|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
31-387 |
4.20e-100 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 306.46 E-value: 4.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 31 QEKVDLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREVSGIKELYETELADARRSLDDTARERARLQLELSKI 110
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 111 SVEHEDLRASFSKKESELESAqarfreteallnsknaalattqsenkslqgevedlkaeigqlESALALAKKQLEEEILI 190
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSA------------------------------------------ENDLVGLRKDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 191 KVDLENRCQSLIEELDFRKNVYEEEIKETRRRH--ETRLVEVDSGKQIEyehkLSQALADMREQHDSQVTLYKEELEHTY 268
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 269 QSKLENARLSSEMNSSAVNSTREELMESRYRIDSLTSQLSELQKESRAWHDRMQELEDMLAKEKDNSRKMLAEREREMAD 348
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 45361241 349 IRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEER 387
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
439-543 |
2.10e-23 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 95.18 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 439 TGDVSIEEVDVDG-----KYIRLKNNSEQDHPLGGWELTRTIGEAsvnFKFTSRYVLKAGQTVTIWAADAGVTAS----P 509
Cdd:pfam00932 4 TGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGGT---YTFPNGTTLAPGQTVVVWTGSGTNSATagywG 80
|
90 100 110
....*....|....*....|....*....|....
gi 45361241 510 PSDLIWKNQNSWatgedvkVILKNSQGEDVAQRT 543
Cdd:pfam00932 81 PSNAVWNNGGDA-------VALYDANGELVDSVG 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-370 |
7.96e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 63 QVTEREEVRSREVSGIK-ELYETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEAL 141
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 142 LNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELDFRKNVYEEEIKETRR 221
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 222 RHETRLVEVDS-----GKQIEYEHKLSQALADMREQHDSQVTLYKEELEHtyQSKLENARLSSEMNSSAVNSTREELMES 296
Cdd:COG1196 377 AEEELEELAEEllealRAAAELAAQLEELEEAEEALLERLERLEEELEEL--EEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45361241 297 RYRIDSLTSQLSELQKESRAWHDRMQELEDMLAKEKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVKLAL 370
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-316 |
1.06e-11 |
|
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: 68.16 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 22 LSPTRISRLQEKvdLQELNDRLAVYIDKVRSLESENSLLHVQVTEREeVRSREVsgikelyETELADARRSLDDTARERA 101
Cdd:TIGR02168 229 LLVLRLEELREE--LEELQEELKEAEEELEELTAELQELEEKLEELR-LEVSEL-------EEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 102 RLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAK 181
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 182 KQLEEEILIKVDLENRCQSLIEELdfrkNVYEEEIKETRRRHEtRLVEVDSGKQIEYEHKLSQALADMREQHDSQVTLYK 261
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEI----ERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45361241 262 EELEhTYQSKLENARLSSEMNSSAVNSTREELMESRYRIDSLTSQLSELQKESRA 316
Cdd:TIGR02168 454 EELE-RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-363 |
3.58e-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: 63.15 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 79 KELYETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELE-------SAQARFRETEALLNSKNAALAT 151
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelrlevsELEEEIEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 152 TQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELDFRKNVYEEEiKETRRRHETRLVEVD 231
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 232 sgKQIEYehkLSQALADMREQ---HDSQVTLYKEELEhtyQSKLENARLSSEMNSSAVNSTREELMESRYRIDSLTSQLS 308
Cdd:TIGR02168 379 --EQLET---LRSKVAQLELQiasLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 45361241 309 ELQKEsrawHDRMQELEDMLAKEKDNSRKMLAEREREMADIR---DQMQQQLNDYEQL 363
Cdd:TIGR02168 451 ELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERLQENLEGF 504
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
83-229 |
5.15e-10 |
|
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: 59.94 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 83 ETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSknaalATTQSENKSLQGE 162
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNNKEYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45361241 163 VEDLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELDFRKNVYEEEIKETRRRHETRLVE 229
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-310 |
8.16e-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: 62.00 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 3 TATPSGPRSSGRRSSMNTPLSPTR-ISRLQEKVDLQE-----LNDRLAVYIDKVRSLESENSLLHVQVTE---------- 66
Cdd:TIGR02168 654 LVRPGGVITGGSAKTNSSILERRReIEELEEKIEELEekiaeLEKALAELRKELEELEEELEQLRKELEElsrqisalrk 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 67 ---REEVRSREVSGIKELYETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLN 143
Cdd:TIGR02168 734 dlaRLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 144 SKNAALATTQSENKSLQGEVEDLKAEIGQLESAlalaKKQLEEEILIKVDLENRCQSLIEE-------LDFRKNVYEEEI 216
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEEleseleaLLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 217 KETRRRHETRLVEVDsgkqiEYEHKLSQALADMRE--QHDSQVTLYKEELEHTYQSKLENAR----LSSEMNSSAVNSTR 290
Cdd:TIGR02168 890 ALLRSELEELSEELR-----ELESKRSELRRELEElrEKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIE 964
|
330 340
....*....|....*....|
gi 45361241 291 EELMESRYRIDSLTSQLSEL 310
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
74-389 |
9.41e-10 |
|
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: 61.62 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 74 EVSGIKElYETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKEsELESAQARFRETEA--LLNSKNAA--- 148
Cdd:TIGR02169 161 EIAGVAE-FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyeLLKEKEALerq 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 149 LATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEE---EILIKVDLE-NRCQSLIEELDFRKNVYEEEIKETRRRHE 224
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkKIKDLGEEEqLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 225 -----TRLVEVDSGKQIEYEHKLSQALADMREQHDSQVTLYKEElehtyQSKLENARLSSEMNSSAVNSTREELMESRYR 299
Cdd:TIGR02169 319 daeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-----KEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 300 IDSLTSQLSELQKESRAWHDRMQ----ELEDMLAKEKDNSRKmLAEREREMADIRDQMQQQLNDYEQLLDVKLALDMEIS 375
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQrlseELADLNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330
....*....|....
gi 45361241 376 AYRKLLEGEEERLK 389
Cdd:TIGR02169 473 DLKEEYDRVEKELS 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-386 |
3.50e-09 |
|
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: 60.08 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 70 VRSREVSGIKELYETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAAL 149
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 150 ATTQSENKSLQGEVEDLKAEIGQLESALA-----LAKKQLEEEILIKVDLENRCQSLIEELdfrknvyeEEIKETRRRHE 224
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEeleedLHKLEEALNDLEARLSHSRIPEIQAEL--------SKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 225 TRLVEVdsgkqieyehklsqaladmrEQHDSQVTLYKEELEHTYQSKLENARLSSEMnssaVNSTREELMESRYRIDSLT 304
Cdd:TIGR02169 812 ARLREI--------------------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELE 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 305 SQLSELQKESRAWHDRMQELEdmlaKEKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGE 384
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
..
gi 45361241 385 EE 386
Cdd:TIGR02169 944 EE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-389 |
1.13e-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: 58.14 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 98 RERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESAL 177
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 178 ALAKKQ---LEEEILIKVDLENRCQSLIEELDFRKNVYEEEIKETRRRHEtRLVEVDSGKQIEYeHKLSQALADMREQHD 254
Cdd:TIGR02168 757 TELEAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-ELRAELTLLNEEA-ANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 255 SQVTLYKEELEHTYQSKLENARLSSEMNS---------SAVNSTREELMESRYRIDSLTSQLSELQKESRAWHDRMQELE 325
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEEleelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45361241 326 DmlakEKDNSRKMLAEREREMADIR---DQMQQQLN-DYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:TIGR02168 915 R----ELEELREKLAQLELRLEGLEvriDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
36-364 |
2.18e-08 |
|
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: 57.49 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 36 LQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREvsgikELYETELADARRSLDdtaRERARLQLELSKISVEHE 115
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE-----EKGRQELEKAKRKLE---GESTDLQEQIAELQAQIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 116 DLRASFSKKESELESAQARFRETEAllnSKNAALattqsenkslqgevedlkAEIGQLESALALAKKQLEEEILIKVDLE 195
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETA---QKNNAL------------------KKIRELEAQISELQEDLESERAARNKAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 196 NRCQSLIEELDFRKNVYEEEI------KETRRRHETRLVEVDsgKQIEYEHKLSQA-LADMREQHDSQVTLYKEELEHTY 268
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLdttaaqQELRSKREQEVTELK--KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQAK 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 269 QSK--LENARLSSEMNSS----AVNSTREELMESRYRIDSLTSQLSELQKESRAWHDRMQELEDMLAK---EKDNSRKML 339
Cdd:pfam01576 370 RNKanLEKAKQALESENAelqaELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKlqsELESVSSLL 449
|
330 340
....*....|....*....|....*...
gi 45361241 340 AERERE---MADIRDQMQQQLNDYEQLL 364
Cdd:pfam01576 450 NEAEGKnikLSKDVSSLESQLQDTQELL 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-342 |
2.27e-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: 57.39 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 65 TEREEVRSREVSGIKELYETELADARRSLDDTARERARLQLELSKI---SVEHEDLRASFSKK-----ESELESAQARFR 136
Cdd:TIGR02169 218 KEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELekrLEEIEQLLEELNKKikdlgEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 137 ETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELDFRKNVYEE-- 214
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvd 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 215 -EIKETRRRHETRLVEVDSGKQIEYEHKLSQA-LADMREQHDSQVTLYKEELEHTYQSKLENArlssemnsSAVNSTREE 292
Cdd:TIGR02169 378 kEFAETRDELKDYREKLEKLKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELE--------EEKEDKALE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 45361241 293 LMESRYRIDSLTSQLSELQKESRAWHDRMQELEDMLAKEKDNSRKMLAER 342
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-344 |
5.89e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 14 RRSSMNTPLSPTRISRLQEKVDLQELNDRLAVYIDKVRSLESENSLLHVQVTE--------REEVRSREvSGIKELyETE 85
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEleseleeaREAVEDRR-EEIEEL-EEE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 86 LADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKN--------------AALAT 151
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 152 TQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKvDLENRCQSLIEELDFRknvyEEEIKETRRRHETRLVEVD 231
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAER----RETIEEKRERAEELRERAA 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 232 sgkqiEYEhklsqalADMREQHDSqvtlyKEELEHTYQSKLENArlssemnsSAVNSTREELMESRYRIDSLTSQLSELQ 311
Cdd:PRK02224 548 -----ELE-------AEAEEKREA-----AAEAEEEAEEAREEV--------AELNSKLAELKERIESLERIRTLLAAIA 602
|
330 340 350
....*....|....*....|....*....|....
gi 45361241 312 kESRAWHDRMQELEDMLAKEKDNSRKMLAE-RER 344
Cdd:PRK02224 603 -DAEDEIERLREKREALAELNDERRERLAEkRER 635
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
95-359 |
1.71e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 95 DTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNsknaaLATTQSENKSLQGEVEDLKAEIGQLE 174
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----YSWDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 175 SA---LALAKKQLEEEILIKVDLENRCQSLIEE---LDFRKNVYEEEIKETRRRHETRLVEVDSGKQIEYEHKLSQALAD 248
Cdd:COG4913 682 ASsddLAALEEQLEELEAELEELEEELDELKGEigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 249 -----MREQHDSQVTLYKEELEhTYQSKLENARlssemnSSAVNSTREELMESRYRIDSLTSQLSELQK-ESRAWHDRMQ 322
Cdd:COG4913 762 avereLRENLEERIDALRARLN-RAEEELERAM------RAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPEYEE 834
|
250 260 270
....*....|....*....|....*....|....*...
gi 45361241 323 ELEDMLAKEKDNSRKMLAER-EREMADIRDQMqQQLND 359
Cdd:COG4913 835 RFKELLNENSIEFVADLLSKlRRAIREIKERI-DPLND 871
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
29-356 |
8.81e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 29 RLQEKV-----DLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEvrsrEVSGIKelyeTELADARRSLDD-------- 95
Cdd:COG3096 344 RQQEKIeryqeDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEE----EVDSLK----SQLADYQQALDVqqtraiqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 96 ----TARERARLQLELSKISVEH-EDLRASFSKKESELesaqarfreTEALLnsknaalattqsenkSLQGEVEDLKAEI 170
Cdd:COG3096 416 qqavQALEKARALCGLPDLTPENaEDYLAAFRAKEQQA---------TEEVL---------------ELEQKLSVADAAR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 171 GQLESALALAKKqleeeILIKVDLEN---RCQSLIEELDFRKNVYEEEIKETRRRHETRlvevdsgKQIEYEHKLSQALA 247
Cdd:COG3096 472 RQFEKAYELVCK-----IAGEVERSQawqTARELLRRYRSQQALAQRLQQLRAQLAELE-------QRLRQQQNAERLLE 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 248 DMREQHDSQVTLYkEELEHtYQSKLENARlssEMNSSAVNSTREELMESRYRIDSLTSQLSELQKESRAWH---DRMQEL 324
Cdd:COG3096 540 EFCQRIGQQLDAA-EELEE-LLAELEAQL---EELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLaaqDALERL 614
|
330 340 350
....*....|....*....|....*....|....*...
gi 45361241 325 EDMLAKEKDNS------RKMLAEREREMADIRDQMQQQ 356
Cdd:COG3096 615 REQSGEALADSqevtaaMQQLLEREREATVERDELAAR 652
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-316 |
2.07e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 97 ARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESA 176
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 177 LALAKKQLEEEI--LIKVDLENRCQSLIEELDF----RKNVYEEEIKETRRRHETRLVEvdsgkQIEYEHKLSQALADMR 250
Cdd:COG4942 99 LEAQKEELAELLraLYRLGRQPPLALLLSPEDFldavRRLQYLKYLAPARREQAEELRA-----DLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45361241 251 EQHDSQVTLYKEELEHTYQSKLENARLSSEMNSSAvNSTREELMESRYRIDSLTSQLSELQKESRA 316
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKEL-AELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-193 |
3.69e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 25 TRISRLQEKvdLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREVSGIKELYETELADARRSLDDTARERARLQ 104
Cdd:COG4913 288 RRLELLEAE--LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 105 LELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSEnksLQGEVEDLKAEIGQLES-------AL 177
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERrksnipaRL 442
|
170
....*....|....*.
gi 45361241 178 ALAKKQLEEEILIKVD 193
Cdd:COG4913 443 LALRDALAEALGLDEA 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-397 |
6.43e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 147 AALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELdfrkNVYEEEIKETRRRHEtr 226
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 227 lvevdsgkqieyehKLSQALADMREQHDSQVTLYKEELEHTYQSKLENA---RLSSE---------MNSSAVNSTREELM 294
Cdd:COG4942 87 --------------ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalLLSPEdfldavrrlQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 295 EsryRIDSLTSQLSELQKESRAWHDRMQELEDMLAKEKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVKLALDMEI 374
Cdd:COG4942 153 E---ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250 260
....*....|....*....|...
gi 45361241 375 SAYRKLLEGEEERLKLSPSPPSR 397
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-215 |
1.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 26 RISRLQEKVD-LQELNDRLAVYIDKVRSLESENSLLHVQVTER----EEVRSREVSGIKELYE--TELADARRSLDDTAR 98
Cdd:PRK03918 540 EIKSLKKELEkLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNeyLELKDAEKELEREEK 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 99 ERARLQLELSKISVEHEDLRASFSKKESELESAQARF-----RETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQL 173
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45361241 174 ESALALAKKQLEEEILIKVDLEnRCQSLIEELDFRKNVYEEE 215
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLKER 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
41-330 |
1.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 41 DRLAVYIDKVRSLESENSLLHVQVTEREEVRsREVSGIKELYE--TELADARRSLDDTARERARLQLELSKISVEHEDLR 118
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 119 ASfskkESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKVDLENRC 198
Cdd:COG4913 689 AL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 199 QSLIEELDFRKnvyeEEIKETRRRHETRLVEVDSGKQIEYEHKLSQALADMREQHDsqvtlYKEELE-------HTYQSK 271
Cdd:COG4913 765 RELRENLEERI----DALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPE-----YLALLDrleedglPEYEER 835
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 45361241 272 LENARLSSEmnssavnstreelmesryrIDSLTSQLSELQKESRAWHDRMQELEDMLAK 330
Cdd:COG4913 836 FKELLNENS-------------------IEFVADLLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
28-393 |
3.46e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 28 SRLQEKVDLQELNDRLA----VYIDKVRSLESENSLLHVQVTEREevrsrevSGIKELyeTELADARRSLDDTARERARL 103
Cdd:pfam05483 209 ARLEMHFKLKEDHEKIQhleeEYKKEINDKEKQVSLLLIQITEKE-------NKMKDL--TFLLEESRDKANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 104 QLELSKISVEHED------------LRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIG 171
Cdd:pfam05483 280 QDENLKELIEKKDhltkeledikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 172 QLESALALAKKQLEEE----ILIKVDLENRCQSLiEELDFRKNVYEEEIKETRRRHETRLVEVDSGKQIEyehKLSQALA 247
Cdd:pfam05483 360 SLEELLRTEQQRLEKNedqlKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE---KIAEELK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 248 DmREQHDSQVTLYKEELEHTYQSKLENARLSSEMNSSAVNSTREELMESRYRIDSLTSQLSELQKESRawhDRMQELEDM 327
Cdd:pfam05483 436 G-KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK---ELTQEASDM 511
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45361241 328 LAKekdnsrkmLAEREREMADIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLL--EGEEERLKLSPS 393
Cdd:pfam05483 512 TLE--------LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqKGDEVKCKLDKS 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-225 |
6.66e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 49 KVRSLESENSLLHVQVTEREEvRSREVSGIKELYETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESEL 128
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 129 ESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEeeilikvdlenRCQSLIEELDFR 208
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-----------GIEAKINELEEE 442
|
170
....*....|....*..
gi 45361241 209 KNVYEEEIKETRRRHET 225
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQ 459
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-389 |
2.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 36 LQELNDRLAVYIDKVRSLESenslLHVQVTEREEVRSREVSGIKELYETELADARRSLDDTARERARLQLELSKISVEHE 115
Cdd:COG4717 148 LEELEERLEELRELEEELEE----LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 116 DLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAkkqLEEEILIKVDLE 195
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL---LFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 196 NRCQSLIEELDFRKNVYEEEIKETRRRHEtRLVEVDSGKQIEYEHKLSQALADMREQHDSQVTLYKEELEHTYQSKLENA 275
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 276 RLSSEMNSSAVNSTREELMESRYRIDSLTSQLSELQKESRAWHDrmQELEDMLAKEKDNSRKMLAEREREMADIRDQMQQ 355
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE--ALDEEELEEELEELEEELEELEEELEELREELAE 457
|
330 340 350
....*....|....*....|....*....|....
gi 45361241 356 QLNDYEQLLDvklalDMEISAYRKLLEGEEERLK 389
Cdd:COG4717 458 LEAELEQLEE-----DGELAELLQELEELKAELR 486
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
26-213 |
2.50e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 26 RISRLQEKVD------------LQELNDRLAVYidkVRSLESENSLLHVQVTEREEVRSR--EVSGIKELYET------- 84
Cdd:PHA02562 214 NIARKQNKYDelveeaktikaeIEELTDELLNL---VMDIEDPSAALNKLNTAAAKIKSKieQFQKVIKMYEKggvcptc 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 85 --ELADARRSLDDTARERARLQLELSKISVEHEDLrasfSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGE 162
Cdd:PHA02562 291 tqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL----EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAA 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45361241 163 VEDLKAEIGQLESALALAKKQLEEeilikvdLENRCQSLIEELDFRKNVYE 213
Cdd:PHA02562 367 IEELQAEFVDNAEELAKLQDELDK-------IVKTKSELVKEKYHRGIVTD 410
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-367 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 84 TELADARRSLDDTARERARLQlELSKISVEHEDLRASFSKKESELESAQARFRETEALLnsknaalattqsenksLQGEV 163
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 164 EDLKAEIGQLESALALAKKQLEEeilikvdLENRCQSLIEELDFRKNVYEEEIKETRRRHETRLVEVdsgkqieyehkls 243
Cdd:COG4913 298 EELRAELARLEAELERLEARLDA-------LREELDELEAQIRGNGGDRLEQLEREIERLERELEER------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 244 qalADMREQHDSQVTLYKEELEHTYQSKLENARLSSEmnssAVNSTREELMESRYRIDSLTSQLSELQKESRAWHDRMQE 323
Cdd:COG4913 358 ---ERRRARLEALLAALGLPLPASAEEFAALRAEAAA----LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45361241 324 LEdmlakekdnSRKMLAerEREMADIRDQMQQQLNDYEQ-------LLDVK 367
Cdd:COG4913 431 LE---------RRKSNI--PARLLALRDALAEALGLDEAelpfvgeLIEVR 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-248 |
4.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 29 RLQEKVDLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREVSGIKELYETELADARRSLD--DTARERARLQLE 106
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEalRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 107 LSKISVEHEDLRASFSKKESELESAQARFRETEALLnskNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEE 186
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEE---EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45361241 187 EILIKVDLENRcQSLIEELDFRKNVYEEEIKETRRRHETRLVEVDSGKQIEYEHKLSQALAD 248
Cdd:COG1196 482 LLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
30-386 |
4.45e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 30 LQEKVDLQELNDRLAVYIDKVRSLESENSLLhVQVTERE----EVRSREVSGIKELYETELADARRSLDDTARERARLQL 105
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFL-LQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 106 ELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQL------------ 173
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevkckldkse 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 174 ESALALAKKQLEEEILIKVdLENRCQSLIEELDFRKNVYEEEIKETRRRHETRLVEVDSGKQIEYE-HKLSQALADMREQ 252
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKI-LENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvNKLELELASAKQK 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 253 HdsqvtlykEELEHTYQSKLENARLSsemnssavnstREELMESRYRIDSLTSQLSELQKE--SRAWHdRMQELEDMLAK 330
Cdd:pfam05483 652 F--------EEIIDNYQKEIEDKKIS-----------EEKLLEEVEKAKAIADEAVKLQKEidKRCQH-KIAEMVALMEK 711
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 45361241 331 EKDNSRKMLAEREREMADIRDQMQQQlNDYEQLLDVKLA-LDMEISAYRKLLEGEEE 386
Cdd:pfam05483 712 HKHQYDKIIEERDSELGLYKNKEQEQ-SSAKAALEIELSnIKAELLSLKKQLEIEKE 767
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
29-367 |
5.02e-04 |
|
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: 42.96 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 29 RLQEKVDLQELNDRLAVYIDKVRsLESENSLLHVQVTEREEV--RSREVSGIKELYETELADARRSLDDTARERARLQLE 106
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQ-WERQRRELESRVAELKEElrQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 107 LSKISVEHEDLRASFSKKESELESAQARFRETEALLNsknAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEE 186
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAG---AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 187 EILIKVDLENRCQSLIEELD--FRKNVYEEEIKETRRRHETRLVEvdSGKQIEyehKLSQALADMREQHD-SQVTLYKEE 263
Cdd:pfam07888 204 RDTQVLQLQDTITTLTQKLTtaHRKEAENEALLEELRSLQERLNA--SERKVE---GLGEELSSMAAQRDrTQAELHQAR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 264 LEHTYQS-KLENARLSSEMNSSAVNSTREELMES----RYRIDSLTSQLseLQKESRAWHDRMQ--ELEDMLAKEKDNSR 336
Cdd:pfam07888 279 LQAAQLTlQLADASLALREGRARWAQERETLQQSaeadKDRIEKLSAEL--QRLEERLQEERMEreKLEVELGREKDCNR 356
|
330 340 350
....*....|....*....|....*....|.
gi 45361241 337 KMLAEREREMADIRDQMQQQLNDYEQLLDVK 367
Cdd:pfam07888 357 VQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
68-365 |
5.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 68 EEVRSReVSGIKELYETELADARRSLDD-----TARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALL 142
Cdd:PRK02224 165 EEYRER-ASDARLGVERVLSDQRGSLDQlkaqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 143 nsknAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELDF----------RKNVY 212
Cdd:PRK02224 244 ----EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaveaRREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 213 EEEIKETRRR-HETRLVEVDSGKQIEyehklsqALADMREQHDSQVTLYKEELEhTYQSKLENARLSSEMNSSAVNSTRE 291
Cdd:PRK02224 320 EDRDEELRDRlEECRVAAQAHNEEAE-------SLREDADDLEERAEELREEAA-ELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45361241 292 ELMESRYRIDSLTSQLSELqkesrawhdrmQELEDMLAKEKDNSRKMLAEREREMADIRDqmqqQLNDYEQLLD 365
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNA-----------EDFLEELREERDELREREAELEATLRTARE----RVEEAEALLE 450
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
24-189 |
6.82e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 24 PTRISRLQEKvdLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSRevsgikelYETELADARrslddTARERARL 103
Cdd:COG1579 30 PAELAELEDE--LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--------YEEQLGNVR-----NNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 104 QLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSEnksLQGEVEDLKAEIGQLESALALAKKQ 183
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAK 171
|
....*.
gi 45361241 184 LEEEIL 189
Cdd:COG1579 172 IPPELL 177
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
46-206 |
8.64e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 46 YIDKVRSLESEnsLLHVQVTEREEVRSREVSGIKElyetELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKE 125
Cdd:pfam05911 635 CIDKVTLSENK--VAQVDNGCSEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCT 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 126 SELESAQARFRETEALLNSKNAALAT---------TQSE-----NKSLQGEVEDLKAEIGQLESALALAKKQLEEEILIK 191
Cdd:pfam05911 709 ENLESTKSQLQESEQLIAELRSELASlkesnslaeTQLKcmaesYEDLETRLTELEAELNELRQKFEALEVELEEEKNCH 788
|
170
....*....|....*
gi 45361241 192 VDLENRCQSLIEELD 206
Cdd:pfam05911 789 EELEAKCLELQEQLE 803
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
30-389 |
9.31e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 30 LQEKVDLQELNDRLA-VYIDKVRSLESENSLLHVQ---VTEREEVRSREVSGIKELYETELADARRSLDD-TARERARLQ 104
Cdd:pfam12128 386 EQNNRDIAGIKDKLAkIREARDRQLAVAEDDLQALeseLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 105 LELSKISVEH--EDLRASFSKKE---SELESAQARFRETEALLNSKNAALATTQSENKSLQ---------------GEVE 164
Cdd:pfam12128 466 LENFDERIERarEEQEAANAEVErlqSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpqagtllhflrKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 165 DLKAEIGQLESALALAKKQLEEEIL------------IKVDLE----NRCQSLIEELDFRKNVYEEEIKETRRRHEtrlv 228
Cdd:pfam12128 546 DWEQSIGKVISPELLHRTDLDPEVWdgsvggelnlygVKLDLKridvPEWAASEEELRERLDKAEEALQSAREKQA---- 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 229 evdsgkqiEYEHKLSQALADMREQhDSQVTLYKEELEhtyQSKLENARLSSEMNSSAV---NSTREELMESRYRIDSLTS 305
Cdd:pfam12128 622 --------AAEEQLVQANGELEKA-SREETFARTALK---NARLDLRRLFDEKQSEKDkknKALAERKDSANERLNSLEA 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 306 QLSELQKESRAWhdrmqeledmlakekdnsrkmLAEREREMADIRDQMQQQLNDYEQLLDVKLA-LDMEISAYRKLLEGE 384
Cdd:pfam12128 690 QLKQLDKKHQAW---------------------LEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAE 748
|
....*
gi 45361241 385 EERLK 389
Cdd:pfam12128 749 LKALE 753
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
85-293 |
1.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 85 ELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVE 164
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 165 DLKAEIGQLESALALAKKQLEEEILIKVDLENRCQSLIEELdfrkNVYEEEIKETRRRHETRLVEVDSGKQIEYEHKLSQ 244
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL----KELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45361241 245 ALADMREQHDSQVTLYKEELEHTYQSKLENARLSSEMNSSAVNSTREEL 293
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-367 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 104 QLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALA-LAKK 182
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdLTNQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 183 QLEEEILIKvDLENRCQSLIEELDfrknVYEEEIKETRRRHETRLVEVDSGKQ-----IEYEHKLSQALADMREQHDSQV 257
Cdd:TIGR04523 449 DSVKELIIK-NLDNTRESLETQLK----VLSRSINKIKQNLEQKQKELKSKEKelkklNEEKKELEEKVKDLTKKISSLK 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 258 TLYKEELEHTYQSKLENARLSSEMNSSAVNSTREELMESRYRIDSLTSQLSELQKESRAWHDRMQELEDMLAKEKDNSRK 337
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
250 260 270
....*....|....*....|....*....|
gi 45361241 338 MLAEREREMADIRDQMQQQLNDYEQLLDVK 367
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-389 |
2.40e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 38 ELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREVSGIKELyETELADARRSLDDTARERARLQLELSKISVEHEDL 117
Cdd:TIGR04523 86 DLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKL-EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 118 RA----------SFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEEE 187
Cdd:TIGR04523 165 KKqkeelenelnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 188 ILIKVDLENRCQSLIEELDFRKNVYEEEIKEtrrrhetrlVEVDSGKQIEYEHKLSQaladmreqhdsqvtlYKEELEHT 267
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---------LEQNNKKIKELEKQLNQ---------------LKSEISDL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 268 YQSKLENarLSSEMNSSAVNSTRE------ELMESRYRIDSLTSQLSELQKESRawhdrmqeledmlAKEKDNS--RKML 339
Cdd:TIGR04523 301 NNQKEQD--WNKELKSELKNQEKKleeiqnQISQNNKIISQLNEQISQLKKELT-------------NSESENSekQREL 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 45361241 340 AEREREMADIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
83-387 |
2.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 83 ETELADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGE 162
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 163 VEDL-------KAEIGQLESALALAKKQ----------LEEEI--------LIKVDLENrCQSLIEELDFRKNVYEEEIK 217
Cdd:PRK02224 351 ADDLeeraeelREEAAELESELEEAREAvedrreeieeLEEEIeelrerfgDAPVDLGN-AEDFLEELREERDELREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 218 ETR---RRHETRLVE----VDSGKQIEYEH-------------------KLSQALADMREQHDS---QVTLYKE--ELEH 266
Cdd:PRK02224 430 ELEatlRTARERVEEaealLEAGKCPECGQpvegsphvetieedrerveELEAELEDLEEEVEEveeRLERAEDlvEAED 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 267 TYQSKLENARLSSEMnssaVNSTREELMESRYRIDSLTSQLSELQKESRAWHDRMQELEDmlakEKDNSRKMLAEREREM 346
Cdd:PRK02224 510 RIERLEERREDLEEL----IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE----EAEEAREEVAELNSKL 581
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 45361241 347 ADIRDQMqQQLNDYEQLLDVKLALDMEISAYRKLLEGEEER 387
Cdd:PRK02224 582 AELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-214 |
3.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 26 RISRLQEKVDLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEvRSREVSGIKELYETELADARRSlddtaRERARLQL 105
Cdd:COG3206 197 ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA-RLAALRAQLGSGPDALPELLQS-----PVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 106 ELSKISVEHEDLRASFSKKESELESAQARFRETEALLNS-KNAALATTQSENKSLQGEVEDLKAEIGQLESALA-LAKKQ 183
Cdd:COG3206 271 QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAeLPELE 350
|
170 180 190
....*....|....*....|....*....|.
gi 45361241 184 LEEEILikvdleNRcqslieELDFRKNVYEE 214
Cdd:COG3206 351 AELRRL------ER------EVEVARELYES 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-222 |
3.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 16 SSMNTPLSPTRISRLQEKVDLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREVSGIKELYETELADARRSLDD 95
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 96 TARERARLQLELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLES 175
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45361241 176 ALALAKKQLEEEILikvdlenrcqsLIEELDFRKNVYEEEIKETRRR 222
Cdd:COG1196 740 ELLEEEELLEEEAL-----------EELPEPPDLEELERELERLERE 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-381 |
3.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 106 ELSKISVEHEDLRASFSKKESELESAQARFRETEALLNSknaaLATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLE 185
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 186 E----------------EILIKVDLENRCQSLIEELDFRKNVYEEEIKETRRRHETRLVEVDSGKQIEYEHK-LSQALAD 248
Cdd:PRK03918 277 EleekvkelkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKeLEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 249 MREQHdsqvtlykEELEHTYQSKLENARLSSEMNSSAVNSTREELMESRYR-------IDSLTSQLSELQKESRAWHDRM 321
Cdd:PRK03918 357 LEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkeeieeeISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45361241 322 QELEDMLAK--------EKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLL 381
Cdd:PRK03918 429 EELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
86-388 |
3.78e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 86 LADARRSLDDTARERARLQLELSKISVEHEDLRASFSKKESELESAQARfretealLNSKNAALAttqsenksLQGEVED 165
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-------LNLVQTALR--------QQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 166 LKAEIGQLESALALAKKQLEEEilikvdlenrcqslieeldfrknvyEEEIKETRRRHETRLVEVDSGKqieyehklSQa 245
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEA-------------------------AEQLAEAEARLEAAEEEVDSLK--------SQ- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 246 LADMREQHDSQVT---LYKEELEhtyqsKLENARLSSEMNSSAVNSTREELMESRYRIDSLTSQLSELQ------KESRA 316
Cdd:COG3096 398 LADYQQALDVQQTraiQYQQAVQ-----ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEqklsvaDAARR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 317 WHDRMQELEDMLAKEKDNSR---------------KMLAER----EREMADIRDQMQQQ------LNDYEQLLDVKLALD 371
Cdd:COG3096 473 QFEKAYELVCKIAGEVERSQawqtarellrryrsqQALAQRlqqlRAQLAELEQRLRQQqnaerlLEEFCQRIGQQLDAA 552
|
330
....*....|....*..
gi 45361241 372 MEISAYRKLLEGEEERL 388
Cdd:COG3096 553 EELEELLAELEAQLEEL 569
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-359 |
4.15e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 73 REVSGIKELYETELADARRSLDDTARERARLQLELSKI-------SVEHEDLRASFSKKESELESAQARfreTEALLNSK 145
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMadirrreSQSQEDLRNQLQNTVHELEAAKCL---KEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 146 NAALATTQSENKSLQGEVEDLKAEIGQLESALAlaKKQLEEEILIKVDLEN---RCQSLIEELDFRKNVYEEEIKETRRR 222
Cdd:pfam15921 169 NTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG--KKIYEHDSMSTMHFRSlgsAISKILRELDTEISYLKGRIFPVEDQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 223 HETrlVEVDSGKQIEYehkLSQALADMREQ----HDSQVTLYKEELEhTYQSKLENARLSSEMNSSAVNSTREELMESRY 298
Cdd:pfam15921 247 LEA--LKSESQNKIEL---LLQQHQDRIEQliseHEVEITGLTEKAS-SARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45361241 299 RIDSLTSQL-SELQKESRAWHDRMQELEDMLAKEKDNSRKMLAERE---REMADIRDQMQQQLND 359
Cdd:pfam15921 321 DLESTVSQLrSELREAKRMYEDKIEELEKQLVLANSELTEARTERDqfsQESGNLDDQLQKLLAD 385
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
98-344 |
4.50e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 98 RERARLQLELSKISVEhedLRASFSKKESELESAQ-ARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLEsa 176
Cdd:PRK05771 46 RKLRSLLTKLSEALDK---LRSYLPKLNPLREEKKkVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELE-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 177 lalakKQLEE-EILIKVDLEnrcqslIEELDFRKNVY-------EEEIKETRRRHETRLVEVDSgkqiEYEHKLSQALAD 248
Cdd:PRK05771 121 -----QEIERlEPWGNFDLD------LSLLLGFKYVSvfvgtvpEDKLEELKLESDVENVEYIS----TDKGYVYVVVVV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 249 MREQHDSQVTLYKeelehtyqsKLENARLS---SEMNSSAVNSTREELMESRYRIDSLTSQLSELQKEsraWHDRMQELE 325
Cdd:PRK05771 186 LKELSDEVEEELK---------KLGFERLEleeEGTPSELIREIKEELEEIEKERESLLEELKELAKK---YLEELLALY 253
|
250 260
....*....|....*....|.
gi 45361241 326 DMLA--KEKDNSRKMLAERER 344
Cdd:PRK05771 254 EYLEieLERAEALSKFLKTDK 274
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
65-382 |
4.97e-03 |
|
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: 39.77 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 65 TEREEV---RSREVSGIKELY---ETELADARRSLDDTARERARLQLEL---SKISVEHEDLRASFSKKESELesaqarf 135
Cdd:pfam01576 1 TRQEEEmqaKEEELQKVKERQqkaESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLAARKQEL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 136 retEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESAL-----ALAKKQLEeeiliKVDLENRCQSLIEELDFRKN 210
Cdd:pfam01576 74 ---EEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaARQKLQLE-----KVTTEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 211 VYEEEIKEtRRRHETRLVEVDSgkQIEYEHKLSQALADMREQHDSQVTLYKEELEHTYQSKLENARLSSEMNSSAvNSTR 290
Cdd:pfam01576 146 QNSKLSKE-RKLLEERISEFTS--NLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGES-TDLQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 291 EELMESRYRIDSLTSQLSELQKESRAWHDRMQEledmLAKEKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVKLAL 370
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEE----ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330
....*....|..
gi 45361241 371 DMEISAYRKLLE 382
Cdd:pfam01576 298 GEELEALKTELE 309
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
63-385 |
6.13e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 63 QVTEREEVRSREVSGIKELYE---TELADARRSLDDTAR-ERARLQ----------LELSKISVEHEDLRASFSKKESEL 128
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSfvvTEFEATTCSLEELLRtEQQRLEknedqlkiitMELQKKSSELEEMTKFKNNKEVEL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 129 ESAQARFRETEALLNsknaalattqsENKSLQGEVEDLKAEIGQLESALALAKKQLEE-EILIKVDLENRCQSLIEELDF 207
Cdd:pfam05483 408 EELKKILAEDEKLLD-----------EKKQFEKIAEELKGKEQELIFLLQAREKEIHDlEIQLTAIKTSEEHYLKEVEDL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 208 RKNVYEEEIKETRRRHETRLVEVDSgkqieyeHKLSQALADMREQHDSQvtlykeelehtyQSKLENARLSSEMNSSAVN 287
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLEN-------KELTQEASDMTLELKKH------------QEDIINCKKQEERMLKQIE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 288 STREELMESRYRIDSLTSQLSELQKESRAWHDRMQELEDMLAKEKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVK 367
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
330
....*....|....*...
gi 45361241 368 LALDMEISAYRKLLEGEE 385
Cdd:pfam05483 618 KALKKKGSAENKQLNAYE 635
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
122-186 |
6.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 6.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45361241 122 SKKESELESAQARFRETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLEE 186
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-210 |
7.71e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 26 RISRLQEKvdLQELNDRLAVYIDKVRSLESENSLLHVQVTEREEVRSREVSGIKELYETELADARRSLDDTARERARLQL 105
Cdd:COG4942 63 RIAALARR--IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45361241 106 eLSKISVEHEDLRASFSKKESELESAQArfrETEALLNSKNAALATTQSENKSLQGEVEDLKAEIGQLESALALAKKQLE 185
Cdd:COG4942 141 -LKYLAPARREQAEELRADLAELAALRA---ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
170 180
....*....|....*....|....*
gi 45361241 186 EEILIKVDLENRCQSLIEELDFRKN 210
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| |
