|
Name |
Accession |
Description |
Interval |
E-value |
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
698-908 |
3.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 698 GEKLKQIQKEIQEQETLLQGYQ-QENERLYNQVKDLQEQNKKneermfkenqslfsEVASLKEQMHKSRflsqvvedsep 776
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRA--------------ELARLEAELERLE----------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 777 trnQNFTDLLAELRMAQKEKDSL-LEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEISR 855
Cdd:COG4913 316 ---ARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622932398 856 LQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLKAESGN-PSIQQKIR 908
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiPARLLALR 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
699-925 |
4.42e-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: 53.92 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQE----NERLYNQVKDLQEQNKKNEERMFKENQSLFSEVASLKEQMHKSR----FLSQV 770
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEiselEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLErsiaEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 771 VEDSEPTRNQNF----------TDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTgEKLY 840
Cdd:TIGR02169 317 LEDAEERLAKLEaeidkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-EKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 841 EIKILEETHKQEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEI-EKLKAESGNPSIQQKIRLKDKA---ADA 916
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaLEIKKQEWKLEQLAADLSKYEQelyDLK 475
|
....*....
gi 1622932398 917 KKIQDLERQ 925
Cdd:TIGR02169 476 EEYDRVEKE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
699-926 |
4.91e-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: 53.91 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQeqnkkneermfKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 778
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLR-----------KELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYV------TGEKLYEIKILEETHKQE 852
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltlLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932398 853 ISRLQKRLQWYAE----NQELLDKDALRLREANEEIEKLRLEIEKLKAESGNPSIQQKIRLKDKAADAKKIQDLERQV 926
Cdd:TIGR02168 833 IAATERRLEDLEEqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
654-926 |
4.95e-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: 53.91 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 654 KQQEK---------ELFKLNQDNYI-----LQAKLSSFEETNKKTRWLHFGEAAD-PVTGEKLKQIQKEIQEQETLLQGY 718
Cdd:TIGR02168 207 RQAEKaerykelkaELRELELALLVlrleeLREELEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 719 QQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRflSQVVEDSEptrnqNFTDLLAELRMAQKEKDS 798
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELE--SKLDELAE-----ELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 799 LLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAyVTGEKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDA--LR 876
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeAE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622932398 877 LREANEEIEKLRLEIEKLKAESGNpSIQQKIRLKDKAADAK-KIQDLERQV 926
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELER-LEEALEELREELEEAEqALDAAEREL 484
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
666-892 |
6.66e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 666 DNYILQAKLSSFEETNKKTRWLhfgeaadpvtGEKLKQIQKEIQEQETLLQGYQQENerlynQVKDLQEQNKKNEERMFK 745
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFL----------EEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 746 ENQSLFSEVASLKEQMHKSRFLSQVVEDSEPT-----RNQNFTDLLAELRMAQKEKDSLLE-------DIKRLKQDKQAL 813
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622932398 814 EvdlEKMKKERDQAKDQIayvtgeklyeikileethKQEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIE 892
Cdd:COG3206 304 R---AQLQQEAQRILASL------------------EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
612-897 |
1.30e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 612 LMFKRVQEAEEKWRGAQALIEQIKAT---FSEKEKELENKLEELKKQQEKELFKLNQdnyiLQAKLSSfeetnkktrwlh 688
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAEleeLEAELAELEAELEELRLELEELELELEE----AQAEEYE------------ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 689 fgeaadpvTGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRFLS 768
Cdd:COG1196 293 --------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 769 QVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAyvtgEKLYEIKILEET 848
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622932398 849 HKQEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLKAE 897
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
694-925 |
3.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 694 DPVTGEKLKQIQKEIQEqetlLQGYQQENERLYNQVKDLQEQNKKNEERmfkenQSLFSEVASLKEQMHKSRFLsqvved 773
Cdd:COG4913 220 EPDTFEAADALVEHFDD----LERAHEALEDAREQIELLEPIRELAERY-----AAARERLAELEYLRAALRLW------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 774 septRNQNFTDLLaelrmaQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEI 853
Cdd:COG4913 285 ----FAQRRLELL------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622932398 854 SRLQKRLQWYaenQELLDKDALRLREANEEIEKLRLEIEKLKAESGnpsiQQKIRLKDKAADAK-KIQDLERQ 925
Cdd:COG4913 355 EERERRRARL---EALLAALGLPLPASAEEFAALRAEAAALLEALE----EELEALEEALAEAEaALRDLRRE 420
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
699-906 |
5.21e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLFSEVASLKEQMHKSRFLSQVVEdseptr 778
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLG------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEvdleKMKKERDQAKDQIAYVTGEKlyeikileETHKQEISRLQk 858
Cdd:COG3883 111 SESFSDFLDRLSALSKIADADADLLEELKADKAELE----AKKAELEAKLAELEALKAEL--------EAAKAELEAQQ- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622932398 859 rlqwyAENQELLDKDALRLREANEEIEKLRLEIEKLKAESGNPSIQQK 906
Cdd:COG3883 178 -----AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
611-909 |
6.96e-06 |
|
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: 49.38 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 611 LLMFKRVQEAEEKWRGAQALIEQIKAtfsekekelenkleeLKKQQEKELFKLNQDnyilQAKLSsfeetnkktrwlhfg 690
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQ---------------EIAELEKELAALKKE----EKALL--------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 691 eaadpvtgEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfKENQSLFSEVASLKEQMHKSRFLSQV 770
Cdd:COG4942 55 --------KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL-EAQKEELAELLRALYRLGRQPPLALL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 771 VEDSEPTRNQNFTDLLAELRMAQKEkdsLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAyvtgEKLYEIKILEETHK 850
Cdd:COG4942 126 LSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELE----EERAALEALKAERQ 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622932398 851 QEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLKAESGNPSIQQKIRL 909
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
693-890 |
7.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 693 ADPVTG----EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQnkKNEERMFKENQSLFSEVASLKEQMH-KSRFL 767
Cdd:COG4913 600 SRYVLGfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQER--REALQRLAEYSWDEIDVASAEREIAeLEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 768 SQVVEDseptrNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQI-AYVTGEKLYEIKILE 846
Cdd:COG4913 678 ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622932398 847 ETHKQEI-SRLQKRL-QWYAENQELLDKdalRLREANEEIEKLRLE 890
Cdd:COG4913 753 ERFAAALgDAVERELrENLEERIDALRA---RLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
605-897 |
9.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 605 ENKEEELLMFKRVQEAEEKWRGAQALIEQIKATFSEKekelenkleelkkqqEKELFKLNQDNYILQAKLSSFEETNKKT 684
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL---------------EEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 685 RwlhfgeaadpvtgEKLKQIQKEIQEQETLLQGYQQENERLynqvkdlqeqnKKNEERMFKENQSLFSEVASLKEQMHKS 764
Cdd:TIGR02168 308 R-------------ERLANLERQLEELEAQLEELESKLDEL-----------AEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 765 RFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVtgeKLYEIKI 844
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---ELKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622932398 845 LEETHKQEISRLQKRLQWYAENQELLDKdalRLREANEEIEKLRLEIEKLKAE 897
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQLQAR 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
699-860 |
1.08e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEErmfkenqslfsEVASLKEQMHKSRFLSQVVEDseptr 778
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-----------EIEEVEARIKKYEEQLGNVRN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGE---KLYEIKILEETHKQEISR 855
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeELAELEAELEELEAEREE 167
|
....*
gi 1622932398 856 LQKRL 860
Cdd:COG1579 168 LAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
699-895 |
1.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEErMFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 778
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYV----TGEKLYEIKILEETHKQEIS 854
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkySEEEYEELREEYLELSRELA 676
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622932398 855 RLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLK 895
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-897 |
4.63e-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: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 619 EAEEKWRGAQALIEQIKATFSEKEKELENkLEELKKQQEKELFKLNQDNYILQAKLSSFEET-NKKTRWLHFGEAADPVT 697
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLARLEAEvEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 698 GEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRFLSQvvedsept 777
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLE-------- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 778 rnqnftDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEISRLQ 857
Cdd:TIGR02168 828 ------SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622932398 858 KRLQWYAENQELLDKdalrLREANEEIEKLRLEIEKLKAE 897
Cdd:TIGR02168 902 ELRELESKRSELRRE----LEELREKLAQLELRLEGLEVR 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
792-926 |
1.07e-04 |
|
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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 792 AQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQI-AYVTGEKLYEIKILEETHKQEISRLQKRLqwyaenqELL 870
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERReALQRLAEYSWDEIDVASAEREIAELEAEL-------ERL 680
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932398 871 DKDALRLREANEEIEKLRLEIEKLKaesgnpsiQQKIRLKDKAADA-KKIQDLERQV 926
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELE--------EELDELKGEIGRLeKELEQAEEEL 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
786-925 |
1.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 786 LAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIayvtgeKLYEIKILEETHKQEISRLQKRLQWYAE 865
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL------EKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622932398 866 NQELLDKDALRLREANEEIEKLRLEIEKLKAE----SGNPSIQQKIRLKDKAADAKKIQDLERQ 925
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEEleelLEQLSLATEEELQDLAEELEELQQRLAE 210
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
784-896 |
1.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 784 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKdqiayvtgEKLYEIKILEEthkqEISRLQKRLqwy 863
Cdd:COG2433 417 RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI--------RKDREISRLDR----EIERLEREL--- 481
|
90 100 110
....*....|....*....|....*....|...
gi 1622932398 864 aenqelldkdalrlREANEEIEKLRLEIEKLKA 896
Cdd:COG2433 482 --------------EEERERIEELKRKLERLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
699-897 |
1.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENErlynQVKDLQEQNKKNEERMFKENQSLFSEVASLKEQMHKsrfLSQVVEDSEPTR 778
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEK---LEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NqnftdllaELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVT-----GEKLYEIKILEETHKQEI 853
Cdd:PRK03918 238 E--------EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622932398 854 SRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLKAE 897
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
651-926 |
2.14e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 651 ELKKQQEK-ELFKLNQDNY-ILQAKLSSFEETNKKTRWLHFGEAADpVTGEKLKQIQKEIQEQETLLQGYQQENERLYNQ 728
Cdd:COG1196 204 PLERQAEKaERYRELKEELkELEAELLLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 729 VKDLQ----------EQNKKNEERMFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDS 798
Cdd:COG1196 283 LEEAQaeeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 799 LLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAyvtgEKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDALRLR 878
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAA----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622932398 879 EANEEIEKLRLEIEKLKAESGNPSIQQKIRLKDKAADAKKIQDLERQV 926
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
784-897 |
2.18e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 784 DLL----AELRMaqkEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDqiayvtgEKLYEIKILEETHKQEISRLQKR 859
Cdd:COG0542 393 DLIdeaaARVRM---EIDSKPEELDELERRLEQLEIEKEALKKEQDEASF-------ERLAELRDELAELEEELEALKAR 462
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622932398 860 lqWYAENQELLDKDALR--LREANEEIEKLRLEIEKLKAE 897
Cdd:COG0542 463 --WEAEKELIEEIQELKeeLEQRYGKIPELEKELAELEEE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
782-925 |
2.63e-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: 45.06 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 782 FTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKE-------RDQAKDQIAYVTGEKLYEIKILEETHKQEIS 854
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeieqlLEELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622932398 855 RLQKRLQWYAENQELLDKdalRLREANEEIEKLRLEIEKLKAESGNPSIqQKIRLKDKAADAKKIQDLERQ 925
Cdd:TIGR02169 305 SLERSIAEKERELEDAEE---RLAKLEAEIDKLLAEIEELEREIEEERK-RRDKLTEEYAELKEELEDLRA 371
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
697-889 |
3.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 697 TGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKneermFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEP 776
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 777 TRNQ--NFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEIS 854
Cdd:COG4717 137 LEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*
gi 1622932398 855 RLQKRLQWYAENQELLDKDALRLrEANEEIEKLRL 889
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAA-ALEERLKEARL 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-861 |
4.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 655 QQEKELFKLNQDNYILQAKLSSFEETNKKTRWLHFGEAAdpvtgEKLKQIQKEIQEQET--LLQGYQQENERLYNQ--VK 730
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-----EELQELLREAEELEEelQLEELEQEIAALLAEagVE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 731 DLQEQNKKNEErmFKENQSLFSEVASLKEQM--HKSRFLSQVVEDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQ 808
Cdd:COG4717 383 DEEELRAALEQ--AEEYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622932398 809 DKQALEVD--LEKMKKERDQAKDQIAYVTgEKLYEIKILEETHKQEISRLQKRLQ 861
Cdd:COG4717 461 ELEQLEEDgeLAELLQELEELKAELRELA-EEWAALKLALELLEEAREEYREERL 514
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
708-908 |
4.70e-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: 43.96 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 708 IQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLfSEVASLKEQMHKSRFLSQVVEDSEPTRNqnftdlLA 787
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK-VEMEQIRAEQEEARQREVRRLEEERARE------ME 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 788 ELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIK--ILEETHKQEIsrLQKRLQwyaE 865
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqaMIEEERKRKL--LEKEME---E 524
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622932398 866 NQELLDKDALRlREANEEIEKlRLEIEKLKaesgnpSIQQKIR 908
Cdd:pfam17380 525 RQKAIYEEERR-REAEEERRK-QQEMEERR------RIQEQMR 559
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
699-897 |
6.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEErmfkENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 778
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE----EAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDL----------------------------------------- 817
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLrtarerveeaealleagkcpecgqpvegsphvetieedrer 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 818 -EKMKKERDQAKDQIAYVTgEKLYEIKILEETHKqEISRLQKRLQwyaENQELLDKDALRLREANEEIEKLRLEIEKLKA 896
Cdd:PRK02224 477 vEELEAELEDLEEEVEEVE-ERLERAEDLVEAED-RIERLEERRE---DLEELIAERRETIEEKRERAEELRERAAELEA 551
|
.
gi 1622932398 897 E 897
Cdd:PRK02224 552 E 552
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
787-897 |
7.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 787 AELRMAQKEKDSLLEDIKR----LKQDKQaLEVDlEKMKKERDQAKDQIAyvtgEKLYEIKILEETHKQEISRLQKRLQW 862
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKeaeaIKKEAL-LEAK-EEIHKLRNEFEKELR----ERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110
....*....|....*....|....*....|....*
gi 1622932398 863 YAENQELLDKDALRLREANEEIEKLRLEIEKLKAE 897
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
698-823 |
1.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 698 GEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERmFKENQSlfsEVASLKEQMHKSRFLSQvvedsept 777
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE-FAALRA---EAAALLEALEEELEALE-------- 404
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932398 778 rnQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKE 823
Cdd:COG4913 405 --EALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
784-897 |
1.81e-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: 41.06 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 784 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGE-KLYEIKILEETHKQ-------EISR 855
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIKKYEEQLgnvrnnkEYEA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622932398 856 LQKRLQWYAENQELLDKdalRLREANEEIEKLRLEIEKLKAE 897
Cdd:COG1579 94 LQKEIESLKRRISDLED---EILELMERIEELEEELAELEAE 132
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
709-824 |
2.09e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 709 QEQETLLQGYQQENERLYNQVKDLQEQNKK-NEERMfkENQSLFSEVASLKEqmhksrflSQVVEDSEPTRNqnFTDLLA 787
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERlQEERM--EREKLEVELGREKD--------CNRVQLSESRRE--LQELKA 371
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622932398 788 ELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKER 824
Cdd:pfam07888 372 SLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
699-879 |
2.18e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMfkenQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 778
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV----AELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEEThKQEISRLQK 858
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT-EEELRSLSK 192
|
170 180
....*....|....*....|.
gi 1622932398 859 RLQWYAENQELLDKDALRLRE 879
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQD 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
615-860 |
2.35e-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: 41.97 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 615 KRVQEAEEKWRGAQALIEQIKATfSEKEKELENKLEELKKQQEKELFKLNQDNYILQAKLSSFEETNKKTRwlhfgeaad 694
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 695 pvtgEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLFSEVAS---LKEQMHKSRFLSQVV 771
Cdd:TIGR02168 810 ----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieeLESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 772 EDSEPTRNQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQ 851
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*....
gi 1622932398 852 EISRLQKRL 860
Cdd:TIGR02168 966 DEEEARRRL 974
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
705-897 |
2.71e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 705 QKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQSLFSEVASLKEqmhksRFLSQVVEDseptrnqnFTD 784
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVE-----EELEKIEKE--------IKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 785 LLAELRMAQKEKDSLLEDIKRLKQDKqALEVDLEKMKKER-----------DQAKDQIAYVTGEKLYEIKILEET----- 848
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPWG-NFDLDLSLLLGFKyvsvfvgtvpeDKLEELKLESDVENVEYISTDKGYvyvvv 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622932398 849 -----HKQEISRLQKRLQWYAEN-------QELLDKDALRLREANEEIEKLRLEIEKLKAE 897
Cdd:PRK05771 184 vvlkeLSDEVEEELKKLGFERLEleeegtpSELIREIKEELEEIEKERESLLEELKELAKK 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
784-897 |
2.91e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 784 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIA--------------------YVTG------- 836
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAeaeaeieerreelgeraralYRSGgsvsyld 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622932398 837 ------------EKLYEIKILEETHKQEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLKAE 897
Cdd:COG3883 107 vllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
699-897 |
4.30e-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: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 699 EKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNeermFKENQSLFSEVASLKEQMHKSRFLSQVVEDSEPTR 778
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY----KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 779 NQNFTDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTGEKLYEIKILEETHKQEISRLQK 858
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622932398 859 RLQWYAENQELLDKdalrLREANEEIEKLRLEIEKLKAE 897
Cdd:TIGR04523 498 LKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
698-890 |
4.49e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 698 GEKLKQIQKEIQEQETllQGYQQENERLYNQVKDLqeqNKKNEERMFKENQSLFSEVAS----------LKEQMHKSRFL 767
Cdd:pfam02029 156 GEEEEDKSEEAEEVPT--ENFAKEEVKDEKIKKEK---KVKYESKVFLDQKRGHPEVKSqngeeevtklKVTTKRRQGGL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 768 SQVVEDSEPTRNQNFTDL-LAELRMAQKEKDSllEDIKRLKQDKQALEVDLEKMKKERDQAKdqiayvtgeklyeiKILE 846
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQkLEELRRRRQEKES--EEFEKLRQKQQEAELELEELKKKREERR--------------KLLE 294
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622932398 847 ETHkqeisrlQKRLQWYAENQELLDKDALRLReanEEIEKLRLE 890
Cdd:pfam02029 295 EEE-------QRRKQEEAERKLREEEEKRRMK---EEIERRRAE 328
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
784-925 |
5.91e-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: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 784 DLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIA------YVTGEKLYEIKILEETH-------- 849
Cdd:COG3883 41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralYRSGGSVSYLDVLLGSEsfsdfldr 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 850 ----KQEISRLQKRLQWYAENQELLDKDALRLREANEEIEKLRLEIEKLKAESGNPSIQQKIRLKDKAADAKKIQDLERQ 925
Cdd:COG3883 121 lsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
615-897 |
6.32e-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: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 615 KRVQEAEEKWRGAQALIEQIKATFSEKEKELENKLEelkkqqekELFKLNQDNYILQAKLSSFEETnkktrwlhFGEAAD 694
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS--------ELKELEARIEELEEDLHKLEEA--------LNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 695 PVTGEKLKQIQKEIQEQETLLQgyqqenerlyNQVKDLQEQNKKNEERMFKEnQSLFSEVASLKEQMhksrflsqvvEDS 774
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVS----------RIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQR----------IDL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932398 775 EPTRNqnftDLLAELRMAQKEKDSLLEDIKRLKQDKQALEVDLEKMKKERDQAKDQIAYVTgEKLYEIKILEETHKQEIS 854
Cdd:TIGR02169 846 KEQIK----SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE-RKIEELEAQIEKKRKRLS 920
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622932398 855 RLQKRLQWYAENQELLDKDALRLREANEE---IEKLRLEIEKLKAE 897
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEE 966
|
|
| |
