|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
90-402 |
7.83e-147 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 421.64 E-value: 7.83e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 90 EESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIFEAQIAGLRGQLEALQVDGGRLEAELRSM 169
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 170 QDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLNETELTELQSQISDTSVVLSM 249
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 250 DNSRSLDLDGIIAEVKAQYEEMAKCSRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQR 329
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119578644 330 AKLEAAIAEAEERGELALKDARAKQEELEAALQRAKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEESR 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
18-87 |
7.95e-14 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 68.91 E-value: 7.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119578644 18 SGRGAQVRLSSARPGGLGSSSLYGLGASRPRVAVRSAYGGPVGA--GIREVTINQSLLAPLRLDADPSLQRV 87
Cdd:pfam16208 85 GGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPpgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-407 |
3.57e-10 |
|
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: 62.38 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 87 VRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIfEAQIAGLRGQLEALQVDGGRLEAEL 166
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 167 RSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDvdaaymsKVELEAKVDALNDEINflrtLNETELTELQSQISDTSVV 246
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 247 LsmdnsrsldldgiiaevkAQYEEMAKCSRAEAEAWyQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIK 326
Cdd:TIGR02168 819 A------------------ANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 327 NQRAKLeaaiaeaeergELALKDARAKQEELEAALQRAKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEESRLAGD 406
Cdd:TIGR02168 880 NERASL-----------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
.
gi 119578644 407 G 407
Cdd:TIGR02168 949 Y 949
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-384 |
1.04e-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: 57.76 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 84 LQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIF------EAQIAGLRGQLEALQV 157
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 158 DGGRLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLrtlnETELTELQ 237
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 238 SQisdtsvvlsmdnsrsldLDGIIAEVKAQYEEMAKCSRAEAEAwyQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQR 317
Cdd:TIGR02168 873 SE-----------------LEALLNERASLEEALALLRSELEEL--SEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119578644 318 LQAEIDNIKNQRAkleaaiaeaeERGELALKDARAKQEELEAALQRAKQDMARQLREYQELMSVKLA 384
Cdd:TIGR02168 934 LEVRIDNLQERLS----------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-410 |
1.87e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 122 KWTLLQEQKSAKSSRLpDIFEAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDV 201
Cdd:COG1196 233 KLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 202 DAAYMSKVELEAKVDALNDEINflrtLNETELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEmakcSRAEAEA 281
Cdd:COG1196 312 RELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----AEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 282 WYQTKFETLQAQAGKHgDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAAL 361
Cdd:COG1196 384 LAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 119578644 362 QRAKQDmARQLREYQELMSVKLALDIEIATYRKLLEGEESRLAGDGVGA 410
Cdd:COG1196 463 ELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-403 |
1.14e-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: 51.21 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 110 RFLEQQNKLLETKWTLLQEQKSAKSSRLpDIFEAQIAGLRGQLEALQVDGGRLEAELrsmqDVVEDFKNKYEDEINRRTA 189
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELEEKL----EELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 190 AENEFVVLKKDVDaayMSKVELEAKVDALNDEINFLrtlnETELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYE 269
Cdd:TIGR02168 289 ELYALANEISRLE---QQKQILRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 270 EMAKCSRAEAEAW--YQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERG-ELA 346
Cdd:TIGR02168 362 ELEAELEELESRLeeLEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 119578644 347 LKDARAKQEELEAALQRAKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEESRL 403
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
83-379 |
7.89e-06 |
|
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: 48.35 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 83 SLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDiFEAQIAGLRGQLEALQVDGGRL 162
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA-HEARIRELEEDIKTLTQRVLER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 163 EAELRSMQDVVEDFKN-KYEDEINRRT------AAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTL------N 229
Cdd:pfam07888 149 ETELERMKERAKKAGAqRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 230 ETELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEE-MAKCSRAEAEA--------------------WYQTKfE 288
Cdd:pfam07888 229 EAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRtQAELHQARLQAaqltlqladaslalregrarWAQER-E 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 289 TLQAQAGKHGDdlrntrnEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAALQRAKQDM 368
Cdd:pfam07888 308 TLQQSAEADKD-------RIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
330
....*....|.
gi 119578644 369 ARQLREYQELM 379
Cdd:pfam07888 381 EQLQAEKQELL 391
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-404 |
2.26e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 253 RSLDLDGIIAEVKAQYEEMAKCSRAEAEAwyQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119578644 333 EAAIAEAEERGELALKDARAKQEELEAALQR---AKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEESRLA 404
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
83-332 |
4.17e-05 |
|
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: 46.17 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 83 SLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIfEAQIAGLRGQLEALQVDGGRL 162
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 163 EAELRSMQDVVEDFKNK---YEDEINR-RTAAEN---EFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLN---ETE 232
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIeklESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 233 LTELQSQISD-TSVVLSMD-NSRSLDLDGIIAEVKAQYEEMA------KCSRAEAE---AWYQTKFETLQAQAGKHGDDL 301
Cdd:TIGR04523 533 KKEKESKISDlEDELNKDDfELKKENLEKEIDEKNKEIEELKqtqkslKKKQEEKQeliDQKEKEKKDLIKEIEEKEKKI 612
|
250 260 270
....*....|....*....|....*....|.
gi 119578644 302 RNTRNEISEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
83-395 |
9.07e-05 |
|
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: 45.01 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 83 SLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKwtlLQEQKsaKSSRLPDIfeaqiaglrgQLEALQVDGGRL 162
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE--KLNQQKDE----------QIKKLQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 163 EAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKdvdaaymSKVELEAKVDALNDEINflrtLNETELTELQSQISD 242
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-------TRESLETQLKVLSRSIN----KIKQNLEQKQKELKS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 243 TSVVLSMDNSRSLDLDGIIAEVKAQYEEMakcsraeaeawyQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQR--LQA 320
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSL------------KEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEK 561
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119578644 321 EIDNIKNQRAKLEAAIAeaeergelALKDARAKQEELEAALQRAKQDMARQLREYQELMSvKLALDIEIAT--YRKL 395
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQK--------SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-SLEKELEKAKkeNEKL 629
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
125-364 |
1.39e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 125 LLQE---QKSAKSSRLPDIfEAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDV 201
Cdd:pfam01576 476 LLQEetrQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 202 DAAYMSKVELEAKVDALndeinflrtlnETELTELQSQISDTSVVLsmDNSRSL---------DLDGIIAEVK---AQYE 269
Cdd:pfam01576 555 EALTQQLEEKAAAYDKL-----------EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 270 EmaKCSRAEAEAW-YQTKFETLqaqaGKHGDDLRNTRNEISEMNRAiqrLQAEIDNI---KNQRAKLEAAIAEAEERGEL 345
Cdd:pfam01576 622 E--ERDRAEAEAReKETRALSL----ARALEEALEAKEELERTNKQ---LRAEMEDLvssKDDVGKNVHELERSKRALEQ 692
|
250
....*....|....*....
gi 119578644 346 ALKDARAKQEELEAALQRA 364
Cdd:pfam01576 693 QVEEMKTQLEELEDELQAT 711
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
109-332 |
1.50e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 109 VRFLEQQNKLLETKWTLLQEQKSAKSSRLpDIFEAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINRRT 188
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRELNQQIQTLDMKI-DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 189 AAENEFVVLKKDVDAAY----MSKVELEAKVDALNDEINFLRTlNETELTELQsQISDTSVVLSMDNSRSLDLDGIIAEV 264
Cdd:PHA02562 241 DELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQ-QISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119578644 265 KAQYEEMAKCSRAEAEAwyQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQ--SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-403 |
3.48e-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: 43.13 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 141 FEAQIAGLRGQLEALQVDGGRLEA---ELRSMQDVVEDFKNKYE--DEINRRTAaENEFVVLKKDVDAAYMSKVELEAKV 215
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLiidEKRQQLERLRREREKAEryQALLKEKR-EYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 216 DALndeinflrtlnETELTELQSQISDTsvvlsmdNSRSLDLDGIIAEVKAQYEEMAKcsraEAEAWYQTKFETLQAQAG 295
Cdd:TIGR02169 247 ASL-----------EEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 296 KHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAALQRAKQDMARQLREY 375
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270
....*....|....*....|....*....|
gi 119578644 376 QELMSVKLALDieiATYRKL--LEGEESRL 403
Cdd:TIGR02169 385 DELKDYREKLE---KLKREIneLKRELDRL 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-403 |
3.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 230 ETELTELQSQISDtsvvlsmdnsrsldLDGIIAEVKAQYEEMAK----CSRAEAEAWYQTKFETLQAQAGKHGD---DLR 302
Cdd:COG4913 616 EAELAELEEELAE--------------AEERLEALEAELDALQErreaLQRLAEYSWDEIDVASAEREIAELEAeleRLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 303 NTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAeergELALKDARAKQEELEAALQRAKQDMARQLREYQELM--- 379
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL----EKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaa 757
|
170 180 190
....*....|....*....|....*....|..
gi 119578644 380 --------SVKLALDIEIATYRKLLEGEESRL 403
Cdd:COG4913 758 algdaverELRENLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-374 |
1.01e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 151 QLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTlne 230
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 231 tELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQ-------YEEMAKCSRAEAEAwYQTKFETLQAQAgkhgDDLRN 303
Cdd:COG4942 98 -ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrlqyLKYLAPARREQAEE-LRADLAELAALR----AELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119578644 304 TRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAALQRAKQDMARQLRE 374
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
93-329 |
1.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 93 EQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLpDIFEAQIAGLRGQLEALQVDGGRLEAELRSMQDV 172
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL-NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 173 VEDFKnKYEDEINRrtaAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLNETELTELQSQISDtsvvLSMDNS 252
Cdd:TIGR04523 210 IQKNK-SLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119578644 253 RSLDLDGIIAEVKAQYEEMAKcsrAEAEAWYQTKFETLQAQAgkhgDDLRNTRNEISEMNRAIQRLQAEIDNIKNQR 329
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNN---QKEQDWNKELKSELKNQE----KKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
68-332 |
1.91e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 68 INQSLLAPLRLDADPSLQRVRQEESEqiktLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIFEAQIAG 147
Cdd:PRK04863 823 IGSHLAVAFEADPEAELRQLNRRRVE----LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 148 LRGQLEALQVD-------GGRLE------AELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKkDVDA-----AYMSKV 209
Cdd:PRK04863 899 IREQLDEAEEAkrfvqqhGNALAqlepivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQrrahfSYEDAA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 210 ELEAKVDALNDEIN-------FLRTLNETELTELQSQISDTSVVL-SMDNSRSLDLDgIIAEVKAQYEEMAKCSRAEAEA 281
Cdd:PRK04863 978 EMLAKNSDLNEKLRqrleqaeQERTRAREQLRQAQAQLAQYNQVLaSLKSSYDAKRQ-MLQELKQELQDLGVPADSGAEE 1056
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 119578644 282 WYQTKFETLQAQagkhgddLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:PRK04863 1057 RARARRDELHAR-------LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL 1100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
77-242 |
2.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 77 RLDADPS-LQRVRQeeseQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIFEAQIAGLRGQLEAl 155
Cdd:COG4913 679 RLDASSDdLAALEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 156 qvdggRLEAEL--RSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAY-MSKVELEAKVDALNDEINFLRTLNETE 232
Cdd:COG4913 754 -----RFAAALgdAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWpAETADLDADLESLPEYLALLDRLEEDG 828
|
170
....*....|
gi 119578644 233 LTELQSQISD 242
Cdd:COG4913 829 LPEYEERFKE 838
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
71-347 |
2.57e-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: 40.13 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 71 SLLAPLRLDADPSLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLEtkwtllqeQKSAKSSRLPDIFEAQIAGLRG 150
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE--------RRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 151 QLEALQVDGGRLEAELRSMQDVVEDFKNKYEdEINRRTAAenEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLNE 230
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALY-RLGRQPPL--ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 231 tELTELQSQIsdtsvvlsmdNSRSLDLDGIIAEVKAQYEEMAKcsraeAEAWYQTKFETLQAQAGKHGDDLRNTRNEISE 310
Cdd:COG4942 161 -ELAALRAEL----------EAERAELEALLAELEEERAALEA-----LKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 119578644 311 MNRAIQRLQAEIDniknQRAKLEAAIAEAEERGELAL 347
Cdd:COG4942 225 LEALIARLEAEAA----AAAERTPAAGFAALKGKLPW 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
300-376 |
3.31e-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: 39.75 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 300 DLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEER----------GELALKDARAKQEELEAALQRAKQDMA 369
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleqelaaLEAELAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 119578644 370 RQLREYQ 376
Cdd:COG4942 108 ELLRALY 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-378 |
4.50e-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: 39.67 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 142 EAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDE 221
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 222 InflrTLNETELTELQSQISDTSVVLSM------DNSRSLD---LDGIIAEVKAQYEEMAKCSRAEAEAWYQTKFETLQA 292
Cdd:TIGR02169 753 I----ENVKSELKELEARIEELEEDLHKleealnDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 293 QAGKhgDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLeaaiAEAEERGELALKDARAKQEELEAALQRAKQDMARQL 372
Cdd:TIGR02169 829 EYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL----EEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
....*.
gi 119578644 373 REYQEL 378
Cdd:TIGR02169 903 RKIEEL 908
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
151-380 |
6.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 151 QLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAymskvELEAKVDALNDEINFLRTLNe 230
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASS- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 231 TELTELQSQIsdtsvvlsmdnsrsldldgiiAEVKAQYEEMAKcsraeaeawyqtKFETLQAQAGKHgddlrntRNEISE 310
Cdd:COG4913 685 DDLAALEEQL---------------------EELEAELEELEE------------ELDELKGEIGRL-------EKELEQ 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 311 MNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAALQRAKQDMARQLREYQELMS 380
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-404 |
7.46e-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: 38.90 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 161 RLEAELRSMQDVVEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINflrTLNEtELTELQSQI 240
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE---KLKE-RLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 241 SDTSVVLSMDNSRSLDLDGIIAEVKAQYEEmakcsraeaeawYQTKFETLQAQAGKHGddlrntrneisemnraIQRLQA 320
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHK------------LEEALNDLEARLSHSR----------------IPEIQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 321 EIDNIKNQRAKLeaaiaeaeergelalkdaRAKQEELEAALQRAKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEE 400
Cdd:TIGR02169 799 ELSKLEEEVSRI------------------EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
|
....
gi 119578644 401 SRLA 404
Cdd:TIGR02169 861 GKKE 864
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
230-374 |
8.98e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.02 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 230 ETELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEmAKCSRAEAEAWY---QTKFETLQAQAGKHGDDLRNTRN 306
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119578644 307 EISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAALQRAKQDMAR-------QLRE 374
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNRyrseffgRLRE 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
79-383 |
9.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 79 DADPSLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKW----TLLQEQKSAKSSRLPDI--FEAQIAGLRGQL 152
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAaeleSELEEAREAVEDRREEIeeLEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 153 EALQVDGGRLEAELRSMQDVVEDFKNKY-EDEINRRTAAEN-----------------EFVVLKKDVDAA--YMSKVE-- 210
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREaELEATLRTARERveeaealleagkcpecgQPVEGSPHVETIeeDRERVEel 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 211 ------LEAKVDALNDEINFLRTLNETEltelqSQISdtsvvlSMDNSRSlDLDGIIAEVKAQYEE---MAKCSRAEAEA 281
Cdd:PRK02224 481 eaeledLEEEVEEVEERLERAEDLVEAE-----DRIE------RLEERRE-DLEELIAERRETIEEkreRAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119578644 282 wYQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELA--------------- 346
Cdd:PRK02224 549 -LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRekrealaelnderre 627
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 119578644 347 -LKDARAKQEELEAALQRAKQDMARQLR----EYQELMSVKL 383
Cdd:PRK02224 628 rLAEKRERKRELEAEFDEARIEEAREDKeraeEYLEQVEEKL 669
|
|
| |
