|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
185-497 |
7.10e-128 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 379.65 E-value: 7.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 185 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 264
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 265 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 344
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 345 DNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESLYQSKYEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQI 424
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845061 425 ANLQQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 497
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
68-181 |
1.97e-11 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 62.37 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 68 LVNLGGSKSISISVARggGRSGFGGGYGGGGFGGGGFGGGGFGGGGFGGGGIGGGGFGGFGSGGGGFGGGGFGGGGYGGG 147
Cdd:pfam16208 45 LYNLGGSKSISISVAG--GGSRPGSGFGFGGGGGGGFGGGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGRGGF 122
|
90 100 110
....*....|....*....|....*....|....
gi 1622845061 148 YGPVCPPGGIQEVTINQSLLQPLNVEIDPEIQKV 181
Cdd:pfam16208 123 GGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-497 |
1.07e-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: 58.53 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 246 RVDQLKSDQSRLDSELKNMQDMVEDYrnkyEDEINKrtnAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLT---A 322
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEL----TAELQE---LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 323 LYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESLyQSKYEELQitagrhgdsvkNSKIE 402
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELEAELE-----------ELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 403 ISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRgesalkdaknkLNDLEDALQQAKEDLARLLRDYQElmNTKLALDL 482
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-----------LERLEDRRERLQQEIEELLKKLEE--AELKELQA 440
|
250
....*....|....*
gi 1622845061 483 EIATYRTLLEGEESR 497
Cdd:TIGR02168 441 ELEELEEELEELQEE 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
240-492 |
1.11e-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: 58.53 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 240 INNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIdf 319
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL-- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 320 ltALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQyeeiAQKSKAEAESLyQSKYEELQITAGRHGDSVKNS 399
Cdd:TIGR02168 757 --TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----LKALREALDEL-RAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 400 KIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESALKdaknKLNDLEDALQQAKEDLARLLRDYQELMNTKLA 479
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLRSELEELSEELRE 905
|
250
....*....|...
gi 1622845061 480 LDLEIATYRTLLE 492
Cdd:TIGR02168 906 LESKRSELRRELE 918
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-473 |
1.46e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 184 REREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQvDTSTRTHNLEpYFESFINNLRRRVDQLKSDQSRLDSELKN 263
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 264 MQDMVEDYRNK---YEDEINKRTNAENEfvtIKKDvdsaymtkvDLQAKLDNLQQEIDFLtalyQAELSQMQTQISETNV 340
Cdd:TIGR02169 756 VKSELKELEARieeLEEDLHKLEEALND---LEAR---------LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 341 ILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESLyqskyEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNV 420
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622845061 421 KKQIANLQQSISDAeqrgESALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 473
Cdd:TIGR02169 895 EAQLRELERKIEEL----EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
242-497 |
2.64e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 242 NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKyedeinkRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLT 321
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 322 ALY---QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEI---AQKSKAEAESLyQSKYEELQITAGRHGDS 395
Cdd:TIGR02168 747 ERIaqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeeLKALREALDEL-RAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 396 VKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLND----------LEDALQQAKEDLAR 465
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleealalLRSELEELSEELRE 905
|
250 260 270
....*....|....*....|....*....|..
gi 1622845061 466 LLRDYQELMNTKLALDLEIATYRTLLEGEESR 497
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-476 |
1.71e-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: 54.69 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 173 EIDPEIQKVKsREREQIKSLNNQFASFIDKVRfleQQNQVLQT-KWELLQQVDTSTRTHNLEPYFESF-INNLRRRVDQL 250
Cdd:TIGR02169 167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR---QQLERLRReREKAERYQALLKEKREYEGYELLKeKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 251 KSDQSRLDSELKNMQDMVEDYRNKYE------DEINKRTNA--ENEFVTIKKDVDSaymtkvdLQAKLDNLQQEIDFlta 322
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGE-------LEAEIASLERSIAE--- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 323 lYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEV---KAQYEEIAQKSKAEAESLyQSKYEELQITAGRHGDSVKNS 399
Cdd:TIGR02169 313 -KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELKEELEDL-RAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 400 KIEISELNRVIQRLRSEIDNVKK-------QIANLQQSISDAEQRG---ESALKDAKNKLNDLEDALQQAKEDLARLLRD 469
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEelqrlseELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
....*..
gi 1622845061 470 YQELMNT 476
Cdd:TIGR02169 471 LYDLKEE 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-473 |
1.74e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 183 SREREqIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQV---------DTSTRTHNLEPYFESF---INNLRRRVDQL 250
Cdd:TIGR02168 674 ERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleELSRQISALRKDLARLeaeVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 251 KSDQSRLDSELKNMQDMVEDYRNKY---EDEINKR----TNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLT-- 321
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELaeaEAEIEELeaqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErr 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 322 -ALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEI--AQKSKAEAESLYQSKYEELQITAGRHGDSVKN 398
Cdd:TIGR02168 833 iAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845061 399 SKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDaeqRGESALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 473
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-492 |
3.65e-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: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 245 RRVDQLKSDQSRLDSELKNMQDmvEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDfltaLY 324
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----EA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 325 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESL---------YQSKYEELQITAGRHGDS 395
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeeleeeleeAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 396 VKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMN 475
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250
....*....|....*..
gi 1622845061 476 TKLALDLEIATYRTLLE 492
Cdd:COG1196 447 AAEEEAELEEEEEALLE 463
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
237-492 |
6.85e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 237 ESFIN-NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQ 315
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 316 EIDFLtalyQAELSQMQTQISETNVILSMDNNrsldlDSIIAEVKAQYEEIAQKsKAEAESLYQSKYEElqitagrhgds 395
Cdd:COG3206 234 ELAEA----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAE-LAELSARYTPNHPD----------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 396 vknskieiselnrvIQRLRSEIDNVKKQIANLQQSISDAEqrgESALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmn 475
Cdd:COG3206 293 --------------VIALRAQIAALRAQLQQEAQRILASL---EAELEALQAREASLQAQLAQLEARLAELPELEAEL-- 353
|
250
....*....|....*....
gi 1622845061 476 TKLALDLEIA--TYRTLLE 492
Cdd:COG3206 354 RRLEREVEVAreLYESLLQ 372
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
237-465 |
1.37e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 237 ESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrtnAENEFVTIKKDVDSaymtkvdLQAKLDNLQQE 316
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDK-------LQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 317 IDFLTALYQAELSQMQTQ---ISETNVILSMDN-----NRSLDLDSIIAEVKAQYEEI--AQKSKAEAESLYQSKYEELQ 386
Cdd:COG3883 81 IEERREELGERARALYRSggsVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845061 387 ITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLAR 465
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
325-465 |
4.78e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 325 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEiAQKSKAEAESLYQSKYEELQITAGRHGD---SVKNSKI 401
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845061 402 EISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGesalKDAKNKLND----LEDALQQAKEDLAR 465
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-429 |
5.63e-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: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 158 QEVTINQSLLQPLNVEIDpEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQ--VDTSTRTHNLEPY 235
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIE-ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESklDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 236 FESfinnLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQ 315
Cdd:TIGR02168 346 LEE----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 316 EI-DFLTALYQAELSQMQTQISETNVILsmdnnrsLDLDSIIAEVKAQYEEIaQKSKAEAESLYQSKYEELQITAGRhgd 394
Cdd:TIGR02168 422 EIeELLKKLEEAELKELQAELEELEEEL-------EELQEELERLEEALEEL-REELEEAEQALDAAERELAQLQAR--- 490
|
250 260 270
....*....|....*....|....*....|....*
gi 1622845061 395 svknskieISELNRVIQRLRSEIDNVKKQIANLQQ 429
Cdd:TIGR02168 491 --------LDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
305-497 |
9.39e-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: 48.90 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 305 DLQAKLDNLQQeidfltALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIaQKSKAEAESLYQSKYEE 384
Cdd:TIGR02168 217 ELKAELRELEL------ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 385 LQitagrhgdsvkNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSIsdaeQRGESALKDAKNKLNDLEDALQQAKEDLA 464
Cdd:TIGR02168 290 LY-----------ALANEISRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190
....*....|....*....|....*....|...
gi 1622845061 465 RLLRDYQELMNTKLALDLEIATYRTLLEGEESR 497
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
201-469 |
9.76e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 201 DKVRFLEQQNQVLQTKWELL-QQVDTSTRthnlepyfesFINNLRRRVDQLKSD-QSRLDSELKNMQDmvedyrnkYEDE 278
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTYNK----------NIEEQRKKNGENIARkQNKYDELVEEAKT--------IKAE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 279 INKRTNAENEFVTIKKDVDSAY----MTKVDLQAKLDNLQQEIDFLTAlyQAELSQMQTQISETNVILsmdnnrsldlds 354
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRI------------ 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 355 iiaevkaqyEEIAQKSKAeaeslYQSKYEELQItagrHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDA 434
Cdd:PHA02562 302 ---------TKIKDKLKE-----LQHSLEKLDT----AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV 363
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622845061 435 E---QRGESALKDAKNKLNDLEDALQQAKEDLARLLRD 469
Cdd:PHA02562 364 KaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-465 |
1.29e-05 |
|
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: 47.84 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 248 DQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLtalyQAE 327
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL----RAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 328 LSQMQTQISETNVILSMDNNRS-----LDLDSIIAEVKAQ--YEEIAQKSKAEAESLyQSKYEELQITAGRHGDSVKNSK 400
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPplallLSPEDFLDAVRRLqyLKYLAPARREQAEEL-RADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845061 401 IEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRgESALKDAKNKLNDLEDALQQAKEDLAR 465
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAE-LAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
170-492 |
4.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 170 LNVEIDpEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVdtSTRTHNLEPYFESfINNLRRRVDQ 249
Cdd:PRK03918 174 IKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL--EKEVKELEELKEE-IEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 250 LKSDQSRLDSELKNmqdmVEDYRNKYEDEINKRTNAENEFVTIKKDVDsAYMTKVDLQAKLDNLQQEIDFLTALYQAELS 329
Cdd:PRK03918 250 LEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 330 QMQTQISEtnviLSMDNNRSLDLDSIIAEVKAQYEEIaqKSKAEAESLYQSKYEELQ-ITAGRHGDSVKNSKIEISELNR 408
Cdd:PRK03918 325 GIEERIKE----LEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 409 VIQRLRSEIDNVKKQIANLQQSISDAEQRGEsALKDAKNK-----------------------LNDLEDALQQAKEDLAR 465
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIE-ELKKAKGKcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERK 477
|
330 340
....*....|....*....|....*..
gi 1622845061 466 LLRDYQELmNTKLALDLEIATYRTLLE 492
Cdd:PRK03918 478 LRKELREL-EKVLKKESELIKLKELAE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
402-476 |
9.23e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 9.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845061 402 EISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQR---GESALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNT 476
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
177-459 |
1.15e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 177 EIQKVKSREREQIKSLNNQFAsfiDKVRFLEQQNQVLQTKWELLQqVDTSTRthnlepyfESFINNLRRRVDQLKSDQSR 256
Cdd:pfam10174 447 EKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQ-PELTEK--------ESSLIDLKEHASSLASSGLK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 257 LDSELKNMQDMVEDYR---NKYEDEINKRTNAEnefvtikkdvdSAYMTKVDLQAKLDNLQQEIdfltALYQAELSQMQT 333
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKeecSKLENQLKKAHNAE-----------EAVRTNPEINDRIRLLEQEV----ARYKEESGKAQA 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 334 QISETNVILSMDNNRSLDLDSIIAE--------VKAQYEEIAQKSKAEAESlyQSKYEELQITAGRHGDSVKN--SKIEI 403
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDKKIAElesltlrqMKEQNKKVANIKHGQQEM--KKKGAQLLEEARRREDNLADnsQQLQL 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845061 404 SELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLNDLEDALQQA 459
Cdd:pfam10174 658 EELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEA 713
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
173-495 |
1.35e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 173 EIDPEIQKVKSRE-REQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQ----------QVDTSTRTHNLEPYFESfIN 241
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgtTLGEEKSNHIINHYNEK-KS 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 242 NLRRRVDQLKSDQSRLDSELKNMQDMvEDYRNKyeDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLT 321
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKR-KEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 322 ALYQAELSQMQTQISETNVILS---MDNNRSL---------DLDSIIAEVKAQYEEIaqksKAEAESLYQSKYEELqita 389
Cdd:PRK01156 557 SLKLEDLDSKRTSWLNALAVISlidIETNRSRsneikkqlnDLESRLQEIEIGFPDD----KSYIDKSIREIENEA---- 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 390 grhgDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLqQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLARLLRD 469
Cdd:PRK01156 629 ----NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
330 340
....*....|....*....|....*.
gi 1622845061 470 YQELMNTKLALDLEIATYRTLLEGEE 495
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLESMK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
367-471 |
2.04e-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: 43.98 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 367 AQKSKAEAEslyQSKYEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRgesaLKDAK 446
Cdd:COG4942 17 AQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELE 89
|
90 100
....*....|....*....|....*
gi 1622845061 447 NKLNDLEDALQQAKEDLARLLRDYQ 471
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALY 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-497 |
2.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 352 LDSIIAEVKAQYEEIA-QKSKAEAESLYQSKYEELQITAGRHGDSVKNSKI-----EISELNRVIQRLRSEIDNVKKQIA 425
Cdd:COG1196 191 LEDILGELERQLEPLErQAEKAERYRELKEELKELEAELLLLKLRELEAELeeleaELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 426 NLQQSISDAEQRGESALKD----------AKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEE 495
Cdd:COG1196 271 ELRLELEELELELEEAQAEeyellaelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
..
gi 1622845061 496 SR 497
Cdd:COG1196 351 EE 352
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
305-476 |
2.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 305 DLQAKLDNLQQEIDFLTALY---QAELSQMQTQISETNVILSMDNNRsLDLDSI---IAEVKAQYEEIaQKSKAEAESLy 378
Cdd:COG4913 614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERL-DASSDDLAAL- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 379 QSKYEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSIS-----DAEQRGESALKDA--KNKLND 451
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAveRELREN 770
|
170 180
....*....|....*....|....*
gi 1622845061 452 LEDALQQAKEDLARLLRDYQELMNT 476
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
237-492 |
3.66e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 237 ESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQE 316
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 317 IDFLTALYQ------AELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESLYQSKYEelqitag 390
Cdd:TIGR04523 203 LSNLKKKIQknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 391 rhgdsVKNSKIEISELNRVIQRLRSEIDNVKKQ-IANLQQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLARLLRD 469
Cdd:TIGR04523 276 -----LEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260
....*....|....*....|...
gi 1622845061 470 YQELMNTKLALDLEIATYRTLLE 492
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIE 373
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
305-497 |
3.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 305 DLQAKLDNLQQEIDFLT-ALYQAELSQMQTQISETNvilsmdnNRSLDLDSIIAEVKAQYEEIAQKSKAEAESLYQSKYE 383
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELE-------AELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 384 ELQITAgrhgdsvknskiEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESA----------LKDAKNKLNDLE 453
Cdd:COG1196 290 EYELLA------------ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeleeleeeLEEAEEELEEAE 357
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622845061 454 DALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 497
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
206-485 |
4.69e-04 |
|
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: 43.57 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 206 LEQQNQVLQTKWELLQQVDTstrthnLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKyeDEINKRTNA 285
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSS------LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 286 EnefvtIKKdvdsaYMTKVDLQ-AKLDNLQQEIDFLTALyQAELSQMQTQISETnvilsmdnnrsldlDSIIAEVKAQYE 364
Cdd:pfam15921 518 E-----ITK-----LRSRVDLKlQELQHLKNEGDHLRNV-QTECEALKLQMAEK--------------DKVIEILRQQIE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 365 EIAQKSKAEAESLYQSKYEELQITagrhgDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQ--------------QS 430
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlRA 647
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845061 431 ISDAEQRGESALKDAKNKLNDLeDALQQAKEDLARLLRDYQELMNT---KLALDLEIA 485
Cdd:pfam15921 648 VKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKRNFRNKSEEMETttnKLKMQLKSA 704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-451 |
6.18e-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: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 158 QEVTINQSLLQPLNVEIDPEIQKVKSRErEQIKSLNNQFASFIDkvRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFE 237
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 238 SFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDsaymtkvDLQAKLDNLQQEI 317
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-------ELSEELRELESKR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 318 DFLTALYQA---ELSQMQTQISETNVilsmdnnrslDLDSIIAEVKAQYE---EIAQKSKAEAESLYQSKYEELqitagr 391
Cdd:TIGR02168 911 SELRRELEElreKLAQLELRLEGLEV----------RIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRL------ 974
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845061 392 hgDSVKNSKIEISELN--------RVIQR---LRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLND 451
Cdd:TIGR02168 975 --KRLENKIKELGPVNlaaieeyeELKERydfLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNE 1043
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
394-485 |
6.24e-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: 42.44 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 394 DSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRgesaLKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 473
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90
....*....|..
gi 1622845061 474 MNTKLALDLEIA 485
Cdd:COG4942 96 RAELEAQKEELA 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
297-474 |
6.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 297 DSAYMTKVDLQAKLDNLQQEIDFLTAlyQAELSQMQTQISEtnvILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAES 376
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA---LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 377 LYQSKYEELQITAGRHGDSVKNskiEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGEsalkdaknkLNDLEDAL 456
Cdd:COG4717 411 LEELLGELEELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQEL 478
|
170
....*....|....*...
gi 1622845061 457 QQAKEDLARLLRDYQELM 474
Cdd:COG4717 479 EELKAELRELAEEWAALK 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
240-473 |
9.67e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 240 INNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSA--YMTKV--DLQAK---LDN 312
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTkeMLRKVveELTAKkmtLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 313 LQQEIDFLTALYQ----------AELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAeAESLYQsKY 382
Cdd:pfam15921 494 SERTVSDLTASLQekeraieatnAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV-IEILRQ-QI 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 383 EELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVK-------KQIANLQQSISDAE----------QRGESALKDA 445
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLElekvklvnagSERLRAVKDI 651
|
250 260
....*....|....*....|....*...
gi 1622845061 446 KNKLNDLEDALQQAKEDLARLLRDYQEL 473
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSLSEDYEVL 679
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
293-498 |
1.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 293 KKDVDSAYMTKVDLQAKLDNLQQEIDFLtalyQAELSQMQTQISETNVILSMDNNRSLDLDSIiaevkAQYEEiAQKSKA 372
Cdd:COG4913 595 RRRIRSRYVLGFDNRAKLAALEAELAEL----EEELAEAEERLEALEAELDALQERREALQRL-----AEYSW-DEIDVA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 373 EAESLYQSKYEELqitagrhgDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLNDL 452
Cdd:COG4913 665 SAEREIAELEAEL--------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622845061 453 EDALQQAKEDL-ARLLRDYQELMNTKL------ALDLEIATYRTLLEGEESRM 498
Cdd:COG4913 737 EAAEDLARLELrALLEERFAAALGDAVerelreNLEERIDALRARLNRAEEEL 789
|
|
| Keratin_2_tail |
pfam16210 |
Keratin type II cytoskeletal 1 tail; |
498-525 |
1.77e-03 |
|
Keratin type II cytoskeletal 1 tail;
Pssm-ID: 406591 [Multi-domain] Cd Length: 135 Bit Score: 39.19 E-value: 1.77e-03
10 20
....*....|....*....|....*...
gi 1622845061 498 MSGECAPNVSLkitelplaAVSTSHTTI 525
Cdd:pfam16210 1 MSGECAPNVSV--------SVSTSHTSI 20
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-498 |
1.94e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 348 RSLDLDSIIAEvKAQYEEIAQKSKAEAESLyQSKYEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANL 427
Cdd:COG1196 230 LLLKLRELEAE-LEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845061 428 QQSISDAEQRgesaLKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESRM 498
Cdd:COG1196 308 EERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-497 |
1.99e-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: 40.29 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 351 DLDSIIAEVKAQYEEI-AQKSKAEAE-SLYQSKYEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVK--KQIAN 426
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845061 427 LQQSISDAEQR---GESALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmntKLALDLEIATYRTLLEGEESR 497
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
240-449 |
2.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 240 INNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEI-D 318
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 319 FLTALY-------------QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESL--YQSKYE 383
Cdd:COG4942 109 LLRALYrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLaeLEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845061 384 ELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGESA-LKDAKNKL 449
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgFAALKGKL 255
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
161-458 |
2.32e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 161 TINQSLLQPLNVEIDPEIQKVKSREREQIKSLNNQFASfidkvrfleQQNQVLQTKWELLQQVdTSTRTHNLEPYFESFI 240
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIEN---------KKNELLDIIVEIKKHI-HGEINKDLNKILEDFK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 241 NNLRRRVDQLkSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEfvtIKKDVDSAYMTKVDLQAKLDNLQQEIDfl 320
Cdd:TIGR01612 762 NKEKELSNKI-NDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIIN-- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 321 talyqaELSQMQTQI-SETNVILSMDNNRSLDLDSiiaeVKAQYEEIAQKSKAEAESLYQSKYEelqitagrhgDSVKNS 399
Cdd:TIGR01612 836 ------EMKFMKDDFlNKVDKFINFENNCKEKIDS----EHEQFAELTNKIKAEISDDKLNDYE----------KKFNDS 895
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845061 400 KIEISELNRVIQRLRSEIDNVKKqianLQQSISDAEQRGESaLKDAKNKLNDLEDALQQ 458
Cdd:TIGR01612 896 KSLINEINKSIEEEYQNINTLKK----VDEYIKICENTKES-IEKFHNKQNILKEILNK 949
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
242-476 |
2.85e-03 |
|
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: 40.98 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 242 NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVT-IKKDVDSAYMTKV--------DLQAKLDN 312
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeQKEQKREARTEKQaywqvvegALDAQLAL 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 313 LQQEIDFLTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAEslyqskYEELQitagRH 392
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLR------YFDWY----QE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 393 GDSVKNskieiselnrviQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLaRLLRDYQE 472
Cdd:pfam12128 804 TWLQRR------------PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENL-RGLRCEMS 870
|
....
gi 1622845061 473 LMNT 476
Cdd:pfam12128 871 KLAT 874
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-484 |
3.33e-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: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 187 EQIKSLNNQFASFIDKVRFLEQQNQVLQTKWEllqqvDTSTRTHNLEPY---FESFINNLRRRVDQLKSDQSRLDSELKN 263
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-----DLKKQKEELENElnlLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 264 MQDMVEDYRnKYEDEINkrtNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLTALYQ---AELSQMQTQISETNV 340
Cdd:TIGR04523 206 LKKKIQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNkikKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 341 ILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKAEAESLYQSKYEELQitagrhgDSVKNSKIEISELNRVIQRLRSEIDNV 420
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ-------NQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 421 ----------------------------KKQIANLQQSISDAEQRgesaLKDAKNKLNDLEDALQQAKEDLARLLRDYQE 472
Cdd:TIGR04523 355 esensekqreleekqneieklkkenqsyKQEIKNLESQINDLESK----IQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
330
....*....|..
gi 1622845061 473 LMNTKLALDLEI 484
Cdd:TIGR04523 431 LKETIIKNNSEI 442
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-487 |
3.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 260 ELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEIDFLTALyQAELSQMQTQISETN 339
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 340 VILSMDNNRSLDLDSIIAEVKAQYEEIAQKSKaEAESL--YQSKYEELqitagrhgdsvknsKIEISELNRVIQRLRSEI 417
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELkeKAEEYIKL--------------SEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 418 DNVKKQIANLQQSISDAEQRgESALKDAKNKLNDLEDALQQAKEDlARLLRDYQELMNTKLALDLEIATY 487
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGL 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
240-464 |
4.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 240 INNLRRRVDQLKSDQSRLDSE-------LKNMQDMVEDYRNKYEdeinkrtnaenEFVTIKKDVDSAYMTKVDLQAKLDN 312
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQreqaretRDEADEVLEEHEERRE-----------ELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 313 LQQEIDFLtalyQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEEI----------AQKSKAEAESL----- 377
Cdd:PRK02224 277 LAEEVRDL----RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrleecrvaAQAHNEEAESLredad 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 378 -YQSKYEELQITAGRHGDSVKNSKIEISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRGE---SALKDAKNKLNDLE 453
Cdd:PRK02224 353 dLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEelrEERDELREREAELE 432
|
250
....*....|.
gi 1622845061 454 DALQQAKEDLA 464
Cdd:PRK02224 433 ATLRTARERVE 443
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
177-473 |
5.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 177 EIQKVKSREREQIKSLNNQFASFIDKVRFLEQqnqvLQTKWELLQQvdtstRTHNLEPYFESFiNNLRRRVDQLKSDQSR 256
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEK-----RLEELEERHELY-EEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 257 LD----SELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDSAYMTKVDLQAKLDNLQQEID-----FLTALYQAE 327
Cdd:PRK03918 381 LTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkELLEEYTAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 328 LSQMQTQISETNVILSMDNNRSLDLDSIIAEVK--AQYEEIAQKSKAEAESLYQSKYEELQitagrhgdsvKNSKiEISE 405
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELE----------KKAE-EYEK 529
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845061 406 LNRVIQRLRSEIDNVKKQIanlqqsisdaeqrgeSALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 473
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKEL---------------EKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
402-498 |
6.10e-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: 38.75 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 402 EISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQrgesALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTK--LA 479
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90
....*....|....*....
gi 1622845061 480 LDLEIATYRTLLEGEESRM 498
Cdd:COG1579 94 LQKEIESLKRRISDLEDEI 112
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
410-474 |
8.93e-03 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 35.43 E-value: 8.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845061 410 IQRLRSEIDNVKKQIANLQQSISDAEQRGESALKDAKNKLNDLEDALQQAKEDLARLLRDYQELM 474
Cdd:pfam11839 3 VEELQSKADQAEQDAAAAQSAADSAKAKADEAAARANAAEAAAEEAQQAAEEANEKADRMFEKSM 67
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-492 |
9.67e-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: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845061 402 EISELNRVIQRLRSEIDNVKKQIANLQQSISDAEQRgesaLKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALD 481
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRK----IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90
....*....|.
gi 1622845061 482 LEIATYRTLLE 492
Cdd:TIGR02169 758 SELKELEARIE 768
|
|
| |
