|
Name |
Accession |
Description |
Interval |
E-value |
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
30-517 |
0e+00 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 817.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 30 MSESDTMNVSNLSQGVMLSHSPICMETTGTTCDLPQNEIKNFERENEYESTLCEDAYGTLDNLLNDNNIENYSTNALIQP 109
Cdd:pfam15066 1 MSESDAMNVSGLSQDLTHSDSPLCMETSSTTSDLPQNEIKNVKRENESKFTLSEDIYSTLDNLLGDINIGSYSQNVLIQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 110 VDTiSISSLRQFETVCKFHWVEAFDDEM------------TEKPEFQSQVYNYAKDNNIKQDSFKEENPMETSVSANTDQ 177
Cdd:pfam15066 81 VDT-SISSLRQFEPICKFHWTEAFNDEMttfqnltegfsyTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 178 LGNEYFRQPPpRSPPLIHCSGEMLKFTEKSLAKSIAKESALNPSQPPSFLCK---------------------------- 229
Cdd:pfam15066 160 LANECVRQSS-RSPPLIHCSGETLPFTEKSLAKSTAKESALNPSQPQSFLYEenvprnvekpfykensfslldlranykt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 230 --TAVPSKEIQNYGEIPEMSVSYEKEVTAEGVERPEIVSTWSSAGISWRSEACRENCEMPDWEQSAESLQPVQEDMALNE 307
Cdd:pfam15066 239 eeTEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIASTWSPAGISWSSGASQENCKTPDTEQSFESLQPLEEDMALNE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 308 VLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEE 387
Cdd:pfam15066 319 VLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 388 VLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATA 467
Cdd:pfam15066 399 ILANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATT 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 282394045 468 SALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVR 517
Cdd:pfam15066 479 SALDLLKREKETREQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-580 |
2.35e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 304 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQV-FIDVINKLKENVEELIEDKYKIIL---EKNDTK 379
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErLANLERQLEELEAQLEELESKLDElaeELAELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 459
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 460 KELE--------KATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSrLEKLLTQVRNLQFMSENERTKNI 531
Cdd:TIGR02168 424 EELLkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-AERELAQLQARLDSLERLQENLE 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 282394045 532 KLQQQINEVKNENAKLKQQVAR-SEEQNYVPKFETAqlkdqLEEVLKSDI 580
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGILGVlSELISVDEGYEAA-----IEAALGGRL 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-567 |
8.16e-09 |
|
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: 58.24 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKK 412
Cdd:COG4942 25 AEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 413 IKANYvclqERYMTEMQQknksVSQYLEMDKTLSKKE-EEVERLQQLKKELEKATASALDLLKREKE---AQEQEFLSLQ 488
Cdd:COG4942 102 QKEEL----AELLRALYR----LGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394045 489 EEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQ 567
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-520 |
8.60e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 289 WEQSAESLQPVQEDMA-LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQ----MKITKQQVFIDVINKLKENVEE 363
Cdd:COG1196 234 LRELEAELEELEAELEeLEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 364 LIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCL--------------QERYMTEMQ 429
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaelaeaeeeleelAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 430 QKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEfLSLQEEFQKLEKENLEERQKLKSRL 509
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEEA 472
|
250
....*....|.
gi 282394045 510 EKLLTQVRNLQ 520
Cdd:COG1196 473 ALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
300-581 |
1.08e-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: 58.91 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 300 QEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTK 379
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 459
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 460 KELEKATA---SALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKsrleKLLTQVRNLQFMSENERTKNIKLQQQ 536
Cdd:TIGR02168 862 EELEELIEeleSELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 282394045 537 INEVK---NENAKLKQQVARSEEQNYVpkFETAQLKDQLEEvLKSDIT 581
Cdd:TIGR02168 938 IDNLQerlSEEYSLTLEEAEALENKIE--DDEEEARRRLKR-LENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-578 |
2.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 334 EKRVKELQMKITKqqvfidvINKLKENVEELIEdkykiilEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKI 413
Cdd:COG1196 221 ELKELEAELLLLK-------LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 414 KANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASA---LDLLKREKEAQEQEFLSLQEE 490
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 491 FQKLEKENLEERQKLKSRLEKLLTQVRNLQfmseNERTKNIKLQQQINEVKNENAKLKQQVARSEEQnyvpKFETAQLKD 570
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEEE 438
|
....*...
gi 282394045 571 QLEEVLKS 578
Cdd:COG1196 439 EEEEALEE 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-572 |
2.48e-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: 57.76 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEkndtkktlqnLEEVLANTQKHLQESRNDKEML--QLQF 410
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELQKELYALANEISRLeqQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 411 KKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEV--ERLQQLKKELEKATASALDLLKREKEAQEQ------ 482
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkEELESLEAELEELEAELEELESRLEELEEQletlrs 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 483 EFLSLQEEFQKLEKE--NLEERQK-LKSRLEKLLTQVRNLQfmSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNY 559
Cdd:TIGR02168 387 KVAQLELQIASLNNEieRLEARLErLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250
....*....|...
gi 282394045 560 VPKFETAQLKDQL 572
Cdd:TIGR02168 465 ELREELEEAEQAL 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-580 |
2.85e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 304 ALNEVLQKLKHTNRKQEVRIQELQCSNLylEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDT----- 378
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAI--ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrv 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 379 KKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQ------ERYMTEMQQKNKSVSQYL-----EMDKTLSK 447
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieelEREIEEERKRRDKLTEEYaelkeELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 448 KEEEVERLQQLKKELeKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKS-----------------RLE 510
Cdd:TIGR02169 373 LEEVDKEFAETRDEL-KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieakineleeekedkalEIK 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 511 KLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQlEEVLKSDI 580
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-EEVLKASI 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-591 |
4.97e-08 |
|
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: 55.93 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 374 EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIkanyvclqERYMTEMQQKNKSVSQYL-EMDKTLSKKEEEV 452
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------ERRIAALARRIRALEQELaALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 453 ERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLE--------------------KENLEERQKLKSRLEKL 512
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylaparreqaeelRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394045 513 LTQVRNLQFMSENERTKnikLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTTHSNL 591
Cdd:COG4942 173 RAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
288-556 |
5.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 288 DWEQSAESLQPVQEDM-ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIE 366
Cdd:PRK03918 159 DYENAYKNLGEVIKEIkRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 367 DKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKaNYVCLQERYMTEMQQKNKSVSQYLEMDKTLS 446
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 447 KKEEEVERLQQLKKELEKATASALDLLKREKEAQEqEFLSLQEEFQKLE--KENLEERQKLKSRLEKLltQVRNLQFMSE 524
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEK-RLEELEERHELYEeaKAKKEELERLKKRLTGL--TPEKLEKELE 394
|
250 260 270
....*....|....*....|....*....|..
gi 282394045 525 NERTKNIKLQQQINEVKNENAKLKQQVARSEE 556
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
304-582 |
5.44e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 304 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKqqvfIDVINKLKENVEELIEDKYKIILEKNDTKKTLQ 383
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 384 NLEEVLANTQKHLQESRNDK---EMLQLQFKKIKANYVCLQERY---------MTEMQQ-----KNKSVSQYLEMDKTLS 446
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHelyeeakakKEELERlkkrlTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 447 KKEEEVE-----------RLQQLKKELEKATaSALDLLKRE-----KEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLE 510
Cdd:PRK03918 398 KAKEEIEeeiskitarigELKKEIKELKKAI-EELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282394045 511 KLLTQVRNLQFMSENERT--KNIKLQQQINEVKNENAKL-KQQVARSEEQNYVPKFETAQLKDQLeEVLKSDITK 582
Cdd:PRK03918 477 KLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEK 550
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
305-551 |
1.18e-07 |
|
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: 55.41 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 305 LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIE--DKYKIILEKN--DTKK 380
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQlkVLSR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 381 TLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKK 460
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 461 --ELEKATASALDLLKREKEAQEqEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQIN 538
Cdd:TIGR04523 556 keNLEKEIDEKNKEIEELKQTQK-SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
250
....*....|...
gi 282394045 539 EVKNENAKLKQQV 551
Cdd:TIGR04523 635 NIKSKKNKLKQEV 647
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
350-541 |
1.91e-07 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 53.35 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 350 FIDVINKLKENVEELIEDKYKIILEKNDT------KKTLQNLEEVLANTQKHL--------QESRNDKEML-----QLQF 410
Cdd:cd16269 84 FKDEDQKFQKKLMEQLEEKKEEFCKQNEEasskrcQALLQELSAPLEEKISQGsysvpggyQLYLEDREKLvekyrQVPR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 411 KKIKANYVcLQErYMTEMQQKNKSVsqyLEMDKTLSKKEEEVERlQQLKKELEKATASAL----DLLKREKEAQEQeflS 486
Cdd:cd16269 164 KGVKAEEV-LQE-FLQSKEAEAEAI---LQADQALTEKEKEIEA-ERAKAEAAEQERKLLeeqqRELEQKLEDQER---S 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 282394045 487 LQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQ--FMSENERTKNIKLQQQINEVK 541
Cdd:cd16269 235 YEEHLRQLKEKMEEERENLLKEQERALESKLKEQeaLLEEGFKEQAELLQEEIRSLK 291
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
305-582 |
3.09e-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: 54.34 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 305 LNEVLQKLKHTNR--KQEVRIQELQCSNLYLEKRVKELQMKitkQQVFI-----DVINKLKE-------NVEELIEDKYK 370
Cdd:pfam05483 217 LKEDHEKIQHLEEeyKKEINDKEKQVSLLLIQITEKENKMK---DLTFLleesrDKANQLEEktklqdeNLKELIEKKDH 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 371 IILEKNDTKKTLQN-------LEEVLANTQKHLQESRNDKEMLQLQFKKIKANY----------VC-LQERYMTEMQQKN 432
Cdd:pfam05483 294 LTKELEDIKMSLQRsmstqkaLEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvvtefeatTCsLEELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 433 KSVSQYLEMDKTLSKKEEEVERLQQLK--KELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKEN---LEERQK--- 504
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKnnKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELiflLQAREKeih 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 505 --------LKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVA----------------RSEEQNYV 560
Cdd:pfam05483 454 dleiqltaIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlelkkhqediincKKQEERML 533
|
330 340
....*....|....*....|....*..
gi 282394045 561 PKFET-----AQLKDQLEEVLKSDITK 582
Cdd:pfam05483 534 KQIENleekeMNLRDELESVREEFIQK 560
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-575 |
3.57e-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: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 361 VEELIEDK---YKIILE--------KNDTKKTLQNLEEVLANTQK---HLQESRNDKEMLQLQ------FKKIKA----- 415
Cdd:TIGR02168 146 ISEIIEAKpeeRRAIFEeaagiskyKERRKETERKLERTRENLDRledILNELERQLKSLERQaekaerYKELKAelrel 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 416 -------NYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldllkrEKEAQEQEFLSLQ 488
Cdd:TIGR02168 226 elallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-----------EIEELQKELYALA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 489 EEFQKLEKenleERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQL 568
Cdd:TIGR02168 295 NEISRLEQ----QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
....*..
gi 282394045 569 KDQLEEV 575
Cdd:TIGR02168 371 ESRLEEL 377
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
356-557 |
8.76e-07 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 52.64 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 356 KLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRndkemLQLQFKKIKANY-VCLQERYMTEMQQKnks 434
Cdd:pfam15818 159 KLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSK-----VTCQYKMGEENInLTIKEQKFQELQER--- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 435 vsqyLEMDKTLSKK-EEEVERLQQLKKELEKATASALDLLKREKEAQ---EQEFLSLQEEFQKLEKENLEERQKLKSRLE 510
Cdd:pfam15818 231 ----LNMELELNKKiNEEITHIQEEKQDIIISFQHMQQLLQQQTQANtemEAELKALKENNQTLERDNELQREKVKENEE 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 282394045 511 KLLtqvrNLQfmseNERTKNIK--------LQQQINEVKNENAKLKQQVARSEEQ 557
Cdd:pfam15818 307 KFL----NLQ----NEHEKALGtwkkhveeLNGEINEIKNELSSLKETHIKLQEH 353
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
294-574 |
1.35e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 294 ESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIIL 373
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 374 EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANyvclqerymTEMQQKNKSVSQYLEMDKTLSKKEEEVE 453
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL---------KLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 454 RLQQLKKELEKATASAldLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKL 533
Cdd:pfam02463 332 KEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394045 534 QQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 574
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
333-555 |
3.29e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNdkemlqlQFKK 412
Cdd:COG3883 21 KQKELSELQAELEAAQ---AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 413 -IKANYVCLQERYMTEMQQKNKSVSQYLE----MDKTLSKKEEEVERLQQLKKELEKATAsALDLLKREKEAQEQEFLSL 487
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKA-ELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282394045 488 QEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSEnERTKNIKLQQQINEVKNENAKLKQQVARSE 555
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA-AAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
305-506 |
5.48e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 305 LNEVLQKLKHTNRKQEVRIQELQcsnlYLEKRVKELQMKITKQQvfIDVINKLKENVEELiEDKYKIILEKNDTKKTLQN 384
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLD----ELEEELAELLKELEELG--FESVEELEERLKEL-EPFYNEYLELKDAEKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 385 LEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYmTEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEK 464
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY-SEEEYEELR-EEYLELSRELAGLRAELEELEKRREEIKK 694
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 282394045 465 atasALDLLKREKEAQEQEflslQEEFQKLEK--ENLEE-RQKLK 506
Cdd:PRK03918 695 ----TLEKLKEELEEREKA----KKELEKLEKalERVEElREKVK 731
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
349-549 |
6.06e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.76 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 349 VFIDVINKLKENvEELIEDKYKIILEKNDTK--KTLQNLEEVLANTQKHLQES-RNDKEMLQLQFKKIKANyvclqerym 425
Cdd:pfam09731 266 IFPDIIPVLKED-NLLSNDDLNSLIAHAHREidQLSKKLAELKKREEKHIERAlEKQKEELDKLAEELSAR--------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 426 temqQKNKSVSQYLEMDKTLSKKEEEV-ERLQQ-LKKELEKATASALDLLKREKEAQEQEflsLQEEFQKLEKENLE-ER 502
Cdd:pfam09731 336 ----LEEVRAADEAQLRLEFEREREEIrESYEEkLRTELERQAEAHEEHLKDVLVEQEIE---LQREFLQDIKEKVEeER 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 282394045 503 QKLKSRLEKLLTQVRNLQfmsenertkniKLQQQINEVKNENAKLKQ 549
Cdd:pfam09731 409 AGRLLKLNELLANLKGLE-----------KATSSHSEVEDENRKAQQ 444
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
333-541 |
7.75e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.47 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITK--------QQVFIDVINKLKENVEELIEDKYKiiLEKNDTKKTLQNLEEVLANTQKHLQESRNDK- 403
Cdd:pfam06160 184 LEEETDALEELMEDipplyeelKTELPDQLEELKEGYREMEEEGYA--LEHLNVDKEIQQLEEQLEENLALLENLELDEa 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 404 -EMLQLQFKKIKANYVCLQ----------------ERYMTEMQQKNKS-VSQYLEMDKTLSKKEEEVERLQQLKKELEKA 465
Cdd:pfam06160 262 eEALEEIEERIDQLYDLLEkevdakkyveknlpeiEDYLEHAEEQNKElKEELERVQQSYTLNENELERVRGLEKQLEEL 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282394045 466 TASALDLLKREKEaQEQEFLSLQEEFqkleKENLEERQKLKSRLEKLLTQVRNLqFMSENE-RTKNIKLQQQINEVK 541
Cdd:pfam06160 342 EKRYDEIVERLEE-KEVAYSELQEEL----EEILEQLEEIEEEQEEFKESLQSL-RKDELEaREKLDEFKLELREIK 412
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
422-576 |
8.71e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 422 ERYMTEMQQKNKSVSQYLEmdkTLSKKEEEVERLQQLKKELEKATASAL----DLLKREKEAQEQEFLSLQEEFQKLEKE 497
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 498 nLEERQKLKSRLEKLLTQV-RNLQFMSENERtknIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVL 576
Cdd:TIGR02169 260 -ISELEKRLEEIEQLLEELnKKIKDLGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-553 |
8.84e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 352 DVINKLKEN-VEELIEDKykiileKNDTKKTLQNLEEVLANTQKHLQESRNDkemLQlQFKKiKANYVCLQERYMTEMQQ 430
Cdd:COG3206 152 AVANALAEAyLEQNLELR------REEARKALEFLEEQLPELRKELEEAEAA---LE-EFRQ-KNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 431 KNKSVSQYLEMDKTLSKKEEeveRLQQLKKELEKATASALDLLkrekeaQEQEFLSLQEEFQKLEKE--NLEER------ 502
Cdd:COG3206 221 LSELESQLAEARAELAEAEA---RLAALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAElaELSARytpnhp 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 282394045 503 --QKLKSRLEKLLTQVRNLQFMSENERTKNIK-LQQQINEVKNENAKLKQQVAR 553
Cdd:COG3206 292 dvIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLAQLEARLAE 345
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
229-575 |
1.16e-05 |
|
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: 48.97 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 229 KTAVPSKEIQNygeIPEMSVSYEKEVtaegvERPEIVSTWSSAGISWRSEACRENCE-MPDWEQSAESLQPVQEDMALNE 307
Cdd:pfam17380 215 MSTVAPKEVQG---MPHTLAPYEKME-----RRKESFNLAEDVTTMTPEYTVRYNGQtMTENEFLNQLLHIVQHQKAVSE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 308 VLQKLKHTNRKQEVRIQELQCSNLYLEKRvKELQMKITKQQVFIDvinklkeNVEELIEDKYKIILEKNdtkktlQNLEE 387
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR-RKLEEAEKARQAEMD-------RQAAIYAEQERMAMERE------RELER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 388 VLANTQKHLQEsRNDKEMLQLQFKKIKAnyvclQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVER--------LQQLK 459
Cdd:pfam17380 353 IRQEERKRELE-RIRQEEIAMEISRMRE-----LERLQMERQQKNERVRQELEAARKVKILEEERQRkiqqqkveMEQIR 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 460 KELEKATASALDLLKREKE-------------AQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQV------RNLQ 520
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAremervrleeqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlekeleERKQ 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 282394045 521 FMSENERTKNIkLQQQINEVKNENAKLKQ-QVARSEEQNYVPKFETAQLKDQLEEV 575
Cdd:pfam17380 507 AMIEEERKRKL-LEKEMEERQKAIYEEERrREAEEERRKQQEMEERRRIQEQMRKA 561
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
289-555 |
1.38e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 289 WEQSAESLQPVQEDMA-----LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEE 363
Cdd:pfam01576 375 LEKAKQALESENAELQaelrtLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 364 liedkyKIIleknDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQK---NKSVS---- 436
Cdd:pfam01576 455 ------KNI----KLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKrnvERQLStlqa 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 437 QYLEMDKTLSKKEEEVERLQQLKKELekatasaldllKREKEAQEQEFLSLQEEFQKLEKenleERQKLKSRLEKLLTQV 516
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRL-----------QRELEALTQQLEEKAAAYDKLEK----TKNRLQQELDDLLVDL 589
|
250 260 270
....*....|....*....|....*....|....*....
gi 282394045 517 RNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSE 555
Cdd:pfam01576 590 DHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAE 628
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-539 |
1.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQVFIDVINKLK-ENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLqlqfK 411
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 412 KIKANYVCLQERYMTEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEF 491
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 282394045 492 QKLEK---ENLEERQKLKSRLEKLLTQVRNLQFMSENErtkniKLQQQINE 539
Cdd:COG4717 202 EELQQrlaELEEELEEAQEELEELEEELEQLENELEAA-----ALEERLKE 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
297-523 |
1.62e-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: 48.53 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 297 QPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKN 376
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKKEELEEELE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 377 DTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQER---YMTEMQQKNKSVSQYLEMDKTLSKKEEEVE 453
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlseLKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282394045 454 RLQQLKKELEKATA--SALD----LLKREKEAQEQEFLSLQEEFQKLEkenlEERQKLKSRLEKLLTQVRNLqFMS 523
Cdd:TIGR02169 952 SLEDVQAELQRVEEeiRALEpvnmLAIQEYEEVLKRLDELKEKRAKLE----EERKAILERIEEYEKKKREV-FME 1022
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
308-571 |
3.03e-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: 47.71 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 308 VLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEE 387
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 388 VLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERymtemQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELekaTA 467
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK-----NQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---TN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 468 SALDLLKREKEAQEQeflslQEEFQKLEKENleerQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKL 547
Cdd:TIGR04523 354 SESENSEKQRELEEK-----QNEIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
250 260
....*....|....*....|....
gi 282394045 548 KQQVARSEEQNYVPKFETAQLKDQ 571
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQ 448
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
443-582 |
3.19e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 443 KTLSKKEEEVER-LQQLKKELE----KATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVR 517
Cdd:PRK12704 31 AKIKEAEEEAKRiLEEAKKEAEaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282394045 518 NLQFMSENERTKNIKLQQQINEVKNenaKLKQQVARSEEQNYVPKFE-TAQLKDQLEEVLKSDITK 582
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEE---LIEEQLQELERISGLTAEEaKEILLEKVEEEARHEAAV 173
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-586 |
3.66e-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: 47.32 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQVFIDVINK-LKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFK 411
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSdLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 412 KI------KANYVCLQERYMTEMQQKNKSV----SQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldlLKREKEAQE 481
Cdd:TIGR04523 160 KYndlkkqKEELENELNLLEKEKLNIQKNIdkikNKLLKLELLLSNLKKKIQKNKSLESQISE--------LKKQNNQLK 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 482 QEFLSLQEEFQKLEKENLEERQKL---KSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQvaRSEEQN 558
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLnqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWN 309
|
250 260
....*....|....*....|....*...
gi 282394045 559 YVPKFETAQLKDQLEEvLKSDITKDTKT 586
Cdd:TIGR04523 310 KELKSELKNQEKKLEE-IQNQISQNNKI 336
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-574 |
6.24e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 440 EMDKTLSKKEEEVE---RLQQLKKELEKATASA-----------LDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKL 505
Cdd:COG1196 197 ELERQLEPLERQAEkaeRYRELKEELKELEAELlllklreleaeLEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394045 506 KsRLEKLLTQVRNLQFMSENERtknIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 574
Cdd:COG1196 277 E-ELELELEEAQAEEYELLAEL---ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-511 |
6.50e-05 |
|
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: 45.30 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQfKK 412
Cdd:COG1579 22 LEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ-KE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 413 IkanyvclqerymtEMQQKNKSV--SQYLEMDKTLSKKEEEVERLQQLKKELEKAtasaldlLKREKEAQEQEFLSLQEE 490
Cdd:COG1579 98 I-------------ESLKRRISDleDEILELMERIEELEEELAELEAELAELEAE-------LEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|.
gi 282394045 491 FQKLEKenleERQKLKSRLEK 511
Cdd:COG1579 158 LEELEA----EREELAAKIPP 174
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
440-553 |
8.05e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 440 EMDKTLSKKEEEVERLQQLKKELEKatasalDLLKREKEAQEQEflslqeefQKLEKENLEERQKLKSRLEklltqVRNL 519
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEA------ELEEKDERIERLE--------RELSEARSEERREIRKDRE-----ISRL 470
|
90 100 110
....*....|....*....|....*....|....
gi 282394045 520 QfmSENERtknikLQQQINEVKNENAKLKQQVAR 553
Cdd:COG2433 471 D--REIER-----LERELEEERERIEELKRKLER 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
306-520 |
8.18e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 306 NEVLQKLKhtnrKQEVRIQElqcsnlyLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKykiilekndtKKTLQNL 385
Cdd:COG4942 51 KALLKQLA----ALERRIAA-------LARRIRALEQELAALE---AELAELEKEIAELRAEL----------EAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 386 EEVLANTQKHlqeSRNDKEMLQLQFKKIKANYVCLQerYMtemqqknKSVSQYLEmdKTLSKKEEEVERLQQLKKELEKA 465
Cdd:COG4942 107 AELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQ--YL-------KYLAPARR--EQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 282394045 466 TAsALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQ 520
Cdd:COG4942 173 RA-ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
427-577 |
1.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 427 EMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldllKREKEAQEQEFLSLQEEFQKLEkenlEERQKLK 506
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE---------ELEKLEKLLQLLPLYQELEALE----AELAELP 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394045 507 SRLEKLLTQVRNLQfmsenertkniKLQQQINEVKNENAKLKQQVARSEEQNYVPKFET-AQLKDQLEEVLK 577
Cdd:COG4717 146 ERLEELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQ 206
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
440-517 |
2.16e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 42.19 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 440 EMDKTLSKKEEEVERLQQ-LKKELEKATASALDLLKREKEAQEQEFLSLQEEFQK--------LEKENLEERQKLKSRLE 510
Cdd:smart00935 22 QLEKEFKKRQAELEKLEKeLQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRkqqklqqdLQKRQQEELQKILDKIN 101
|
....*..
gi 282394045 511 KLLTQVR 517
Cdd:smart00935 102 KAIKEVA 108
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
449-569 |
2.38e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 449 EEEVERLQQLKKELE---KATASALDLLKREKEAQEQEFLSLQEEFQKLeKENLEER-----QKLKSRLEKLLTQVRNLQ 520
Cdd:PRK00409 519 NELIASLEELERELEqkaEEAEALLKEAEKLKEELEEKKEKLQEEEDKL-LEEAEKEaqqaiKEAKKEADEIIKELRQLQ 597
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 282394045 521 FMSenerTKNIKLQQQINEVKnenaKLKQQVARSEEQNYVPKFETAQLK 569
Cdd:PRK00409 598 KGG----YASVKAHELIEARK----RLNKANEKKEKKKKKQKEKQEELK 638
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
300-578 |
2.88e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 300 QEDM-ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKI------------------TKQQVFIDVINKLKEN 360
Cdd:pfam01576 4 EEEMqAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeemrarlaARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 361 VEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLE 440
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 441 MDKTLSKKEEEVERLQQLKKELEKATASALDLLKRE----------KEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLE 510
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEekgrqelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282394045 511 KLLTQVRNL--QFMSENERTKNIK-LQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKS 578
Cdd:pfam01576 244 ELQAALARLeeETAQKNNALKKIReLEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDT 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
432-643 |
3.07e-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: 44.66 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 432 NKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASA----------LDLLKREKEAQEQEFLSLQEEFQKLEKenleE 501
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeleeleeeLEQLRKELEELSRQISALRKDLARLEA----E 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 502 RQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEvLKSDIT 581
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAA 820
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394045 582 kDTKTTHSNLLPDCSPCEERLNPADiKRASQLASKMHSLLALMVGLLTCQDIINSDAEHFKE 643
Cdd:TIGR02168 821 -NLRERLESLERRIAATERRLEDLE-EQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
318-556 |
3.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 318 KQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIdvinKLKENVEELIEDKYK----IILEKNDTKKTLQNLEEVLANTQ 393
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKeleeVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 394 KHLQESRNDKEM---LQLQFKKIKANYVCLQER------YMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK 464
Cdd:PRK03918 228 KEVKELEELKEEieeLEKELESLEGSKRKLEEKireleeRIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 465 atasALDLLKREKEAQEQEFLSLQEEFQKLE------KENLEERQKLKSRLEKLLTQVRNLQ-FMSENERTKNIKLQQQI 537
Cdd:PRK03918 308 ----ELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEeAKAKKEELERLKKRLTG 383
|
250
....*....|....*....
gi 282394045 538 NEVKNENAKLKQQVARSEE 556
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEE 402
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
329-538 |
3.31e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 329 SNLYLEKRVKELQMKITKQQVFIDV-INKLKENVEELiEDKYKIILEKND-------TKKTLQNLEEV---LANTQKHLQ 397
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEqLPELRKELEEA-EAALEEFRQKNGlvdlseeAKLLLQQLSELesqLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 398 ESRNDKEML--QLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK----ATASALD 471
Cdd:COG3206 237 EAEARLAALraQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAqlqqEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394045 472 LLKREKEAQEQEFLSLQEEFQKLEKEnLEERQKLKSRLEKLLTQVRNLQ--FMSENERTKNIKLQQQIN 538
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEAR-LAELPELEAELRRLEREVEVARelYESLLQRLEEARLAEALT 384
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
305-575 |
3.79e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 305 LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKElqmkitkqqvfidvinkLKENVEELiedkykiilekndtkktlqn 384
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRE-----------------LESRVAEL-------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 385 leevlantQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMD---KTLSKKEEEVE-RLQQLKK 460
Cdd:pfam07888 86 --------KEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediKTLTQRVLEREtELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 461 ELEKATAsaldlLKREKEAQEQeflSLQEEFQKLEKEN---LEERQKLKSRLEKLLTQVRNLQfmseNERTKNIKLQQQI 537
Cdd:pfam07888 158 RAKKAGA-----QRKEEEAERK---QLQAKLQQTEEELrslSKEFQELRNSLAQRDTQVLQLQ----DTITTLTQKLTTA 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 282394045 538 NEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEV 575
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
442-578 |
3.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 442 DKTLSKKEEEVERLQQLKKELEKATASA---LDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRN 518
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 519 LQ--------------------FMSENERTKNIKLQQQ--INEVKNENAKLKQQVARSEEQnyvpKFETAQLKDQLEEVL 576
Cdd:COG3883 95 LYrsggsvsyldvllgsesfsdFLDRLSALSKIADADAdlLEELKADKAELEAKKAELEAK----LAELEALKAELEAAK 170
|
..
gi 282394045 577 KS 578
Cdd:COG3883 171 AE 172
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
439-541 |
4.41e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.04 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 439 LEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRN 518
Cdd:pfam02841 193 LQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQ 272
|
90 100
....*....|....*....|....*
gi 282394045 519 LQ--FMSENERTKNIKLQQQINEVK 541
Cdd:pfam02841 273 EQeeLLKEGFKTEAESLQKEIQDLK 297
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-583 |
5.03e-04 |
|
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: 43.79 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 383 QNLEEVLANTQKHLQESRNDKEMLqlqfkkikanyvclqERYMTEMQQKNKSVSQYLEmdktlskkeEEVERLQQLKKEL 462
Cdd:COG3096 532 QNAERLLEEFCQRIGQQLDAAEEL---------------EELLAELEAQLEELEEQAA---------EAVEQRSELRQQL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 463 EKATASAldllkREKEAQEQEFLSLQEEFQKLEK---ENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINE 539
Cdd:COG3096 588 EQLRARI-----KELAARAPAWLAAQDALERLREqsgEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 282394045 540 VknenaklkQQVARSEEQnyvpkfETAQLKDQLEEVLKSDITKD 583
Cdd:COG3096 663 L--------SQPGGAEDP------RLLALAERLGGVLLSEIYDD 692
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
342-574 |
7.73e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 43.12 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 342 MKITKQQVFIDVINK-----LKENVEELIEDKYKI----ILEKNDTKKTLQNLEEVLANT-----QKHL----------- 396
Cdd:PRK12903 660 LRITHFKFSEKDFENyhkeeLAQYLIEALNEIYFKkrqvILDKIALNTFFESERYIILSAldkywQNHIdtmdklrsgvn 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 397 --QESRND-------------KEMLQ-------LQFKKIKANYVCLQERYMTEMQQKNKSVSQ-YLEMDKTLSKKEEEVE 453
Cdd:PRK12903 740 lvQYSQKNpyqvyteegtkkfNILLQeiaydviVSLFNNPNAEKILIITEILSDGINNSDINDrPQELIDQIIESEEERL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 454 RLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKlltqvrnlqfmsENERTKNIKL 533
Cdd:PRK12903 820 KALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEF------------KNDPKKLNKL 887
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394045 534 qqqinevKNENAKLKQQVARSEEQNYVPKfETAQLKDQLEE 574
Cdd:PRK12903 888 -------IIAKDVLIKLVISSDEIKQDEK-TTKKKKKDLEK 920
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
354-585 |
8.05e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 354 INKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNK 433
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 434 SVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASAldllKREKEAQEQEFLSLQEEFQKLEKENLE-ERQKLKSRLEKL 512
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER----EEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDEL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282394045 513 LTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
300-548 |
8.09e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 300 QEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVfidvINKLKENVEELIEDKYKIILEKNDTK 379
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL----LQELLLKEEELEEQKLKDELESKEEK 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKAnyvcLQERYMTEMQQKNKSVSQYLEMDKTLsKKEEEVERLQQLK 459
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL----LKYEEEPEELLLEEADEKEKEENNKE-EEEERNKRLLLAK 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 460 KELEKATASALDLLKREKEaqeqeflslQEEFQKLEKENL-EERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQIN 538
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEE---------RYNKDELEKERLeEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
250
....*....|
gi 282394045 539 EVKNENAKLK 548
Cdd:pfam02463 1041 ELGGSAELRL 1050
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
439-540 |
8.24e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 439 LEMDKT---LSKKEEEVERL----QQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKlEKENLEERQKLKSRLEK 511
Cdd:COG0542 404 MEIDSKpeeLDELERRLEQLeiekEALKKEQDEASFERLAELRDELAELEEELEALKARWEA-EKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 282394045 512 LLTQVRNLQFMSENERTKNIKLQQQINEV 540
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
276-520 |
9.23e-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: 43.13 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 276 RSEACRENCE-MPDWEQSAESLQPVQEDMAlnEVLQKLKHTNRKQEVRIQELQcsnlYLEKRVKELQMKITKQQV----- 349
Cdd:TIGR02169 711 LSDASRKIGEiEKEIEQLEQEEEKLKERLE--ELEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEalndl 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 350 -------FIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDkemlqlqfkkikanyvclqe 422
Cdd:TIGR02169 785 earlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-------------------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 423 rymteMQQKNKSVSQYLEMDKT-LSKKEEEVERLQQLKKELEKatasALDLLKREKEAQEQEFLSLQEEFQKLEkenlEE 501
Cdd:TIGR02169 845 -----LKEQIKSIEKEIENLNGkKEELEEELEELEAALRDLES----RLGDLKKERDELEAQLRELERKIEELE----AQ 911
|
250
....*....|....*....
gi 282394045 502 RQKLKSRLEKLLTQVRNLQ 520
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALE 930
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
335-585 |
1.02e-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: 42.70 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 335 KRVKELQMKITKQQVFIDVINKLKENVE----ELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQ----------ESR 400
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELEnelnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqisELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 401 NDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK---ATASALDLLKREK 477
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnQLKSEISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 478 EAQEQEFLSLQEEFQKLEKENLE-ERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEE 556
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQnQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
250 260
....*....|....*....|....*....
gi 282394045 557 QNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
347-570 |
1.31e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 347 QQVFIDVINKLKENVEELIE------DKYKIILEK---NDTKKTLQNLEEVLANTQKHL-----QESRNDKEMLQLQ--F 410
Cdd:pfam06160 51 RKKWDDIVTKSLPDIEELLFeaeelnDKYRFKKAKkalDEIEELLDDIEEDIKQILEELdelleSEEKNREEVEELKdkY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 411 KKIKANYvcLQERYM-------------------TEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEKAtasaLD 471
Cdd:pfam06160 131 RELRKTL--LANRFSygpaidelekqlaeieeefSQFEELTES-GDYLEAREVLEKLEEETDALEELMEDIPPL----YE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 472 LLKREKEAQEQEflsLQEEFQKLEKEN--------LEERQKLKSRLEKLLTQVRNLQFmsENERTKNIKLQQQI------ 537
Cdd:pfam06160 204 ELKTELPDQLEE---LKEGYREMEEEGyalehlnvDKEIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIdqlydl 278
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394045 538 --------NEVKNENAKLKQQVARSEEQNYVPKFETAQLKD 570
Cdd:pfam06160 279 lekevdakKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQ 319
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
333-585 |
1.33e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 333 LEKRVKELQMKITKQQVFIdviNKLKENVEELIEDKYKIILEKNDTKKTLQNLEE---VLANTQKHLQESRNDKEmlqlq 409
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFL---NKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERkinVLQKKIENLQEQLRDKD----- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 410 fkKIKANyvcLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQ---------------QLKKELeKATASALDLLK 474
Cdd:pfam10174 415 --KQLAG---LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKeqreredrerleeleSLKKEN-KDLKEKVSALQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 475 REKEAQEQEFLSLQEEFQKLEKENLEERQKLKSrLEKLLTQVRN--LQFMSENERTKNIKLQQQINEVKNENAK-LKQQV 551
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSLASSGLKKDSKLKS-LEIAVEQKKEecSKLENQLKKAHNAEEAVRTNPEINDRIRlLEQEV 567
|
250 260 270
....*....|....*....|....*....|....
gi 282394045 552 ARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
336-611 |
1.47e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 336 RVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKA 415
Cdd:COG5022 756 RGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRET 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 416 NYVCLQERYMTEMQQKNKSVsQYLEMDKTLSKKE---EEVERLQQLKKEL--EKATASALDLLKREKEAQEQEFLSLQEE 490
Cdd:COG5022 836 EEVEFSLKAEVLIQKFGRSL-KAKKRFSLLKKETiylQSAQRVELAERQLqeLKIDVKSISSLKLVNLELESEIIELKKS 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 491 FQKLEKENLEERQKLKSRLEKLltqvrNLQFMSENERTKNIKLQQQINEVKNENAKLKQQvarSEEQNYVPKFETAQLKD 570
Cdd:COG5022 915 LSSDLIENLEFKTELIARLKKL-----LNNIDLEEGPSIEYVKLPELNKLHEVESKLKET---SEEYEDLLKKSTILVRE 986
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394045 571 QLEEVLKSDITKDTKTTHSNLLPDCSPCEERLNPADIKRAS 611
Cdd:COG5022 987 GNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
382-555 |
1.57e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 382 LQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTemQQKNKSVS--------QYLEMDKTLSKKE---- 449
Cdd:PRK11637 77 LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA--QERLLAAQldaafrqgEHTGLQLILSGEEsqrg 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 450 ---------------EEVERLQQLKKELEKATASALdllkrEKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLT 514
Cdd:PRK11637 155 erilayfgylnqarqETIAELKQTREELAAQKAELE-----EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 282394045 515 qvrnlqfmsenertkniKLQQQINEVKNENAKLKQQVARSE 555
Cdd:PRK11637 230 -----------------KDQQQLSELRANESRLRDSIARAE 253
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
299-535 |
1.59e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 299 VQEDMALNEVLQKLKHTNRKQEVRIQ-------ELQCSNLYLEKRVKELQM--KITKQQVFIDVINK-LKENVEELIEDK 368
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNaavrektSLSASVASLEKQLLELTRvnELLKAKFSEDGTQKkMSSLSMELMKLR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 369 YKIILEKNDTKKTLQNLEEVLANTQKHLQESRndKEMLQLQFKKIKANYVCLQERYMTEmqqknksvsQYLEMDKTLSKK 448
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSK--GKVAQLEEKLVSTEKEKIEEKSETE---------KLLEYITELSCV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 449 EEEVERLQ---QLKKELEKATASALDLLKREKEAQEQEFL----SLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQF 521
Cdd:pfam15905 235 SEQVEKYKldiAQLEELLKEKNDEIESLKQSLEEKEQELSkqikDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKE 314
|
250
....*....|....
gi 282394045 522 MSENERTKNIKLQQ 535
Cdd:pfam15905 315 KLTLEEQEHQKLQQ 328
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
388-587 |
1.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 388 VLANTQkhLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQ----QLKKELE 463
Cdd:COG3883 12 AFADPQ--IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEaeieERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 464 KATASA-------------------------LDLLKREKEAQE---QEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQ 515
Cdd:COG3883 90 ERARALyrsggsvsyldvllgsesfsdfldrLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394045 516 VRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTT 587
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-494 |
1.81e-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: 41.67 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 304 ALNEVLQKLKHTNRKQEVRIQELQcsnlyleKRVKELQMKITKQQ-VFIDVINKLKENVEeliEDKYKIIL---EKNDTK 379
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELE-------KEIAELRAELEAQKeELAELLRALYRLGR---QPPLALLLspeDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 459
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 282394045 460 KELEKATASALDLLKR-EKEAQEQEFLSLQEEFQKL 494
Cdd:COG4942 216 AELQQEAEELEALIARlEAEAAAAAERTPAAGFAAL 251
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
336-527 |
2.39e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 336 RVKELQMKITKQQVFIDVINKLKENVE-ELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIK 414
Cdd:pfam13868 7 ELRELNSKLLAAKCNKERDAQIAEKKRiKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 415 ANYVCLQERYMTEMQQKNKSVSQYLEMDktLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQE---EF 491
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEED--QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkEK 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 282394045 492 QKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENER 527
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
376-571 |
2.83e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 376 NDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKikanyvclQERYMTEMQQKNKSVSQYLE-MDKTLSKKEEEVER 454
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK--------QEEAISQASRKLRETQNTLNqLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 455 LQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEK-------ENlEERQKLKSRLEKLLTQVRNLQFMSENER 527
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGERilayfgyLN-QARQETIAELKQTREELAAQKAELEEKQ 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 282394045 528 TKniklQQQI-NEVKNENAKLKQqvARSEEQNYVPKFETAQLKDQ 571
Cdd:PRK11637 194 SQ----QKTLlYEQQAQQQKLEQ--ARNERKKTLTGLESSLQKDQ 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
440-575 |
3.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 440 EMDKTLSKKEEEVERLQQLKKELE------KATASALDLLKREKEAQ---------EQEFLSLQEEFQKLEKEnLEERQK 504
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEeleaelEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEER-LEELRE 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394045 505 LKSRLEKLLTQVRNLQF-MSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEV 575
Cdd:COG4717 161 LEEELEELEAELAELQEeLEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
294-688 |
3.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 294 ESLQPVQEDMALNEVLQKLKhtNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFI----DVINKLKENVEELIEDKY 369
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLK--KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAKG 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 370 KIILEKNDTkkTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVclqerymtEMQQKNKSVSQYLEMDKTLSKKE 449
Cdd:PRK03918 437 KCPVCGREL--TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR--------ELEKVLKKESELIKLKELAEQLK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 450 EEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLE------KENLEERQKLKSRLEKLLTQVRNLQFMS 523
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkklAELEKKLDELEEELAELLKELEELGFES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 524 ENERTKNIK--------------LQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKsditKDTKTTHS 589
Cdd:PRK03918 587 VEELEERLKelepfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK----KYSEEEYE 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 590 NLLpdcspceerlnpadiKRASQLASKMHSLLALMVGLLTCQDIINSDAEHFKESEKvsdimlqklksLHLKKKTLDKEL 669
Cdd:PRK03918 663 ELR---------------EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-----------EREKAKKELEKL 716
|
410
....*....|....*....
gi 282394045 670 LKHKDRITTFRELIAKEKA 688
Cdd:PRK03918 717 EKALERVEELREKVKKYKA 735
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
351-573 |
4.07e-03 |
|
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: 40.78 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 351 IDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKAnyvcLQERYMTEMQQ 430
Cdd:pfam05667 275 QDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE----LQEQLEDLESS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 431 KNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATAS---ALDLLkreKEAQEQEflslqEEFQKLEKENLEERQKLKS 507
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVkkkTLDLL---PDAEENI-----AKLQALVDASAQRLVELAG 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394045 508 RLEK----LLTQVRNLqfmSENERTKNIKLQQQINEVKNENAKLKQ--QVARSEEQNYvpkfetAQLKDQLE 573
Cdd:pfam05667 423 QWEKhrvpLIEEYRAL---KEAKSNKEDESQRKLEEIKELREKIKEvaEEAKQKEELY------KQLVAEYE 485
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
348-497 |
4.75e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 348 QVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANyvcLQERYMTE 427
Cdd:smart00787 140 KLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDR---AKEKLKKL 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 428 MQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKE 497
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
440-518 |
5.17e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 440 EMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRL-EKLLTQVRN 518
Cdd:pfam03938 23 QLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELlQPIQDKINK 102
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
353-510 |
5.39e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 353 VINKLKENVEELIEDKYKII----LEKNDTKKTLQNLEEVLANTQKHLqesrnDKEMLQLQFKKIKANyvcLQERYMTEM 428
Cdd:pfam05262 182 VVEALREDNEKGVNFRRDMTdlkeRESQEDAKRAQQLKEELDKKQIDA-----DKAQQKADFAQDNAD---KQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 429 QQKNKS------VSQYLEMDKTLSKKEEEVERLQQLKK----ELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKEN 498
Cdd:pfam05262 254 QQEAKNlpkpadTSSPKEDKQVAENQKREIEKAQIEIKkndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPV 333
|
170
....*....|..
gi 282394045 499 LEERQKLKSRLE 510
Cdd:pfam05262 334 AEDLQKTKPQVE 345
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
283-556 |
5.48e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 283 NCEMPDWEQSA-----------ESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfi 351
Cdd:pfam12128 541 RKEAPDWEQSIgkvispellhrTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR--- 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 352 DVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLantQKHLQESRNDKEMLQLQFKKIKANYVclQERYMTEMQQK 431
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASREETFARTALKNARLDL---RRLFDEKQSEKDKKNKALAERKDSAN--ERLNSLEAQLK 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 432 NKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEK 511
Cdd:pfam12128 693 QLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAK 772
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282394045 512 LLTQVRNL------------------QFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEE 556
Cdd:pfam12128 773 LKREIRTLerkieriavrrqevlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA 835
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
447-588 |
5.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 447 KKEEEVERLQQLKKE----LEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLltqvrnlqfm 522
Cdd:PRK12705 31 LAKEAERILQEAQKEaeekLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL---------- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282394045 523 sENERTKNIKLQQQINEVKNENAKLKQQVARSEEQnyVPKFETAQLKDQLEEVLKSDITKDTKTTH 588
Cdd:PRK12705 101 -DNLENQLEEREKALSARELELEELEKQLDNELYR--VAGLTPEQARKLLLKLLDAELEEEKAQRV 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
382-574 |
5.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 382 LQNLEEVL-ANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEmdkTLSKKEEEVERLQQLKK 460
Cdd:PTZ00121 1551 LKKAEELKkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE---EAKKAEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 461 ELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEV 540
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190
....*....|....*....|....*....|....
gi 282394045 541 KNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 574
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
440-516 |
6.08e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 38.28 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 440 EMDKTLSKKEEEVERLQQ-LKKELEKATASALDLLKREKEAQEQEFLSLQEEFQK--------LEKENLEERQKLKSRLE 510
Cdd:COG2825 47 KLEKEFKKRQAELQKLEKeLQALQEKLQKEAATLSEEERQKKERELQKKQQELQRkqqeaqqdLQKRQQELLQPILEKIQ 126
|
....*.
gi 282394045 511 KLLTQV 516
Cdd:COG2825 127 KAIKEV 132
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
367-585 |
6.58e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 367 DKYKIILEKNDtKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKsvsqyLEMDKTLS 446
Cdd:pfam02463 142 GKIEIIAMMKP-ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK-----KALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 447 KKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKL-LTQVRNLQFMSEN 525
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKkLQEEELKLLAKEE 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394045 526 E--RTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:pfam02463 296 EelKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
307-557 |
7.51e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 307 EVLQKLKHTNRKQEVRIQELQCSNLYLEK--RVKElQMKITKQQVfIDVINKLKENVEELieDKYKIILEKnDTKKTLQN 384
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKidRQKE-ETEQLKQQL-AQAPAKLRQAQAEL--EALKDDNDE-ETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 385 -----LEEVLANTQKHLQEsrndkemLQLQFKKIKANYVCLQ---ERYMTEMQQKNKsvsqylemdktlskkeeeveRLQ 456
Cdd:PRK11281 121 lslrqLESRLAQTLDQLQN-------AQNDLAEYNSQLVSLQtqpERAQAALYANSQ--------------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 457 QLKKELEKATASALDLL--KREKEAQEQEFLSLQEEFQKLEKENleerqklKSRLEKLLTQVRNLqfMSENERtkniKLQ 534
Cdd:PRK11281 174 QIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRKSLEG-------NTQLQDLLQKQRDY--LTARIQ----RLE 240
|
250 260
....*....|....*....|....
gi 282394045 535 QQINEVKNE-NAKLKQQvarSEEQ 557
Cdd:PRK11281 241 HQLQLLQEAiNSKRLTL---SEKT 261
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
302-549 |
7.65e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 302 DMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEdKYKIILEKNDTKKT 381
Cdd:TIGR00606 300 DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR-ARDSLIQSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 382 LQNLEE------VLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTlsKKEEEVERL 455
Cdd:TIGR00606 379 LDGFERgpfserQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE--ILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 456 QQLKKELEKATASALDLLKREKEAQEQEflslqEEFQKLEKenleerqklKSRLEKLLTQVRNLQFMSENERTKNIKLQQ 535
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAE-----RELSKAEK---------NSLTETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
250
....*....|....
gi 282394045 536 QINEVKNENAKLKQ 549
Cdd:TIGR00606 523 EMEQLNHHTTTRTQ 536
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
443-590 |
7.73e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 443 KTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLE---KENLEERQKLKSRLEKLLTQVRNL 519
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYllyLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282394045 520 QFMSENERTKNIKLQQQINEVKNENAKLKQQVarSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTTHSN 590
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ--EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
427-557 |
8.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 427 EMQQKNKSVSQYLEMDKTLSKKEEEVERLQQ--LKKElekatasalDLLKREKEAQEQEFLSLQEEFQKLEK--ENLEER 502
Cdd:PRK12704 59 LLEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKE---------ENLDRKLELLEKREEELEKKEKELEQkqQELEKK 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 282394045 503 QK-LKSRLEKLLTQVRNLQFMSENErTKNIKLQQQINEVKNENAKLkqqVARSEEQ 557
Cdd:PRK12704 130 EEeLEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVL---IKEIEEE 181
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
284-573 |
8.58e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 284 CEMPDWEQSAESLQP---------VQEDMALNEVLQKLKHTNRKQEVRIQELQCS-NLYLEKRVKE-LQMKITKQQVFID 352
Cdd:TIGR00618 584 EDIPNLQNITVRLQDlteklseaeDMLACEQHALLRKLQPEQDLQDVRLHLQQCSqELALKLTALHaLQLTLTQERVREH 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 353 VInKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKN 432
Cdd:TIGR00618 664 AL-SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 433 KSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFlslQEEFQKLEKENLEERQKLKSRLEKL 512
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR---EEDTHLLKTLEAEIGQEIPSDEDIL 819
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282394045 513 LTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARsEEQNYVPKFETAQLKDQLE 573
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ-LAQLTQEQAKIIQLSDKLN 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
447-575 |
8.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 447 KKEEEVERLQQLKKELEKAtASALDLLKREKEAQEQEFLSLQ--EEFQKLEKENL---EERQKLKSRLEKLLT---QVRN 518
Cdd:COG4913 611 KLAALEAELAELEEELAEA-EERLEALEAELDALQERREALQrlAEYSWDEIDVAsaeREIAELEAELERLDAssdDLAA 689
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 282394045 519 LQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEqnyvpkfETAQLKDQLEEV 575
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-------ELDELQDRLEAA 739
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
276-512 |
9.09e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 276 RSEACRENCEMPDWEQSAESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVIN 355
Cdd:pfam02463 269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 356 KLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSV 435
Cdd:pfam02463 349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282394045 436 SQYLEMDKTLSKKEEEVERLQQLKKELEKATasaLDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKL 512
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEKQELK---LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
362-553 |
9.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 362 EELIEDKYKIILEKNDTKKTLQNLE-EVLANTQKHLQESRNDKEMLQLQFKkikanyvclQERYMTEMQQ-----KNKSV 435
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQ---------LEELEQEIAAllaeaGVEDE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394045 436 SQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQ-EQEFLSLQEEFQKLEKE---NLEERQKLKSRLEK 511
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEEleeLREELAELEAELEQ 464
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 282394045 512 LLTQvRNLQfmsenertkniKLQQQINEVKNENAKLKQQVAR 553
Cdd:COG4717 465 LEED-GELA-----------ELLQELEELKAELRELAEEWAA 494
|
|
| |
