|
Name |
Accession |
Description |
Interval |
E-value |
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
170-477 |
2.46e-116 |
|
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: 346.17 E-value: 2.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 170 KEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQ 249
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 250 RHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKH 329
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 330 KDLQQQLVDAKLQQAQemlkEAEERHQREKDflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFT 409
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777376017 410 TFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 477
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-487 |
1.13e-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: 55.06 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 286 LQMEQHNERNSKLRQENMELAERLKKL---IEQYELR-EEHIDKVFKHKDLQQQLVDA--KLQQAQEMLKEAEERHQREK 359
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELtaeLQELEEKlEELRLEVSELEEEIEELQKElyALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 360 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKEttmyrsrWESS 439
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1777376017 440 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 487
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
194-490 |
3.05e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 194 KKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLAR--SKLESLCRELQRHNRSLKEEGvQRAREEEEKRK 271
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleAELAELEAELEELRLELEELE-LELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 272 EVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEhidkvfkhKDLQQQLVDAKLQQAQEMLKEA 351
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE--------LEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 352 EERhqrekdflLKEAVESQRmcELMKQQETHLKQQLALYTEKfEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTM 431
Cdd:COG1196 364 EEA--------LLEAEAELA--EAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1777376017 432 YRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 490
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-461 |
4.72e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 161 EKKKAKGLGKEITLLMQTLNTLstpEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSK 240
Cdd:COG1196 223 KELEAELLLLKLRELEAELEEL---EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 241 LESLCRELQRHNRSLKEEGVQRAREEEEkrkevtshfqvtlndIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELRE 320
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAE---------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 321 EHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALyTEKFEEFQNT 400
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEA 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777376017 401 LSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQ 461
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-478 |
2.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 2 KNQDKKNGAAKQSNPKSSPGQPEAGPEGAQERPSQAAPAVEAEGPGSSQAPRKPEGAQARTAQSGALRDVSEELSRQLED 81
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 82 ILSTycvDNNQGGPGEDGAQGEPAEPEDAEKSRTYVARNGEPEptpvvngEKEPSKGDPNTEEIRQSDEVgdrdHRRPQE 161
Cdd:PTZ00121 1390 KKKA---DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-------KKKADEAKKKAEEAKKADEA----KKKAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 162 KKKAKGLGKEITLLMQTLNTLSTPEEKLAA-LCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSK 240
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 241 LESLCR--------ELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKL 312
Cdd:PTZ00121 1536 ADEAKKaeekkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 313 iEQYELREEHIDKVFKHKDLQQQLVDA---KLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLAL 389
Cdd:PTZ00121 1616 -EEAKIKAEELKKAEEEKKKVEQLKKKeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 390 YTEKFEefqntlSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEK 469
Cdd:PTZ00121 1695 KKEAEE------AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
....*....
gi 1777376017 470 LCRALQTER 478
Cdd:PTZ00121 1769 KAEEIRKEK 1777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-488 |
2.55e-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: 47.36 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 278 QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKL---IEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEEr 354
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 355 hqrEKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRS 434
Cdd:TIGR02168 783 ---EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1777376017 435 RWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDL 488
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
303-490 |
4.04e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 303 MEL--AERlKKLIEqyELRE----EHIDKVFKHK--DLQQQL--VDAKLQQAQEMLKeAEERHQREKDFLLKEAV-ESQR 371
Cdd:PHA02562 145 MQLsaPAR-RKLVE--DLLDisvlSEMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENIaRKQN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 372 MCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYR---------SRWESSNKA 442
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDR 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1777376017 443 LLEMAEEKTVRDKELEGLQVKIQRLEK-------LCRALQTERNDLNKRVQDLSA 490
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEEimdefneQSKKLLELKNKISTNKQSLIT 355
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-494 |
7.80e-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: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 149 DEVGDRDHRRPQEKKKA---KGLGKEITLLMQT--LNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQE 223
Cdd:TIGR02169 194 DEKRQQLERLRREREKAeryQALLKEKREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 224 KDHLRGEHSK-----AVLARSKLESLCRELQRHNRSL--KEEGVQRAREEEEKRkevtshfQVTLNDIQLQMEQHNERNS 296
Cdd:TIGR02169 274 LEELNKKIKDlgeeeQLRVKEKIGELEAEIASLERSIaeKERELEDAEERLAKL-------EAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 297 KLRQENMELAERLKKLIEQYE-LREEHIDKVFKHKDLQQQLVDakLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCEL 375
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEdLRAELEEVDKEFAETRDELKD--YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 376 MKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYrsrwessnkallemaeektvrDK 455
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV---------------------EK 483
|
330 340 350
....*....|....*....|....*....|....*....
gi 1777376017 456 ELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSAGGQG 494
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
9-161 |
8.44e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.36 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 9 GAAKQSNPKSSPGQPEAGPEGAQERPSQAAPAVEAEGPGSSQAPRKPEGAQARTAQSGALRDVSEElsrqledilstycV 88
Cdd:PRK07764 660 PDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA-------------Q 726
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777376017 89 DNNQGGPGEDGAQGEPAEPEDAEKSRTYVAR---NGEPEPTPVVNGEKEPSKGDPNTEEIRQSD-EVGDRDHRRPQE 161
Cdd:PRK07764 727 GASAPSPAADDPVPLPPEPDDPPDPAGAPAQpppPPAPAPAAAPAAAPPPSPPSEEEEMAEDDApSMDDEDRRDAEE 803
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-427 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 160 QEKKKAKGLGKEITLLMQTLntlstpEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARS 239
Cdd:TIGR02168 246 EELKEAEEELEELTAELQEL------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 240 KLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTShFQVTLNDIQLQMEQHNERNSKLRQEnmelAERLKKLIEQYELR 319
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 320 EEHIDKvfkhkdlQQQLVDAKLQQAQEML-KEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQ 398
Cdd:TIGR02168 395 IASLNN-------EIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260
....*....|....*....|....*....
gi 1777376017 399 NTLSKSSEVFTTFKQEMEKMTKKIKKLEK 427
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-414 |
1.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 186 EEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGeHSKAVLARSKLESLCRELQRhnrslkeegvqrare 265
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREIAE--------------- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 266 eeekrkevtshfqvtlndIQLQMEQHNERNSKLRqenmELAERLKKLIEQY-ELREEHIDKVFKHKDLQQQLVDAK--LQ 342
Cdd:COG4913 673 ------------------LEAELERLDASSDDLA----ALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEeeLD 730
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777376017 343 QAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKsseVFTTFKQE 414
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELER---AMRAFNRE 799
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-490 |
2.38e-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: 43.60 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 281 LNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVfkhkDLQQQLVDAKLQQAQEMLKEAEERHQREKD 360
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 361 FLLKEAVESQRMcelmkqqETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSN 440
Cdd:COG4942 105 ELAELLRALYRL-------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1777376017 441 KALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 490
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
138-475 |
5.07e-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: 42.90 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 138 GDPNTEEIRQSDEVGDRDHRRPQEKKKAKGlgkEITLLMQTLNTLSTPEEKLAALCKKY-------AELLEEHRNSQKQM 210
Cdd:pfam12128 212 VPPKSRLNRQQVEHWIRDIQAIAGIMKIRP---EFTKLQQEFNTLESAELRLSHLHFGYksdetliASRQEERQETSAEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 211 K-LLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQME 289
Cdd:pfam12128 289 NqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 290 QHNERNSKLRQENMELAERLKKLIEQYElreEHIDKVFKHKDLQQQLVDAKLQQaqemlKEAEERHQREKDflLKEAVES 369
Cdd:pfam12128 369 KHQDVTAKYNRRRSKIKEQNNRDIAGIK---DKLAKIREARDRQLAVAEDDLQA-----LESELREQLEAG--KLEFNEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 370 QrmcELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVfTTFKQEMEKMTKKIKKLEKETTMYRSRwessnkallemaee 449
Cdd:pfam12128 439 E---YRLKSRLGELKLRLNQATATPELLLQLENFDERI-ERAREEQEAANAEVERLQSELRQARKR-------------- 500
|
330 340
....*....|....*....|....*.
gi 1777376017 450 ktvRDKELEGLQVKIQRLEKLCRALQ 475
Cdd:pfam12128 501 ---RDQASEALRQASRRLEERQSALD 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-490 |
5.45e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 330 KDLQQQLVDAK--LQQAQEMLKEAEERHQRekdfLLKEAVESQRMCELmKQQETHLkqQLALYTEKFEEFQNTLSkssev 407
Cdd:TIGR02168 175 KETERKLERTRenLDRLEDILNELERQLKS----LERQAEKAERYKEL-KAELREL--ELALLVLRLEELREELE----- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 408 ftTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 487
Cdd:TIGR02168 243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
...
gi 1777376017 488 LSA 490
Cdd:TIGR02168 321 LEA 323
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
9-157 |
1.04e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 9 GAAKQSNPkSSPGQPEAGPEGAQERPSQAAPAVEAEGPGSSQAPRKPEGAQARTAQSGALRDVSEELSrqlEDILSTYCV 88
Cdd:PRK13108 310 SAASAVGP-VGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQP---GDLAGQAPA 385
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777376017 89 DNNQGGPGEDGAQGEPA--EPEDAEKSRTYVARNGEPEPTP-----VVNGEKEPSKGDPntEEIRQSDEVGDRDHR 157
Cdd:PRK13108 386 AHQVDAEAASAAPEEPAalASEAHDETEPEVPEKAAPIPDPakpdeLAVAGPGDDPAEP--DGIRRQDDFSSRRRR 459
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
289-468 |
1.11e-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: 41.93 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 289 EQHNERNSKLRQENMELAERLKKlIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFLLKEAVE 368
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQE-IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 369 SQRMCELMKQQET----------HLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWES 438
Cdd:TIGR04523 442 IKDLTNQDSVKELiiknldntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190
....*....|....*....|....*....|
gi 1777376017 439 SNKALLEMAEEKTVRDKELEGLQVKIQRLE 468
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
140-387 |
1.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 140 PNTEEIRQS-DEVGDRDHrrPQEKKKAKglgkeITLLMQTLNTLSTPE---EKLAALCKKYAELLEEHRNSQKQMKLLQK 215
Cdd:PRK11281 36 PTEADVQAQlDALNKQKL--LEAEDKLV-----QQDLEQTLALLDKIDrqkEETEQLKQQLAQAPAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 216 KQSQLVQEkdhlrgEHSKAVLAR--SKLESLCRELQRHNRSLKE--------------------EGVQRARE------EE 267
Cdd:PRK11281 109 DNDEETRE------TLSTLSLRQleSRLAQTLDQLQNAQNDLAEynsqlvslqtqperaqaalyANSQRLQQirnllkGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 268 EKRKEVTSHFQVTLNDIQLQM-EQHNERNSKLRQENMELAERLKKlieQYELREEHIDKVFKHKDLQQQLVDAK-LQQAQ 345
Cdd:PRK11281 183 KVGGKALRPSQRVLLQAEQALlNAQNDLQRKSLEGNTQLQDLLQK---QRDYLTARIQRLEHQLQLLQEAINSKrLTLSE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 346 EMLKEAEERHQREK------------------DFLLKeavESQRMCELMkQQETHLKQQL 387
Cdd:PRK11281 260 KTVQEAQSQDEAARiqanplvaqeleinlqlsQRLLK---ATEKLNTLT-QQNLRVKNWL 315
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
278-486 |
1.62e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 278 QVTLNDIQLQMEQHNER-----NSKLRQENMELAERLKKLIEQYELREEhidkvfkhkDLQQQLVDA--KLQQAQEMLke 350
Cdd:PRK11281 35 LPTEADVQAQLDALNKQklleaEDKLVQQDLEQTLALLDKIDRQKEETE---------QLKQQLAQApaKLRQAQAEL-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 351 aeERHQREKDFLLKEAVESQRMCELMKQQETHLKQQlalytekfEEFQNTLSK-SSEVFTTFKQ---------EMEKMTK 420
Cdd:PRK11281 104 --EALKDDNDEETRETLSTLSLRQLESRLAQTLDQL--------QNAQNDLAEyNSQLVSLQTQperaqaalyANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 421 KIKKLEKETTMYRSRWESSNKALLEmAEEKTV------RDKELEG--------------LQVKIQRLEKLCRALQTERND 480
Cdd:PRK11281 174 QIRNLLKGGKVGGKALRPSQRVLLQ-AEQALLnaqndlQRKSLEGntqlqdllqkqrdyLTARIQRLEHQLQLLQEAINS 252
|
....*.
gi 1777376017 481 lnKRVQ 486
Cdd:PRK11281 253 --KRLT 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-482 |
3.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 143 EEIRQSDEVGDRdhRRPQEKKKAKGLgKEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQ 222
Cdd:PRK03918 183 KFIKRTENIEEL--IKEKEKELEEVL-REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 223 EKDHLRGEHSKAVLARSKLESLCRELQ---------RHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQlQMEQHNE 293
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKelkekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 294 RNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEER------------------H 355
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkeeieeeiskitarigelK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 356 QREKDflLKEAVE----SQRMCELMKQQ--ETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKET 429
Cdd:PRK03918 419 KEIKE--LKKAIEelkkAKGKCPVCGREltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1777376017 430 TMY------RSRWESSNKALLEMAEEKTvrdKELEGLQVKIQRLEKLCRALQTERNDLN 482
Cdd:PRK03918 497 KLKelaeqlKELEEKLKKYNLEELEKKA---EEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-428 |
3.63e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 161 EKKKAKGLGKEITLLMQTLNTLstpEEKLAALCKKYAEllEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSK 240
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKL---EEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 241 LESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTShFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELRE 320
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 321 EHIDKvfkhKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFLLKEAVES--QRMCELMKQQETHLKQQLALYTEKFEEFQ 398
Cdd:TIGR02169 910 AQIEK----KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
250 260 270
....*....|....*....|....*....|
gi 1777376017 399 NTLSKSSEVFTTFKQEMEKMTKKIKKLEKE 428
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
283-396 |
4.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 283 DIQLQMEQ-HNERNSKL-RQEN--MELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQRE 358
Cdd:PRK12704 68 KLRNEFEKeLRERRNELqKLEKrlLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 1777376017 359 KDFLLKEAVEsqrmcELMKQQETHLKQQLALYTEKFEE 396
Cdd:PRK12704 148 SGLTAEEAKE-----ILLEKVEEEARHEAAVLIKEIEE 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
307-484 |
4.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 307 ERLKKLIEQYELREEHIDKVFKHKDLQQQLvDAKLQQAQEMLKEAEERHQRekdflLKEAVESQRMCELMKQqethLKQQ 386
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEK-----LEKLLQLLPLYQELEA----LEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 387 LALYTEKFEEFQNTLskssEVFTTFKQEMEKMTKKIKKLEKE--------TTMYRSRWESSNKALLEMAEEKTVRDKELE 458
Cdd:COG4717 141 LAELPERLEELEERL----EELRELEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180
....*....|....*....|....*.
gi 1777376017 459 GLQVKIQRLEKLCRALQTERNDLNKR 484
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-442 |
5.78e-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: 38.98 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 201 EEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEgvqrareeeekrkevtshfqvt 280
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 281 LNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYE-----------LREEHIDKVFKHKDLQQQLVDAKLQQAQEMLK 349
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 350 EAEERHQREKDfLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKET 429
Cdd:COG4942 158 DLAELAALRAE-LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|...
gi 1777376017 430 TMYRSRWESSNKA 442
Cdd:COG4942 237 AAAAERTPAAGFA 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-490 |
8.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 304 ELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDflLKEAVESQRmcELMKQQETHL 383
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA--ELEELEAEL--AELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376017 384 KQQLALYTEKFEEFQntlskssevfttfkQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVK 463
Cdd:COG1196 273 RLELEELELELEEAQ--------------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180
....*....|....*....|....*..
gi 1777376017 464 IQRLEKLCRALQTERNDLNKRVQDLSA 490
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| |
