEQLQKAIRDRD 406
Cdd:pfam05483 657 DnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiAEMVALMEKH------------KHQYDKIIEERD 724
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578824469 407 -----------EAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLE 448
Cdd:pfam05483 725 selglyknkeqEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-297 |
2.84e-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: 50.06 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEgrvsELESDVKQLQDELERQQIHLREADREKSR 197
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----TLRSKVAQLELQIASLNNEIERLEARLER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 198 AVQELSEQNQRLLDQLSRASEVERQ-LSMQVHALREDFREKNSSTNQHIIRLESLQaEQVLEIKMLSDRKRELEHRLSAT 276
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQAR 490
|
170 180
....*....|....*....|.
gi 578824469 277 LEENDLLQGTVEELQDRVLIL 297
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKAL 511
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
168-352 |
4.46e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 168 SELESDVKQLQDELERQQIHLREADREksraVQELSEQNQRLLdqlSRASEVERQLSmqvhalrEDFREKNSSTNQHIIR 247
Cdd:COG5022 867 ETIYLQSAQRVELAERQLQELKIDVKS----ISSLKLVNLELE---SEIIELKKSLS-------SDLIENLEFKTELIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 248 LESLQAEqvLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVL---ILERQGHDKDLQLHQSQLELQEVRLSCRQ 324
Cdd:COG5022 933 LKKLLNN--IDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGA 1010
|
170 180
....*....|....*....|....*...
gi 578824469 325 LQVKVEELTEERSLQSSAATSTSLLSEI 352
Cdd:COG5022 1011 LQESTKQLKELPVEVAELQSASKIISSE 1038
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
105-319 |
5.96e-06 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 48.10 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 105 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---------------FENREGEWEGRVSE 169
Cdd:pfam04849 77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKddllqiysndaeeseTESSCSTPLRRNES 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 170 LESDVKQLQDELERQQIHLREADREKSRA--------VQELSEQNQRLL----DQLSRASEverqlsmQVHALREDFREK 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLRGLEEENLKLRSeashlkteTDTYEEKEQQLMsdcvEQLSEANQ-------QMAELSEELARK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 238 NSSTNQHIIRLESLQAEQV---LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLE 314
Cdd:pfam04849 230 MEENLRQQEEITSLLAQIVdlqHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEE 302
|
....*
gi 578824469 315 LQEVR 319
Cdd:pfam04849 303 LKELR 307
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
118-408 |
3.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTD----------KLEHLEQEKHELRRRFENREGEWEGRVSELESdvkqLQDELERqqIH 187
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEareavedrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE----LREERDE--LR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 188 LREADREKS-RAVQELSEQNQRLLDQ---------------LSRASEVERQLSmQVHALREDFREKNSSTNQHIIRLESL 251
Cdd:PRK02224 426 EREAELEATlRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVE-ELEAELEDLEEEVEEVEERLERAEDL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 252 qAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:PRK02224 505 -VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469 332 LTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQvTLLSVEMTALKEERDRLRvTSEDKEPKEQLQKAIRDRDEA 408
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKRERKR-ELEAEFDEARIEEAREDKERA 658
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-319 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 98 ELLSVIRQKEKDLVLAARLGKALLERNQdmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 178 QDE----LERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhALREDFREKNSSTNQHIIRLESLQA 253
Cdd:COG1196 368 LEAeaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824469 254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVR 319
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-337 |
5.68e-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: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 139 TDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELER-QQIHLREADREKSRAVQELSEQNQRLLDQLSRAS 217
Cdd:COG4913 609 RAKLAALEAELAELEEELA----EAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 218 EVERQLSMQVHALREDFREknsstnqhiirleslqAEQvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLIL 297
Cdd:COG4913 685 DDLAALEEQLEELEAELEE----------------LEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578824469 298 ERQGHDKDLQLHQSQLELQEVRlscRQLQVKVEELTEERS 337
Cdd:COG4913 747 LRALLEERFAAALGDAVERELR---ENLEERIDALRARLN 783
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-472 |
1.71e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 125 QDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAvqelsE 204
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI-----E 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 205 QNQRLLDQLSRASEVERQLSMQV---HALREDFREKNSSTNQHIIRLESLQAEqvLEIKMLSDRKRELEHRLSATLEEND 281
Cdd:TIGR00606 769 EQETLLGTIMPEEESAKVCLTDVtimERFQMELKDVERKIAQQAAKLQGSDLD--RTVQQVNQEKQEKQHELDTVVSKIE 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 282 LLQGTVEELQDRVLILERQGHD---KDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEA 358
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 359 EELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQ--LQKAIRDRDEAIAKKNAvelELAKCRMDMMSLNSQlLDA 436
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgKDDYLKQKETELNTVNA---QLEECEKHQEKINED-MRL 1002
|
330 340 350
....*....|....*....|....*....|....*..
gi 578824469 437 IQQKLNLSQQLEAW-QDDMHRVIDRQLMDTHLKERSQ 472
Cdd:TIGR00606 1003 MRQDIDTQKIQERWlQDNLTLRKRENELKEVEEELKQ 1039
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-452 |
2.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 155 RFENREGEWEGRVSELESDVKQLQD---ELERQQIHLrEADREKSRAVQELSEQnqrlldqlsrasevERQLSMQVHALR 231
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDilnELERQLKSL-ERQAEKAERYKELKAE--------------LRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 232 -EDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQ 310
Cdd:TIGR02168 234 lEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 311 SQLELQEVRLSCRQLQVKVEELTEErsLQSSAATSTSLLSEIEQ-----SMEAEELEQEREQVTLLSVEMTALKEERDRL 385
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELESleaelEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469 386 RVT--------SEDKEPKEQLQKAIRDRDEAIAK--KNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQD 452
Cdd:TIGR02168 392 ELQiaslnneiERLEARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-424 |
2.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELE--RQQIHLREADREK 195
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEelEEELEQLENELEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 196 SRAVQELSEQNQRLL-------------DQLSRASEVE--RQLSMQVHALREDFREKNSSTNQHII-RLESLQAEQVLEI 259
Cdd:COG4717 239 AALEERLKEARLLLLiaaallallglggSLLSLILTIAgvLFLVLGLLALLFLLLAREKASLGKEAeELQALPALEELEE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 260 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDrvLILERQGHDKDLQLHQSQLELQEVRLSC---------------RQ 324
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQE--LLREAEELEEELQLEELEQEIAALLAEAgvedeeelraaleqaEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 325 LQVKVEELTE-ERSLQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIR 403
Cdd:COG4717 397 YQELKEELEElEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
|
330 340
....*....|....*....|.
gi 578824469 404 DRDEAIAKKNAVELELAKCRM 424
Cdd:COG4717 477 ELEELKAELRELAEEWAALKL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-452 |
2.68e-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: 43.90 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 170 LESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmqvhALREDFREKNSSTNQHIIRLE 249
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 250 SLQAeqvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqgHDKDLQLHQSQLELQEVRLSCRQLQVKV 329
Cdd:TIGR02169 741 ELEE----DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 330 EELteERSLQSSAATSTSLLSEIEQSMEAEEL-----EQEREQVTLLSVEMTALKEERDRLRVTSEDKEpkEQLQKAIRD 404
Cdd:TIGR02169 815 REI--EQKLNRLTLEKEYLEKEIQELQEQRIDlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLE--SRLGDLKKE 890
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 578824469 405 RDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQD 452
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
153-456 |
3.50e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 153 RRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASE----VERQLSMQVH 228
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQsqedLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 229 ------ALREDFREkNSSTNQHIIRLESLQAEQVL-EIKML-------SDRK------------RELEHRLSATLEEND- 281
Cdd:pfam15921 153 eleaakCLKEDMLE-DSNTQIEQLRKMMLSHEGVLqEIRSIlvdfeeaSGKKiyehdsmstmhfRSLGSAISKILRELDt 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 282 ---LLQGTVEELQDRVLILERQGHDK-DLQLHQSQLELQEVrlsCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSME 357
Cdd:pfam15921 232 eisYLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 358 AEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKepkeqlqkaIRDRDEAIAKKNAvELELAKCRMDMMSlnsqlldai 437
Cdd:pfam15921 309 RNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---------IEELEKQLVLANS-ELTEARTERDQFS--------- 369
|
330
....*....|....*....
gi 578824469 438 QQKLNLSQQLEAWQDDMHR 456
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHK 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-300 |
5.73e-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: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---FENREGEWEGRVSELESDVKQLQDELERQQIHLRE------- 190
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 191 ---ADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKR 267
Cdd:COG4942 116 lgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190
....*....|....*....|....*....|...
gi 578824469 268 ELEHRLSATLEENDLLQGTVEELQDRVLILERQ 300
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-453 |
8.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 201 ELSE-QNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEE 279
Cdd:COG4717 228 ELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 280 NDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRlSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAE 359
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 360 ELEQEREQVtllsvEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEaiakknaVELELAKCRMDMMSLNSQLLDAIQQ 439
Cdd:COG4717 387 LRAALEQAE-----EYQELKEELEELEEQLEELLGELEELLEALDEEE-------LEEELEELEEELEELEEELEELREE 454
|
330
....*....|....
gi 578824469 440 KLNLSQQLEAWQDD 453
Cdd:COG4717 455 LAELEAELEQLEED 468
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-254 |
9.14e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 127 MSRQYEQMHKELTDKLEHLeQEKHELRRRFENREGEWEGRVSELEsdvkqlqdeleRQQIHLREADREKSRAVQELSEQN 206
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLE-----------LEKVKLVNAGSERLRAVKDIKQER 655
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578824469 207 QRLLDQLSRASEVERQLSMQVHALREDFREKN----SSTNQHIIRLESLQAE 254
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSeemeTTTNKLKMQLKSAQSE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-300 |
9.79e-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: 41.98 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGE---WEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 195 KSRAVQELSEQNQRLLDQLSRASEVERQLS------MQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRE 268
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDrlqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190
....*....|....*....|....*....|..
gi 578824469 269 LEHRLSATLEENDLLQGTVEELQDRVLILERQ 300
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-449 |
1.08e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEER- 336
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELt 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 337 -------SLQSSAATSTSLLSEIEQSMEAEELE--QEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQ--------LQ 399
Cdd:TIGR02168 758 eleaeieELEERLEEAEEELAEAEAEIEELEAQieQLKEELKALREALDELRAELTLLNEEAANLRERLEslerriaaTE 837
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578824469 400 KAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEA 449
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-462 |
1.12e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 247 RLESL--QAEQVLEIKMLSDRKRELEHRLsaTLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQ 324
Cdd:COG1196 201 QLEPLerQAEKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 325 LQVKVEELTEERSLQSSAatstslLSEIEQsmeaeeleqereqvtllsvEMTALKEERDRLRVTSEDKEpkEQLQKAIRD 404
Cdd:COG1196 279 LELELEEAQAEEYELLAE------LARLEQ-------------------DIARLEERRRELEERLEELE--EELAELEEE 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578824469 405 RDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 462
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-282 |
1.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 136 KELTDKLEHLEQEKHELRRRFENR----EGEWEGRVSELES------DVKQLQDELERQQIHLREADREKSRAVQELSEQ 205
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824469 206 NQRLLDQLSRASEVERQLSMQVHA-LREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDL 282
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-315 |
1.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELER--QQIHLREADREKSRAVQELSEQNQRLlDQL 213
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVERQLSMQVHALREDFREKNSSTNQHiirLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|..
gi 578824469 294 VLILERQGHDKDLQLHQSQLEL 315
Cdd:COG4717 229 LEQLENELEAAALEERLKEARL 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-224 |
2.43e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 112 LAARLGKALLERN--QDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELESDVKQLQDELERQQI 186
Cdd:TIGR02169 817 IEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
90 100 110
....*....|....*....|....*....|....*...
gi 578824469 187 HLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLS 224
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-413 |
3.09e-03 |
|
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: 40.39 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELERQQIHLREADREKsravQELSEQNQRLLDQLSR 215
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK----ELLEKEIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 216 ASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAE-----------------QVLEIKMLSDRKRELEHRLSATLE 278
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnleqkqkelksKEKELKKLNEEKKELEEKVKDLTK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 279 ENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRL--SCRQLQVKVEELTEE-RSLQSSAATSTSLLSEIEQS 355
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIEELKQTqKSLKKKQEEKQELIDQKEKE 597
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824469 356 MEAEELEQEREQVTLLSV--EMTALKEERDRL----RVTSEDKEPKEQLQKAIRDR-DEAIAKKN 413
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLekELEKAKKENEKLssiiKNIKSKKNKLKQEVKQIKETiKEIRNKWP 662
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
168-386 |
3.18e-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: 39.75 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 168 SELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQ----------LSMQVHALREDFREK 237
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaleaelaeLEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 238 NSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLsatleenDLLQGTVEELQDRVLILERQghDKDLQLHQSQLELQE 317
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRAD--LAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824469 318 VRLScrqlQVKVEELTEERSLQSSAATSTSLLSEIEQsmeaeeleqereQVTLLSVEMTALKEERDRLR 386
Cdd:COG4942 174 AELE----ALLAELEEERAALEALKAERQKLLARLEK------------ELAELAAELAELQQEAEELE 226
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
129-289 |
3.20e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.93 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 129 RQYEQMHKELTDKLEHLEQEKHELR-RRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLRaERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 208 RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLE-SLQAEQVLEIKMLSDRKRELEHRLSatlEENDLLQGT 286
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQLA---EEQKRLMEM 471
|
...
gi 578824469 287 VEE 289
Cdd:pfam15709 472 AEE 474
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
98-300 |
3.73e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQ----------EKHELRRRFENREGEwegrV 167
Cdd:pfam05557 52 ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknELSELRRQIQRAELE----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 168 SELESDVKQLQDELERQQIHLREAdrekSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalrEDFREKNSSTNQHIIR 247
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----EQDSEIVKNSKSELAR 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578824469 248 LESLQAEQvleikmlsDRKRELEHRLSATLEENDLLQGTVEELQDRvliLERQ 300
Cdd:pfam05557 199 IPELEKEL--------ERLREHNKHLNENIENKLLLKEEVEDLKRK---LERE 240
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
108-345 |
4.47e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 108 KDLVLAARLGKALLERNqdmsrqyeqmhkELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELER---Q 184
Cdd:pfam07888 28 RAELLQNRLEECLQERA------------ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsreK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 185 QIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNqhiiRLESLQAEQVLEIKMLSD 264
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE----RMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 265 RKRELEHRLSATLEENDLLQGTVEELQDrvliLERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAA 343
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQERLN 247
|
..
gi 578824469 344 TS 345
Cdd:pfam07888 248 AS 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
134-293 |
4.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 134 MHKELtDKLEHLeQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL 213
Cdd:COG1579 2 MPEDL-RALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVE-----RQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVE 288
Cdd:COG1579 80 EQLGNVRnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*
gi 578824469 289 ELQDR 293
Cdd:COG1579 160 ELEAE 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
121-418 |
4.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 121 LERNQDMSRQYEQMHK--ELTDKLEHLEQEKHELRRRFENREGEWEGRVSElesDVKQLQDELERQQIHLREADREKSRA 198
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD---EAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 199 VQELSEQNQRLLDQLSRASEVERQlsmqvhalrEDFREKNSSTNQHIIRlESLQAEQVLEIKMLSDRKRELEHRLSATLE 278
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKA---------DEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 279 ENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLElqevrlscrqlQVKVEELTEERSLQSSAatsTSLLSEIEQSMEA 358
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-----------KIKAEELKKAEEEKKKV---EQLKKKEAEEKKK 1648
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 359 EELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELE 418
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
118-337 |
5.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEH---LEQEKHELRRRFENREGEWEgRVSELESDVKQLQDELERQQIHLR---EA 191
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRkleEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 192 DREKSRAVQELSEQNQRLLDQLSRASEVER--QLSMQVHALREDFREKNSSTNQHIIRLESLQA---EQVLEIKMLSDRK 266
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEkaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieERIKELEEKEERL 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824469 267 RELEHRLSATLEENDLLQGTVEELQD-RVLILERQGHDK---DLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEaKAKKEELERLKKrltGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
174-354 |
5.28e-03 |
|
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: 39.55 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 174 VKQLQDELERQQIHlrEADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQ--VHALREDFREKNSSTNQHIIRLESL 251
Cdd:COG3096 481 VCKIAGEVERSQAW--QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQqnAERLLEEFCQRIGQQLDAAEELEEL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLI-------LERQGHdkdlQLHQSQLELQEVrLSCRQ 324
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqdaLERLRE----QSGEALADSQEV-TAAMQ 633
|
170 180 190
....*....|....*....|....*....|.
gi 578824469 325 LQVKVE-ELTEERSLqsSAATSTSLLSEIEQ 354
Cdd:COG3096 634 QLLERErEATVERDE--LAARKQALESQIER 662
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
122-349 |
5.47e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 122 ERNQDMSRQYEQMHKELTDKLEHLE----QEKHELRRRFENREgewegrVSELESDVKQLQDELERQQIHLREADrekSR 197
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTLS------LRQLESRLAQTLDQLQNAQNDLAEYN---SQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 198 AV--QELSEQNQRLLDQ-LSRASEVERQLsmqvhalredfreKNSSTNQHIIRLES---LQAEQVLEIKMLSDRKRELEH 271
Cdd:PRK11281 151 LVslQTQPERAQAALYAnSQRLQQIRNLL-------------KGGKVGGKALRPSQrvlLQAEQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824469 272 rlSATLEenDLLQGTVEELQDRVLILERQghdkdLQLhqsqleLQEVrLSCRQLQVKVEELTEERSLQSSAATSTSLL 349
Cdd:PRK11281 218 --NTQLQ--DLLQKQRDYLTARIQRLEHQ-----LQL------LQEA-INSKRLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-418 |
5.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEK---HELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADR- 193
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEl 1557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 194 ---EKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLES--LQAEQVLEIKMLSDRKRE 268
Cdd:PTZ00121 1558 kkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQ 1637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 269 LEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSL 348
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824469 349 LSEIEQSmeaeeleqerEQVTLLSVEMTALKEERDR-----LRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELE 418
Cdd:PTZ00121 1718 AEELKKA----------EEENKIKAEEAKKEAEEDKkkaeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
118-467 |
6.40e-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: 39.26 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRfenregewegrVSELESDVKQLQDELERQQIHLREADREKsr 197
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQE-----------KTELLVEQGRLQLQADRHQEHIRARDSLI-- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 198 avqeLSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSatl 277
Cdd:TIGR00606 371 ----QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE--- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 278 EENDLLQGTVEELQDRVLILER-QGHDKDLQLHQSQLELQEVRLSCRQLQVKVE-ELTEERSLQSSAATSTSLLSEIEQS 355
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKELQQlEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 356 MEAEELEQEREQVTLLSVEMTALKEER---------DRLRVTSEDKEPKEQLQKAIRDRDEaiaKKNAVELELAKCRMDM 426
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrhsDELTSLLGYFPNKKQLEDWLHSKSK---EINQTRDRLAKLNKEL 600
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578824469 427 MSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHL 467
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL 641
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
131-493 |
7.63e-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: 39.05 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 131 YEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRV------SELESDVKQLQDELERQQIHLREADREKSRAVQE--- 201
Cdd:pfam12128 417 LQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVERLQSElrq 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 202 -----------LSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLES------------LQAEQVLE 258
Cdd:pfam12128 497 arkrrdqaseaLRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISpellhrtdldpeVWDGSVGG 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 259 IKMLSDRKRELEHrlsatLEENDLLQGTvEELQDRVLILErqghdKDLQLHQSQLELQEVRLScrQLQVKVEELTEERSL 338
Cdd:pfam12128 577 ELNLYGVKLDLKR-----IDVPEWAASE-EELRERLDKAE-----EALQSAREKQAAAEEQLV--QANGELEKASREETF 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 339 QSSAATSTSL----LSEIEQSMEAEELEQEREQVTLLSVEMTALKEERDRLrvtseDKEPKEQLQKAIRDRDEAIAKKNA 414
Cdd:pfam12128 644 ARTALKNARLdlrrLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQL-----DKKHQAWLEEQKEQKREARTEKQA 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 415 VELELAKCRMDMMSLNSQLLDAIQQklNLSQQLEAWQDDMHRVIDRQLMD-THLKERSQPAAALCRGHSAGRGDEPSIAE 493
Cdd:pfam12128 719 YWQVVEGALDAQLALLKAAIAARRS--GAKAELKALETWYKRDLASLGVDpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-405 |
7.65e-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: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 120 LLERNQDMSRQYEQMHK----ELTDKLEHLEQEKHELRRRFE-------NREGEWEGRVSELESDVKQLQDELerqqihl 188
Cdd:pfam15921 261 LLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEiiqeqarNQNSMYMRQLSDLESTVSQLRSEL------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLeSLQAEQVleiKMLSDR--- 265
Cdd:pfam15921 334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQN---KRLWDRdtg 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 266 --------KRELEHRLSATLEENDLLQGTVEELQDRvliLERQG---HDKDLQLHQSQLELQEVRLSCRQLQVKVEELTE 334
Cdd:pfam15921 410 nsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469 335 ER-SLQSSAATSTSL---LSEIEQSMEAEELE--QEREQVTLLSVEMTALKEERDRLRVTSEDKEPKeQLQKAIRDR 405
Cdd:pfam15921 487 KKmTLESSERTVSDLtasLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL-KLQMAEKDK 562
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
129-421 |
7.76e-03 |
|
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: 38.85 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 129 RQYEQMHKELTDKLEHLEQEKhelrrrfenregewegrvSELESDVKQLQDELERQQIHLREADREKSRAVQE---LSEQ 205
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKEL------------------TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknLESQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 206 NQRLLDQLSRASEVERQLSMQVHALR----------EDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSA 275
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQqekellekeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 276 TLEENDLLQGTVEELQDRVLILERQghDKDLQLHQSQLELQEVRLSCRQ--LQVKVEELTEERSLQSSAAtsTSLLSEIE 353
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKE--LKKLNEEKKELEEKVKDLTKKIssLKEKIEKLESEKKEKESKI--SDLEDELN 548
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824469 354 QSMEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPK-EQLQKAIRDRDEAIAKKNAVELELAK 421
Cdd:TIGR04523 549 KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELiDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
131-447 |
8.38e-03 |
|
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: 38.85 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 131 YEQMHKELTDKLEHLEQEKhelrrrfenregewegrvSELESDVKQLQDELERQQIHLREADREksraVQELSEQNQRLL 210
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQN------------------NQLKDNIEKKQQEINEKTTEISNTQTQ----LNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 211 DQLSR-ASEVERQlsmqvhalREDFREKNSSTNQHIIRLESL--QAEQVL------EIKMLSDRKRELEHRLSATLEEND 281
Cdd:TIGR04523 267 KQLSEkQKELEQN--------NKKIKELEKQLNQLKSEISDLnnQKEQDWnkelksELKNQEKKLEEIQNQISQNNKIIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 282 LLQGTVEELQDRVLILERQGHDKDLQLHQSQLEL-------QEVRLSCRQLQVKVEELteERSLQSSAATSTSLLSEIEQ 354
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIeklkkenQSYKQEIKNLESQINDL--ESKIQNQEKLNQQKDEQIKK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 355 smEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKE--------PKEQLQKAIRDRDEAIakkNAVELELAKCRMDM 426
Cdd:TIGR04523 417 --LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKVLSRSI---NKIKQNLEQKQKEL 491
|
330 340
....*....|....*....|.
gi 578824469 427 MSLNSQLLDAIQQKLNLSQQL 447
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKV 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
120-483 |
8.41e-03 |
|
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: 38.93 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 120 LLERNQDMSRQYEQMHK-------ELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVK---QLQDELERQQIHLR 189
Cdd:pfam05483 262 LLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKticQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 190 EADREKSRAVQELSEQ----NQRLLDQLSRASEVERQL---SMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKML 262
Cdd:pfam05483 342 KAKAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLkiiTMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 263 SDRKrelehRLSATLEEndlLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVeeltEERSLQSSA 342
Cdd:pfam05483 422 DEKK-----QFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL----EKEKLKNIE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 343 ATSTSLLSEIEQSMEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQlqkAIRDRDEAIAKKNAVELELAKC 422
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM---NLRDELESVREEFIQKGDEVKC 566
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578824469 423 RMDMMSLNSQLLD-AIQQKLNLSQQLEAWQDDMHRVIDRQlmDTHLKERSQPAAALCRGHSA 483
Cdd:pfam05483 567 KLDKSEENARSIEyEVLKKEKQMKILENKCNNLKKQIENK--NKNIEELHQENKALKKKGSA 626
|
|
|