|
Name |
Accession |
Description |
Interval |
E-value |
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
170-477 |
1.35e-118 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 352.33 E-value: 1.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 170 KEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQ 249
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 250 RHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKH 329
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 330 KDLQQQLVDAKLQQAQemlkEAEERHQREKEflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFT 409
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 314122227 410 TFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 477
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-511 |
4.99e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 286 LQMEQHNERNSKLRQENMELAERLKKL---IEQYELR-EEHIDKVFKHKDLQQQLVDA--KLQQAQEMLKEAEERHQREK 359
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELtaeLQELEEKlEELRLEVSELEEEIEELQKElyALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 360 EFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKEttmyrsrWESS 439
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETL 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 314122227 440 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTAGGITDIGSERRPEATTASKEQ 511
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
194-490 |
2.58e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 194 KKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLAR--SKLESLCRELQRHNRSLKEEGvQRAREEEEKRK 271
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleAELAELEAELEELRLELEELE-LELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 272 EVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEhidkvfkhKDLQQQLVDAKLQQAQEMLKEA 351
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE--------LEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 352 EERhqrekeflLKEAVESQRmcELMKQQETHLKQQLALYTEKfEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTM 431
Cdd:COG1196 364 EEA--------LLEAEAELA--EAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 314122227 432 YRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTA 490
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-461 |
2.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 161 EKKKAKGLGKEITLLMQTLNTLstpEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSK 240
Cdd:COG1196 223 KELEAELLLLKLRELEAELEEL---EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 241 LESLCRELQRHNRSLKEEGVQRAREEEEkrkevtshfqvtlndIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELRE 320
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAE---------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 321 EHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALyTEKFEEFQNT 400
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEA 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 314122227 401 LSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQ 461
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-490 |
6.07e-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: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 278 QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKL---IEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEEr 354
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 355 hqrEKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRS 434
Cdd:TIGR02168 783 ---EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 314122227 435 RWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTA 490
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
303-515 |
9.75e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 303 MEL--AERlKKLIEqyELRE----EHIDKVFKHK--DLQQQL--VDAKLQQAQEMLKeAEERHQREKEFLLKEAV-ESQR 371
Cdd:PHA02562 145 MQLsaPAR-RKLVE--DLLDisvlSEMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENIaRKQN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 372 MCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYR---------SRWESSNKA 442
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDR 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 314122227 443 LLEMAEEKTVRDKELEGLQVKIQRLEKlcraLQTERNDLNKRVQDLTaggiTDIGSERRPEATTASKEQGVES 515
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEE----IMDEFNEQSKKLLELK----NKISTNKQSLITLVDKAKKVKA 365
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
278-526 |
1.40e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 278 QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYEL---REEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEER 354
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 355 H---QREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTM 431
Cdd:COG1196 332 LeelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 432 YRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDL---TAGGITDIGSERRPEATTAS 508
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELleeAALLEAALAELLEELAEAAA 491
|
250
....*....|....*...
gi 314122227 509 KEQGVESPGAQPASSPRA 526
Cdd:COG1196 492 RLLLLLEAEADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-427 |
6.07e-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: 46.20 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 160 QEKKKAKGLGKEITLLMQTLntlstpEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARS 239
Cdd:TIGR02168 246 EELKEAEEELEELTAELQEL------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 240 KLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTShFQVTLNDIQLQMEQHNERNSKLRQEnmelAERLKKLIEQYELR 319
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 320 EEHIDKvfkhkdlQQQLVDAKLQQAQEML-KEAEERHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQ 398
Cdd:TIGR02168 395 IASLNN-------EIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260
....*....|....*....|....*....
gi 314122227 399 NTLSKSSEVFTTFKQEMEKMTKKIKKLEK 427
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-414 |
6.27e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 186 EEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGeHSKAVLARSKLESLCRELQRhnrslkeegvqrare 265
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREIAE--------------- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 266 eeekrkevtshfqvtlndIQLQMEQHNERNSKLRqenmELAERLKKLIEQY-ELREEHIDKVFKHKDLQQQLVDAK--LQ 342
Cdd:COG4913 673 ------------------LEAELERLDASSDDLA----ALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEeeLD 730
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 314122227 343 QAQEMLKEAEERHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKsseVFTTFKQE 414
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELER---AMRAFNRE 799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-478 |
6.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 143 EEIRASDEVgdrdHRRPQEKKKAKGLGKEITLLMQTLNTLSTPEE--KLAALCKKYAEL--LEEHRNSQKQMKLLQKKQS 218
Cdd:PTZ00121 1467 EEAKKADEA----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAkkADEAKKAEEAKKADEAKKA 1542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 219 QLVQEKDHLR-GEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQlqmEQHNERNSK 297
Cdd:PTZ00121 1543 EEKKKADELKkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE---EAKKAEEAK 1619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 298 LRQENMELAERLKKLIEQYELREEHidkvfkhkdlqqqlvdaKLQQAQEMLKEAEERHQREKEFLLKEAVESQRMCELMK 377
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAE-----------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 378 QQETHLKQQLALYTEKFEefqntlSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKEL 457
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEE------AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
330 340
....*....|....*....|.
gi 314122227 458 EGLQVKIQRLEKLCRALQTER 478
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEK 1777
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
171-475 |
1.06e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 171 EITLLMQTLNTLSTPEEKLAALCKKY-------AELLEEHRNSQKQMK-LLQKKQSQLVQEKDHLRGEHSKAVLARSKLE 242
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYksdetliASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 243 SLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYElreEH 322
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK---DK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 323 IDKVFKHKDLQQQLVDAKLQQAQEMLK---EAEERHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQN 399
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESELReqlEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 314122227 400 TLskssevfttfkqemEKMTKKIKKLEKETTMYRSRwessnkallemaeektvRDKELEGLQVKIQRLEKLCRALQ 475
Cdd:pfam12128 479 EQ--------------EAANAEVERLQSELRQARKR-----------------RDQASEALRQASRRLEERQSALD 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-490 |
1.26e-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: 44.37 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 281 LNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVfkhkDLQQQLVDAKLQQAQEMLKEAEERHQREKE 360
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 361 FLLKEAVESQRMcelmkqqETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSN 440
Cdd:COG4942 105 ELAELLRALYRL-------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 314122227 441 KALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTA 490
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-459 |
2.10e-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: 44.29 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 149 DEVGDRDHRRPQEKKKA---KGLGKEITLLMQT--LNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQE 223
Cdd:TIGR02169 194 DEKRQQLERLRREREKAeryQALLKEKREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 224 KDHLRGEHSK-----AVLARSKLESLCRELQRHNRSL--KEEGVQRAREEEEKRkevtshfQVTLNDIQLQMEQHNERNS 296
Cdd:TIGR02169 274 LEELNKKIKDlgeeeQLRVKEKIGELEAEIASLERSIaeKERELEDAEERLAKL-------EAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 297 KLRQENMELAERLKKLIEQYE-LREEHIDKVFKHKDLQQQLVDakLQQAQEMLKEAEERHQREKEFLLKEAVESQRMCEL 375
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEdLRAELEEVDKEFAETRDELKD--YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 376 MKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEM-AEEKTVRD 454
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeAQARASEE 504
|
....*
gi 314122227 455 KELEG 459
Cdd:TIGR02169 505 RVRGG 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
289-468 |
2.30e-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: 44.24 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 289 EQHNERNSKLRQENMELAERLKKlIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKEFLLKEAVE 368
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQE-IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 369 SQRMCELMKQQET----------HLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWES 438
Cdd:TIGR04523 442 IKDLTNQDSVKELiiknldntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190
....*....|....*....|....*....|
gi 314122227 439 SNKALLEMAEEKTVRDKELEGLQVKIQRLE 468
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-428 |
6.32e-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: 42.75 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 161 EKKKAKGLGKEITLLMQTLNTLstpEEKLAALCKKYAEllEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSK 240
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKL---EEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 241 LESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTShFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELRE 320
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 321 EHIDKvfkhKDLQQQLVDAKLQQAQEMLKEAEERHQREKEFLLKEAVES--QRMCELMKQQETHLKQQLALYTEKFEEFQ 398
Cdd:TIGR02169 910 AQIEK----KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
250 260 270
....*....|....*....|....*....|
gi 314122227 399 NTLSKSSEVFTTFKQEMEKMTKKIKKLEKE 428
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
163-387 |
1.19e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 163 KKAKGLGKEITLLMQTLN-TLST------PEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEkdhlrgEHSKAV 235
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE------TLSTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 236 LAR--SKLESLCRELQRHNRSLKE--------------------EGVQRARE------EEEKRKEVTSHFQVTLNDIQLQ 287
Cdd:PRK11281 123 LRQleSRLAQTLDQLQNAQNDLAEynsqlvslqtqperaqaalyANSQRLQQirnllkGGKVGGKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 288 M-EQHNERNSKLRQENMELAERLKKlieQYELREEHIDKVFKHKDLQQQLVDAK-LQQAQEMLKEAEERHQREK------ 359
Cdd:PRK11281 203 LlNAQNDLQRKSLEGNTQLQDLLQK---QRDYLTARIQRLEHQLQLLQEAINSKrLTLSEKTVQEAQSQDEAARiqanpl 279
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 314122227 360 ------------EFLLKeavESQRMCELMkQQETHLKQQL 387
Cdd:PRK11281 280 vaqeleinlqlsQRLLK---ATEKLNTLT-QQNLRVKNWL 315
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
278-486 |
1.25e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 278 QVTLNDIQLQMEQHNER-----NSKLRQENMELAERLKKLIEQYELREEhidkvfkhkDLQQQLvdaklQQAQEMLKEAE 352
Cdd:PRK11281 35 LPTEADVQAQLDALNKQklleaEDKLVQQDLEQTLALLDKIDRQKEETE---------QLKQQL-----AQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 353 ERHQRekeflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSK-SSEVFTTFKQ---------EMEKMTKKI 422
Cdd:PRK11281 101 AELEA-----LKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEyNSQLVSLQTQperaqaalyANSQRLQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 423 KKLEKETTMYRSRWESSNKALLEmAEEKTV------RDKELEG--------------LQVKIQRLEKLCRALQTERNDln 482
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVLLQ-AEQALLnaqndlQRKSLEGntqlqdllqkqrdyLTARIQRLEHQLQLLQEAINS-- 252
|
....
gi 314122227 483 KRVQ 486
Cdd:PRK11281 253 KRLT 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-442 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 201 EEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEgvqrareeeekrkevtshfqvt 280
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 281 LNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYE-----------LREEHIDKVFKHKDLQQQLVDAKLQQAQEMLK 349
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 350 EAEERHQREKEfLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKET 429
Cdd:COG4942 158 DLAELAALRAE-LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|...
gi 314122227 430 TMYRSRWESSNKA 442
Cdd:COG4942 237 AAAAERTPAAGFA 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-482 |
2.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 143 EEIRASDEVGDRdhRRPQEKKKAKGLgKEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQ 222
Cdd:PRK03918 183 KFIKRTENIEEL--IKEKEKELEEVL-REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 223 EKDHLRGEHSKAVLARSKLESLCRELQ---------RHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQlQMEQHNE 293
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKelkekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 294 RNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEER------------------H 355
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkeeieeeiskitarigelK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 356 QREKEflLKEAVE----SQRMCELMKQQ--ETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKET 429
Cdd:PRK03918 419 KEIKE--LKKAIEelkkAKGKCPVCGREltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 314122227 430 TMY------RSRWESSNKALLEMAEEKTvrdKELEGLQVKIQRLEKLCRALQTERNDLN 482
Cdd:PRK03918 497 KLKelaeqlKELEEKLKKYNLEELEKKA---EEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-489 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 162 KKKAKGLGKEITLlmqTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKL 241
Cdd:TIGR04523 130 EKQKKENKKNIDK---FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 242 ESLCRElqrhNRSLKEEGVQRAREEEEKRKEVTSHfQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREE 321
Cdd:TIGR04523 207 KKKIQK----NKSLESQISELKKQNNQLKDNIEKK-QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 322 HIDKVFKH-KDLQQQLVDAKLQQAQEMLKEAEE---RHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEF 397
Cdd:TIGR04523 282 KIKELEKQlNQLKSEISDLNNQKEQDWNKELKSelkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 398 QNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRwessnkaLLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 477
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK-------IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330
....*....|..
gi 314122227 478 RNDLNKRVQDLT 489
Cdd:TIGR04523 435 IIKNNSEIKDLT 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
307-484 |
2.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 307 ERLKKLIEQYELREEHIDKVFKHKDLQQQLvDAKLQQAQEMLKEAEERHQRekeflLKEAVESQRMCELMKQqethLKQQ 386
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEK-----LEKLLQLLPLYQELEA----LEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 387 LALYTEKFEEFQNTLskssEVFTTFKQEMEKMTKKIKKLEKE--------TTMYRSRWESSNKALLEMAEEKTVRDKELE 458
Cdd:COG4717 141 LAELPERLEELEERL----EELRELEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180
....*....|....*....|....*.
gi 314122227 459 GLQVKIQRLEKLCRALQTERNDLNKR 484
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
283-396 |
3.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 283 DIQLQMEQ-HNERNSKL-RQEN--MELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQRE 358
Cdd:PRK12704 68 KLRNEFEKeLRERRNELqKLEKrlLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 314122227 359 KEFLLKEAVEsqrmcELMKQQETHLKQQLALYTEKFEE 396
Cdd:PRK12704 148 SGLTAEEAKE-----ILLEKVEEEARHEAAVLIKEIEE 180
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
333-488 |
3.58e-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: 40.32 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 333 QQQLVDAKLQQAQEMLKEAEER--HQREKEFLLKE-AVESQRMCELMKQQETHLKQQlalyTEKFEEFQNTLSKSSEVFT 409
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRlrQQQNAERLLEEfCQRIGQQLDAAEELEELLAEL----EAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 314122227 410 TFKQEMEKMTKKIKKLEKETtmyrSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDL 488
Cdd:COG3096 582 ELRQQLEQLRARIKELAARA----PAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQAL 656
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-519 |
4.55e-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: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 282 NDIQLQMEQHNERnsklrqenmelaerLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKEF 361
Cdd:pfam15921 256 NKIELLLQQHQDR--------------IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 362 LlkEAVESQRMCELMKQQETH------LKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSR 435
Cdd:pfam15921 322 L--ESTVSQLRSELREAKRMYedkieeLEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 436 wessNKALLEMAEEKTVR----DKELEGLQVKIQRLEKLCRALQTE--------------------------------RN 479
Cdd:pfam15921 400 ----NKRLWDRDTGNSITidhlRRELDDRNMEVQRLEALLKAMKSEcqgqmerqmaaiqgkneslekvssltaqlestKE 475
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 314122227 480 DLNKRVQDLTAGGITDIGSERRPEATTAS---KEQGVESPGAQ 519
Cdd:pfam15921 476 MLRKVVEELTAKKMTLESSERTVSDLTASlqeKERAIEATNAE 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-490 |
4.77e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 304 ELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKEflLKEAVESQRmcELMKQQETHL 383
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA--ELEELEAEL--AELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 384 KQQLALYTEKFEEFQntlskssevfttfkQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVK 463
Cdd:COG1196 273 RLELEELELELEEAQ--------------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180
....*....|....*....|....*..
gi 314122227 464 IQRLEKLCRALQTERNDLNKRVQDLTA 490
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
257-490 |
5.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 257 EEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERN-----SKLRQENMELAERLKKLIEQYE----LREEHIDKVF 327
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREqareTRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 328 KHKDLQQQLvdAKLQQAQEMLKEAEERHQREKEfLLKEAVESQRM---------------CELMKQQETHLKQQLALYTE 392
Cdd:PRK02224 245 EHEERREEL--ETLEAEIEDLRETIAETERERE-ELAEEVRDLRErleeleeerddllaeAGLDDADAEAVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 393 KFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEK--- 469
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfg 401
|
250 260 270
....*....|....*....|....*....|..
gi 314122227 470 -----------LCRALQTERNDLNKRVQDLTA 490
Cdd:PRK02224 402 dapvdlgnaedFLEELREERDELREREAELEA 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
278-428 |
5.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 278 QVTLNDIQLQMEQHNERNSKLRQENMELAE------RLKKLIEQYELREEHIDKVFKHKDLQQQL--VDAKLQQAQEMLK 349
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEEleaeleELREELEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLE 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 314122227 350 EAEERHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKE 428
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
275-492 |
5.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 275 SHFQvTLNDIQLQMEqhnernsKLRQEnmelAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEER 354
Cdd:COG4913 232 EHFD-DLERAHEALE-------DAREQ----IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 355 HQREKEFLLKEAVESQRMCELMKQQETHLKQQLA-LYTEKFEEFQNTLSkssevftTFKQEMEKMTKKIKKLEKETTMYR 433
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRgNGGDRLEQLEREIE-------RLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 314122227 434 SRWESSNKALLEMAEE----KTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTAGG 492
Cdd:COG4913 373 LPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-429 |
6.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 132 EKETSKGEPGTEEIRASDEVgdrdhRRPQEKKKAKGLGKEitllmqtlNTLSTPEEKLAALCKKYAEllEEHRNSQKQMK 211
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEA-----KKAEEKKKADELKKA--------EELKKAEEKKKAEEAKKAE--EDKNMALRKAE 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 212 LLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQV----TLNDIQLQ 287
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAA 1664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 288 MEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKvfKHKDLQQQLVDAKlQQAQEMLKEAEERHQREKEFLLKEAV 367
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK--KAEELKKKEAEEK-KKAEELKKAEEENKIKAEEAKKEAEE 1741
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 314122227 368 ESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKET 429
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-499 |
6.86e-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: 39.28 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 338 DAKLQQAQEMLKEAEERhqrEKEFLLKEAVESQRMCELMKQQETHLKQQlALYTEKFEEFQNTLSKssevfttfkqEMEK 417
Cdd:TIGR02169 169 DRKKEKALEELEEVEEN---IERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYEGYELLK----------EKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 418 MTKKIKKLEKEttmyrsrwessnkalLEMAEEktvrdkELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTAGGITDIG 497
Cdd:TIGR02169 235 LERQKEAIERQ---------------LASLEE------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293
|
..
gi 314122227 498 SE 499
Cdd:TIGR02169 294 EK 295
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
300-483 |
7.07e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 300 QENMELAERLKKLIEQYELREEHIDKVfkhKDLQQQLVDAKLQQAqemlKEAEERHQREKEFLLKEAVESQRMCELMKQQ 379
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDL---EELKLQELKLKEQAK----KALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122227 380 ETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEG 459
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180
....*....|....*....|....
gi 314122227 460 LQVKIQRLEKLCRALQTERNDLNK 483
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEK 342
|
|
| |
