|
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: 802.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 30 MSESDTMNVSNLSQGVMLSHSPICMETTGTTCDLPQNEIKNFERENEYESTLCEDAYGTLDNLLNDNNIENYSTNALIQP 109
Cdd:pfam15066 1 MSESDAMNVSGLSQDLTHSDSPLCMETSSTTSDLPQNEIKNVKRENESKFTLSEDIYSTLDNLLGDINIGSYSQNVLIQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 110 VDTiSISSLRQFETVCKFHWVEAFDDEM------------TEKPEFQSQVYNYAKDNNIKQDSFKEENPMETSVSANTDQ 177
Cdd:pfam15066 81 VDT-SISSLRQFEPICKFHWTEAFNDEMttfqnltegfsyTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 178 LGNEYFRQPPpRSPPLIHCSGEMLKFTEKSLAKSIAKESALNPSQPPSFLCK---------------------------- 229
Cdd:pfam15066 160 LANECVRQSS-RSPPLIHCSGETLPFTEKSLAKSTAKESALNPSQPQSFLYEenvprnvekpfykensfslldlranykt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 230 --TAVPSKEIQNYGEIPEMSVSYEKEVTAEGVERPEIVSTWSSAGISWRSEACRENCEMPDWEQSAESLQPVQEDMALNE 307
Cdd:pfam15066 239 eeTEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIASTWSPAGISWSSGASQENCKTPDTEQSFESLQPLEEDMALNE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 308 VLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEE 387
Cdd:pfam15066 319 VLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 388 VLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATA 467
Cdd:pfam15066 399 ILANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATT 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 282394043 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 |
5.54e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 304 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQV-FIDVINKLKENVEELIEDKYKIIL---EKNDTK 379
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErLANLERQLEELEAQLEELESKLDElaeELAELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 459
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 460 KELE--------KATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSrLEKLLTQVRNLQFMSENERTKNI 531
Cdd:TIGR02168 424 EELLkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-AERELAQLQARLDSLERLQENLE 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 282394043 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 |
1.32e-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: 57.85 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKK 412
Cdd:COG4942 25 AEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 413 IKANYvclqERYMTEMQQknksVSQYLEMDKTLSKKE-EEVERLQQLKKELEKATASALDLLKREKE---AQEQEFLSLQ 488
Cdd:COG4942 102 QKEEL----AELLRALYR----LGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394043 489 EEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQ 567
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-520 |
1.60e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 289 WEQSAESLQPVQEDMA-LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQ----MKITKQQVFIDVINKLKENVEE 363
Cdd:COG1196 234 LRELEAELEELEAELEeLEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 364 LIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCL--------------QERYMTEMQ 429
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaelaeaeeeleelAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 430 QKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEfLSLQEEFQKLEKENLEERQKLKSRL 509
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEEA 472
|
250
....*....|.
gi 282394043 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 |
2.52e-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: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 300 QEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTK 379
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 459
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 460 KELEKATA---SALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKsrleKLLTQVRNLQFMSENERTKNIKLQQQ 536
Cdd:TIGR02168 862 EELEELIEeleSELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 282394043 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 |
4.27e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 334 EKRVKELQMKITKqqvfidvINKLKENVEELIEdkykiilEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKI 413
Cdd:COG1196 221 ELKELEAELLLLK-------LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 414 KANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASA---LDLLKREKEAQEQEFLSLQEE 490
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 491 FQKLEKENLEERQKLKSRLEKLLTQVRNLQfmseNERTKNIKLQQQINEVKNENAKLKQQVARSEEQnyvpKFETAQLKD 570
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEEE 438
|
....*...
gi 282394043 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 |
6.58e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKykiilekndtKKTLQNLEEVLANTQKHLQESRNDKEML--QLQF 410
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEEL----------RLEVSELEEEIEELQKELYALANEISRLeqQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 411 KKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEV--ERLQQLKKELEKATASALDLLKREKEAQEQ------ 482
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkEELESLEAELEELEAELEELESRLEELEEQletlrs 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 483 EFLSLQEEFQKLEKE--NLEERQK-LKSRLEKLLTQVRNLQfmSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNY 559
Cdd:TIGR02168 387 KVAQLELQIASLNNEieRLEARLErLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250
....*....|...
gi 282394043 560 VPKFETAQLKDQL 572
Cdd:TIGR02168 465 ELREELEEAEQAL 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-591 |
7.83e-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: 55.54 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 374 EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIkanyvclqERYMTEMQQKNKSVSQYL-EMDKTLSKKEEEV 452
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------ERRIAALARRIRALEQELaALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 453 ERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLE--------------------KENLEERQKLKSRLEKL 512
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylaparreqaeelRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394043 513 LTQVRNLQFMSENERTKnikLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTTHSNL 591
Cdd:COG4942 173 RAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-580 |
8.69e-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: 56.23 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 304 ALNEVLQKLKHTNRKQEVRIQELQCSNLylEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDT----- 378
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAI--ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrv 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 379 KKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQ------ERYMTEMQQKNKSVSQYL-----EMDKTLSK 447
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieelEREIEEERKRRDKLTEEYaelkeELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 448 KEEEVERLQQLKKELeKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKS-----------------RLE 510
Cdd:TIGR02169 373 LEEVDKEFAETRDEL-KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieakineleeekedkalEIK 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 511 KLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQlEEVLKSDI 580
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-EEVLKASI 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
288-556 |
2.36e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 288 DWEQSAESLQPVQEDM-ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIE 366
Cdd:PRK03918 159 DYENAYKNLGEVIKEIkRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 367 DKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKaNYVCLQERYMTEMQQKNKSVSQYLEMDKTLS 446
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 447 KKEEEVERLQQLKKELEKATASALDLLKREKEAQEqEFLSLQEEFQKLE--KENLEERQKLKSRLEKLltQVRNLQFMSE 524
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEK-RLEELEERHELYEeaKAKKEELERLKKRLTGL--TPEKLEKELE 394
|
250 260 270
....*....|....*....|....*....|..
gi 282394043 525 NERTKNIKLQQQINEVKNENAKLKQQVARSEE 556
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
304-582 |
4.28e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 304 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKqqvfIDVINKLKENVEELIEDKYKIILEKNDTKKTLQ 383
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 384 NLEEVLANTQKHLQESRNDK---EMLQLQFKKIKANYVCLQERY---------MTEMQQ-----KNKSVSQYLEMDKTLS 446
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHelyeeakakKEELERlkkrlTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 447 KKEEEVE-----------RLQQLKKELEKATaSALDLLKRE-----KEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLE 510
Cdd:PRK03918 398 KAKEEIEeeiskitarigELKKEIKELKKAI-EELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282394043 511 KLLTQVRNLQFMSENERT--KNIKLQQQINEVKNENAKL-KQQVARSEEQNYVPKFETAQLKDQLeEVLKSDITK 582
Cdd:PRK03918 477 KLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEK 550
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
350-541 |
8.03e-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: 51.81 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 350 FIDVINKLKENVEELIEDKYKIILEKNDT------KKTLQNLEEVLANTQKHL--------QESRNDKEML-----QLQF 410
Cdd:cd16269 84 FKDEDQKFQKKLMEQLEEKKEEFCKQNEEasskrcQALLQELSAPLEEKISQGsysvpggyQLYLEDREKLvekyrQVPR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 411 KKIKANYVcLQErYMTEMQQKNKSVsqyLEMDKTLSKKEEEVERlQQLKKELEKATASAL----DLLKREKEAQEQeflS 486
Cdd:cd16269 164 KGVKAEEV-LQE-FLQSKEAEAEAI---LQADQALTEKEKEIEA-ERAKAEAAEQERKLLeeqqRELEQKLEDQER---S 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 282394043 487 LQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQ--FMSENERTKNIKLQQQINEVK 541
Cdd:cd16269 235 YEEHLRQLKEKMEEERENLLKEQERALESKLKEQeaLLEEGFKEQAELLQEEIRSLK 291
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-575 |
1.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 361 VEELIEDK---YKIILE--------KNDTKKTLQNLEEVLANTQK---HLQESRNDKEMLQLQ------FKKIKA----- 415
Cdd:TIGR02168 146 ISEIIEAKpeeRRAIFEeaagiskyKERRKETERKLERTRENLDRledILNELERQLKSLERQaekaerYKELKAelrel 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 416 -------NYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldllkrEKEAQEQEFLSLQ 488
Cdd:TIGR02168 226 elallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-----------EIEELQKELYALA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 489 EEFQKLEKenleERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQL 568
Cdd:TIGR02168 295 NEISRLEQ----QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
....*..
gi 282394043 569 KDQLEEV 575
Cdd:TIGR02168 371 ESRLEEL 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
305-551 |
1.36e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 305 LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIE--DKYKIILEKN--DTKK 380
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQlkVLSR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 381 TLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKK 460
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 461 --ELEKATASALDLLKREKEAQEqEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQIN 538
Cdd:TIGR04523 556 keNLEKEIDEKNKEIEELKQTQK-SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
250
....*....|...
gi 282394043 539 EVKNENAKLKQQV 551
Cdd:TIGR04523 635 NIKSKKNKLKQEV 647
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
333-555 |
2.78e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNdkemlqlQFKK 412
Cdd:COG3883 21 KQKELSELQAELEAAQ---AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 413 -IKANYVCLQERYMTEMQQKNKSVSQYLE----MDKTLSKKEEEVERLQQLKKELEKATAsALDLLKREKEAQEQEFLSL 487
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKA-ELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282394043 488 QEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSEnERTKNIKLQQQINEVKNENAKLKQQVARSE 555
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA-AAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
356-557 |
2.85e-06 |
|
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: 51.10 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 356 KLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRndkemLQLQFKKIKANY-VCLQERYMTEMQQKnks 434
Cdd:pfam15818 159 KLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSK-----VTCQYKMGEENInLTIKEQKFQELQER--- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 435 vsqyLEMDKTLSKK-EEEVERLQQLKKELEKATASALDLLKREKEAQ---EQEFLSLQEEFQKLEKENLEERQKLKSRLE 510
Cdd:pfam15818 231 ----LNMELELNKKiNEEITHIQEEKQDIIISFQHMQQLLQQQTQANtemEAELKALKENNQTLERDNELQREKVKENEE 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 282394043 511 KLLtqvrNLQfmseNERTKNIK--------LQQQINEVKNENAKLKQQVARSEEQ 557
Cdd:pfam15818 307 KFL----NLQ----NEHEKALGtwkkhveeLNGEINEIKNELSSLKETHIKLQEH 353
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
305-552 |
5.57e-06 |
|
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: 50.11 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 305 LNEVLQKLKHTNR--KQEVRIQELQCSNLYLEKRVKELQMKITK--QQVFIDVINKLKE-------NVEELIEDKYKIIL 373
Cdd:pfam05483 217 LKEDHEKIQHLEEeyKKEINDKEKQVSLLLIQITEKENKMKDLTflLEESRDKANQLEEktklqdeNLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 374 EKNDTKKTLQN-------LEEVLANTQK-----------HLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSV 435
Cdd:pfam05483 297 ELEDIKMSLQRsmstqkaLEEDLQIATKticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 436 SQYLEMDKTLSKKEEEVERLQQLK--KELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKEN---LEERQK------ 504
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKnnKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELiflLQAREKeihdle 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 282394043 505 -----LKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVA 552
Cdd:pfam05483 457 iqltaIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
294-574 |
6.43e-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: 49.97 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 294 ESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIIL 373
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 374 EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANyvclqerymTEMQQKNKSVSQYLEMDKTLSKKEEEVE 453
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL---------KLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 454 RLQQLKKELEKATASAldLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKL 533
Cdd:pfam02463 332 KEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394043 534 QQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 574
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-553 |
1.08e-05 |
|
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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 352 DVINKLKEN-VEELIEDKykiileKNDTKKTLQNLEEVLANTQKHLQESRNDkemLQlQFKKiKANYVCLQERYMTEMQQ 430
Cdd:COG3206 152 AVANALAEAyLEQNLELR------REEARKALEFLEEQLPELRKELEEAEAA---LE-EFRQ-KNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 431 KNKSVSQYLEMDKTLSKKEEeveRLQQLKKELEKATASALDLLkrekeaQEQEFLSLQEEFQKLEKE--NLEER------ 502
Cdd:COG3206 221 LSELESQLAEARAELAEAEA---RLAALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAElaELSARytpnhp 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 282394043 503 --QKLKSRLEKLLTQVRNLQFMSENERTKNIK-LQQQINEVKNENAKLKQQVAR 553
Cdd:COG3206 292 dvIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLAQLEARLAE 345
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
349-549 |
1.52e-05 |
|
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: 48.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 349 VFIDVINKLKENvEELIEDKYKIILEKNDTK--KTLQNLEEVLANTQKHLQES-RNDKEMLQLQFKKIKANyvclqerym 425
Cdd:pfam09731 266 IFPDIIPVLKED-NLLSNDDLNSLIAHAHREidQLSKKLAELKKREEKHIERAlEKQKEELDKLAEELSAR--------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 426 temqQKNKSVSQYLEMDKTLSKKEEEV-ERLQQ-LKKELEKATASALDLLKREKEAQEQEflsLQEEFQKLEKENLE-ER 502
Cdd:pfam09731 336 ----LEEVRAADEAQLRLEFEREREEIrESYEEkLRTELERQAEAHEEHLKDVLVEQEIE---LQREFLQDIKEKVEeER 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 282394043 503 QKLKSRLEKLLTQVRNLQfmsenertkniKLQQQINEVKNENAKLKQ 549
Cdd:pfam09731 409 AGRLLKLNELLANLKGLE-----------KATSSHSEVEDENRKAQQ 444
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
422-576 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 422 ERYMTEMQQKNKSVSQYLEmdkTLSKKEEEVERLQQLKKELEKATASAL----DLLKREKEAQEQEFLSLQEEFQKLEKE 497
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 498 nLEERQKLKSRLEKLLTQV-RNLQFMSENERtknIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVL 576
Cdd:TIGR02169 260 -ISELEKRLEEIEQLLEELnKKIKDLGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
333-541 |
3.22e-05 |
|
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: 47.54 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITK--------QQVFIDVINKLKENVEELIEDKYKiiLEKNDTKKTLQNLEEVLANTQKHLQESRNDK- 403
Cdd:pfam06160 184 LEEETDALEELMEDipplyeelKTELPDQLEELKEGYREMEEEGYA--LEHLNVDKEIQQLEEQLEENLALLENLELDEa 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 404 -EMLQLQFKKIKANYVCLQ----------------ERYMTEMQQKNKS-VSQYLEMDKTLSKKEEEVERLQQLKKELEKA 465
Cdd:pfam06160 262 eEALEEIEERIDQLYDLLEkevdakkyveknlpeiEDYLEHAEEQNKElKEELERVQQSYTLNENELERVRGLEKQLEEL 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282394043 466 TASALDLLKREKEaQEQEFLSLQEEFqkleKENLEERQKLKSRLEKLLTQVRNLqFMSENE-RTKNIKLQQQINEVK 541
Cdd:pfam06160 342 EKRYDEIVERLEE-KEVAYSELQEEL----EEILEQLEEIEEEQEEFKESLQSL-RKDELEaREKLDEFKLELREIK 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-539 |
3.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQVFIDVINKLK-ENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLqlqfK 411
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 412 KIKANYVCLQERYMTEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEF 491
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 282394043 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 |
3.72e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 297 QPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKN 376
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKKEELEEELE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 377 DTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQER---YMTEMQQKNKSVSQYLEMDKTLSKKEEEVE 453
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlseLKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282394043 454 RLQQLKKELEKATA--SALD----LLKREKEAQEQEFLSLQEEFQKLEkenlEERQKLKSRLEKLLTQVRNLqFMS 523
Cdd:TIGR02169 952 SLEDVQAELQRVEEeiRALEpvnmLAIQEYEEVLKRLDELKEKRAKLE----EERKAILERIEEYEKKKREV-FME 1022
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
297-557 |
4.49e-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: 47.04 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 297 QPVQEDMALNEVLQKLKH----TNRKQEVRIQELQCSNLYLEKRVKELQMKITKQqvfidvINKLKENVEELIEDKYKII 372
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHqkavSERQQQEKFEKMEQERLRQEKEEKAREVERRRK------LEEAEKARQAEMDRQAAIY 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 373 LEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKAnyvclQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEV 452
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVRQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 453 ER--------LQQLKKELEKATASALDLLKREKE-------------AQEQEFLSLQEEFQKLEKENLEERQKLKSRLEK 511
Cdd:pfam17380 412 QRkiqqqkveMEQIRAEQEEARQREVRRLEEERAremervrleeqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 282394043 512 LLTQV------RNLQFMSENERTKNIkLQQQINEVKNENAKLKQQVARSEEQ 557
Cdd:pfam17380 492 QRRKIlekeleERKQAMIEEERKRKL-LEKEMEERQKAIYEEERRREAEEER 542
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
443-582 |
5.02e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 443 KTLSKKEEEVER-LQQLKKELE----KATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVR 517
Cdd:PRK12704 31 AKIKEAEEEAKRiLEEAKKEAEaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282394043 518 NLQFMSENERTKNIKLQQQINEVKNenaKLKQQVARSEEQNYVPKFE-TAQLKDQLEEVLKSDITK 582
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEE---LIEEQLQELERISGLTAEEaKEILLEKVEEEARHEAAV 173
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
289-555 |
6.22e-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: 46.71 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 289 WEQSAESLQPVQEDMA-----LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEE 363
Cdd:pfam01576 375 LEKAKQALESENAELQaelrtLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 364 liedkykiilEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQK---NKSVS---- 436
Cdd:pfam01576 455 ----------KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKrnvERQLStlqa 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 437 QYLEMDKTLSKKEEEVERLQQLKKELekatasaldllKREKEAQEQEFLSLQEEFQKLEKenleERQKLKSRLEKLLTQV 516
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRL-----------QRELEALTQQLEEKAAAYDKLEK----TKNRLQQELDDLLVDL 589
|
250 260 270
....*....|....*....|....*....|....*....
gi 282394043 517 RNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSE 555
Cdd:pfam01576 590 DHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAE 628
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-574 |
1.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 440 EMDKTLSKKEEEVE---RLQQLKKELEKATASA-----------LDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKL 505
Cdd:COG1196 197 ELERQLEPLERQAEkaeRYRELKEELKELEAELlllklreleaeLEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394043 506 kSRLEKLLTQVRNLQFMSENERtknIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 574
Cdd:COG1196 277 -EELELELEEAQAEEYELLAEL---ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
440-553 |
1.11e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 440 EMDKTLSKKEEEVERLQQLKKELEKatasalDLLKREKEAQEQEflslqeefQKLEKENLEERQKLKSRLEklltqVRNL 519
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEA------ELEEKDERIERLE--------RELSEARSEERREIRKDRE-----ISRL 470
|
90 100 110
....*....|....*....|....*....|....
gi 282394043 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 |
1.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 306 NEVLQKLKhtnrKQEVRIQElqcsnlyLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKykiilekndtKKTLQNL 385
Cdd:COG4942 51 KALLKQLA----ALERRIAA-------LARRIRALEQELAALE---AELAELEKEIAELRAEL----------EAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 386 EEVLANTQKHlqeSRNDKEMLQLQFKKIKANYVCLQerYMtemqqknKSVSQYLEmdKTLSKKEEEVERLQQLKKELEKA 465
Cdd:COG4942 107 AELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQ--YL-------KYLAPARR--EQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 282394043 466 TAsALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQ 520
Cdd:COG4942 173 RA-ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-511 |
2.18e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQfKK 412
Cdd:COG1579 22 LEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ-KE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 413 IkanyvclqerymtEMQQKNKSV--SQYLEMDKTLSKKEEEVERLQQLKKELEKAtasaldlLKREKEAQEQEFLSLQEE 490
Cdd:COG1579 98 I-------------ESLKRRISDleDEILELMERIEELEEELAELEAELAELEAE-------LEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|.
gi 282394043 491 FQKLEKenleERQKLKSRLEK 511
Cdd:COG1579 158 LEELEA----EREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
442-578 |
2.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 442 DKTLSKKEEEVERLQQLKKELEKATASA---LDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRN 518
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 519 LQ--------------------FMSENERTKNIKLQQQ--INEVKNENAKLKQQVARSEEQnyvpKFETAQLKDQLEEVL 576
Cdd:COG3883 95 LYrsggsvsyldvllgsesfsdFLDRLSALSKIADADAdlLEELKADKAELEAKKAELEAK----LAELEALKAELEAAK 170
|
..
gi 282394043 577 KS 578
Cdd:COG3883 171 AE 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
329-538 |
3.57e-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: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 329 SNLYLEKRVKELQMKITKQQVFIDV-INKLKENVEELiEDKYKIILEKND-------TKKTLQNLEEV---LANTQKHLQ 397
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEqLPELRKELEEA-EAALEEFRQKNGlvdlseeAKLLLQQLSELesqLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 398 ESRNDKEML--QLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK----ATASALD 471
Cdd:COG3206 237 EAEARLAALraQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAqlqqEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282394043 472 LLKREKEAQEQEFLSLQEEFQKLEKEnLEERQKLKSRLEKLLTQVRNLQ--FMSENERTKNIKLQQQIN 538
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEAR-LAELPELEAELRRLEREVEVARelYESLLQRLEEARLAEALT 384
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
449-569 |
4.10e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 449 EEEVERLQQLKKELE---KATASALDLLKREKEAQEQEFLSLQEEFQKLeKENLEER-----QKLKSRLEKLLTQVRNLQ 520
Cdd:PRK00409 519 NELIASLEELERELEqkaEEAEALLKEAEKLKEELEEKKEKLQEEEDKL-LEEAEKEaqqaiKEAKKEADEIIKELRQLQ 597
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 282394043 521 FMSenerTKNIKLQQQINEVKnenaKLKQQVARSEEQNYVPKFETAQLK 569
Cdd:PRK00409 598 KGG----YASVKAHELIEARK----RLNKANEKKEKKKKKQKEKQEELK 638
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
440-517 |
4.11e-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: 41.42 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 440 EMDKTLSKKEEEVERLQQ-LKKELEKATASALDLLKREKEAQEQEFLSLQEEFQK--------LEKENLEERQKLKSRLE 510
Cdd:smart00935 22 QLEKEFKKRQAELEKLEKeLQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRkqqklqqdLQKRQQEELQKILDKIN 101
|
....*..
gi 282394043 511 KLLTQVR 517
Cdd:smart00935 102 KAIKEVA 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
427-577 |
4.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 427 EMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldllKREKEAQEQEFLSLQEEFQKLEkenlEERQKLK 506
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE---------ELEKLEKLLQLLPLYQELEALE----AELAELP 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394043 507 SRLEKLLTQVRNLQfmsenertkniKLQQQINEVKNENAKLKQQVARSEEQNYVPKFET-AQLKDQLEEVLK 577
Cdd:COG4717 146 ERLEELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQ 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-586 |
5.51e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQVFIDVINK-LKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFK 411
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSdLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 412 KI------KANYVCLQERYMTEMQQKNKSV----SQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldlLKREKEAQE 481
Cdd:TIGR04523 160 KYndlkkqKEELENELNLLEKEKLNIQKNIdkikNKLLKLELLLSNLKKKIQKNKSLESQISE--------LKKQNNQLK 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 482 QEFLSLQEEFQKLEKENLEERQKL---KSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQvaRSEEQN 558
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLnqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWN 309
|
250 260
....*....|....*....|....*...
gi 282394043 559 YVPKFETAQLKDQLEEvLKSDITKDTKT 586
Cdd:TIGR04523 310 KELKSELKNQEKKLEE-IQNQISQNNKI 336
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
432-643 |
6.73e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 432 NKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASA----------LDLLKREKEAQEQEFLSLQEEFQKLEKenleE 501
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeleeleeeLEQLRKELEELSRQISALRKDLARLEA----E 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 502 RQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEvLKSDIT 581
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAA 820
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394043 582 kDTKTTHSNLLPDCSPCEERLNPADiKRASQLASKMHSLLALMVGLLTCQDIINSDAEHFKE 643
Cdd:TIGR02168 821 -NLRERLESLERRIAATERRLEDLE-EQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-583 |
7.10e-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: 43.40 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 383 QNLEEVLANTQKHLQESRNDKEMLqlqfkkikanyvclqERYMTEMQQKNKSVSQYLEmdktlskkeEEVERLQQLKKEL 462
Cdd:COG3096 532 QNAERLLEEFCQRIGQQLDAAEEL---------------EELLAELEAQLEELEEQAA---------EAVEQRSELRQQL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 463 EKATASAldllkREKEAQEQEFLSLQEEFQKLEK---ENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINE 539
Cdd:COG3096 588 EQLRARI-----KELAARAPAWLAAQDALERLREqsgEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 282394043 540 VknenaklkQQVARSEEQnyvpkfETAQLKDQLEEVLKSDITKD 583
Cdd:COG3096 663 L--------SQPGGAEDP------RLLALAERLGGVLLSEIYDD 692
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
439-541 |
8.30e-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: 42.27 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 439 LEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRN 518
Cdd:pfam02841 193 LQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQ 272
|
90 100
....*....|....*....|....*
gi 282394043 519 LQ--FMSENERTKNIKLQQQINEVK 541
Cdd:pfam02841 273 EQeeLLKEGFKTEAESLQKEIQDLK 297
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
439-540 |
9.02e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 439 LEMDKT---LSKKEEEVERL----QQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKlEKENLEERQKLKSRLEK 511
Cdd:COG0542 404 MEIDSKpeeLDELERRLEQLeiekEALKKEQDEASFERLAELRDELAELEEELEALKARWEA-EKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 282394043 512 LLTQVRNLQFMSENERTKNIKLQQQINEV 540
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
300-578 |
1.05e-03 |
|
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: 42.85 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 300 QEDM-ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKI------------------TKQQVFIDVINKLKEN 360
Cdd:pfam01576 4 EEEMqAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeemrarlaARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 361 VEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLE 440
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 441 MDKTLSKKEEEVERLQQLKKELEKATASALDLLKRE----------KEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLE 510
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEekgrqelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282394043 511 KL---LTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKS 578
Cdd:pfam01576 244 ELqaaLARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDT 314
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
312-573 |
1.08e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 312 LKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELI-------EDKYKIILEKNDTKKTLQN 384
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTaqlestkEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 385 LEEVLANTQKHLQESRNDKEMLQLQFKKIKA---------NYVCLQERYMTEMQQKNKSVS-QYLEMDKTLSKKEEEVER 454
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSrvdlklqelQHLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 455 LQQLKKELEKaTASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKL-LTQVRNLQFMSENER-TKNIK 532
Cdd:pfam15921 574 MTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLeLEKVKLVNAGSERLRaVKDIK 652
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 282394043 533 LQ--QQINEVKNENAKLKQQVARSE--EQNYVPKFE-----TAQLKDQLE 573
Cdd:pfam15921 653 QErdQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEemettTNKLKMQLK 702
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
388-587 |
1.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 388 VLANTQkhLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQ----QLKKELE 463
Cdd:COG3883 12 AFADPQ--IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEaeieERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 464 KATASA-------------------------LDLLKREKEAQE---QEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQ 515
Cdd:COG3883 90 ERARALyrsggsvsyldvllgsesfsdfldrLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394043 516 VRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTT 587
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
318-556 |
1.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 318 KQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIdvinKLKENVEELIEDKYK----IILEKNDTKKTLQNLEEVLANTQ 393
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKeleeVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 394 KHLQESRNDKEM---LQLQFKKIKANYVCLQER------YMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK 464
Cdd:PRK03918 228 KEVKELEELKEEieeLEKELESLEGSKRKLEEKireleeRIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 465 atasALDLLKREKEAQEQEFLSLQEEFQKLE------KENLEERQKLKSRLEKLLTQVRNLQ-FMSENERTKNIKLQQQI 537
Cdd:PRK03918 308 ----ELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEeAKAKKEELERLKKRLTG 383
|
250
....*....|....*....
gi 282394043 538 NEVKNENAKLKQQVARSEE 556
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEE 402
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
305-575 |
1.59e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 305 LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKElqmkitkqqvfidvinkLKENVEELiedkykiilekndtkktlqn 384
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRE-----------------LESRVAEL-------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 385 leevlantQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMD---KTLSKKEEEVE-RLQQLKK 460
Cdd:pfam07888 86 --------KEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediKTLTQRVLEREtELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 461 ELEKATAsaldlLKREKEAQEQeflSLQEEFQKLEKEN---LEERQKLKSRLEKLLTQVRNLQfmseNERTKNIKLQQQI 537
Cdd:pfam07888 158 RAKKAGA-----QRKEEEAERK---QLQAKLQQTEEELrslSKEFQELRNSLAQRDTQVLQLQ----DTITTLTQKLTTA 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 282394043 538 NEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEV 575
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
342-574 |
1.76e-03 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 41.96 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 342 MKITKQQVFIDVINK-----LKENVEELIEDKYKI----ILEKNDTKKTLQNLEEVLANT-----QKHL----------- 396
Cdd:PRK12903 660 LRITHFKFSEKDFENyhkeeLAQYLIEALNEIYFKkrqvILDKIALNTFFESERYIILSAldkywQNHIdtmdklrsgvn 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 397 --QESRND-------------KEMLQ-------LQFKKIKANYVCLQERYMTEMQQKNKSVSQ-YLEMDKTLSKKEEEVE 453
Cdd:PRK12903 740 lvQYSQKNpyqvyteegtkkfNILLQeiaydviVSLFNNPNAEKILIITEILSDGINNSDINDrPQELIDQIIESEEERL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 454 RLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKlltqvrnlqfmsENERTKNIKL 533
Cdd:PRK12903 820 KALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEF------------KNDPKKLNKL 887
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394043 534 qqqinevKNENAKLKQQVARSEEQNYVPKfETAQLKDQLEE 574
Cdd:PRK12903 888 -------IIAKDVLIKLVISSDEIKQDEK-TTKKKKKDLEK 920
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
382-555 |
1.96e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 382 LQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTemQQKNKSVS--------QYLEMDKTLSKKE---- 449
Cdd:PRK11637 77 LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA--QERLLAAQldaafrqgEHTGLQLILSGEEsqrg 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 450 ---------------EEVERLQQLKKELEKATASALdllkrEKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLT 514
Cdd:PRK11637 155 erilayfgylnqarqETIAELKQTREELAAQKAELE-----EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 282394043 515 qvrnlqfmsenertkniKLQQQINEVKNENAKLKQQVARSE 555
Cdd:PRK11637 230 -----------------KDQQQLSELRANESRLRDSIARAE 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
276-520 |
2.36e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 276 RSEACRENCE-MPDWEQSAESLQPVQEDMAlnEVLQKLKHTNRKQEVRIQELQcsnlYLEKRVKELQMKITKQQV----- 349
Cdd:TIGR02169 711 LSDASRKIGEiEKEIEQLEQEEEKLKERLE--ELEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEalndl 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 350 -------FIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDkemlqlqfkkikanyvclqe 422
Cdd:TIGR02169 785 earlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-------------------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 423 rymteMQQKNKSVSQYLEMDKT-LSKKEEEVERLQQLKKELEKatasALDLLKREKEAQEQEFLSLQEEFQKLEkenlEE 501
Cdd:TIGR02169 845 -----LKEQIKSIEKEIENLNGkKEELEEELEELEAALRDLES----RLGDLKKERDELEAQLRELERKIEELE----AQ 911
|
250
....*....|....*....
gi 282394043 502 RQKLKSRLEKLLTQVRNLQ 520
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALE 930
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-494 |
2.47e-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: 40.90 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 304 ALNEVLQKLKHTNRKQEVRIQELQcsnlyleKRVKELQMKITKQQ-VFIDVINKLKENVEeliEDKYKIIL---EKNDTK 379
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELE-------KEIAELRAELEAQKeELAELLRALYRLGR---QPPLALLLspeDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 459
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 282394043 460 KELEKATASALDLLKR-EKEAQEQEFLSLQEEFQKL 494
Cdd:COG4942 216 AELQQEAEELEALIARlEAEAAAAAERTPAAGFAAL 251
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
336-611 |
2.82e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 336 RVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKA 415
Cdd:COG5022 756 RGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRET 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 416 NYVCLQERYMTEMQQKNKSVsQYLEMDKTLSKKE---EEVERLQQLKKEL--EKATASALDLLKREKEAQEQEFLSLQEE 490
Cdd:COG5022 836 EEVEFSLKAEVLIQKFGRSL-KAKKRFSLLKKETiylQSAQRVELAERQLqeLKIDVKSISSLKLVNLELESEIIELKKS 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 491 FQKLEKENLEERQKLKSRLEKLltqvrNLQFMSENERTKNIKLQQQINEVKNENAKLKQQvarSEEQNYVPKFETAQLKD 570
Cdd:COG5022 915 LSSDLIENLEFKTELIARLKKL-----LNNIDLEEGPSIEYVKLPELNKLHEVESKLKET---SEEYEDLLKKSTILVRE 986
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394043 571 QLEEVLKSDITKDTKTTHSNLLPDCSPCEERLNPADIKRAS 611
Cdd:COG5022 987 GNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
376-571 |
3.13e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 376 NDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKikanyvclQERYMTEMQQKNKSVSQYLE-MDKTLSKKEEEVER 454
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK--------QEEAISQASRKLRETQNTLNqLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 455 LQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEK-------ENlEERQKLKSRLEKLLTQVRNLQFMSENER 527
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGERilayfgyLN-QARQETIAELKQTREELAAQKAELEEKQ 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 282394043 528 TKniklQQQI-NEVKNENAKLKQqvARSEEQNYVPKFETAQLKDQ 571
Cdd:PRK11637 194 SQ----QKTLlYEQQAQQQKLEQ--ARNERKKTLTGLESSLQKDQ 232
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
354-585 |
3.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 354 INKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNK 433
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 434 SVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASAldllKREKEAQEQEFLSLQEEFQKLEKENLE-ERQKLKSRLEKL 512
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER----EEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDEL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282394043 513 LTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
449-807 |
3.70e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 449 EEEVERLQQLKKELEKAtasaLDLLKREKEAQEQEFLSLQEEFQKLEKEnLEERQKlksRLEKLLTQVRNLQFMSENERT 528
Cdd:TIGR02169 673 PAELQRLRERLEGLKRE----LSSLQSELRRIENRLDELSQELSDASRK-IGEIEK---EIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 529 KNIKLQQQINEVKNENAKLKQQVARSEEQnyvpkfeTAQLKDQLEEVlksditkdtktthsnllpdcspcEERLNPADIK 608
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEED-------LHKLEEALNDL-----------------------EARLSHSRIP 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 609 RASQLASKMhsllalmvglltcqdiinsDAEHFKESEKVSDImlqklkSLHLKKKTLDKELLkhkdrittfreliakEKA 688
Cdd:TIGR02169 795 EIQAELSKL-------------------EEEVSRIEARLREI------EQKLNRLTLEKEYL---------------EKE 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 689 FQDHAIKVIDCDsDEAKSIRDVPTLLGAKLDKyhsLNEELDFLITKLGHLLESKENhcnrLIEENDKYQRHLGNLIKKVT 768
Cdd:TIGR02169 835 IQELQEQRIDLK-EQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIE 906
|
330 340 350
....*....|....*....|....*....|....*....
gi 282394043 769 SYEEIIECADQRLAISHSQIAHLEERNKHLEDLIRKPRE 807
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
300-548 |
4.87e-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: 40.73 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 300 QEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVfidvINKLKENVEELIEDKYKIILEKNDTK 379
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL----LQELLLKEEELEEQKLKDELESKEEK 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 380 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKAnyvcLQERYMTEMQQKNKSVSQYLEMDKTLsKKEEEVERLQQLK 459
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL----LKYEEEPEELLLEEADEKEKEENNKE-EEEERNKRLLLAK 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 460 KELEKATASALDLLKREKEaqeqeflslQEEFQKLEKENL-EERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQIN 538
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEE---------RYNKDELEKERLeEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
250
....*....|
gi 282394043 539 EVKNENAKLK 548
Cdd:pfam02463 1041 ELGGSAELRL 1050
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
333-585 |
6.13e-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: 40.19 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 333 LEKRVKELQMKITKQQVFIdviNKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLqesrndkEMLQLQFKK 412
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFL---NKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKI-------ENLQEQLRD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 413 IKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQ---------------QLKKELeKATASALDLLKREK 477
Cdd:pfam10174 413 KDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKeqreredrerleeleSLKKEN-KDLKEKVSALQPEL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 478 EAQEQEFLSLQEEFQKLEKENLEERQKLKSrLEKLLTQVRN--LQFMSENERTKNIKLQQQINEVKNENAK-LKQQVARS 554
Cdd:pfam10174 492 TEKESSLIDLKEHASSLASSGLKKDSKLKS-LEIAVEQKKEecSKLENQLKKAHNAEEAVRTNPEINDRIRlLEQEVARY 570
|
250 260 270
....*....|....*....|....*....|.
gi 282394043 555 EEQNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:pfam10174 571 KEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
299-535 |
7.01e-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: 39.41 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 299 VQEDMALNEVLQKLKHTNRKQEVRIQ-------ELQCSNLYLEKRVKELQM--KITKQQVFIDVINK-LKENVEELIEDK 368
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNaavrektSLSASVASLEKQLLELTRvnELLKAKFSEDGTQKkMSSLSMELMKLR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 369 YKIILEKNDTKKTLQNLEEVLANTQKHLQESRndKEMLQLQFKKIKANYVCLQERYMTEmqqknksvsQYLEMDKTLSKK 448
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSK--GKVAQLEEKLVSTEKEKIEEKSETE---------KLLEYITELSCV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 449 EEEVERLQ---QLKKELEKATASALDLLKREKEAQEQEFL----SLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQF 521
Cdd:pfam15905 235 SEQVEKYKldiAQLEELLKEKNDEIESLKQSLEEKEQELSkqikDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKE 314
|
250
....*....|....
gi 282394043 522 MSENERTKNIKLQQ 535
Cdd:pfam15905 315 KLTLEEQEHQKLQQ 328
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
347-570 |
7.56e-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: 39.84 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 347 QQVFIDVINKLKENVEELIE------DKYKIILEK---NDTKKTLQNLEEVLANTQKHL-----QESRNDKEMLQLQ--F 410
Cdd:pfam06160 51 RKKWDDIVTKSLPDIEELLFeaeelnDKYRFKKAKkalDEIEELLDDIEEDIKQILEELdelleSEEKNREEVEELKdkY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 411 KKIKANYvcLQERYM-------------------TEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEKAtasaLD 471
Cdd:pfam06160 131 RELRKTL--LANRFSygpaidelekqlaeieeefSQFEELTES-GDYLEAREVLEKLEEETDALEELMEDIPPL----YE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 472 LLKREKEAQEQEflsLQEEFQKLEKEN--------LEERQKLKSRLEKLLTQVRNLQFmsENERTKNIKLQQQI------ 537
Cdd:pfam06160 204 ELKTELPDQLEE---LKEGYREMEEEGyalehlnvDKEIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIdqlydl 278
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 282394043 538 --------NEVKNENAKLKQQVARSEEQNYVPKFETAQLKD 570
Cdd:pfam06160 279 lekevdakKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQ 319
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
351-573 |
8.03e-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: 39.63 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 351 IDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKAnyvcLQERYMTEMQQ 430
Cdd:pfam05667 275 QDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE----LQEQLEDLESS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 431 KNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATAS---ALDLLkreKEAQEQEflslqEEFQKLEKENLEERQKLKS 507
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVkkkTLDLL---PDAEENI-----AKLQALVDASAQRLVELAG 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282394043 508 RLEK----LLTQVRNLqfmSENERTKNIKLQQQINEVKNENAKLKQ--QVARSEEQNYvpkfetAQLKDQLE 573
Cdd:pfam05667 423 QWEKhrvpLIEEYRAL---KEAKSNKEDESQRKLEEIKELREKIKEvaEEAKQKEELY------KQLVAEYE 485
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
447-588 |
8.14e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 447 KKEEEVERLQQLKKE----LEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLltqvrnlqfm 522
Cdd:PRK12705 31 LAKEAERILQEAQKEaeekLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL---------- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282394043 523 sENERTKNIKLQQQINEVKNENAKLKQQVARSEEQnyVPKFETAQLKDQLEEVLKSDITKDTKTTH 588
Cdd:PRK12705 101 -DNLENQLEEREKALSARELELEELEKQLDNELYR--VAGLTPEQARKLLLKLLDAELEEEKAQRV 163
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
335-585 |
8.29e-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: 39.62 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 335 KRVKELQMKITKQQVFIDVINKLKENVE----ELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQ----------ESR 400
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELEnelnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqisELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 401 NDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK---ATASALDLLKREK 477
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnQLKSEISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 478 EAQEQEFLSLQEEFQKLEKENLE-ERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEE 556
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQnQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
250 260
....*....|....*....|....*....
gi 282394043 557 QNYVPKFETAQLKDQLEEVLKSDITKDTK 585
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
440-518 |
8.50e-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: 37.56 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 440 EMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRL-EKLLTQVRN 518
Cdd:pfam03938 23 QLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELlQPIQDKINK 102
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
307-557 |
8.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 307 EVLQKLKHTNRKQEVRIQELQCSNLYLEK--RVKElQMKITKQQVfIDVINKLKENVEELieDKYKIILEKnDTKKTLQN 384
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKidRQKE-ETEQLKQQL-AQAPAKLRQAQAEL--EALKDDNDE-ETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 385 -----LEEVLANTQKHLQEsrndkemLQLQFKKIKANYVCLQ---ERYMTEMQQKNKsvsqylemdktlskkeeeveRLQ 456
Cdd:PRK11281 121 lslrqLESRLAQTLDQLQN-------AQNDLAEYNSQLVSLQtqpERAQAALYANSQ--------------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 457 QLKKELEKATASALDLL--KREKEAQEQEFLSLQEEFQKLEKENleerqklKSRLEKLLTQVRNLqfMSENERtkniKLQ 534
Cdd:PRK11281 174 QIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRKSLEG-------NTQLQDLLQKQRDY--LTARIQ----RLE 240
|
250 260
....*....|....*....|....
gi 282394043 535 QQINEVKNE-NAKLKQQvarSEEQ 557
Cdd:PRK11281 241 HQLQLLQEAiNSKRLTL---SEKT 261
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
348-497 |
9.05e-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: 39.23 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 348 QVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANyvcLQERYMTE 427
Cdd:smart00787 140 KLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDR---AKEKLKKL 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 428 MQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKE 497
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
353-510 |
9.55e-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: 39.22 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 353 VINKLKENVEELIEDKYKII----LEKNDTKKTLQNLEEVLANTQKHLqesrnDKEMLQLQFKKIKANyvcLQERYMTEM 428
Cdd:pfam05262 182 VVEALREDNEKGVNFRRDMTdlkeRESQEDAKRAQQLKEELDKKQIDA-----DKAQQKADFAQDNAD---KQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 429 QQKNKS------VSQYLEMDKTLSKKEEEVERLQQLKK----ELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKEN 498
Cdd:pfam05262 254 QQEAKNlpkpadTSSPKEDKQVAENQKREIEKAQIEIKkndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPV 333
|
170
....*....|..
gi 282394043 499 LEERQKLKSRLE 510
Cdd:pfam05262 334 AEDLQKTKPQVE 345
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
440-516 |
9.90e-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: 37.89 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282394043 440 EMDKTLSKKEEEVERLQQ-LKKELEKATASALDLLKREKEAQEQEFLSLQEEFQK--------LEKENLEERQKLKSRLE 510
Cdd:COG2825 47 KLEKEFKKRQAELQKLEKeLQALQEKLQKEAATLSEEERQKKERELQKKQQELQRkqqeaqqdLQKRQQELLQPILEKIQ 126
|
....*.
gi 282394043 511 KLLTQV 516
Cdd:COG2825 127 KAIKEV 132
|
|
| |
