|
Name |
Accession |
Description |
Interval |
E-value |
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
2-381 |
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: 629.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 2 TEKPEFQSQVYNYAKDNNIKQDSFKEENPMETSVSANTDQLGNEYFRQPPpRSPPLIHCSGEMLKFTEKSLAKSIAKESA 81
Cdd:pfam15066 120 TEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQLANECVRQSS-RSPPLIHCSGETLPFTEKSLAKSTAKESA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 82 LNPSQPPSFLCK------------------------------TAVPSKEIQNYGEIPEMSVSYEKEVTAEGVERPEIVST 131
Cdd:pfam15066 199 LNPSQPQSFLYEenvprnvekpfykensfslldlranykteeTEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIAST 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 132 WSSAGISWRSEACRENCEMPDWEQSAESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQ 211
Cdd:pfam15066 279 WSPAGISWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQ 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 212 QVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTE 291
Cdd:pfam15066 359 QVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 292 MQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKS 371
Cdd:pfam15066 439 MQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKREKETREQEFLSLQEEFQKHEKENLEERQKLKS 518
|
410
....*....|
gi 45505178 372 RLEKLLTQVR 381
Cdd:pfam15066 519 RLEKLVAQVK 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-444 |
3.95e-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: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 168 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQV-FIDVINKLKENVEELIEDKYKIIL---EKNDTK 243
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErLANLERQLEELEAQLEELESKLDElaeELAELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 244 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 323
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 324 KELE--------KATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSrLEKLLTQVRNLQFMSENERTKNI 395
Cdd:TIGR02168 424 EELLkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-AERELAQLQARLDSLERLQENLE 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 45505178 396 KLQQQINEVKNENAKLKQQVAR-SEEQNYVPKFETAqlkdqLEEVLKSDI 444
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGILGVlSELISVDEGYEAA-----IEAALGGRL 547
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-384 |
7.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 168 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFI----DVINKLKENVEELIEDKYKIILEKNDTK 243
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRreleERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 244 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 323
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45505178 324 KELEKATASALDLLKREKEAQEQEfLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQ 384
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-431 |
1.13e-07 |
|
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: 54.38 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 197 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKK 276
Cdd:COG4942 25 AEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 277 IKANYvclqERYMTEMQQknksVSQYLEMDKTLSKKE-EEVERLQQLKKELEKATASALDLLKREKE---AQEQEFLSLQ 352
Cdd:COG4942 102 QKEEL----AELLRALYR----LGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45505178 353 EEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQ 431
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-445 |
1.56e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 164 QEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTK 243
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 244 KTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLK 323
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 324 KELEKATA---SALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKsrleKLLTQVRNLQFMSENERTKNIKLQQQ 400
Cdd:TIGR02168 862 EELEELIEeleSELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 45505178 401 INEVK---NENAKLKQQVARSEEQNYVpkFETAQLKDQLEEvLKSDIT 445
Cdd:TIGR02168 938 IDNLQerlSEEYSLTLEEAEALENKIE--DDEEEARRRLKR-LENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-419 |
2.04e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 153 WEQSAESLQPVQEDMA-LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQ----MKITKQQVFIDVINKLKENVEE 227
Cdd:COG1196 234 LRELEAELEELEAELEeLEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 228 LIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDK 307
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 308 TLSKK-------EEEVERLQQLKKELEKAtasaldllKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQV 380
Cdd:COG1196 394 AAAELaaqleelEEAEEALLERLERLEEE--------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270
....*....|....*....|....*....|....*....
gi 45505178 381 RNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSE 419
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-442 |
2.21e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 198 EKRVKELQMKITKqqvfidvINKLKENVEELIEdkykiilEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKI 277
Cdd:COG1196 221 ELKELEAELLLLK-------LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 278 KANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASA---LDLLKREKEAQEQEFLSLQEE 354
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 355 FQKLEKENLEERQKLKSRLEKLLTQVRNLQfmseNERTKNIKLQQQINEVKNENAKLKQQVARSEEQnyvpKFETAQLKD 434
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEEE 438
|
....*...
gi 45505178 435 QLEEVLKS 442
Cdd:COG1196 439 EEEEALEE 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-436 |
4.50e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 197 LEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKykiilekndtKKTLQNLEEVLANTQKHLQESRNDKEML--QLQF 274
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEEL----------RLEVSELEEEIEELQKELYALANEISRLeqQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 275 KKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEV--ERLQQLKKELEKATASALDLLKREKEAQEQ------ 346
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkEELESLEAELEELEAELEELESRLEELEEQletlrs 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 347 EFLSLQEEFQKLEKE--NLEERQK-LKSRLEKLLTQVRNLQfmSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNY 423
Cdd:TIGR02168 387 KVAQLELQIASLNNEieRLEARLErLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250
....*....|...
gi 45505178 424 VPKFETAQLKDQL 436
Cdd:TIGR02168 465 ELREELEEAEQAL 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
238-455 |
7.03e-07 |
|
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: 51.69 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 238 EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIkanyvclqERYMTEMQQKNKSVSQYL-EMDKTLSKKEEEV 316
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------ERRIAALARRIRALEQELaALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 317 ERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLE--------------------KENLEERQKLKSRLEKL 376
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylaparreqaeelRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45505178 377 LTQVRNLQFMSENERTKnikLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKSDITKDTKTTHSNL 455
Cdd:COG4942 173 RAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-444 |
8.31e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 168 ALNEVLQKLKHTNRKQEVRIQELQCSNLylEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDT----- 242
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAI--ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrv 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 243 KKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQ------ERYMTEMQQKNKSVSQYL-----EMDKTLSK 311
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieelEREIEEERKRRDKLTEEYaelkeELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 312 KEEEVERLQQLKKELeKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKS-----------------RLE 374
Cdd:TIGR02169 373 LEEVDKEFAETRDEL-KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieakineleeekedkalEIK 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 375 KLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQlEEVLKSDI 444
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-EEVLKASI 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-420 |
2.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 152 DWEQSAESLQPVQEDM-ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIE 230
Cdd:PRK03918 159 DYENAYKNLGEVIKEIkRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 231 DKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKaNYVCLQERYMTEMQQKNKSVSQYLEMDKTLS 310
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 311 KKEEEVERLQQLKKELEKATASALDLLKREKEAQEqEFLSLQEEFQKLE--KENLEERQKLKSRLEKLltQVRNLQFMSE 388
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEK-RLEELEERHELYEeaKAKKEELERLKKRLTGL--TPEKLEKELE 394
|
250 260 270
....*....|....*....|....*....|..
gi 45505178 389 NERTKNIKLQQQINEVKNENAKLKQQVARSEE 420
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-439 |
7.41e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 225 VEELIEDK---YKIILE--------KNDTKKTLQNLEEVLANTQK---HLQESRNDKEMLQLQ------FKKIKA----- 279
Cdd:TIGR02168 146 ISEIIEAKpeeRRAIFEeaagiskyKERRKETERKLERTRENLDRledILNELERQLKSLERQaekaerYKELKAelrel 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 280 -------NYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldllkrEKEAQEQEFLSLQ 352
Cdd:TIGR02168 226 elallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-----------EIEELQKELYALA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 353 EEFQKLEKenleERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQL 432
Cdd:TIGR02168 295 NEISRLEQ----QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
....*..
gi 45505178 433 KDQLEEV 439
Cdd:TIGR02168 371 ESRLEEL 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
169-415 |
8.51e-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: 48.86 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 169 LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIE--DKYKIILEKN--DTKK 244
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQlkVLSR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 245 TLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQ-LK 323
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 324 KELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINE 403
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
250
....*....|..
gi 45505178 404 VKNENAKLKQQV 415
Cdd:TIGR04523 636 IKSKKNKLKQEV 647
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-407 |
8.68e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 168 ALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKqqvfIDVINKLKENVEELIEDKYKIILEKNDTKKTLQ 247
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 248 NLEEVLANTQKHLQESRNDK---EMLQLQFKKIKANYVCLQERY---------MTEMQQ-----KNKSVSQYLEMDKTLS 310
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHelyeeakakKEELERlkkrlTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 311 KKEEEVER----LQQLKKELEKATAS---ALDLLKREK--------EAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEK 375
Cdd:PRK03918 398 KAKEEIEEeiskITARIGELKKEIKElkkAIEELKKAKgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
250 260 270
....*....|....*....|....*....|....
gi 45505178 376 LLTQVRNLQFMSENERT--KNIKLQQQINEVKNE 407
Cdd:PRK03918 478 LRKELRELEKVLKKESEliKLKELAEQLKELEEK 511
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
220-421 |
1.02e-05 |
|
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: 48.79 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 220 KLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRndkemLQLQFKKIKANY-VCLQERYMTEMQQKnks 298
Cdd:pfam15818 159 KLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSK-----VTCQYKMGEENInLTIKEQKFQELQER--- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 299 vsqyLEMDKTLSKK-EEEVERLQQLKKELEKATASALDLLKREKEAQ---EQEFLSLQEEFQKLEKENLEERQKLKSRLE 374
Cdd:pfam15818 231 ----LNMELELNKKiNEEITHIQEEKQDIIISFQHMQQLLQQQTQANtemEAELKALKENNQTLERDNELQREKVKENEE 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45505178 375 KLLtqvrNLQfmseNERTKNIK--------LQQQINEVKNENAKLKQQVARSEEQ 421
Cdd:pfam15818 307 KFL----NLQ----NEHEKALGtwkkhveeLNGEINEIKNELSSLKETHIKLQEH 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-577 |
1.26e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 218 INKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANyvclQERYMTEMQQKNK 297
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 298 SVSQYL-EMDKTLSKKEEEVERLQQLKKELEKATASALDLlKREKEAQEQEFLSLQEEFQKLEkenlEERQKLKSRLEKL 376
Cdd:TIGR02168 755 ELTELEaEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALREALDELRAELTLLN----EEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 377 LTQVRNLQFMSENertknikLQQQINEVKNENAKLKQQVARSEEQnyvpkfeTAQLKDQLEEVLKSditKDTKTTHSNLL 456
Cdd:TIGR02168 830 ERRIAATERRLED-------LEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNE---RASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 457 PD-CSPCEERLNPADiKRASQLASKMHSLLALMVGLLTCQDIINSDAEHFKESEKVSDIMLQKLKSLHLKKKTLDKEVID 535
Cdd:TIGR02168 893 RSeLEELSEELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 45505178 536 cdsDEAKSIRDVPTLLG----AKLDKYHSLNEELDFLVTSYEEIIE 577
Cdd:TIGR02168 972 ---RRLKRLENKIKELGpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
214-405 |
1.75e-05 |
|
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: 47.19 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 214 FIDVINKLKENVEELIEDKYKIILEKNDT------KKTLQNLEEVLANTQKHL--------QESRNDKEML-----QLQF 274
Cdd:cd16269 84 FKDEDQKFQKKLMEQLEEKKEEFCKQNEEasskrcQALLQELSAPLEEKISQGsysvpggyQLYLEDREKLvekyrQVPR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 275 KKIKANYVcLQErYMTEMQQKNKSVsqyLEMDKTLSKKEEEVERlQQLKKELEKATASAL----DLLKREKEAQEQeflS 350
Cdd:cd16269 164 KGVKAEEV-LQE-FLQSKEAEAEAI---LQADQALTEKEKEIEA-ERAKAEAAEQERKLLeeqqRELEQKLEDQER---S 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45505178 351 LQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQ--FMSENERTKNIKLQQQINEVK 405
Cdd:cd16269 235 YEEHLRQLKEKMEEERENLLKEQERALESKLKEQeaLLEEGFKEQAELLQEEIRSLK 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
202-419 |
3.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 202 KELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNdkemlqlQFKK-IKAN 280
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELGErARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 281 YVCLQERYMTEMQQKNKSVSQYLE----MDKTLSKKEEEVERLQQLKKELEKATAsALDLLKREKEAQEQEFLSLQEEFQ 356
Cdd:COG3883 96 YRSGGSVSYLDVLLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKA-ELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45505178 357 KLEKENLEERQKLKSRLEKLLTQVRNLQFMSEnERTKNIKLQQQINEVKNENAKLKQQVARSE 419
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELA-AAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
158-438 |
7.37e-05 |
|
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: 46.12 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 158 ESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIIL 237
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 238 EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANyvclqerymTEMQQKNKSVSQYLEMDKTLSKKEEEVE 317
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL---------KLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 318 RLQQLKKELEKATASAldLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKL 397
Cdd:pfam02463 332 KEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 45505178 398 QQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 438
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
307-446 |
7.79e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 307 KTLSKKEEEVER-LQQLKKELE----KATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVR 381
Cdd:PRK12704 31 AKIKEAEEEAKRiLEEAKKEAEaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45505178 382 NLQFMSENERTKNIKLQQQINEVKNenaKLKQQVARSEEQNYVPKFE-TAQLKDQLEEVLKSDITK 446
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEE---LIEEQLQELERISGLTAEEaKEILLEKVEEEARHEAAV 173
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
169-416 |
8.89e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 169 LNEVLQKLKHTNR--KQEVRIQELQCSNLYLEKRVKELQMKITK--QQVFIDVINKLKE-------NVEELIEDKYKIIL 237
Cdd:pfam05483 217 LKEDHEKIQHLEEeyKKEINDKEKQVSLLLIQITEKENKMKDLTflLEESRDKANQLEEktklqdeNLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 238 EKNDTKKTLQN-------LEEVLANTQK-----------HLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSV 299
Cdd:pfam05483 297 ELEDIKMSLQRsmstqkaLEEDLQIATKticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 300 SQYLEMDKTLSKKEEEVERLQQLK--KELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKEN---LEERQK------ 368
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKnnKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELiflLQAREKeihdle 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 45505178 369 -----LKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVA 416
Cdd:pfam05483 457 iqltaIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-440 |
9.72e-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: 45.83 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 286 ERYMTEMQQKNKSVSQYLEmdkTLSKKEEEVERLQQLKKELEKATASAL----DLLKREKEAQEQEFLSLQEEFQKLEKE 361
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 362 nLEERQKLKSRLEKLLTQV-RNLQFMSENERtknIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVL 440
Cdd:TIGR02169 260 -ISELEKRLEEIEQLLEELnKKIKDLGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
216-417 |
1.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 216 DVINKLKEN-VEELIEDKykiileKNDTKKTLQNLEEVLANTQKHLQESRNDKEmlqlQFKKiKANYVCLQERYMTEMQQ 294
Cdd:COG3206 152 AVANALAEAyLEQNLELR------REEARKALEFLEEQLPELRKELEEAEAALE----EFRQ-KNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 295 KNKSVSQYLEMDKTLSKKEEeveRLQQLKKELEKATASALDLLkrekeaQEQEFLSLQEEFQKLEKE--NLEER------ 366
Cdd:COG3206 221 LSELESQLAEARAELAEAEA---RLAALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAElaELSARytpnhp 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45505178 367 --QKLKSRLEKLLTQVRNLQFMSENERTKNIK-LQQQINEVKNENAKLKQQVAR 417
Cdd:COG3206 292 dvIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLAQLEARLAE 345
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
197-405 |
1.30e-04 |
|
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: 44.84 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 197 LEKRVKELQMKITK--------QQVFIDVINKLKENVEELIEDKYKiiLEKNDTKKTLQNLEEVLANTQKHLQESRNDK- 267
Cdd:pfam06160 184 LEEETDALEELMEDipplyeelKTELPDQLEELKEGYREMEEEGYA--LEHLNVDKEIQQLEEQLEENLALLENLELDEa 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 268 -EMLQLQFKKIKANYVCLQ----------------ERYMTEMQQKNKS-VSQYLEMDKTLSKKEEEVERLQQLKKELEKA 329
Cdd:pfam06160 262 eEALEEIEERIDQLYDLLEkevdakkyveknlpeiEDYLEHAEEQNKElKEELERVQQSYTLNENELERVRGLEKQLEEL 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45505178 330 TASALDLLKREKEaQEQEFLSLQEEFqkleKENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVK 405
Cdd:pfam06160 342 EKRYDEIVERLEE-KEVAYSELQEEL----EEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIK 412
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
213-413 |
1.34e-04 |
|
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: 45.13 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 213 VFIDVINKLKENvEELIEDKYKIILEKNDTK--KTLQNLEEVLANTQKHLQES-RNDKEMLQLQFKKIKANyvclqerym 289
Cdd:pfam09731 266 IFPDIIPVLKED-NLLSNDDLNSLIAHAHREidQLSKKLAELKKREEKHIERAlEKQKEELDKLAEELSAR--------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 290 temqQKNKSVSQYLEMDKTLSKKEEEV-ERLQQ-LKKELEKATASALDLLKREKEAQEQEflsLQEEFQKLEKENLE-ER 366
Cdd:pfam09731 336 ----LEEVRAADEAQLRLEFEREREEIrESYEEkLRTELERQAEAHEEHLKDVLVEQEIE---LQREFLQDIKEKVEeER 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45505178 367 QKLKSRLEKLLTQVRNLQfmsenertkniKLQQQINEVKNENAKLKQ 413
Cdd:pfam09731 409 AGRLLKLNELLANLKGLE-----------KATSSHSEVEDENRKAQQ 444
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-387 |
2.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 161 QPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKN 240
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKKEELEEELE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 241 DTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQER---YMTEMQQKNKSVSQYLEMDKTLSKKEEEVE 317
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlseLKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45505178 318 RLQQLKKELEKATA--SALD----LLKREKEAQEQEFLSLQEEFQKLEkenlEERQKLKSRLEKLLTQVRNLqFMS 387
Cdd:TIGR02169 952 SLEDVQAELQRVEEeiRALEpvnmLAIQEYEEVLKRLDELKEKRAKLE----EERKAILERIEEYEKKKREV-FME 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-384 |
2.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 140 RSEACRENCEMPDWEQSAESLQPVQEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVIN 219
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 220 KLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSV 299
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 300 SQYLEMDKTLSKKEEEVERLQQLKKELEKATASA-------------------------LDLLKREKEAQEQEFLSLQEE 354
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLelrleglevridnlqerlseeysltLEEAEALENKIEDDEEEARRR 973
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45505178 355 FQKLEKE-------NL---EERQKLKSRLEKLLTQVRNLQ 384
Cdd:TIGR02168 974 LKRLENKikelgpvNLaaiEEYEELKERYDFLTAQKEDLT 1013
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
304-417 |
2.28e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 304 EMDKTLSKKEEEVERLQQLKKELEKatasalDLLKREKEAQEQEflslqeefQKLEKENLEERQKLKSRLEklltqVRNL 383
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEA------ELEEKDERIERLE--------RELSEARSEERREIRKDRE-----ISRL 470
|
90 100 110
....*....|....*....|....*....|....
gi 45505178 384 QfmSENERtknikLQQQINEVKNENAKLKQQVAR 417
Cdd:COG2433 471 D--REIER-----LERELEEERERIEELKRKLER 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-394 |
2.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 197 LEKRVKELQMKITKQQVFIDVINKLK-ENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLqlqfK 275
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 276 KIKANYVCLQERYMTEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEF 355
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45505178 356 QKLEK---ENLEERQKLKSRLEKLLTQVRNLQFMSENERTKN 394
Cdd:COG4717 202 EELQQrlaELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
211-439 |
2.47e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 211 QQVFIDVINKLKENVEELIEDKYKiiLEKNDTKKTLQNLEEVLANTQKHLQESRNDK-------------EMLQLQFKKI 277
Cdd:PRK04778 225 QTELPDQLQELKAGYRELVEEGYH--LDHLDIEKEIQDLKEQIDENLALLEELDLDEaeekneeiqeridQLYDILEREV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 278 KANYVCLQE-----RYMTEMQQKNKSVSQYLE-MDKTLSKKEEEVERLQQLKKELEKATASALDLLKReKEAQEQEFLSL 351
Cdd:PRK04778 303 KARKYVEKNsdtlpDFLEHAKEQNKELKEEIDrVKQSYTLNESELESVRQLEKQLESLEKQYDEITER-IAEQEIAYSEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 352 QEEFQKLEK--ENLEERQklksrlEKLLTQVRNLqfmseneRTKNIKLQQQINEVKNENAKLKQQVARSE----EQNYVP 425
Cdd:PRK04778 382 QEELEEILKqlEEIEKEQ------EKLSEMLQGL-------RKDELEAREKLERYRNKLHEIKRYLEKSNlpglPEDYLE 448
|
250
....*....|....*....
gi 45505178 426 KFETA-----QLKDQLEEV 439
Cdd:PRK04778 449 MFFEVsdeieALAEELEEK 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-438 |
3.68e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 304 EMDKTLSKKEEEVE---RLQQLKKELEKATASA-----------LDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKL 369
Cdd:COG1196 197 ELERQLEPLERQAEkaeRYRELKEELKELEAELlllklreleaeLEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45505178 370 KsRLEKLLTQVRNLQFMSENERtknIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEE 438
Cdd:COG1196 277 E-ELELELEEAQAEEYELLAEL---ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-370 |
4.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 169 LNEVLQKLKHTNRKQEVRIQELQcsnlYLEKRVKELQMKITKQQvfIDVINKLKENVEELiEDKYKIILEKNDTKKTLQN 248
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLD----ELEEELAELLKELEELG--FESVEELEERLKEL-EPFYNEYLELKDAEKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 249 LEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYmTEMQQKNKSvSQYLEMDKTLSKKEEEVERLQQLKKELEK 328
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY-SEEEYEELR-EEYLELSRELAGLRAELEELEKRREEIKK 694
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45505178 329 atasALDLLKREKEAQEQEflslQEEFQKLEK--ENLEE-RQKLK 370
Cdd:PRK03918 695 ----TLEKLKEELEEREKA----KKELEKLEKalERVEElREKVK 731
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-433 |
6.30e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 313 EEEVERLQQLKKELE---KATASALDLLKREKEAQEQEFLSLQEEFQKLeKENLEER-----QKLKSRLEKLLTQVRNLQ 384
Cdd:PRK00409 519 NELIASLEELERELEqkaEEAEALLKEAEKLKEELEEKKEKLQEEEDKL-LEEAEKEaqqaiKEAKKEADEIIKELRQLQ 597
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45505178 385 FMSenerTKNIKLQQQINEVKnenaKLKQQVARSEEQNYVPKFETAQLK 433
Cdd:PRK00409 598 KGG----YASVKAHELIEARK----RLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-421 |
6.31e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 161 QPVQEDMALNEVLQKLKH----TNRKQEVRIQELQCSNLYLEKRVKELQMKITKQqvfidvINKLKENVEELIEDKYKII 236
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHqkavSERQQQEKFEKMEQERLRQEKEEKAREVERRRK------LEEAEKARQAEMDRQAAIY 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 237 LEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKAnyvclQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEV 316
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVRQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 317 ER--------LQQLKKELEKATASALDLLKREKE-------------AQEQEFLSLQEEFQKLEKENLEERQKLKSRLEK 375
Cdd:pfam17380 412 QRkiqqqkveMEQIRAEQEEARQREVRRLEEERAremervrleeqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 45505178 376 LLTQV------RNLQFMSENERTKNIkLQQQINEVKNENAKLKQQVARSEEQ 421
Cdd:pfam17380 492 QRRKIlekeleERKQAMIEEERKRKL-LEKEMEERQKAIYEEERRREAEEER 542
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-419 |
9.38e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 169 LNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEEliedkykiilEKNDTKKTLQN 248
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG----------KNIKLSKDVSS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 249 LEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQK---NKSVS----QYLEMDKTLSKKEEEVERLQQ 321
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKrnvERQLStlqaQLSDMKKKLEEDAGTLEALEE 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 322 LKKELekatasaldllKREKEAQEQEFLSLQEEFQKLEKenleERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQI 401
Cdd:pfam01576 546 GKKRL-----------QRELEALTQQLEEKAAAYDKLEK----TKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML 610
|
250
....*....|....*...
gi 45505178 402 NEVKNENAKLKQQVARSE 419
Cdd:pfam01576 611 AEEKAISARYAEERDRAE 628
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
303-404 |
1.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 303 LEMDKT---LSKKEEEVERL----QQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKlEKENLEERQKLKSRLEK 375
Cdd:COG0542 404 MEIDSKpeeLDELERRLEQLeiekEALKKEQDEASFERLAELRDELAELEEELEALKARWEA-EKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 45505178 376 LLTQVRNLQFMSENERTKNIKLQQQINEV 404
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-358 |
1.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 170 NEVLQKLKHTNRK---QEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELI--------EDKYKIIL- 237
Cdd:COG4942 51 KALLKQLAALERRiaaLARRIRALEQELAALEAELAELEKEIAELR---AELEAQKEELAELLralyrlgrQPPLALLLs 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 238 --EKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEE 315
Cdd:COG4942 128 peDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45505178 316 VERLQQLKKELEKATASALDLLKR-EKEAQEQEFLSLQEEFQKL 358
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARlEAEAAAAAERTPAAGFAAL 251
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
303-405 |
2.15e-03 |
|
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: 40.73 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 303 LEMDKTLSKKEEEVERLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRN 382
Cdd:pfam02841 193 LQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQ 272
|
90 100
....*....|....*....|....*
gi 45505178 383 LQ--FMSENERTKNIKLQQQINEVK 405
Cdd:pfam02841 273 EQeeLLKEGFKTEAESLQKEIQDLK 297
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
247-447 |
2.18e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 247 QNLEEVLANTQKHLQESRNDKEMLqlqfkkikanyvclqERYMTEMQQKNKSVSQYLEmdktlskkeEEVERLQQLKKEL 326
Cdd:COG3096 532 QNAERLLEEFCQRIGQQLDAAEEL---------------EELLAELEAQLEELEEQAA---------EAVEQRSELRQQL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 327 EKATASAldllkREKEAQEQEFLSLQEEFQKLEK---ENLEERQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINE 403
Cdd:COG3096 588 EQLRARI-----KELAARAPAWLAAQDALERLREqsgEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45505178 404 VknenaklkQQVARSEEQnyvpkfETAQLKDQLEEVLKSDITKD 447
Cdd:COG3096 663 L--------SQPGGAEDP------RLLALAERLGGVLLSEIYDD 692
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
193-402 |
2.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 193 SNLYLEKRVKELQMKITKQQVFIDV-INKLKENVEELiEDKYKIILEKND-------TKKTLQNLEEV---LANTQKHLQ 261
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEqLPELRKELEEA-EAALEEFRQKNGlvdlseeAKLLLQQLSELesqLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 262 ESRNDKEML--QLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEK----ATASALD 335
Cdd:COG3206 237 EAEARLAALraQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAqlqqEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45505178 336 LLKREKEAQEQEFLSLQEEFQKLEKEnLEERQKLKSRLEKLLTQVRNLQ--FMSENERTKNIKLQQQIN 402
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEAR-LAELPELEAELRRLEREVEVARelYESLLQRLEEARLAEALT 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-507 |
2.46e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 296 NKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKATASA----------LDLLKREKEAQEQEFLSLQEEFQKLEKenleE 365
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeleeleeeLEQLRKELEELSRQISALRKDLARLEA----E 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 366 RQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEvLKSDIT 445
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAA 820
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45505178 446 kDTKTTHSNLLPDCSPCEERLNPADiKRASQLASKMHSLLALMVGLLTCQDIINSDAEHFKE 507
Cdd:TIGR02168 821 -NLRERLESLERRIAATERRLEDLE-EQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
172-435 |
2.56e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 172 VLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEE 251
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 252 VLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERymtemQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELekaTA 331
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK-----NQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---TN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 332 SALDLLKREKEAQEQeflslQEEFQKLEKENleerQKLKSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKL 411
Cdd:TIGR04523 354 SESENSEKQRELEEK-----QNEIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
250 260
....*....|....*....|....
gi 45505178 412 KQQVARSEEQNYVPKFETAQLKDQ 435
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQ 448
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
304-381 |
2.56e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 304 EMDKTLSKKEEEVERLQQ-LKKELEKATASALDLLKREKEAQEQEFLSLQEEFQK--------LEKENLEERQKLKSRLE 374
Cdd:smart00935 22 QLEKEFKKRQAELEKLEKeLQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRkqqklqqdLQKRQQEELQKILDKIN 101
|
....*..
gi 45505178 375 KLLTQVR 381
Cdd:smart00935 102 KAIKEVA 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-441 |
2.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 291 EMQQKNKSVSQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldllKREKEAQEQEFLSLQEEFQKLEkenlEERQKLK 370
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE---------ELEKLEKLLQLLPLYQELEALE----AELAELP 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45505178 371 SRLEKLLTQVRNLQfmsenertkniKLQQQINEVKNENAKLKQQVARSEEQNYVPKFET-AQLKDQLEEVLK 441
Cdd:COG4717 146 ERLEELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQ 206
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
206-438 |
2.88e-03 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 40.81 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 206 MKITKQQVFIDVINK-----LKENVEELIEDKYKI----ILEKNDTKKTLQNLEEVLANT-----QKHL----------- 260
Cdd:PRK12903 660 LRITHFKFSEKDFENyhkeeLAQYLIEALNEIYFKkrqvILDKIALNTFFESERYIILSAldkywQNHIdtmdklrsgvn 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 261 --QESRND-------------KEMLQ-------LQFKKIKANYVCLQERYMTEMQQKNKSVSQ-YLEMDKTLSKKEEEVE 317
Cdd:PRK12903 740 lvQYSQKNpyqvyteegtkkfNILLQeiaydviVSLFNNPNAEKILIITEILSDGINNSDINDrPQELIDQIIESEEERL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 318 RLQQLKKELEKATASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKlltqvrnlqfmsENERTKNIKL 397
Cdd:PRK12903 820 KALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEF------------KNDPKKLNKL 887
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 45505178 398 qqqinevKNENAKLKQQVARSEEQNYVPKfETAQLKDQLEE 438
Cdd:PRK12903 888 -------IIAKDVLIKLVISSDEIKQDEK-TTKKKKKDLEK 920
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
197-375 |
3.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 197 LEKRVKELQMKITKQQvfiDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQfKK 276
Cdd:COG1579 22 LEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ-KE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 277 IkanyvclqerymtEMQQKNKSV--SQYLEMDKTLSKKEEEVERLQQLKKELEKAtasaldlLKREKEAQEQEFLSLQEE 354
Cdd:COG1579 98 I-------------ESLKRRISDleDEILELMERIEELEEELAELEAELAELEAE-------LEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|.
gi 45505178 355 FQKLEKenleERQKLKSRLEK 375
Cdd:COG1579 158 LEELEA----EREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
306-442 |
3.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 306 DKTLSKKEEEVERLQQLKKELEKATASA---LDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTQVRN 382
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 383 LQ--------------------FMSENERTKNIKLQQQ--INEVKNENAKLKQQVARSEEQnyvpKFETAQLKDQLEEVL 440
Cdd:COG3883 95 LYrsggsvsyldvllgsesfsdFLDRLSALSKIADADAdlLEELKADKAELEAKKAELEAK----LAELEALKAELEAAK 170
|
..
gi 45505178 441 KS 442
Cdd:COG3883 171 AE 172
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
200-475 |
3.51e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 200 RVKELQMKITKQQVFIDVINKLKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKA 279
Cdd:COG5022 756 RGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRET 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 280 NYVCLQERYMTEMQQKNKSVsQYLEMDKTLSKKE---EEVERLQQLKKEL--EKATASALDLLKREKEAQEQEFLSLQEE 354
Cdd:COG5022 836 EEVEFSLKAEVLIQKFGRSL-KAKKRFSLLKKETiylQSAQRVELAERQLqeLKIDVKSISSLKLVNLELESEIIELKKS 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 355 FQKLEKENLEERQKLKSRLEKLltqvrNLQFMSENERTKNIKLQQQINEVKNENAKLKQQvarSEEQNYVPKFETAQLKD 434
Cdd:COG5022 915 LSSDLIENLEFKTELIARLKKL-----LNNIDLEEGPSIEYVKLPELNKLHEVESKLKET---SEEYEDLLKKSTILVRE 986
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 45505178 435 QLEEVLKSDITKDTKTTHSNLLPDCSPCEERLNPADIKRAS 475
Cdd:COG5022 987 GNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
176-437 |
5.38e-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: 40.10 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 176 LKHTNRKQEVRIQELQCSNLYLEKRVKELQMKITKQQVFIDVINKLKENVEELI-------EDKYKIILEKNDTKKTLQN 248
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTaqlestkEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 249 LEEVLANTQKHLQESRNDKEMLQLQFKKIKA---------NYVCLQERYMTEMQQKNKSVS-QYLEMDKTLSKKEEEVER 318
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSrvdlklqelQHLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 319 LQQLKKELEKaTASALDLLKREKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKL-LTQVRNLQFMSENERT-KNIK 396
Cdd:pfam15921 574 MTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLeLEKVKLVNAGSERLRAvKDIK 652
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 45505178 397 LQ--QQINEVKNENAKLKQQVARSE--EQNYVPKFE-----TAQLKDQLE 437
Cdd:pfam15921 653 QErdQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEemettTNKLKMQLK 702
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
197-450 |
5.92e-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: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 197 LEKRVKELQMKITKQQVFIDVINK-LKENVEELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFK 275
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSdLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 276 KI------KANYVCLQERYMTEMQQKNKSV----SQYLEMDKTLSKKEEEVERLQQLKKELEKatasaldlLKREKEAQE 345
Cdd:TIGR04523 160 KYndlkkqKEELENELNLLEKEKLNIQKNIdkikNKLLKLELLLSNLKKKIQKNKSLESQISE--------LKKQNNQLK 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 346 QEFLSLQEEFQKLEKENLEERQKL---KSRLEKLLTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQvaRSEEQN 422
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLnqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWN 309
|
250 260
....*....|....*....|....*...
gi 45505178 423 YVPKFETAQLKDQLEEvLKSDITKDTKT 450
Cdd:TIGR04523 310 KELKSELKNQEKKLEE-IQNQISQNNKI 336
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
312-419 |
8.07e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 38.91 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 312 KEEEVERLQQLKKELEKATASALdllkrEKEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEKLLTqvrnlqfmsener 391
Cdd:PRK11637 168 RQETIAELKQTREELAAQKAELE-----EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ------------- 229
|
90 100
....*....|....*....|....*...
gi 45505178 392 tkniKLQQQINEVKNENAKLKQQVARSE 419
Cdd:PRK11637 230 ----KDQQQLSELRANESRLRDSIARAE 253
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-442 |
9.62e-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: 39.39 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 164 QEDMALNEVLQKLKHTNRKQEVRIQELQCSNLYLEKRVKELQMKI------------------TKQQVFIDVINKLKENV 225
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeemrarlaARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 226 EELIEDKYKIILEKNDTKKTLQNLEEVLANTQKHLQESRNDKEMLQLQFKKIKANYVCLQERYMTEMQQKNKSVSQYLEM 305
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 306 DKTLSKKEEEVERLQQLKKELEKATASALDLLKRE----------KEAQEQEFLSLQEEFQKLEKENLEERQKLKSRLEK 375
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEekgrqelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45505178 376 L---LTQVRNLQFMSENERTKNIKLQQQINEVKNENAKLKQQVARSEEQNYVPKFETAQLKDQLEEVLKS 442
Cdd:pfam01576 245 LqaaLARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDT 314
|
|
| |
