|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
24-117 |
9.96e-40 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 141.65 E-value: 9.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 24 WAVRVEEKAKFDGIFESLLP-INGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 102
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 1953011266 103 VPSVLPPSLIPPSKR 117
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
172-267 |
1.65e-36 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 132.40 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 172 WVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSkGI 251
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80
|
90
....*....|....*.
gi 1953011266 252 DPPQVLSPDMVPPSER 267
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
34-99 |
5.81e-25 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 98.45 E-value: 5.81e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 34 FDGIFESLLPIN-GLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 99
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
30-117 |
1.02e-24 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 98.98 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 30 EKAKFDGIFESLLPINGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPSVL 107
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDEL 87
|
90
....*....|
gi 1953011266 108 PPSLIPPSKR 117
Cdd:pfam12763 88 PDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
182-248 |
6.74e-24 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 95.36 E-value: 6.74e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 182 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVS 248
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
284-471 |
3.37e-19 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 90.35 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 284 TGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkVQLETIIKSLKSTQDEI 443
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQALDELLKEA 192
|
170 180
....*....|....*....|....*...
gi 1953011266 444 NQARSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEEL 220
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-474 |
1.34e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR 447
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|....*..
gi 1953011266 448 SKLSQLQESHQEAHRTLEQYDEALDGA 474
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-494 |
1.67e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 358
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS 438
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 439 TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-494 |
6.70e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011266 447 RSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-494 |
1.10e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQD-------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 439
Cdd:COG1196 368 LEAEAELAEaeeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 440 QDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
295-487 |
3.59e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 295 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 374
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 375 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQ 454
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190
....*....|....*....|....*....|...
gi 1953011266 455 ESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 487
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-474 |
5.56e-17 |
|
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: 85.88 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE-------ETQLEQSIQAGKVQLETIIKSLKSTQ 440
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190
....*....|....*....|....*....|....
gi 1953011266 441 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 474
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-503 |
6.00e-17 |
|
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: 85.88 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV-----QLETIIKSLKSTQ 440
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQ 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 441 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG------ASLTNLADLSEGVS--LAERGGFGAMDDP 503
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQArldsleRLQENLEGFSEGVKalLKNQSGLSGILGV 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
293-474 |
1.78e-16 |
|
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: 84.34 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 293 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvrQK 372
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 373 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQ 452
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170 180
....*....|....*....|..
gi 1953011266 453 LQEshQEAHRTLEQYDEALDGA 474
Cdd:TIGR02168 433 AEL--KELQAELEELEEELEEL 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-479 |
8.61e-16 |
|
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: 80.19 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 359
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlQQEETQLEQSIQAGKVQLETIIKSLKST 439
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 440 QDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASL 479
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
293-487 |
1.00e-15 |
|
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: 82.03 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 293 SQEIAQLqrekyslEQDIREKEEAIRQKSNEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 372
Cdd:TIGR02168 676 RREIEEL-------EEKIEELEEKIAELEKALAELR-------KELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 373 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEIN-------Q 445
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaN 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011266 446 ARSKLSQLQESHQEAHRTLEQYDEALDG--AHGASLT-NLADLSE 487
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEElsEDIESLAaEIEELEE 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-474 |
1.61e-15 |
|
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: 79.42 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 366
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 sDVRQK------------CQDETQMISSLKTqIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIK 434
Cdd:COG4942 111 -RALYRlgrqpplalllsPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 435 SLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 474
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
310-517 |
1.84e-15 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 79.18 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 310 IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 389
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 390 QESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEahRTLEQYDE 469
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011266 470 ALDGAHGASLTNLADLSEGVSLAERGGFGAMDDPFKNKALLFSNNAQE 517
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
288-476 |
4.06e-15 |
|
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: 75.73 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVR-----QKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 442
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 443 INQARSKL-SQLQEshqeahRTLEQYDEALDGAHG 476
Cdd:COG1579 161 LEAEREELaAKIPP------ELLALYERIRKRKNG 189
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-487 |
8.08e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELT----RLQQEETQL---EQSIQAGKVQLETIIKSLKS 438
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALleaEAELAEAEEELEELAEELLE 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011266 439 TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 487
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-459 |
9.43e-15 |
|
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: 78.52 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSL 436
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
170 180
....*....|....*....|...
gi 1953011266 437 KSTQDEINQARSKLSQLQESHQE 459
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQ 292
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-494 |
1.28e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQkqdaQDRLDE----------- 354
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER----LEELEEelaeleeelee 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 355 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIK 434
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 435 SLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-455 |
2.71e-14 |
|
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: 76.98 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKSTQD----E 442
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEklesE 532
|
170
....*....|...
gi 1953011266 443 INQARSKLSQLQE 455
Cdd:TIGR04523 533 KKEKESKISDLED 545
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
296-471 |
3.44e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.34 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 296 IAQLQREKYSLE-----------QDIREKEEAIRQKSNEV---QELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDM--LSDVRQKCQDETQMISSLKTQIQsqesDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV-QLETIIKSLKS 438
Cdd:COG4717 128 LPLYqeLEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1953011266 439 TQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-466 |
4.20e-14 |
|
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: 76.65 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 278 LGSGEFTGVKE-LDDISQEIAQLQR--------------EKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELE 342
Cdd:TIGR02169 284 LGEEEQLRVKEkIGELEAEIASLERsiaekereledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 343 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI-------QSQESDLKSQEDDLNRAKSELTRLQQEE 415
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 416 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-491 |
5.26e-14 |
|
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: 76.25 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 S-------DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA-------GKVQLETI 432
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALL 892
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 433 IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSL 491
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-474 |
8.20e-14 |
|
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: 75.86 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:TIGR02168 326 EELESKLDE-------LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 447 RS-------KLSQLQESHQEAHRTLEQYDEALDGA 474
Cdd:TIGR02168 399 NNeierleaRLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
286-428 |
2.77e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKS--NEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 364 DMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 428
Cdd:COG4717 174 ELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-466 |
3.39e-13 |
|
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: 73.56 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD-----AQDRLDEMDQQKAK 361
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDMLSDVR----------QKCQDETQMISSLKTQIQSQESDLKSQEDDlNRAKSELTRLQQEEtqLEQSIQAGKVQLET 431
Cdd:TIGR02169 803 LEEEVSRIEarlreieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKS-IEKEIENLNGKKEE--LEEELEELEAALRD 879
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 432 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-459 |
3.69e-13 |
|
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: 73.13 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|...
gi 1953011266 447 RSKLSQLQESHQE 459
Cdd:TIGR04523 495 EKELKKLNEEKKE 507
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
286-471 |
3.75e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDetqmISSLKTQIQSQESDLK-SQEDDLNRAKSELTRLQQEETQLEQsiqagkvqletiikSLKSTQDE 442
Cdd:COG4717 160 ELEEELEELEAE----LAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEE--------------ELEEAQEE 221
|
170 180
....*....|....*....|....*....
gi 1953011266 443 INQARSKLSQLQEShQEAHRTLEQYDEAL 471
Cdd:COG4717 222 LEELEEELEQLENE-LEAAALEERLKEAR 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-499 |
4.19e-13 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 71.78 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 363
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 ---------DMLSDVRQKCQDETQMISSLKTQIQSQESD---LKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 431
Cdd:COG3883 103 syldvllgsESFSDFLDRLSALSKIADADADLLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 432 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGFGA 499
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-494 |
4.83e-13 |
|
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: 73.17 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 295 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 374
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 375 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQ 454
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011266 455 ESHQEAHRTLEQYD---EALDGAHGASLTNLADLSEGVSLAER 494
Cdd:TIGR02168 393 LQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEEAEL 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
286-445 |
1.18e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.59 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMI-SSLKTQI---QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 439
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....*.
gi 1953011266 440 QDEINQ 445
Cdd:COG3206 378 RLAEAL 383
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-494 |
2.00e-12 |
|
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: 71.25 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQK-SNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQ 445
Cdd:TIGR02169 331 IDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 446 ARSKLSQLQESHQEAHRTLEQYDEALDGA---HGASLTNLADLSEGVSLAER 494
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEDKALEIKKQEW 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-461 |
3.14e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD-- 364
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEEle 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 365 -MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 443
Cdd:COG1196 407 eAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
170
....*....|....*...
gi 1953011266 444 NQARSKLSQLQESHQEAH 461
Cdd:COG1196 487 AEAAARLLLLLEAEADYE 504
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-466 |
3.55e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 70.05 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKSN------EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 360
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNGlvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 361 KLRDMLSDVRQkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE----ETQLEQSIQAGKVQLETIIKSL 436
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQiaalRAQLQQEAQRILASLEAELEAL 325
|
170 180 190
....*....|....*....|....*....|....
gi 1953011266 437 KST----QDEINQARSKLSQLQESHQEAHRtLEQ 466
Cdd:COG3206 326 QAReaslQAQLAQLEARLAELPELEAELRR-LER 358
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
288-495 |
5.90e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKSNEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 362
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 RDMLSDVRqkcqdetqmisslkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 442
Cdd:PRK02224 327 RDRLEECR--------------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 443 INQARSKLSQLQESHQEAHRTLEQYDEALDGAHG------ASLTNLAD-LSEGVSLAERG 495
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREreaeleATLRTARErVEEAEALLEAG 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-466 |
7.15e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKSNEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 351
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 LDEMDQQKAKLRDMLSDVRQKC-QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLE 430
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953011266 431 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
287-436 |
1.09e-11 |
|
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: 65.33 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 366
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSEltrLQQEETQLEQSIQAGKVQLETIIKSL 436
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-424 |
1.51e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 283 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 362 LRDMLSDVRQKCQDETQMISSLKTQIQSQ----ESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 424
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
301-471 |
2.06e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 301 REKYSLEQDIREKEEAIRQksnEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDmLSDVRQKCQDetqmI 380
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEEL-------AEAEERLEALEAELDALQERREALQR-LAEYSWDEID----V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 381 SSLKTQIQSQESDLksqeDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 460
Cdd:COG4913 664 ASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170
....*....|.
gi 1953011266 461 HRTLEQYDEAL 471
Cdd:COG4913 740 EDLARLELRAL 750
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
295-460 |
4.72e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 66.30 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 295 EIAQLQREKYSLEQDIREKEEAIRqksNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 374
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLK---NELSELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 375 DETQMISSLKTQIQSQESDLKSQEDD---LNRAKSELTRLQQEETQLEQSIQAGKvQLETIIKSLKSTQDEINQARSKLS 451
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELERLREHNK-HLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 1953011266 452 QLQESHQEA 460
Cdd:pfam05557 239 REEKYREEA 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-466 |
5.67e-11 |
|
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: 66.20 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKyslEQDI-REKEEAIRQKSNEVQELQNDLDRETSSLQEL-------EAQKQDAQDRLDEMDQQ 358
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLneqisqlKKELTNSESENSEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ---------- 428
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknnseikd 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011266 429 -------LETIIKSLKSTQDEINQarsKLSQLQESHQEAHRTLEQ 466
Cdd:TIGR04523 445 ltnqdsvKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
288-415 |
5.77e-11 |
|
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: 66.63 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1953011266 368 DVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE 415
Cdd:TIGR02169 466 KYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
294-494 |
1.25e-10 |
|
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: 64.53 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREKYSLEQDiREKEEAIRQKS---NEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 370
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 371 QKCQDETQMISSLKTQIQSQESDLKSQEDdlnRAKSELTRLQQEETQLEQSiqagKVQLETIIKSLKSTQDEINQARSKL 450
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL----QAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011266 451 SQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
287-466 |
1.33e-10 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 62.32 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDML-------SDVRQKCQDETQM-ISSLKTQIQSQESDLKS--QEDDLNRAKSELTRLQQEetQLEQSIQAgkvqL 429
Cdd:pfam12795 130 QQIRNRLngpappgEPLSEAQRWALQAeLAALKAQIDMLEQELLSnnNRQDLLKARRDLLTLRIQ--RLEQQLQA----L 203
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011266 430 ETIIKSLKSTQDEinQARSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam12795 204 QELLNEKRLQEAE--QAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
286-470 |
1.53e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLD------RETSSLQE-------LEAQKQDAQDRL 352
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEkaeeyikLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 353 DEMDQQKAKLRDMLSDVRQKCQD------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE-QSIQAG 425
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKL 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011266 426 KVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 470
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-487 |
1.72e-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: 65.09 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQeIAQLQREKysleQDIREKEEAIRQKSNEVQ----ELQNDLDR-------------------ET------SS 337
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 338 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI------------------QSQESDLKSQED 399
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 400 DLNR-----------AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYD 468
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260
....*....|....*....|..
gi 1953011266 469 EALDGA---HGASLTNLADLSE 487
Cdd:TIGR02169 392 EKLEKLkreINELKRELDRLQE 413
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
295-442 |
2.01e-10 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 62.85 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 295 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQ-------KCQDETQMISSLKTQIQSQeSDLKSQEDDLNRAKSELTR-LQQEETQLEqSIQAGK----VQLETIIK 434
Cdd:pfam09787 128 EELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELENRLHQLTEtLIQKQTMLE-ALSTEKnslvLQLERMEQ 205
|
....*...
gi 1953011266 435 SLKSTQDE 442
Cdd:pfam09787 206 QIKELQGE 213
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-469 |
2.16e-10 |
|
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: 64.27 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELTRLQQEETQleQSIQAGKVQLETIIKSLKST 439
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKK 583
|
170 180 190
....*....|....*....|....*....|
gi 1953011266 440 QDEINQarsKLSQLQESHQEAHRTLEQYDE 469
Cdd:TIGR04523 584 QEEKQE---LIDQKEKEKKDLIKEIEEKEK 610
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-459 |
2.48e-10 |
|
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: 64.27 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLE---QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQ--EDDLNRAKSELT----RLQQEETQLEQSIQAGKvQLETIIK 434
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELKnqekKLEEIQNQISQNNKIIS-QLNEQIS 345
|
170 180
....*....|....*....|....*.
gi 1953011266 435 SLKSTQDEINQARSKLS-QLQESHQE 459
Cdd:TIGR04523 346 QLKKELTNSESENSEKQrELEEKQNE 371
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-459 |
2.89e-10 |
|
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: 63.89 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQ---KSNEVQELQNDLDRETSSLQELEAQ-----KQDAQDRL----DE 354
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNkelkSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 355 MDQQKAKLRDMLSDVRQKcqdeTQMISSLKTQIqsqeSDLKSQEDDLNRAKSELTR-LQQEETQLE----------QSIQ 423
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQN----NKIISQLNEQI----SQLKKELTNSESENSEKQReLEEKQNEIEklkkenqsykQEIK 387
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 424 agkvQLETIIKSLKST---QDEINQAR-SKLSQLQESHQE 459
Cdd:TIGR04523 388 ----NLESQINDLESKiqnQEKLNQQKdEQIKKLQQEKEL 423
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
297-485 |
3.08e-10 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 63.17 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 297 AQLQrekySLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 376
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 377 TQMISSLKTQIQSQESDLKSQEDDLNRaKSELTRLQ----QEETQLEQSIQA-----GKVQLETIIKsLKSTQDEINQAR 447
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETIAE-LKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953011266 448 SKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADL 485
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGL 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
326-485 |
5.92e-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: 60.32 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 326 ELQnDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 405
Cdd:COG1579 11 DLQ-ELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 406 S--ELTRLQQEETQLEQSIQagkvQLEtiikslkstqDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLA 483
Cdd:COG1579 87 NnkEYEALQKEIESLKRRIS----DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
..
gi 1953011266 484 DL 485
Cdd:COG1579 153 EL 154
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
281-363 |
8.60e-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: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 281 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 360
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 1953011266 361 KLR 363
Cdd:COG1579 160 ELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
296-466 |
9.92e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 296 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQnDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDVRQk 372
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDvasAEREIAELEAELERLDASSDDLAA- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 373 cqdetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQ 452
Cdd:COG4913 690 ----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170
....*....|....
gi 1953011266 453 LQESHQEAHRTLEQ 466
Cdd:COG4913 760 GDAVERELRENLEE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-469 |
1.11e-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: 62.39 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL-------DEMDQQK 359
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkerDELEAQL 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSE------LTRLQQEETQLEQSIQAgkvqLETI- 432
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA----LEPVn 974
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 433 ---IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDE 469
Cdd:TIGR02169 975 mlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
288-471 |
1.83e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 61.00 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKSNEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 355
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 356 ---DQQKAKLRDMLSDVR---QKCQDETQMISslktqiQS---QESDLKSQ---EDDLNRAKSELTRLQQEETQLEQSIQ 423
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKeqnKELKEEIDRVK------QSytlNESELESVrqlEKQLESLEKQYDEITERIAEQEIAYS 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011266 424 AGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-481 |
2.13e-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: 61.24 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqLETIIKSLKSTQDEINQA 446
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA----SEERVRGGRAVEEVLKAS 519
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953011266 447 RS----KLSQLQeshqeahRTLEQYDEALDGAHGASLTN 481
Cdd:TIGR02169 520 IQgvhgTVAQLG-------SVGERYATAIEVAAGNRLNN 551
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
286-460 |
2.33e-09 |
|
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: 61.19 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 356
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSiqagkvqLETIIKSL 436
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170 180
....*....|....*....|....
gi 1953011266 437 KSTQDEINQARSKLSQLQESHQEA 460
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKES 671
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
287-472 |
2.50e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 59.55 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIR------EKEEAIRQKS-NEVQELQNDLDRETSSLQELEAQKQDAQDRLD------ 353
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRLAAEdfrqkyEDELNLRTSAeNDLVGLRKDLDEATLARVDLEAKIESLKEELAflkknh 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 354 --EMDQQKAKLRD-----------------MLSDVRQkcQDEtQMISSLKTQI----QSQESDLKSQ----EDDLNRAKS 406
Cdd:pfam00038 141 eeEVRELQAQVSDtqvnvemdaarkldltsALAEIRA--QYE-EIAAKNREEAeewyQSKLEELQQAaarnGDALRSAKE 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 407 ELT----RLQQEETQLeQSIQAGKVQLETIIKSLKSTQD-EINQARSKLS----QLQESHQEAHRTLEQYDEALD 472
Cdd:pfam00038 218 EITelrrTIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQELLN 291
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
287-475 |
2.56e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.15 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelaekrdELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQDETQM---ISSLKTQIQSQESDLKsQEDDLNRAKSEL-TRLQQEETQLEQsiqagKVQLETIIKS 435
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLrkeIERLEWRQQTEVLSPE-EEKELVEKIKELeKELEKAKKALEK-----NEKLKELRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1953011266 436 LKSTQDEINQARSKLSQLQESHQEAH-------RTLEQYDEALDGAH 475
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHeemielyKEADELRKEADELH 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
287-474 |
2.74e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 360
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 361 KLRDMLSDVRQKC-----QDET--QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 433
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 474
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
287-469 |
6.62e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 59.10 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEeaIRQKSNEVQELQNDLDRetsslQELEaqkqDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALLEN-----LELD----EAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 ---SDVRQKCQDETQMISSLKTQIQSQESDLKSqeddlnraksELTRLQQ------EETQLEQSIQAgkvQLETIIKSLK 437
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKE----------ELERVQQsytlneNELERVRGLEK---QLEELEKRYD 346
|
170 180 190
....*....|....*....|....*....|..
gi 1953011266 438 STQDEINQARSKLSQLQESHQEAHRTLEQYDE 469
Cdd:pfam06160 347 EIVERLEEKEVAYSELQEELEEILEQLEEIEE 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-460 |
7.59e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKysleQDIREKEEAIRQKSNEVQELQN------DLDRETSSLQELEAQKQD---AQDRLDEMDQ 357
Cdd:COG4913 617 AELAELEEELAEAEERL----EALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERldaSSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 358 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE--ETQLEQSIQAGKVQ--LETII 433
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERelRENLE 772
|
170 180
....*....|....*....|....*..
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQESHQEA 460
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
314-494 |
9.00e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 314 EEAIRqksnEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQMISSLKTQI 387
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 388 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqletiikslkSTQDEINQARSKLSQLQESHQEAHRTLEQY 467
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180
....*....|....*....|....*..
gi 1953011266 468 DEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAA 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
286-474 |
1.72e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKCQDEtqmissLKTQIQSQES------DLKSQEDDLnraKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST 439
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPfyneylELKDAEKEL---EREEKELKKLEEELDKAFE----ELAETEKRLEEL 645
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 440 QDEINQARSKLSqlQESHQEAHRTLEQYDEALDGA 474
Cdd:PRK03918 646 RKELEELEKKYS--EEEYEELREEYLELSRELAGL 678
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-472 |
2.06e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 341 LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD--ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL 418
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 419 EQSIQAGKVQLETIIKS--LKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:COG3206 246 RAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-445 |
2.16e-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: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKCQDETQMISSLKTQIQSQESD---------------------------------------------------- 393
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealenkieddeeearrrlkrlenkikelgpvnlaaieeyeelkeryd 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1953011266 394 -LKSQEDDLNRAKseltrlqqeeTQLEQSIQagkvQLETIIKS-LKSTQDEINQ 445
Cdd:TIGR02168 1004 fLTAQKEDLTEAK----------ETLEEAIE----EIDREARErFKDTFDQVNE 1043
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
288-475 |
2.21e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 55.14 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQksneVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVRQKCQD------ETQMISSLKTQIQSQESDLKSQE--DDLNRAKSELTRLQqeetQLEQSIQAGKVQLETIIKSLKS- 438
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHK----ELEEELEAHEPRLKSLNELAEEl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011266 439 ----TQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 475
Cdd:cd00176 173 leegHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
287-432 |
3.17e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.10 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKSNEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 357
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 358 QKAKLRDMLSDVRQKCQDetqmISSLkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI 432
Cdd:PRK12704 129 KEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAI 198
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-472 |
3.94e-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: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMdqqKAKLRDM 365
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENL---NGKKEEL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQdE 442
Cdd:TIGR02169 867 EEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-E 945
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011266 443 INQARSKLSQLQESHQEAHRTL-----------EQYDEALD 472
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIralepvnmlaiQEYEEVLK 986
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-487 |
4.75e-08 |
|
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: 55.93 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 343 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSI 422
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 423 QAGKVQL------------------------------------------ETIIKSLKSTQDEINQARSKLSQLQESHQEA 460
Cdd:COG4942 100 EAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180
....*....|....*....|....*..
gi 1953011266 461 HRTLEQYDEALDGAHGASLTNLADLSE 487
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEK 206
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
294-428 |
6.46e-08 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 51.87 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREKYSLEQDIREKEEAIrqksnevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 373
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 374 QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSeltRLQQEETQLEQSIQAGKVQ 428
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
299-470 |
7.46e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 299 LQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 363
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 ---------DMLSDVRQKC------QDETQMISSLKTQIQSQESDLKSQEDDLNRAkseltRLQQEETQLEQSIQAGKVQ 428
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011266 429 LETIIKSLKSTQDEINQARS--KLSQLQESHQEAHRTLEQYDEA 470
Cdd:COG4717 448 LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
286-455 |
9.91e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIrEKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLdemDQQKAKLRDM 365
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDI-EEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI---AQQAAKLQGS 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 -----LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE---QSIQAGKVQLETIIKSLK 437
Cdd:TIGR00606 819 dldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlQRRQQFEEQLVELSTEVQ 898
|
170
....*....|....*...
gi 1953011266 438 STQDEINQARSKLSQLQE 455
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLET 916
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-497 |
1.03e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQK 359
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEElqkerqdLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQ-----ESDLKSQEDDLNRA--KSELTRLQQEETQLEQSIQAGKVQLETI 432
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALseaeaEQALDELLKEANRNaeKEEELAEAEKLIESLPRELAEELLEAKD 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 433 IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGF 497
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
308-474 |
1.04e-07 |
|
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: 55.95 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 308 QDIREKEEAIRQksnEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 387
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 388 QSQESDLKSQEDDLN-----RAKSELTR------LQQEETQLEQSI------QAGKVQLETIIKSLKSTQDEinQARSKL 450
Cdd:pfam01576 267 RELEAQISELQEDLEseraaRNKAEKQRrdlgeeLEALKTELEDTLdttaaqQELRSKREQEVTELKKALEE--ETRSHE 344
|
170 180
....*....|....*....|....
gi 1953011266 451 SQLQESHQEAHRTLEQYDEALDGA 474
Cdd:pfam01576 345 AQLQEMRQKHTQALEELTEQLEQA 368
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
297-456 |
1.08e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 297 AQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 351
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS 421
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 422 IQagkvQLETIIKSLKSTQDEINQARSKLsQLQES 456
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEI-QSQEQ 184
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
282-454 |
1.09e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 282 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKSNEVQELQNDLDRET-SSLQELEAQKQ---------- 346
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneyl 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 347 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQEETQLEQSIQ 423
Cdd:PRK03918 606 elkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|....
gi 1953011266 424 AGKVQLETIIKS---LKSTQDEINQARSKLSQLQ 454
Cdd:PRK03918 684 ELEKRREEIKKTlekLKEELEEREKAKKELEKLE 717
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-448 |
1.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQEL--------------------------------------- 327
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsyldvllgsesfsdfldrlsalskiada 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 328 QNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS 406
Cdd:COG3883 131 DADLLEELKADKaELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953011266 407 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARS 448
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
288-462 |
1.49e-07 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 54.70 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKSNEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 351
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 ---LD-----------------EMDQQKAKLR---DMLSDVRQKCqdetqmISSLK---TQIQSQEsdlKSQEDDLNRAK 405
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQET------IAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 406 SELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHR 462
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
282-478 |
1.50e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.96 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 282 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 357
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 358 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQEsdlksqeddlnrAKSELTRLQQEETQLEQSIQAGKVQLETII---- 433
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRakle 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGAS 478
Cdd:COG5185 510 RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-493 |
1.55e-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: 55.34 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQksneVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKstqdEINQAR 447
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVER 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011266 448 SKLSQLQESHQEAHRTLEQYdealDGAHGASLTNLADLSEGVSLAE 493
Cdd:COG3096 647 DELAARKQALESQIERLSQP----GGAEDPRLLALAERLGGVLLSE 688
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
290-462 |
1.66e-07 |
|
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: 54.52 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 369
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 370 RQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSK 449
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERKVEGLGEE 259
|
170
....*....|....*..
gi 1953011266 450 LS----QLQESHQEAHR 462
Cdd:pfam07888 260 LSsmaaQRDRTQAELHQ 276
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
287-460 |
1.94e-07 |
|
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: 55.12 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAqkqdaqdRLDEMDQQKAKLRDML 366
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA-------RVSDLELEKVKLVNAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtRLQQEEtqLEQSIQAGKVQLetiikslKSTQDEINQA 446
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF-RNKSEE--METTTNKLKMQL-------KSAQSELEQT 711
|
170
....*....|....
gi 1953011266 447 RSKLSQLQESHQEA 460
Cdd:pfam15921 712 RNTLKSMEGSDGHA 725
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
290-459 |
2.07e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 358
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 KAKLRDMLSDVRQK--CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETiiKSL 436
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL--ADP 436
|
170 180
....*....|....*....|...
gi 1953011266 437 KSTQDEINQARSKLSQLQESHQE 459
Cdd:pfam05557 437 SYSKEEVDSLRRKLETLELERQR 459
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-487 |
2.20e-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: 54.96 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQ-------LQREKYSLEQDIREK---------EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQ----- 346
Cdd:COG3096 793 ERDELAEQYAKasfdvqkLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeq 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 347 -----------------DAQDRLDEMDQQKAKLRDMLSDVRQKCqdetQMISSLKTQIQSQESDLKSQED---DLNRAKS 406
Cdd:COG3096 873 lqllnkllpqanlladeTLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLVAVLQSDPEQFEQlqaDYLQAKE 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 407 ELTRLQQEETQLEQSIQ-------AGKVQL--------ETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLeqydEAL 471
Cdd:COG3096 949 QQRRLKQQIFALSEVVQrrphfsyEDAVGLlgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL----ASL 1024
|
250
....*....|....*.
gi 1953011266 472 DGAHGASLTNLADLSE 487
Cdd:COG3096 1025 KSSRDAKQQTLQELEQ 1040
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
294-494 |
2.29e-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: 54.96 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREKYSLEQDiREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 354
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 355 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL------------NRAKSELTRLQQE-------E 415
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 416 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES-----------------------HQEAHRTLEQYDEALD 472
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGwcavlrlardndverrlhrrelaYLSADELRSMSDKALG 1155
|
250 260
....*....|....*....|....*..
gi 1953011266 473 GAHGA-----SLTNLADLSEGVSLAER 494
Cdd:COG3096 1156 ALRLAvadneHLRDALRLSEDPRRPER 1182
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
287-475 |
2.49e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDiREKEEAIRQKSNEVQELQndldRETSSLQELEAQKQDAQDRLDeMDQQKAKL---R 363
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQLR----ARIEELRAQEAVLEETQERIN-RARKAAPLaahI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ------SIQAGKVQLETIIK 434
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSkmrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatSIREISCQQHTLTQ 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011266 435 SLKSTQ-------DEINQARSKLSQLQ-ESHQEAHRTLEQYDEALDGAH 475
Cdd:TIGR00618 380 HIHTLQqqkttltQKLQSLCKELDILQrEQATIDTRTSAFRDLQGQLAH 428
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-472 |
2.57e-07 |
|
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: 54.74 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 362
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 RDMLSDVRQKCQDETQMI--------------SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE----QSIQA 424
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNA 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 425 GKVQLETiIKSLKSTQD----EINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:pfam15921 641 GSERLRA-VKDIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
278-462 |
2.70e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 278 LGSGEFTGVKELDDISQEIAQLQRekysLEQDIREKEEAIRQKSNEvQELQNDLDR-ETSSLQELEA---QKQDAQDRLD 353
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELKE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 354 EMDQQKAKLRDMLSDVRQKCQDETQmiSSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS--IQAGKVQLET 431
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEE 480
|
170 180 190
....*....|....*....|....*....|....
gi 1953011266 432 IIKSLKSTQDE---INQARSKLSQLQESHQEAHR 462
Cdd:COG4717 481 LKAELRELAEEwaaLKLALELLEEAREEYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-472 |
2.91e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 305 SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELeaqkqdaQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLK 384
Cdd:TIGR02169 643 TLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRL-------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 385 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQEShqEAHRTL 464
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRI 793
|
....*...
gi 1953011266 465 EQYDEALD 472
Cdd:TIGR02169 794 PEIQAELS 801
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-499 |
3.78e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 330 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL-NRAKS-- 406
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 407 ----------------------------------------ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 447 RSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGFGA 499
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
287-450 |
4.11e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 349
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 350 DRLDEMDQQ--KAK---------LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE--- 415
Cdd:pfam05667 415 QRLVELAGQweKHRvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011266 416 --TQ--LE--QSIQAGKVQLETIIKSLKSTQDEINQARSKL 450
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
287-462 |
4.51e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 356
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 QQKAKLRDMLSDVRqkcQDETQMISSLKTQIQSqESDLKSQEDDLNR----AKSELTRL---QQEETQLEQSiqagkvQL 429
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRksleGNTQLQDLlqkQRDYLTARIQ------RL 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011266 430 ETIIKSLkstQDEINQARSKLSQLQ----ESHQEAHR 462
Cdd:PRK11281 240 EHQLQLL---QEAINSKRLTLSEKTvqeaQSQDEAAR 273
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
289-475 |
4.56e-07 |
|
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: 53.69 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKSNEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 360
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 361 KLRDMLSDVRQKCQDEtqmisslKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvqLETIIKSLKSTQ 440
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREE----QEAANAEVERLQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 441 DEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 475
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
358-466 |
5.00e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 358 QKAKLRdmLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE----ETQLEQS---IQAGKVQLE 430
Cdd:COG4372 9 GKARLS--LFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseLEQLEEELE 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 1953011266 431 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
317-469 |
5.32e-07 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 49.71 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 317 IRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDemdqqkaklrdmlsDVRQKCQDETQMISSlktQIQSQESDLKs 396
Cdd:pfam07321 5 LRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQ--------------DYRAWRPQEEQRLYA---EIQGKLVLLK- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 397 qedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR---SKLSQLQESHQEAHRTLEQYDE 469
Cdd:pfam07321 67 ---ELEKVKQQVALLRENEADLEKQVAEARQQLEAEREALRQARQALAEARravEKFAELVRLVQAEELRQQERQE 139
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-486 |
5.51e-07 |
|
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: 53.64 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 439
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1953011266 440 QDEINQARSKLSQLQE---SHQEAHRTLEQYDEALDGAHGASLTNLADLS 486
Cdd:pfam01576 179 SKLKNKHEAMISDLEErlkKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
286-459 |
7.05e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.71 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDdisQEIAQLQREKYSLEQDIREKEEAI---RQKSNE-VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:PHA02562 176 IRELN---QQIQTLDMKIDHIQQQIKTYNKNIeeqRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDMLSDVRQK--------------------------C----QDETQMISSLKT---QIQSQESDLKSQEDDLNRAKSEL 408
Cdd:PHA02562 253 PSAALNKLNTAaakikskieqfqkvikmyekggvcptCtqqiSEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 409 TRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA-------RSKLSQLQESHQE 459
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvdnAEELAKLQDELDK 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-483 |
8.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 366
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQleqsiqagkvqletiikSLKSTQDEINQA 446
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA-----------------DLDADLESLPEY 817
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011266 447 RSKLSQLQESHQEAHRtlEQYDEALDGAHGASLTNLA 483
Cdd:COG4913 818 LALLDRLEEDGLPEYE--ERFKELLNENSIEFVADLL 852
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-469 |
8.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKS--NEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 364
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 365 MLSDVRQKCQDETQMIsSLKTQIQSQESDLK-----------SQEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETII 433
Cdd:PRK03918 544 LKKELEKLEELKKKLA-ELEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDAEK----ELEREE 618
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ----YDE 469
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEElekkYSE 658
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-480 |
1.00e-06 |
|
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: 52.48 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 363
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQEDDLNRAKSE----LTRLQQEETQLEQSIQAGKVQLETIIKSLKST 439
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011266 440 QDEINQARSKLSQLQESHQEAHRTLEQY--------DEALDGAHGASLT 480
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAqqerdelaDEIASGASGKSAL 880
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
294-493 |
1.25e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 373
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 374 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQqeetqlEQS--IQAGKVQLETIIKSLKSTQDEINQARSKLS 451
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLR------EQSgeEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953011266 452 QLQEShqeahrtLEQYDEALDGAHGASLTNLADLSE---GVSLAE 493
Cdd:PRK04863 652 ARKQA-------LDEEIERLSQPGGSEDPRLNALAErfgGVLLSE 689
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
257-474 |
1.34e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 257 LSPDMVPPSERGTpipDGSSCLGSGEFTGVKELDDISQEIAQLQREkyslEQDIREKEEAIRQKSNEVQE----LQNDLD 332
Cdd:TIGR00618 522 NPGPLTRRMQRGE---QTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCDNRSKEdipnLQNITV 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 333 R---ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmissLKTQIQSQESDLKSQEDdlnRAKSELT 409
Cdd:TIGR00618 595 RlqdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSI 667
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 410 RLQQEetQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGA 474
Cdd:TIGR00618 668 RVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-459 |
1.49e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIaqlqREKYSLEQDIREKEEAIRQKSNEVQELQ---NDLDRETSSLQ----ELEAQKQDAQDRLDEMDQQK 359
Cdd:PRK03918 200 KELEEVLREI----NEISSELPELREELEKLEKEVKELEELKeeiEELEKELESLEgskrKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVR--QKCQDETQMISSLKTQIqsqesdlksqEDDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLK 437
Cdd:PRK03918 276 EELEEKVKELKelKEKAEEYIKLSEFYEEY----------LDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLE 341
|
170 180
....*....|....*....|..
gi 1953011266 438 STQDEINQARSKLSQLQESHQE 459
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHEL 363
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
276-454 |
1.57e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.75 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 276 SCLgSGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELE---AQKQ----- 346
Cdd:pfam10174 376 STL-AGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKEriier 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 347 -------DAQDRLDEMDQQKAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESD-------LKSQEDDLNRAKSELT 409
Cdd:pfam10174 455 lkeqrerEDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKEECS 534
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 410 RLQ--------QEET------------QLEQSIQ-----AGKVQ--LETIIKSLKSTQDEINQARSKLSQLQ 454
Cdd:pfam10174 535 KLEnqlkkahnAEEAvrtnpeindrirLLEQEVArykeeSGKAQaeVERLLGILREVENEKNDKDKKIAELE 606
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
289-466 |
1.60e-06 |
|
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: 52.10 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLEQDIREKEEairqksnEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQKAK 361
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALES-------ENAELQAELRTLQQAKQDsehkrkkLEGQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDMLSdvrqKCQDETQMISSLktqiqsqesdlksqeddLNRAKSELTRLQQEETQLEQSIQAGKVQL--ETIIK----- 434
Cdd:pfam01576 431 LAEKLS----KLQSELESVSSL-----------------LNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQKlnlst 489
|
170 180 190
....*....|....*....|....*....|..
gi 1953011266 435 SLKSTQDEinqaRSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam01576 490 RLRQLEDE----RNSLQEQLEEEEEAKRNVER 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-471 |
1.79e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQ---DRLDEMDQQKAKLR 363
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISSLKTQI---QSQESDLKSQEDD----------LNRAKSELTRLQQEETQLEQSIQAgkvqLE 430
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLSRLEEEING----IE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953011266 431 TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
286-485 |
2.03e-06 |
|
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: 51.76 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 358
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 -------------KAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlQQEETQLEQSI 422
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 423 QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHrtLEQYDEALDGAHGASLTNLADL 485
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLK--EDANSEQAQGSIGERLAQLEDL 898
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
300-413 |
2.17e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 300 QREKYSLEQDIREKEEAIRQKSNEVQELqndldretsslqelEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDE--- 376
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERL--------------EAEVEELEAELEEKDERIERLERELSEARSEERREirk 463
|
90 100 110
....*....|....*....|....*....|....*..
gi 1953011266 377 TQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ 413
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-405 |
2.22e-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: 50.92 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREkysLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 368
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 1953011266 369 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 405
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
288-472 |
2.61e-06 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 50.34 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL---QELE--------AQKQDAQD---RLD 353
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAewkLELErvlpqlkvTIKADAKDwraHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 354 EMDQQKAKLRDMLSDVRQKcqdetqmisslktqiqsqesdLKSQEDDLNRAkseLTRLQQEETQLEQsiqagkvQLETII 433
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:pfam10498 275 QEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELE 313
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
285-475 |
2.98e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 285 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ---NDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDMLSDVRQKCQDETQMISSLKTQ----IQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVqletiiKSLK 437
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD------DYLK 973
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953011266 438 STQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 475
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
294-472 |
3.06e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRE-TSSLQELEAQKQDA------QDRLDEMDQQKAKLR 363
Cdd:TIGR00618 462 QESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISSLKTQIQsqesdlksqeddlnrakseltRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 443
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQ---------------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
170 180 190
....*....|....*....|....*....|
gi 1953011266 444 N-QARSKLSQLQESHQEahrtLEQYDEALD 472
Cdd:TIGR00618 601 EkLSEAEDMLACEQHAL----LRKLQPEQD 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-456 |
3.34e-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: 50.83 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 313 KEEAIRQ--KSNE----VQELQNDLDRetsSLQELEAQKQDAQ------------------DRLDEMDQQKAKLRDMLSD 368
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELER---QLKSLERQAEKAErykelkaelrelelallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 369 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARS 448
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
....*...
gi 1953011266 449 KLSQLQES 456
Cdd:TIGR02168 331 KLDELAEE 338
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
285-445 |
4.03e-06 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 49.85 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 285 GVKEL-----DDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKSNEV 324
Cdd:pfam03148 130 GIQELlqrtlEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 325 -----QELQN--DLdRET--SSLQ----ELEAQKQDA----QDRLDEMDQQKAKLRDMLsdvrQKCQDEtqmISSLKTQI 387
Cdd:pfam03148 210 ieraeKERAAsaQL-RELidSILEqtanDLRAQADAVnfalRKRIEETEDAKNKLEWQL----KKTLQE---IAELEKNI 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 388 QSQESDLKSQEDDL--------NRAK---SELTR------LQQEETQLEQSIQAGKVQL---ETIIKSLKSTQDEINQ 445
Cdd:pfam03148 282 EALEKAIRDKEAPLklaqtrleNRTYrpnVELCRdeaqygLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-472 |
4.35e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 343 AQKQDAQDRLDEMDQQKAKLRDMLSDVR-------------------QKCQDETQMISSLKtQIQSQESDLKSQEDDLNR 403
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGELErqleplerqaekaeryrelKEELKELEAELLLL-KLRELEAELEELEAELEE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 404 AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
288-470 |
4.64e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLdreTSSLQELEAQKQDAQDRLDE-MDQQKAKLR 363
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCqtlLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDALNQSLKElMHQARTVLK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMIsslktQIQSQESDLKSQEDDLNRAKSELT-RLQQEETQLEQSI----QAGKVQLETIIKSLKS 438
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAAL-----QTGAELSHLAAEIQFFNRLREEDThLLKTLEAEIGQEIpsdeDILNLQCETLVQEEEQ 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011266 439 TQDEINQARSKL--------------SQLQESHQEAHRTLEQYDEA 470
Cdd:TIGR00618 833 FLSRLEEKSATLgeithqllkyeecsKQLAQLTQEQAKIIQLSDKL 878
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
305-494 |
4.93e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 305 SLEQDIREKEEAIRQksnEVQELQNDLDRETSSL-------QELEAQKQDAQDRLDEMdQQKAKL----------RDMLS 367
Cdd:COG1842 16 ALLDKAEDPEKMLDQ---AIRDMEEDLVEARQALaqvianqKRLERQLEELEAEAEKW-EEKARLalekgredlaREALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DvRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQlETIIKSLKSTQDEinQAR 447
Cdd:COG1842 92 R-KAELEAQ---AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEALSGIDSD--DAT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011266 448 SKLSQLQESHQEahrtLEQYDEALDG-AHGASLTN-LADLSEGVSLAER 494
Cdd:COG1842 165 SALERMEEKIEE----MEARAEAAAElAAGDSLDDeLAELEADSEVEDE 209
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
385-472 |
4.97e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 385 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 464
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
....*...
gi 1953011266 465 EQYDEALD 472
Cdd:COG4372 104 ESLQEEAE 111
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
314-487 |
5.44e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.45 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 314 EEAIRQKSNEVQ--ELQNDLDRETSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQMIS 381
Cdd:pfam12795 3 DELEKAKLDEAAkkKLLQDLQQALSLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 382 SLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI---IKSLKSTQDEINQARSKLSQLQESHQ 458
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrnrLNGPAPPGEPLSEAQRWALQAELAAL 161
|
170 180
....*....|....*....|....*....
gi 1953011266 459 EAhrTLEQYDEALdgahgASLTNLADLSE 487
Cdd:pfam12795 162 KA--QIDMLEQEL-----LSNNNRQDLLK 183
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
284-490 |
5.54e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 284 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 D------MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRA-KSELTRLQQEETQLEQSIQAGKVQLETIIKSL 436
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 437 KSTQDEINQAR-----SKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVS 490
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE 502
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
286-414 |
5.79e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQrekySLEQDIREKEEAIRQKSNEVQEL--------QNDLDRETSSLQELEAQKQDAQDRLDEMDQ 357
Cdd:smart00787 157 KEDYKLLMKELELLN----SIKPKLRDRKDALEEELRQLKQLedeledcdPTELDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 358 QKAKLRDMLSDVRQKCQDetqmissLKTQIQSQESDLKS----QEDDLNRAKSELTRLQQE 414
Cdd:smart00787 233 ELQELESKIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
288-472 |
6.14e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSL----------------QELEAQKQDAQDR 351
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehalsirvlpKELLASRQLALQK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 424
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011266 425 GKVQLETI-IKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:TIGR00618 765 NNNEEVTAaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-470 |
6.86e-06 |
|
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: 49.63 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEaqkqdaqDRLDEMDQQKAKlrdml 366
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-------DELNKDDFELKK----- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 sdvrqkcqdetqmiSSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:TIGR04523 557 --------------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
170 180
....*....|....*....|....*..
gi 1953011266 447 R---SKLSQLQESHQEAHRTLEQYDEA 470
Cdd:TIGR04523 623 KkenEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
296-466 |
7.04e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 296 IAQLQREKYSLEQDiREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 356
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN----RAKSEL-TRLQQEETQLEQSIQAGKVQLET 431
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAeERARARRDELHARLSANRSRRNQ 1078
|
170 180 190
....*....|....*....|....*....|....*
gi 1953011266 432 IIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
385-455 |
7.34e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 7.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 385 TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQE 455
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
286-414 |
7.65e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.65 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 365
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1953011266 366 lsdvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE 414
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-477 |
8.60e-06 |
|
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: 49.79 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------SNEVQELQNDLDRETSSLQEL 341
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 342 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEE 415
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 416 TQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGA 477
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
287-478 |
8.75e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQ-------------------KC----------------QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSeltrL 411
Cdd:PRK02224 429 AELEAtlrtarerveeaealleagKCpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED----L 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 412 QQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGAS 478
Cdd:PRK02224 505 VEAEDRIERLEE----RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
287-391 |
1.07e-05 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 45.25 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKKE---QELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|....*
gi 1953011266 367 SDVRQKcqdetqmISSLKTQIQSQE 391
Cdd:pfam13863 83 KKLTAQ-------IEELKSEISKLE 100
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
287-467 |
1.08e-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: 49.33 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ----QEETQLEQsiqagKVQLETIIKSLKSTQDE 442
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 1953011266 443 IN---QARSKLSQLQESHQEAHRTLEQY 467
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
287-470 |
1.08e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQeIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRET-SSLQELEAQKQDA----------------- 348
Cdd:pfam02463 156 LEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKeQAKKALEYYQLKEkleleeeyllyldylkl 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 349 -QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV 427
Cdd:pfam02463 235 nEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011266 428 QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEA 470
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
306-459 |
1.20e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 49.08 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIReKEEAIRQKSNEV-QELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET 377
Cdd:pfam09726 400 LEQDIK-KLKAELQASRQTeQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQ 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 378 QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQ-LEQSIQagkvQLETIIKSL----KSTQDEINQARSK--- 449
Cdd:pfam09726 479 EARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKR----ELESEIKKLthdiKLKEEQIRELEIKvqe 554
|
170
....*....|
gi 1953011266 450 LSQLQESHQE 459
Cdd:pfam09726 555 LRKYKESEKD 564
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
323-458 |
1.31e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.09 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 323 EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmisslktqiqSQESDLKSQEDDLN 402
Cdd:smart00787 152 NLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQEIM 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 403 RAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQAR----SKLSQLQESHQ 458
Cdd:smart00787 222 IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLK 281
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
289-424 |
1.32e-05 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 46.53 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLeqdiREKEEAIrqkSNEVQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 368
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSEL---SERLQQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 369 VRQKCQDET-----QMISSLKTQIQSQESDLK-----SQEDDLNRA-KSELTRLQQeetQLEQSIQA 424
Cdd:pfam16043 81 VSRDQFDETleelnQMLQELLDKLEGQEDAWKkaletLSEELDTKLdRLELDPLKE---LLERRIKA 144
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
194-267 |
1.60e-05 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 44.29 E-value: 1.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 194 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 267
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
286-474 |
1.60e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKSNEVQELQNDLDRetsslqeLEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERREDLEELIAERRETIEEKRER 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKvQLETIIKSLKSTQDEINQ 445
Cdd:PRK02224 539 AEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953011266 446 ARSKLSQLQESHQEAHRTLE-------QYDEALDGA 474
Cdd:PRK02224 611 LREKREALAELNDERRERLAekrerkrELEAEFDEA 646
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
338-456 |
1.72e-05 |
|
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: 48.58 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 338 LQELEAQKQDAQDRLDEMDQ----QKAKLRDMLSDVRQKCQdETQMISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQ 413
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElhekQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES--QSQEDLRNQLQNTVHELEA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953011266 414 EETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 456
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEA 199
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
297-434 |
1.87e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.42 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 297 AQLQREKYslEQDIREKEEAIRQKSNEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 376
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 377 TQMIsslktQIQSQESDLKSQEDD----LNRAKseltRLQQEetqlEQSIQAGKVQLETIIK 434
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
338-470 |
1.93e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.95 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 338 LQELEAQKQDAQDRLDEMDQQKAKLRDmlsdVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAkseLTRLQQEETQ 417
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEK----RAEKAEAE---VAALNRRIQLLEEELERTEERLAEA---LEKLEEAEKA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 418 LEQSIQAGKVqLETiikslKSTQDEiNQARSKLSQLQESHQEAHRTLEQYDEA 470
Cdd:pfam00261 73 ADESERGRKV-LEN-----RALKDE-EKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
300-420 |
2.09e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 44.52 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 300 QREKYSLEQDIREKEEAIRQKsnevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQM 379
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953011266 380 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE--ETQLEQ 420
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
338-466 |
2.25e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.32 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 338 LQELEAQKQDAQDRLDEMDQQKAKLRD---MLSDVRQKCQDETQmisSLKTQIQSqesdLKSQEDDLNRAK-SELTRLQQ 413
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKeleLLNSIKPKLRDRKD---ALEEELRQ----LKQLEDELEDCDpTELDRAKE 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 414 EETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-469 |
2.43e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQdirEKEEAIRQKSNevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 363
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQ---EKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCQDETQMISSLKTQIQSQESdlksqeddlnRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEI 443
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKER----------LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
170 180
....*....|....*....|....*....
gi 1953011266 444 NQARSKLSQLQESHQE---AHRTLEQYDE 469
Cdd:TIGR00606 464 QQLEGSSDRILELDQElrkAERELSKAEK 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
298-455 |
2.73e-05 |
|
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: 47.81 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 298 QLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDaqdrLDEMDQQKAKLRDMLSDV--RQKCQD 375
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD----FEEASGKKIYEHDSMSTMhfRSLGSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 376 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTR-----LQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKL 450
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
....*
gi 1953011266 451 SQLQE 455
Cdd:pfam15921 302 EIIQE 306
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
287-455 |
2.90e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 366
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 sdvrqkcqdetQMISSLKTQIQSQESDLKSQEDDLNrakselTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*....
gi 1953011266 447 RSKLSQLQE 455
Cdd:pfam15905 320 EQEHQKLQQ 328
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
293-460 |
2.94e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 46.64 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 293 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 372
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 373 CQDETQ----------MISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEqsiqagkvqletiikslKSTQDE 442
Cdd:pfam06008 119 DLSRMLaeaqrmlgeiRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA-----------------NALRDS 181
|
170
....*....|....*...
gi 1953011266 443 INQARSKLSQLQESHQEA 460
Cdd:pfam06008 182 LAEYEAKLSDLRELLREA 199
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
286-471 |
2.96e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRL 352
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 353 DEMdQQKAKLrdmlsdvrqkcqdeTQMISSLKTQIQSQESDLKSQE-DDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 431
Cdd:PRK03918 355 EEL-EERHEL--------------YEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011266 432 IIKSLKSTQDEINQARSKL----SQLQESHQEahRTLEQYDEAL 471
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKCpvcgRELTEEHRK--ELLEEYTAEL 461
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
356-493 |
3.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 356 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLE----- 430
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 431 --------------------------------------TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|.
gi 1953011266 473 GAHGASLTNLADLSEGVSLAE 493
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAE 195
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
288-469 |
3.14e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ-LALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DV---RQKCQDETQMISSLKTQIQSQES---------------DLKSQEDDLNRAKSELTRLQQ---EETQLEQSIQAGK 426
Cdd:TIGR00618 712 HIeeyDREFNEIENASSSLGSDLAAREDalnqslkelmhqartVLKARTEAHFNNNEEVTAALQtgaELSHLAAEIQFFN 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 427 VQLETIIKSLKSTQDEINQAR-------------------SKLSQLQESHQEAH---RTLEQYDE 469
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIpsdedilnlqcetlvqeeeQFLSRLEEKSATLGeitHQLLKYEE 856
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
307-431 |
3.15e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 307 EQDIREKEEAIRQKSNEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSD----VRQKc 373
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPnspqVRQL- 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 374 qdETQmISSLKTQIQSQESDL--KSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET 431
Cdd:COG3524 255 --RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
288-495 |
3.32e-05 |
|
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: 47.81 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEET---------QLEQSIQAGKVQ-LETIIKSL 436
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlRRELDDRNMEVQrLEALLKAM 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 437 KS-TQDEI----------NQARSKLSQLQ---ESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERG 495
Cdd:pfam15921 439 KSeCQGQMerqmaaiqgkNESLEKVSSLTaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-472 |
3.39e-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: 47.71 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQ---DETQMISSLKTQIQSQESDLKSQEDDLNraksELTRLQQEEtqleqsiqaGKVQLETIIKSLKSTQDEI 443
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDII----ELMKDWLKE---------LSLHYKKYITRMIRIKDLP 707
|
170 180
....*....|....*....|....*....
gi 1953011266 444 nqarsKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:TIGR04523 708 -----KLEEKYKEIEKELKKLDEFSKELE 731
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
287-451 |
3.45e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.83 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQKcqdetqmISSLKTQIQsqesDLKSQEDDLnrakseLTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEIN- 444
Cdd:pfam04012 113 VEQLRKQ-------LAALETKIQ----QLKAKKNLL------KARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIEe 175
|
....*...
gi 1953011266 445 -QARSKLS 451
Cdd:pfam04012 176 rEARADAA 183
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
308-455 |
3.55e-05 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family consists of the coiled-coil (alpha) domain of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). STAT3 continuously shuttles between nuclear and cytoplasmic compartments. The coiled-coil domain (CCD) of STAT3 appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the STAT3 CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 in the testis, and importin-alpha6 NLS adapters in most cells. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment.
Pssm-ID: 341078 [Multi-domain] Cd Length: 180 Bit Score: 45.37 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 308 QDIREKEEAIRQKSNEVQELQNDLDRETSSLqeleaqKQDAQDRLDEMDQQKAklrdmlsdVRQKCQDETQMISSLKTQI 387
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTL------KSQGDMQDLNGNNQSV--------TRQKMQQLEQMLTALDQMR 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 388 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQ--AGKV-----QLETIIKSLKSTQDEINQARSKLSQLQE 455
Cdd:cd16853 77 RQIVSELAGLLSAMEYVQKNLTDEELADWKRRQQIAciGGPPnicldRLENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
336-455 |
3.56e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.17 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 336 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISslkTQIQSQESDLKSqeddLNRAKSELTRLQQEE 415
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1953011266 416 TQLEQSIQAGKVQLETIIKSLKST----QDEINQARSKLSQLQE 455
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNE 117
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
306-453 |
3.84e-05 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 45.87 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVRQKCQDETQMISSLKT 385
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 386 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLET--IIKSLKSTQDEINQARSKLSQL 453
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAafLQADLKAAKADWNQLYEQAKSL 224
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
296-465 |
3.84e-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: 47.41 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 296 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqqkakLRDMLSDvRQKCQD 375
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE-------LKKILAE-DEKLLD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 376 ETQMISSLKTQIQSQESD----LKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETiiKSLKSTQDEINQARSKLS 451
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK--EKLKNIELTAHCDKLLLE 500
|
170
....*....|....
gi 1953011266 452 QLQESHQEAHRTLE 465
Cdd:pfam05483 501 NKELTQEASDMTLE 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
284-469 |
3.94e-05 |
|
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: 47.48 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 284 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKSNEVQELQNDLDRETSS-------------- 337
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 338 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQ 417
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 418 LEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDE 469
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLND 910
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
298-472 |
4.56e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.51 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 298 QLQREKYSLEQDIREKEEAIRQKSNEvqelqndldretSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlSDVRQKCQDET 377
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG------------DDLESVEALLKKHEALEAELAAHEERV----EALNELGEQLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 378 QMISSLKTQIQSQESDLKSQEDDLNRAKSE-LTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 456
Cdd:cd00176 68 EEGHPDAEEIQERLEELNQRWEELRELAEErRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK 147
|
170
....*....|....*.
gi 1953011266 457 HQEAHRTLEQYDEALD 472
Cdd:cd00176 148 HKELEEELEAHEPRLK 163
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-471 |
4.67e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQLETIIKSlkstqDEIN 444
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIrdEKKGLGRTIELKKEILE-----KKQE 454
|
170 180
....*....|....*....|....*..
gi 1953011266 445 QARSKLSQLQESHQEAHRTLEQyDEAL 471
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILEL-DQEL 480
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
285-380 |
4.70e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.11 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 285 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 363
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 1953011266 364 DMLSDVRQKCQDETQMI 380
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-496 |
4.72e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 396 SQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 475
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100
....*....|....*....|.
gi 1953011266 476 GASLTNLADLSEGVSLAERGG 496
Cdd:COG4942 97 AELEAQKEELAELLRALYRLG 117
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
291-465 |
5.16e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREKYSLeqdiREK-EEAIRQKSNEVQELqndLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 369
Cdd:pfam05622 279 EIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 370 RQKCQDEtqmiSSLKtqiqsqeSDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQ-LETIIKSLKSTQDEINQARS 448
Cdd:pfam05622 352 GSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEE 420
|
170
....*....|....*..
gi 1953011266 449 KLSQLQESHQEAHRTLE 465
Cdd:pfam05622 421 RYKKYVEKAKSVIKTLD 437
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
284-476 |
5.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 284 TGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA--- 360
Cdd:PRK02224 509 DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 361 -------KLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL---------TRLQQEETQLEQSIQA 424
Cdd:PRK02224 586 eriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeariEEAREDKERAEEYLEQ 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 425 GKVQLETIIKSLKSTQDEINQARSKLSQLqESHQEAHRTLEQYDEALDGAHG 476
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEEL-EELRERREALENRVEALEALYD 715
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
287-460 |
5.36e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKSNEVQ------ELQNDLDRETSSL-QELEAQKQ--DAQDRLDE 354
Cdd:COG1340 85 EKLNELREELDELRKELAELNKaggSIDKLRKEIERLEWRQQtevlspEEEKELVEKIKELeKELEKAKKalEKNEKLKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 355 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqesdLKSQEDDLNR----AKSELTRLQQEETQLEQSIQAGKVQLE 430
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRKeadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
170 180 190
....*....|....*....|....*....|..
gi 1953011266 431 TIIKSLKSTQDEINQARSKLSQ--LQESHQEA 460
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEI 272
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
298-459 |
5.56e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 298 QLQREKYSLEQdIREKEEAIRQKsnEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLRdmlsdvRQKCQD 375
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKLE------LEKEKR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 376 ETQMISSLKTQIQSQESDLKSQ---EDDLNR--------------AKSELTRLQQEETQLEQSIQAGKVQLETIIKSL-- 436
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQamiEEERKRkllekemeerqkaiYEEERRREAEEERRKQQEMEERRRIQEQMRKATee 564
|
170 180
....*....|....*....|...
gi 1953011266 437 KSTQDEINQARSKLSQLQESHQE 459
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEKA 587
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
288-471 |
5.62e-05 |
|
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: 47.09 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEE---------------------AIRQKSNEVQELQNDLDRETSSL-------- 338
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEelqaalarleeetaqknnalkKIRELEAQISELQEDLESERAARnkaekqrr 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 339 ---QELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSEL 408
Cdd:pfam01576 296 dlgEELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKANL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 409 trlqqEETQleQSIQAGKVQLETIIKSLKSTQDEINQARSKL-SQLQE---SHQEAHRTLEQYDEAL 471
Cdd:pfam01576 376 -----EKAK--QALESENAELQAELRTLQQAKQDSEHKRKKLeGQLQElqaRLSESERQRAELAEKL 435
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
275-414 |
6.02e-05 |
|
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: 46.71 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 275 SSCLGSGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDR 351
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 352 LDEMdqqKAKLRDMLSDVRQKCQDETQMISSLKTQIQsQESDLKSQEDDLNRAKselTRLQQE 414
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLEALEEGKKRLQRELEALTQ-QLEEKAAAYDKLEKTK---NRLQQE 581
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
290-458 |
7.91e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKySLEQDirekEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 369
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 370 RQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQqeeTQLEQ---SIQAGKVQLETIIKSLKSTQDEINQA 446
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ---TQPERaqaALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170
....*....|..
gi 1953011266 447 RSKLSQLQESHQ 458
Cdd:PRK11281 190 RPSQRVLLQAEQ 201
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
389-459 |
7.93e-05 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 42.17 E-value: 7.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 389 SQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQE 459
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
335-468 |
7.94e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.49 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 335 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK------ 405
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapig 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 406 --------SELTRLQQEETQLEQSI-QAGKVQLE---TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYD 468
Cdd:pfam00529 137 gisreslvTAGALVAQAQANLLATVaQLDQIYVQitqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
323-517 |
8.06e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.44 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 323 EVQELQNDLDRETSSlQELEAQKQDAQDRLDEMdQQKAKlrdmlsDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN 402
Cdd:cd22656 95 EILELIDDLADATDD-EELEEAKKTIKALLDDL-LKEAK------KYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 403 RA--KSELTRLQQEETQLEQSIQAgkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH---GA 477
Cdd:cd22656 167 DLltDEGGAIARKEIKDLQKELEK---LNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLaliGP 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 478 SLTNLADLsegvslaeRGGFGAMDDPFKNKALLFSNNAQE 517
Cdd:cd22656 244 AIPALEKL--------QGAWQAIATDLDSLKDLLEDDISK 275
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
289-466 |
8.17e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 355
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 356 DQQKAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ---SI 422
Cdd:PRK04863 389 EEEVDELKSQLADYQQaldvqqtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsVA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 423 QAGKVQLETIIKSLKSTQDEI------NQARSKLSQLQESHQEA---------HRTLEQ 466
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAeqlqqlrmrLSELEQ 527
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
284-471 |
8.31e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 284 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKS-------NEVQELQNDLDRETSSLQELEAQKQDAQDR- 351
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKEtsnkkaqDKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI--QSQESDLKSQEDDLNRAKSEL-----TR 410
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMgqmqvLQ 1051
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 411 LQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEahrtlEQYDEAL 471
Cdd:TIGR00606 1052 MKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAE-----EKYREMM 1107
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
287-424 |
8.55e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.51 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLqREKysLEQDIREKEEAIRQKSN---EVQELQNDLDRETSSLQELEAQKQDAQDRLD-------EMD 356
Cdd:pfam13851 47 KLMSEIQQENKRL-TEP--LQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELKDLKWEHEVLEQrfekverERD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 357 QQKAKLRDMLSDVRQKCQDETQMissLKTQIQSQESDLKSQEDDLN----RAKSELTRLQQEETQLEQSIQA 424
Cdd:pfam13851 124 ELYDKFEAAIQDVQQKTGLKNLL---LEKKLQALGETLEKKEAQLNevlaAANLDPDALQAVTEKLEDVLES 192
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
313-460 |
8.94e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 44.49 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 313 KEEAIRQKSNEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqmisslk 384
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 385 tqiQSQESDLKSQEDDLNRAKSELTRLQQEETQ-LEQSIQAGKVQLETIIksLKSTQDEINQARSKLsqLQESHQEA 460
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLERISGLTSEEAKEIL--LDEVEEELRHEAAVM--IKEIEEEA 178
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
293-465 |
9.26e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 293 SQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQK 372
Cdd:pfam10174 543 AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQ 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 373 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEetqleqsiqagkVQLETIIKSLKSTQDEINQARSKLSQ 452
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ------------LQLEELMGALEKTRQELDATKARLSS 680
|
170
....*....|...
gi 1953011266 453 LQESHQEAHRTLE 465
Cdd:pfam10174 681 TQQSLAEKDGHLT 693
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
286-441 |
9.30e-05 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 45.76 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 358
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 KAKLRDMLSDVRQKCQdetQMISSLKTQIQSQESDLK----SQEDDLNRAKSELTRLQQEETQLEQS-IQAGKVQLETII 433
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
....*....
gi 1953011266 434 -KSLKSTQD 441
Cdd:pfam03999 298 dKLFYSTEQ 306
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
380-472 |
9.48e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 45.49 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 380 ISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKS-LKSTQDEINQARSKLSQLQESHQ 458
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQaLQTAQNNLATAQAALANAEARLA 335
|
90
....*....|....
gi 1953011266 459 EAHRTLEQYDEALD 472
Cdd:TIGR04320 336 KAKEALANLNADLA 349
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
300-484 |
9.87e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 300 QREKYSLEQDIREKEEAIRQksnevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 377
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 378 -QMISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELTRLQQEETQLEQSIQA--GKVQLETI 432
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 433 IK-------SLKSTQD-------------EINQARSKLSQLQESHQeahrTLEQYD-EALDGAHGASLTNLAD 484
Cdd:PRK11281 342 LYqqqqalpSADLIEGladriadlrleqfEINQQRDALFQPDAYID----KLEAGHkSEVTDEVRDALLQLLD 410
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
299-466 |
9.94e-05 |
|
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: 46.32 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 299 LQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ-KCQDET 377
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 378 QMiSSLKTQIqsqESDLKSQEDD-------LNRAKSEL-TRLQQEETQLEQSIqAGKVQLETIIKSLKSTQDEINQARS- 448
Cdd:pfam01576 721 NM-QALKAQF---ERDLQARDEQgeekrrqLVKQVRELeAELEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGREe 795
|
170 180
....*....|....*....|.
gi 1953011266 449 ---KLSQLQESHQEAHRTLEQ 466
Cdd:pfam01576 796 avkQLKKLQAQMKDLQRELEE 816
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
288-423 |
1.14e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLeqdIREKEEAirqksnevqelqndldretsslqeleaqkqdAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG0542 412 ELDELERRLEQLEIEKEAL---KKEQDEA-------------------------------SFERLAELRDELAELEEELE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 368 DVRQKCQDETQMISslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQ 423
Cdd:COG0542 458 ALKARWEAEKELIE----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
297-459 |
1.30e-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: 45.94 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 297 AQLQREKYSLEQDIREKEEAirqkSNEVQELQNDLDRETSSLQE--------------LEAQKQDAQDRLDEMDQQKAKL 362
Cdd:pfam01576 412 GQLQELQARLSESERQRAEL----AEKLSKLQSELESVSSLLNEaegkniklskdvssLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 RdmlSDVRQKCQDETQMISSLKTQIQSQESdLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 442
Cdd:pfam01576 488 S---TRLRQLEDERNSLQEQLEEEEEAKRN-VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
170
....*....|....*..
gi 1953011266 443 INQARSKLSQLQESHQE 459
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQ 580
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
324-467 |
1.37e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 44.35 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 324 VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdETQMISSL---KTQ----IQSQESDLKS 396
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKH----ENDNLSSMlnrKERrlkdLEDQLSELKN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 397 QEDDLNRAKSELT----RLQQEETQLEQSIQAGKVQLETIIKSLK----STQDEINQARSKLSQLQeshQEAHRTLEQY 467
Cdd:pfam17078 81 SYEELTESNKQLKkrleNSSASETTLEAELERLQIQYDALVDSQNeykdHYQQEINTLQESLEDLK---LENEKQLENY 156
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
303-460 |
1.37e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 303 KYSLEQDIREKEEAIRQKsneVQELQNDLDrETSSLQELEAQkqdaqdrlDEMDQQKaklRDMLSDVRQKcqdetqmiss 382
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLR---NEFEKELRER---------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 383 lKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLqeSHQEA 460
Cdd:PRK12704 81 -RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEA 155
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
382-465 |
1.44e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 42.69 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 382 SLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQL--QESHQE 459
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIktQFAHEV 135
|
....*.
gi 1953011266 460 AHRTLE 465
Cdd:pfam11559 136 KKRDRE 141
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
287-407 |
1.51e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKSNEVQELQNDLD-----------RETSSLQELEAQKQ-- 346
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 347 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDL------KSQEddLNRAKSE 407
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
291-418 |
1.53e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREKYSLE---------QDIREKEEAIrqksnevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI-------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953011266 362 LRDMLSDvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA-------KSELTRLQQEETQL 418
Cdd:PHA02562 339 LLELKNK-----------ISTNKQSLITLVDKAKKVKAAIEELqaefvdnAEELAKLQDELDKI 391
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
293-464 |
1.53e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 293 SQEIAQLQRekysLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 369
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 370 ---RQKCQDETQMISSLKTQIQSQESDLKSQE-------DDLNRAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST 439
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQETRK 488
|
170 180 190
....*....|....*....|....*....|.
gi 1953011266 440 QDEINQARSKLSQL------QESHQEAHRTL 464
Cdd:TIGR00618 489 KAVVLARLLELQEEpcplcgSCIHPNPARQD 519
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
285-459 |
1.65e-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: 45.48 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 285 GVKELD-DISQEIAQLQREKYSLEQDIRE----KEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:pfam05483 64 GLKDSDfENSEGLSRLYSKLYKEAEKIKKwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQ--DETQMISSLKT---QIQSQES-----DLKSQEDDLNRAKSELtRLQQEETQLEQSIQAgKVQL 429
Cdd:pfam05483 144 KDLIKENNATRHLCNllKETCARSAEKTkkyEYEREETrqvymDLNNNIEKMILAFEEL-RVQAENARLEMHFKL-KEDH 221
|
170 180 190
....*....|....*....|....*....|..
gi 1953011266 430 ETIIKSLKSTQDEINQARSKLSQL--QESHQE 459
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLliQITEKE 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
289-465 |
1.69e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQrekyslEQDIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 368
Cdd:PRK02224 189 LDQLKAQIEEKE------EKDLHERLNGLESELAELDE---EIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 369 VRQKCQDETQMIS---SLKTQIQSQESDLKSQEDDLN--RAKSELTRLQQEETQLeqsiqagkvQLETIIKSLKSTQDEI 443
Cdd:PRK02224 260 IEDLRETIAETERereELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEA---------RREELEDRDEELRDRL 330
|
170 180
....*....|....*....|....*
gi 1953011266 444 NQARSKLSQLQ---ESHQEAHRTLE 465
Cdd:PRK02224 331 EECRVAAQAHNeeaESLREDADDLE 355
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
306-476 |
1.75e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIREKEEAIRQKSNEVQELqnDLDRetsSLQELEAQKQDAQDRLDEMDQQKAKLRDMLsdvrqkcQDETQMISSLKT 385
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGS--DLDR---TVQQVNQEKQEKQHELDTVVSKIELNRKLI-------QDQQEQIQHLKS 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 386 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLE 465
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
170
....*....|.
gi 1953011266 466 QYDEALDGAHG 476
Cdd:TIGR00606 945 DIKEKVKNIHG 955
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
287-466 |
1.77e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKsNEVQELQNDL-DRETSSLQELEAQKQDAQDRL---------DEMD 356
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERK-RYRQELEEQIeEREQKRQEEYEEKLQEREQMDeiveriqeeDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 -QQKAKLRDMLSDVRQKCQDETQMISSLKtQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLE--QSIQAgkvQLETII 433
Cdd:pfam13868 118 aEEKLEKQRQLREEIDEFNEEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIA---RLRAQQ 193
|
170 180 190
....*....|....*....|....*....|...
gi 1953011266 434 KSLKSTQDEINQARSKLsqLQESHQEAHRTLEQ 466
Cdd:pfam13868 194 EKAQDEKAERDELRAKL--YQEEQERKERQKER 224
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
300-477 |
1.91e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 300 QREKYSLEQDIREKEEAIRQKSNEV---QELQNDLDRETSSLQELEAQ-------------KQDAQDRLDEMDQQK--AK 361
Cdd:pfam05701 218 EQDKLNWEKELKQAEEELQRLNQQLlsaKDLKSKLETASALLLDLKAElaaymesklkeeaDGEGNEKKTSTSIQAalAS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDMLSDVR---QKCQDETQMISSLKTQIQSqesdlksqedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS 438
Cdd:pfam05701 298 AKKELEEVKaniEKAKDEVNCLRVAAASLRS----------ELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIAL 367
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011266 439 TQDEINQARSKLS----QLQESHQEAhrtleqyDEALDGAHGA 477
Cdd:pfam05701 368 VQAKEKEAREKMVelpkQLQQAAQEA-------EEAKSLAQAA 403
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
297-430 |
1.94e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 41.80 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 297 AQLQREKysleQDIREKEEAIRQ---KSNEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDvRQKC 373
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEE-KEIE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 374 QDETQMisslktqiqsQESDLKSQeddLNRAKSELTRLQQeetQLEQSIQAGKVQLE 430
Cdd:pfam18595 73 LRELER----------REERLQRQ---LENAQEKLERLRE---QAEEKREAAQARLE 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
325-487 |
2.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 325 QELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLSDVRQkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA 404
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 405 KSELTRLQQEETQLEQS---IQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTn 481
Cdd:PRK03918 237 KEEIEELEKELESLEGSkrkLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR- 315
|
....*.
gi 1953011266 482 LADLSE 487
Cdd:PRK03918 316 LSRLEE 321
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
287-420 |
2.08e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 355
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 356 ---DQQKAKLRD-MLSDVRQKCQDETQMISSLKTQIQSQEsDLKSQEDDLNRA-KSELTRLQQEETQLEQ 420
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE-RRLAEEAEREEEeFERMLRKQAEDEEIEQ 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
294-392 |
2.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREkysleqdIREKEEAIRQKSNEVQELQNDLDR----ETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 369
Cdd:COG4913 338 DRLEQLERE-------IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100
....*....|....*....|...
gi 1953011266 370 RQKCQDETQMISSLKTQIQSQES 392
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLER 433
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
306-414 |
2.22e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLkt 385
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 1953011266 386 qiqsqESDLKSQEDDLNRAKSELTRLQQE 414
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
290-420 |
2.30e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.90 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQdirEKEEAIRQKSN---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 366
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 367 sdvrqkCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL-TRLQQEETQLEQ 420
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
310-470 |
2.38e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 310 IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRldemdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQS 389
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR----------KQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 390 QESDLKSQEDDLNRAKSELTRLQQEETQLEQSI---QAGKV------QLETIIKSLKSTQDEINQARSKLSQLQESHQEA 460
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyEKGGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170
....*....|
gi 1953011266 461 HRTLEQYDEA 470
Cdd:PHA02562 326 EEIMDEFNEQ 335
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
313-472 |
2.41e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 313 KEEAIRQkSNEVQELQND---LDRETS-SLQELEAQKQDAQDRLDEMDQQKAKLRDMLSdvRQKCQDETQMISSLKTQIQ 388
Cdd:TIGR01612 1103 KEENIKY-ADEINKIKDDiknLDQKIDhHIKALEEIKKKSENYIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIENIV 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 389 SQESDLKSQEDDLNRAKSELTRLQQEETQLEQ--------SIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEA 460
Cdd:TIGR01612 1180 TKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEvkginlsyGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKS 1259
|
170
....*....|..
gi 1953011266 461 HRTLEQYDEALD 472
Cdd:TIGR01612 1260 PEIENEMGIEMD 1271
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
381-487 |
2.44e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.33 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 381 SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESH-QE 459
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNlAT 322
|
90 100
....*....|....*....|....*....
gi 1953011266 460 AHRTLEQYDEALDGAhGASLTNL-ADLSE 487
Cdd:TIGR04320 323 AQAALANAEARLAKA-KEALANLnADLAK 350
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
328-487 |
2.47e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 328 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD-------------ETqmISSLKTQIQSQESDL 394
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrksllanrfsfgPA--LDELEKQLENLEEEF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 395 kSQEDDLN------RAKSELTRLQQEETQLEQSIQagkvQLETIIKSLKST-QDEINQARSKLSQLQES-----HQEAHR 462
Cdd:PRK04778 182 -SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAGYRELVEEgyhldHLDIEK 256
|
170 180
....*....|....*....|....*
gi 1953011266 463 TLEQYDEALDgahgaslTNLADLSE 487
Cdd:PRK04778 257 EIQDLKEQID-------ENLALLEE 274
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
289-455 |
3.14e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKysleQDIREKEEAIRQKSNEV----QELQNDL--DRET--SSLQELEAQKQDAQDRLDEMDQ--- 357
Cdd:PRK04778 114 LDLIEEDIEQILEEL----QELLESEEKNREEVEQLkdlyRELRKSLlaNRFSfgPALDELEKQLENLEEEFSQFVElte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 358 ----QKA-----KLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELtrlqqEETQLEQSIQAGKVQ 428
Cdd:PRK04778 190 sgdyVEAreildQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHL-----DHLDIEKEIQDLKEQ 264
|
170 180
....*....|....*....|....*..
gi 1953011266 429 LETIIKSLKSTqdEINQARSKLSQLQE 455
Cdd:PRK04778 265 IDENLALLEEL--DLDEAEEKNEEIQE 289
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
290-421 |
3.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 364
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 365 MLSDVRQKCqdetqmiSSLKTQIQSQESDLKSQEddlNRAKSELTRLQQEETQLEQS 421
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA 1114
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
288-456 |
3.29e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqksnEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEmdqqkAKl 362
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKE-----AK- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 rdmlsdvrqkcQDETQMISSLKTQIQSQESDLKSQE-----DDLNRAKSELTRLQQEETQLEQSIQAG-KVQLET----- 431
Cdd:PRK00409 584 -----------KEADEIIKELRQLQKGGYASVKAHEliearKRLNKANEKKEKKKKKQKEKQEELKVGdEVKYLSlgqkg 652
|
170 180 190
....*....|....*....|....*....|
gi 1953011266 432 IIKSLKSTQDEINQA-----RSKLSQLQES 456
Cdd:PRK00409 653 EVLSIPDDKEAIVQAgimkmKVPLSDLEKI 682
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
288-493 |
3.33e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQE---LEAQKQDAQDRLDEMDQQKAKL-- 362
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSMELEKNNYYke 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 --------------------RDMLSDVRQkCQDETQMISSLKTQIQSQE------SDL----------KSQEDDLNRAKS 406
Cdd:PRK01156 278 leerhmkiindpvyknrnyiNDYFKYKND-IENKKQILSNIDAEINKYHaiikklSVLqkdyndyikkKSRYDDLNNQIL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 407 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQ----ARSKLSQLQESHQEAHRTLEQYD---EALDGAHGASL 479
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEilkiQEIDPDAIKKELNEINVKLQDISskvSSLNQRIRALR 436
|
250
....*....|....
gi 1953011266 480 TNLADLSEGVSLAE 493
Cdd:PRK01156 437 ENLDELSRNMEMLN 450
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
289-459 |
3.33e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 361
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LrDMLSDvRQKCQ----DETQMISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELTRLQQEETQLeQSIQ 423
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953011266 424 AGKVQLETIIKSLKSTQDEINQARS-KLSQLQESHQE 459
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvALDNWRQVHEQ 725
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-466 |
3.37e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-----------DLDRETSSLQELEAQKQ--------- 346
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 347 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE---DDLNRAKSELTRLQQEETQLEQ 420
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953011266 421 SIQAGKVQLEtiIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:TIGR00606 493 NSLTETLKKE--VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
286-473 |
3.45e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQD---AQDRLD--EMDQQKA 360
Cdd:COG1340 49 NAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIErlEWRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 361 KL-----RDMLSDVRQKCQ--DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 433
Cdd:COG1340 129 VLspeeeKELVEKIKELEKelEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDG 473
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
288-389 |
3.52e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQ-----------KSNEVQELQ---NDLDRETSSLQELEAQKQDAQDRLD 353
Cdd:pfam07926 9 EIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqnyerelvlHAEDIKALQalrEELNELKAEIAELKAEAESAKAELE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1953011266 354 EM----DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 389
Cdd:pfam07926 89 ESeeswEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
292-464 |
3.76e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.53 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 292 ISQEIAQLQREKYSLEQDIrekEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 368
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVL---NELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 369 --VRQKCQdetQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQ-------------QEETQLEQSI----------- 422
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMasllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 423 ----QAGKV-----------------QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTL 464
Cdd:pfam04108 192 dqcvTAVKLteggraemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
291-472 |
3.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 365
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 366 LSDVRQ-------------KCQDETQMISSLK---TQIQSQESDLKSQEDDL-----NRAK---SELTRLQQEETQLEQS 421
Cdd:PRK04863 910 KRFVQQhgnalaqlepivsVLQSDPEQFEQLKqdyQQAQQTQRDAKQQAFALtevvqRRAHfsyEDAAEMLAKNSDLNEK 989
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 422 IQAGKVQLE----TIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:PRK04863 990 LRQRLEQAEqertRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQ 1044
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-495 |
3.97e-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: 44.01 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQK-------QDAQDRLDEMD--- 356
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAlslaralEEALEAKEELErtn 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 -QQKAKLRDMLS---DV--------RQKCQDETQMiSSLKTQIQSQESDLKSQEDdlnrAKseltrlqqeeTQLEQSIQA 424
Cdd:pfam01576 660 kQLRAEMEDLVSskdDVgknvheleRSKRALEQQV-EEMKTQLEELEDELQATED----AK----------LRLEVNMQA 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 425 GKVQLETIIkslkSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASL-TNLADLSEGVSLAERG 495
Cdd:pfam01576 725 LKAQFERDL----QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLeLDLKELEAQIDAANKG 792
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
315-472 |
3.98e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 315 EAIRQKSNEVQELQNDLDretSSLQELEAQKQDAQDRLD----EMDQQKAKLRDMLSDVrqkcQDETQMISSLKTQI--- 387
Cdd:PRK01156 583 ETNRSRSNEIKKQLNDLE---SRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEI----QENKILIEKLRGKIdny 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 388 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKV---QLETIIKSLKSTQDEINQARSKLSQLQESHQE---AH 461
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAnraRLESTIEILRTRINELSDRINDINETLESMKKikkAI 735
|
170
....*....|.
gi 1953011266 462 RTLEQYDEALD 472
Cdd:PRK01156 736 GDLKRLREAFD 746
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
359-492 |
4.00e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.07 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQL--------- 429
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrq 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 430 -----ETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALdGAHGASLTNLADLSEGVSLA 492
Cdd:COG5283 82 lsaaqRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLA-GAGAAAAAIGAALAASVKPA 148
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
329-471 |
4.02e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 43.28 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 329 NDLDRETSSLQE----LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMIS-SLKTQIQSQESDLKS------Q 397
Cdd:pfam09755 24 EQLQKRIESLQQenrvLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISnTLLKKIQALKKEKETlamnyeQ 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 398 EDDL--NRAKSELTRLQQEETQLEQSI-QAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:pfam09755 104 EEEFltNDLSRKLTQLRQEKVELEQTLeQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEAL 180
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
337-466 |
4.15e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 337 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQMISSLKTQIQS--QESDLKSQEDDL 401
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 402 NRAKSEL-TRLQQEETQLeQSIQAgkvQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQN---QLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNG 138
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
287-455 |
4.30e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldreTSSLQELEAQKQDAQDR-------LDEMDQQK 359
Cdd:PRK10929 72 QVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQV-----SSQLLEKSRQAQQEQDRareisdsLSQLPQQQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQ----DETQMISSLKTQIQSQESDLKSQEDDLNRA------KSELTRLQQE-----ETQLEQSIQA 424
Cdd:PRK10929 147 TEARRQLNEIERRLQtlgtPNTPLAQAQLTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQA 226
|
170 180 190
....*....|....*....|....*....|.
gi 1953011266 425 GKVQLETiikslkSTQDEINQARSKLSQLQE 455
Cdd:PRK10929 227 LRNQLNS------QRQREAERALESTELLAE 251
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
287-424 |
4.40e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIR----------QKSNEvqelqnDLDRET-SSLQELEAQKQDAQDRLDEM 355
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlalEKGRE------DLAREAlERKAELEAQAEALEAQLAQL 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953011266 356 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE----DDLNRAKSELTRLQQEETQLEQSIQA 424
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA 183
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
287-352 |
4.61e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.02 E-value: 4.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDretsslQELEAQKQDAQDRL 352
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
339-466 |
4.78e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 40.63 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 339 QELEAQKQDAQDRLDEMDQQKAKLRDMlsdvRQKCQDETQMIsslktqiqsqESDLKSQEDDLNRAKseltRLQQEETQL 418
Cdd:pfam13863 13 LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKF----------DKFLKENDAKRRRAL----KKAEEETKL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1953011266 419 eqsiqagKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam13863 75 -------KKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
378-465 |
4.79e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 378 QMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ----SIQAGKVQLETIIKSLKSTQDEINQARSKLSQL 453
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90
....*....|..
gi 1953011266 454 QESHQEAHRTLE 465
Cdd:PRK00409 600 GYASVKAHELIE 611
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
343-495 |
5.40e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 343 AQKQDAQDRLDEMdQQKAKL---RDMLSDVR---QKCQDETQ-MISSLKTQIQSQESdlKSQEDDLNRAKSELTRLQQE- 414
Cdd:PRK02224 146 ATPSDRQDMIDDL-LQLGKLeeyRERASDARlgvERVLSDQRgSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEi 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 415 ---ETQLEQSIQAgKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSL 491
Cdd:PRK02224 223 eryEEQREQARET-RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE 301
|
....
gi 1953011266 492 AERG 495
Cdd:PRK02224 302 AGLD 305
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
288-487 |
5.41e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQ------NDLDRET--SSLQELEAQKQDAQD--------- 350
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlNLLADETlaDRVEEIREQLDEAEEakrfvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 351 -RLDEMDQQKAKLRdmlsdvrqkcQDETQmISSLK---TQIQSQESDLKSQEDDL-----NRAK---SELTRLQQEETQL 418
Cdd:PRK04863 918 nALAQLEPIVSVLQ----------SDPEQ-FEQLKqdyQQAQQTQRDAKQQAFALtevvqRRAHfsyEDAAEMLAKNSDL 986
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 419 EQSIQAGKVQLEtiikslkstqdeinQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSE 487
Cdd:PRK04863 987 NEKLRQRLEQAE--------------QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
292-397 |
5.92e-04 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 43.04 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 292 ISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 367
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 1953011266 368 DVRQKCQDETQMISSLKTQIQSQESDLKSQ 397
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
292-464 |
6.11e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 292 ISQEIAQLQREKYSLEQ------DIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQ---------DRLDEMD 356
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQlegssdRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADldrklrkldQEMEQLN 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 QQKAKLRDMLSDVRQKcQDETQMISSLKTQIQSQ--------------ESDLKSQEDDLNRAKSELTRLQQEETQLEQSI 422
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDK-MDKDEQIRKIKSRHSDEltsllgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011266 423 QAGKVQLETIIKSLKSTQDEINQA------RSKLSQLQESHQEAHRTL 464
Cdd:TIGR00606 608 NHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEKSSKQR 655
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
310-423 |
6.22e-04 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 40.33 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 310 IREK-EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQMISSLKTQIQ 388
Cdd:smart00502 1 QREAlEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKE 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1953011266 389 SQESDLKSQeddlnrakseLTRLQQEETQLEQSIQ 423
Cdd:smart00502 72 NKLKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
304-446 |
6.74e-04 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 40.97 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 304 YSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQqkakLRDMLSD--VRQKCQDETQMI 380
Cdd:pfam16789 3 YPLEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVrKHKKAKMQQ----LRDEMDRgtTSDKILQMKRYI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953011266 381 SSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--------TQDEINQA 446
Cdd:pfam16789 79 KVVKERLKQEEKKVQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKeeedqeerEQDEIGSA 152
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
290-462 |
6.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQDIREK-EEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDaqdrldEMDQQKAKLRDMLSd 368
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEYLALLDRLEED------GLPEYEERFKELLN- 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 369 vrqkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAkseLTRLQ-QEETQLEqsIQAGKVQLETIikslKSTQDEINQAR 447
Cdd:COG4913 842 -----ENSIEFVADLLSKLRRAIREIKERIDPLNDS---LKRIPfGPGRYLR--LEARPRPDPEV----REFRQELRAVT 907
|
170
....*....|....*
gi 1953011266 448 SKLSQLQESHQEAHR 462
Cdd:COG4913 908 SGASLFDEELSEARF 922
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
291-494 |
7.42e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREKYSLEQ------DIREK-----------EEAIRQKSNEVQELQN---DLDRETSSLQELEAQKQDAQD 350
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQykekacEIRDQitskeaqlessREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 351 RLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLK-TQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQL 429
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 430 ETIIKSLKSTQDEI--NQARSKLSQLQE---SHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:TIGR00606 357 DRHQEHIRARDSLIqsLATRLELDGFERgpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
288-475 |
7.57e-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: 43.24 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKSNEVQELQNDLDRETSSLQ------- 339
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 340 ELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDVRQKcqdetqmISSLKTQIQsQESDLKSQEDDLNRA-----KSELTRLQQ 413
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFKSSIAALEAK-------IAQLEEQLE-QESRERQAANKLVRRtekklKEVLLQVED 1013
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 414 EETQLEQSiqagKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAH 475
Cdd:pfam01576 1014 ERRHADQY----KDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
306-508 |
7.62e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.59 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIREKEEAIRQKSNEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQMISSLKT 385
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 386 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKS--TQDEINQARSKLSQlqeshQEAHRT 463
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLST-----SSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 464 LEQYD------EALDGAHgASLTNLADLSEGVSLAERGGFGAMDDPFKNKA 508
Cdd:pfam04012 166 FERIEekieerEARADAA-AELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
365-467 |
7.95e-04 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 42.50 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 365 MLSDVRQKCQDET-QMISSLKTQIQSQESDLKSQEDDL------NRAKSELTRLQQEEtqleQSIQAgkvQLETIIKSLK 437
Cdd:pfam05816 33 MLDNVRTKDLGEVgDLLNELRRTLKDFDPDELGEEKKLgflplfKKAGNKIEKYFAKY----QTAGA---QIDKIVVELE 105
|
90 100 110
....*....|....*....|....*....|
gi 1953011266 438 STQDEINQARSKLSQLQESHQEAHRTLEQY 467
Cdd:pfam05816 106 KGQDELLKDNAMLDQMYEKNLEYFKELEKY 135
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
287-471 |
8.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSleqdIREKEEAIRQKSNEVQElqnDLDRETSSLQELEAQKQDAQDRL----DEMDQQKaKL 362
Cdd:PRK04863 279 NERRVHLEEALELRRELYT----SRRQLAAEQYRLVEMAR---ELAELNEAESDLEQDYQAASDHLnlvqTALRQQE-KI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 RDMLSDVRQKCQ--DETQMISSLKTQIQSQ-ESDLKSQEDDLNRAKSELTRLQQ----EET---QLEQSIQA-GKVQ--- 428
Cdd:PRK04863 351 ERYQADLEELEErlEEQNEVVEEADEQQEEnEARAEAAEEEVDELKSQLADYQQaldvQQTraiQYQQAVQAlERAKqlc 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 429 ---------LETIIKSLKSTQDEINQARSKLSQLQESHQEAHrtlEQYDEAL 471
Cdd:PRK04863 431 glpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH---SQFEQAY 479
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
288-471 |
8.35e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.32 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREkysleqdIREKEEAIRQKSNEVQELQNDlDRETSSLQELEAQKQ-------DA-QDRLDEMDQQK 359
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETE-SSCSTPLRRNESFSSlhgcvqlDAlQEKLRGLEEEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 AKLRDMLSDVRQKCQD----ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL-------EQSIQAGKVQ 428
Cdd:pfam04849 181 LKLRSEASHLKTETDTyeekEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLlaqivdlQHKCKELGIE 260
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953011266 429 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:pfam04849 261 NEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEEL 303
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
291-460 |
8.45e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.37 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREKY-SLEQDIREKEEAIRQKSNEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAklrdmlsdv 369
Cdd:pfam12718 10 ENAQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVE-------KLEEQLKEAKEKAEESEKLKT--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 370 rqkcQDEtqmisSLKTQIQSQESDLKSQEDDLnraKSELTRLQQEETQLEQSiqagkvqlETIIKSLkstQDEINQARSK 449
Cdd:pfam12718 74 ----NNE-----NLTRKIQLLEEELEESDKRL---KETTEKLRETDVKAEHL--------ERKVQAL---EQERDEWEKK 130
|
170
....*....|.
gi 1953011266 450 LSQLQESHQEA 460
Cdd:pfam12718 131 YEELEEKYKEA 141
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
287-470 |
8.96e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLR 363
Cdd:pfam06008 75 AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQNAEAELKAAQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVR---QKCQDETQmisSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAgkvQLETIIKSLKSTQ 440
Cdd:pfam06008 155 DLLSRIQtwfQSPQEENK---ALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA---NLREFQRKKEEVS 228
|
170 180 190
....*....|....*....|....*....|
gi 1953011266 441 DEINQARSKLSQLQESHQEAHRTLEQYDEA 470
Cdd:pfam06008 229 EQKNQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
319-470 |
9.52e-04 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 42.57 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 319 QKSNEVQELQNDLDRETSSLQELEAQKQD-AQDRLDEMDQQK---------------AKLRD-MLSDVRQKCQDET-QMI 380
Cdd:COG3853 25 PEVPEQAAGMVDPEEAEVDLSKLSAEADAfVEALAAQIDLSDvnailqygakaqrklAAFSNrMLDRVKTKDLGEVgDSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 381 SSLKTQIQsqESDLKSQEDD---------LNRAKSELTRLQQEEtqleQSIQAgkvQLETIIKSLKSTQDEINQARSKLS 451
Cdd:COG3853 105 SELRRTLE--DLDPSELDDLkkkgllgklFPKGGNKLEKYFAKY----QSAQT---QIDKISVALEKGQDELLKDNAMLD 175
|
170
....*....|....*....
gi 1953011266 452 QLQESHQEAHRTLEQYDEA 470
Cdd:COG3853 176 QLYEKNWEYFKELNQYIAA 194
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-476 |
9.94e-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: 42.85 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 363
Cdd:pfam01576 833 KKLKNLEAELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQsnt 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 DMLSDVRQKCqdeTQMISSLKTQIQSQESDLKSQED---DLNRAKSEL-TRLQQEETQ-----------LEQSIQAGKVQ 428
Cdd:pfam01576 906 ELLNDRLRKS---TLQVEQLTTELAAERSTSQKSESarqQLERQNKELkAKLQEMEGTvkskfkssiaaLEAKIAQLEEQ 982
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953011266 429 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG 476
Cdd:pfam01576 983 LEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNS 1030
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
287-438 |
1.06e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 41.75 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKSNEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 359
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 360 aKLRDMLSDVR--QKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELTRLQQEETQLEQSIQagkvQLETIIKSLK 437
Cdd:COG5325 144 -FLRNKNNDQHplEEEEDEESLSSLGSQQTLQQQGLSNEELEY---QQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
.
gi 1953011266 438 S 438
Cdd:COG5325 216 S 216
|
|
| Flagellar_rod |
pfam05149 |
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod ... |
300-415 |
1.15e-03 |
|
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod component proteins. The eukaryotic flagellum represents one of the most complex macromolecular structures found in any organizm and contains more than 250 proteins. In addition to its locomotive role, the flagellum is probably involved in nutrient uptake since receptors for host low-density lipoproteins are localized on the flagellar membrane as well as on the flagellar pocket membrane.
Pssm-ID: 368306 [Multi-domain] Cd Length: 287 Bit Score: 41.96 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 300 QREKYSLEQdiREKEEAIRQKSNEVQELQNDLDRETSSLQEL-EAQKQDAQDRLDEM-----------------DQQKAK 361
Cdd:pfam05149 38 QRKRFKTQR--RESDKFLQQNVEQQQKLWREIEELERELQKLaEERREEVEDRIEAVereaqrrtdhesflnfaDQHKQR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1953011266 362 LRDMLSDVrQKCQDETQMISSLktqIQSQESDLKSQEDDLNRAKSELTRLQQEE 415
Cdd:pfam05149 116 LRRTLENC-DGALDCARSLEEY---VQEGCDHLPAKQDKLRNALNELLDAVRKE 165
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
359-470 |
1.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 359 KAKLRDMLSDVRQKCQDETQMISSLK----TQIQSQESDLKSQ-EDDLNRAKSELT----RLQQEETQLE---QSIQAGK 426
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKkealLEAKEEIHKLRNEfEKELRERRNELQklekRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1953011266 427 VQLETIIKSLKSTQDEINQARSKLSQLQESHQEAhrtLEQY-----DEA 470
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERIsgltaEEA 155
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
327-472 |
1.17e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.45 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 327 LQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKS 406
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRAL-------KAELESLEVYNRQLERLVASQEQEIASLER 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 407 ELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARskLSQLQESHQEAHRTL-EQYD---EALD 472
Cdd:pfam11932 84 QIEEIERTERELVPLMLKMLDRLEQFVALDLPFLLEERQAR--LARLRELMDDADVSLaEKYRrilEAYQ 151
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
289-487 |
1.21e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 360
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 361 KLRDMLSDVRQKCQDETQ----MISSLKTQIQSQES---DLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI- 432
Cdd:COG0497 223 KLREALQEALEALSGGEGgaldLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVe 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 433 -----IKSLK----STQDEI----NQARSKLSQLQESHQEahrtLEQYDEALDGAHgASLTNLAD-LSE 487
Cdd:COG0497 303 erlalLRRLArkygVTVEELlayaEELRAELAELENSDER----LEELEAELAEAE-AELLEAAEkLSA 366
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
349-494 |
1.23e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 349 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKtqiqsqesdlksqeDDLNRAKSELTRLQQEETQLEQSIQAGKVQ 428
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 429 LETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALDGAHG---ASLTNLADLSE--GVSLAER 494
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKrdrESQAKIADLGRrlNVALAQR 188
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
287-455 |
1.24e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQRekySLEQDIREKEEAIRQKSNEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam04108 171 KELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQKLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 S---DVRQKCQDETQMISSLKTQIqsqeSDLKSQEDDL-NRAKSELTRLQQEETQLEQSIQAgKVQLETIIKSL------ 436
Cdd:pfam04108 245 EqknSLIDELLSALQLIAEIQSRL----PEYLAALKEFeERWEEEKETIEDYLSELEDLREF-YEGFPSAYGSLllever 319
|
170 180
....*....|....*....|....
gi 1953011266 437 -KSTQDEI----NQARSKLSQLQE 455
Cdd:pfam04108 320 rREWAEKMkkilRKLAEELDRLQE 343
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
289-455 |
1.25e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:cd22656 123 LDDLLKEAKKYQ-------DKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLNEEY 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDEtqmissLKTQIQSQESDLKSQE---DDLNRAKSELTRLQQeetQLEQSIQA-GKVQ---------LETII 433
Cdd:cd22656 196 AAKLKAKIDE------LKALIADDEAKLAAALrliADLTAADTDLDNLLA---LIGPAIPAlEKLQgawqaiatdLDSLK 266
|
170 180
....*....|....*....|..
gi 1953011266 434 KSLKSTQDEINQARSKLSQLQE 455
Cdd:cd22656 267 DLLEDDISKIPAAILAKLELEK 288
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
289-471 |
1.27e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.71 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQrekyslEQDIREKEEAIRQKSNEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 368
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 369 VRQKCQDETQMI-SSLKTQIQSQESDLKSQEDDL-NRAKSELTRLQqeeTQLEQSIQAGKVQLETIIKSLKSTQDEinQA 446
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAP--YA 145
|
170 180
....*....|....*....|....*
gi 1953011266 447 RSKLSQLQESHQEAHRTLEQYDEAL 471
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDL 170
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
295-418 |
1.28e-03 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 40.12 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 295 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 366
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL 418
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
286-375 |
1.32e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 39.28 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSN---------EVQELQNDLDREtSSLQELEAQKQDAQDRLDEMD 356
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKlpddtpiykIVGNLLVKVDKT-KVEKELKERKELLELRSRTLE 91
|
90
....*....|....*....
gi 1953011266 357 QQKAKLRDMLSDVRQKCQD 375
Cdd:PRK09343 92 KQEKKLREKLKELQAKINE 110
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
287-467 |
1.32e-03 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 41.73 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREkysLEQDI----REKE---EAIRQKSNEV---QELQNDLDRETssLQELEAQKQDAQDRldeMD 356
Cdd:pfam05816 95 AQIDKIVVELEKGQDE---LLKDNamldQMYEknlEYFKELEKYIaagELKLEELDAEL--LPELEAKAAASGDP---ED 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 357 QQKAK-LRDMLSDVRQKCQD-ETQM-------------------------------ISSLKTQ------IQSQESDLKSQ 397
Cdd:pfam05816 167 AQALRdLRQALFRLEQRIHDlELQRavsiqtapqirlvqnnnqeliekiqsaitttIPLWKNQlvvalaLKRQKLALEAQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 398 E------DDLNRAKSELTRLQQEETQlEQSiQAGKVQLETIIK---SLKSTQDEINQ----ARSKLSQLQESHQEAHRTL 464
Cdd:pfam05816 247 KavndttNELLLKNAEMLKTQSIETA-KEA-ERGIVDIETLKKtnqTLIATIDETLQiqeeGREKRREAEAELEQLEEEL 324
|
...
gi 1953011266 465 EQY 467
Cdd:pfam05816 325 KQK 327
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
288-462 |
1.38e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 363
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 dmlsdvrqkcqDETQMISslKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQL--EQSIQAGKVQlETIIKSL---KS 438
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSASKeieKT 181
|
170 180
....*....|....*....|....*....
gi 1953011266 439 TQD---EINQARSKLSQLQESHQEA--HR 462
Cdd:pfam05701 182 VEEltiELIATKESLESAHAAHLEAeeHR 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-494 |
1.49e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 363
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQDEESDLERLKEEIEKSSKQRAMLAgat 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 364 -------DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQ----EDDLNRAKSELTRLQQeetqlEQSIQAGKVQLETI 432
Cdd:TIGR00606 663 avysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlaPDKLKSTESELKKKEK-----RRDEMLGLAPGRQS 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 433 IKSLKstQDEINQARSKLSQLQESHQEAHRTLEQyDEALDGAHGASLTNLADLSEGVSLAER 494
Cdd:TIGR00606 738 IIDLK--EKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMER 796
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
287-472 |
1.52e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQrEKYSLEQDireKEEAIRQKSNEVQELQNDLDRET----------SSLQ----ELEAQKQDAQDRL 352
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLNEN---ELERVRGLEKQLEELEKRYDEIVerleekevaySELQeeleEILEQLEEIEEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 353 DEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqeSDL----KSQEDDLNRAKSELTRLQQeetQLEQS---IQAG 425
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEVplnMDEV 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 426 KVQLETIIKSL----KSTQDEINQA-------------RSKLSQLQESHQEAHRTLE--QYDEALD 472
Cdd:pfam06160 456 NRLLDEAQDDVdtlyEKTEELIDNAtlaeqliqyanryRSSNPEVAEALTEAELLFRnyDYEKALE 521
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
297-364 |
1.63e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 39.65 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 297 AQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 364
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
349-466 |
1.65e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 349 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQeddLNRAKSELTRLQQEETQLEQSiqagkvq 428
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR---VAELKEELRQSREKHEELEEK------- 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 1953011266 429 letiIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam07888 103 ----YKELSASSEELSEEKDALLAQRAAHEARIRELEE 136
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
289-420 |
1.70e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 39.47 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLdretsslqeLEAQKqdaqdrldemdqqkaklrdMLSD 368
Cdd:pfam05103 27 LDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTL---------ILAQE-------------------TAEE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1953011266 369 VRQKCQDETQMISSlKTQIQSQESdLKSQEDDLNRAKSELTRLQQEETQLEQ 420
Cdd:pfam05103 79 VKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-450 |
1.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVRQkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSElTRLQQEETQLEQSIQA-GKV---------QLETIIKSLK 437
Cdd:COG1196 725 ALEE--QLEAEREELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEAlGPVnllaieeyeELEERYDFLS 801
|
170
....*....|...
gi 1953011266 438 STQDEINQARSKL 450
Cdd:COG1196 802 EQREDLEEARETL 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
296-469 |
1.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 296 IAQLQREKYSLEQDIrEKEEAI----RQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK---AKLRDMLSD 368
Cdd:PRK03918 171 IKEIKRRIERLEKFI-KRTENIeeliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKeeiEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 369 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS---------ELTRLQQEETQLEQSIQAGKVQLETIIKSLKST 439
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190
....*....|....*....|....*....|
gi 1953011266 440 QDEINQARSKLSQLQESHQEAHRTLEQYDE 469
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEE 359
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
299-452 |
1.92e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.63 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 299 LQREKYSLEQDIREkeeaiRQKSNEVQelqndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetq 378
Cdd:PRK06975 344 LNRKVDRLDQELVQ-----RQQANDAQ------------TAELRVKTEQAQASVHQLDSQFAQLDGKLADAQSAQQ---- 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 379 misslktQIQSQESDLKSQEDDLNRAKSE-LTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQD-EINQARSKLSQ 452
Cdd:PRK06975 403 -------ALEQQYQDLSRNRDDWMIAEVEqMLSSASQQLQLTGNVQLALIALQNADARLATSDSpQAVAVRKAIAQ 471
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
308-470 |
1.97e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 308 QDIREKEEAIRQKSNE-------VQELQNDLDRETSSLQELEAQKQDAQD-------RLDEMDQQKAKLRDML------- 366
Cdd:pfam05622 3 SEAQEEKDELAQRCHEldqqvslLQEEKNSLQQENKKLQERLDQLESGDDsgtpggkKYLLLQKQLEQLQEENfrletar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDetqmissLKTQIQsqesDLKSQEDDLNRAKSELTRLQQEETQLEQSiqAGKV-QLETIIKSLKSTQDEINQ 445
Cdd:pfam05622 83 DDYRIKCEE-------LEKEVL----ELQHRNEELTSLAEEAQALKDEMDILRES--SDKVkKLEATVETYKKKLEDLGD 149
|
170 180
....*....|....*....|....*.
gi 1953011266 446 ARSKLSQLQESHQE-AHRTLEQYDEA 470
Cdd:pfam05622 150 LRRQVKLLEERNAEyMQRTLQLEEEL 175
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
295-460 |
2.10e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.41 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 295 EIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDL-DRE-------TSSLQELEAQKQDAQDRLDEmdqqkaKLRDML 366
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVeERElkaeaehRQRVVELSREVEEAKRAFEE------KLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS-ELTRLQQEetqLEQSIQAGKVQLETIIKSLKSTQDEINQ 445
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVEDLRKEKKKLAEEYEQ 197
|
170
....*....|....*
gi 1953011266 446 arsKLSQLQESHQEA 460
Cdd:pfam15665 198 ---KLSKAQAFYERE 209
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
287-418 |
2.15e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.47 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQrekysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 359
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDLNRAKSELTRLQQEETQL 418
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
306-488 |
2.28e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSdvrqkcqdetqmisslkt 385
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN------------------ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 386 qiqsqeSDLKSQEDDLNRAKSELTRLqqeETQLEQSIQAGkvqletiIKSLKSTQDEINQARSKLSQLQESHQ---EAHR 462
Cdd:pfam12128 308 ------GELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAADQEQLPSWQSELENLEERLKaltGKHQ 371
|
170 180
....*....|....*....|....*..
gi 1953011266 463 TLEQYDEALDGAHGASL-TNLADLSEG 488
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNnRDIAGIKDK 398
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
289-433 |
2.35e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 39.81 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 289 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 368
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 369 vrqkcqdETQMISSLktqiqsqesdlksqedDLNRAKSELTRLQQEETQLEQSIQAGKVQLETII 433
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
315-434 |
2.60e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 315 EAIRQKSNEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetqmisslktQIQSQESD 393
Cdd:pfam03938 8 QKILEESPEGKAAQAQLEKKFKKRQaELEAKQKELQKLYEELQKDGALLEEEREEKEQ--------------ELQKKEQE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1953011266 394 LKSQEDDLNRAkseltrLQQEETQLEQSIQAgkvQLETIIK 434
Cdd:pfam03938 74 LQQLQQKAQQE------LQKKQQELLQPIQD---KINKAIK 105
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
309-371 |
2.66e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 39.93 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 309 DIREKEEAIRQKSNEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 371
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
279-493 |
2.66e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 279 GSGEFTGVKELDDisqeiaqLQREKYSLEQDIrekeEAIRQKSNEVQELQND---LDRETS----SLQELEAQKQDAQDR 351
Cdd:PLN02939 218 GLCVHSLSKELDV-------LKEENMLLKDDI----QFLKAELIEVAETEERvfkLEKERSlldaSLRELESKFIVAQED 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 LDEMDQQKAklrDMLSDVRQKCQDetqMISSLKTQIQsQESDLKSQEDDLnRAKSEltrlqqeetQLEQSIQAGKVQlet 431
Cdd:PLN02939 287 VSKLSPLQY---DCWWEKVENLQD---LLDRATNQVE-KAALVLDQNQDL-RDKVD---------KLEASLKEANVS--- 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953011266 432 iikSLKSTQDEINQARSKL--SQLQESHQEAHRTLEQYDEALDGAHGaSLTNLADLSEGVSLAE 493
Cdd:PLN02939 347 ---KFSSYKVELLQQKLKLleERLQASDHEIHSYIQLYQESIKEFQD-TLSKLKEESKKRSLEH 406
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
306-424 |
2.67e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 306 LEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKT 385
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 1953011266 386 QIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQA 424
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAA 155
|
|
| COG5074 |
COG5074 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
304-459 |
3.05e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 40.26 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 304 YSLEQDIREKEEAIRQKSNEVQELQNdldRETSSLQEL-EAQKQDAQDRLDEMDQQKAKLR-----DMLSDVRQKCQDET 377
Cdd:COG5074 21 VTFMNKILSINKNLSVYEKEINQIDN---LHKDLLTEVfEEQSRKLRRSLDNFSSQTTDLQrnlkkDIKSAERDGIHLAN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 378 QMISS------LKTQIQS-QESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKL 450
Cdd:COG5074 98 KQAQAenvrqkFLKLIQDyRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRGEAKTAL 177
|
....*....
gi 1953011266 451 SQLQESHQE 459
Cdd:COG5074 178 AEVQARHQE 186
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
297-466 |
3.09e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 297 AQLQREKYSLEQDIREKEEAIRQKSNEVQElqndldRETSSLQELEAQKQDAQD---RLDEMDQQKAKLRDMLSDVRQKC 373
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLE------KELKHLREALQQTQQSHAyltQKREAQEEQLKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 374 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELtRLQQEETQLEQSIQagkvQLETIIKSLKSTQDEINQARSKLSQL 453
Cdd:TIGR00618 270 E-----------ELRAQEAVLEETQERINRARKAA-PLAAHIKAVTQIEQ----QAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170
....*....|....*
gi 1953011266 454 --QESHQEAHRTLEQ 466
Cdd:TIGR00618 334 vkQQSSIEEQRRLLQ 348
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
321-456 |
3.17e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.09 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 321 SNEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDD 400
Cdd:cd21116 72 QSYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATK 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 401 LNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQES 456
Cdd:cd21116 142 AQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESS 197
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
296-423 |
3.20e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 296 IAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNdldretsSLQELEAQKQDAQDRLDEmdqqkaklrdmlsdvRQK--- 372
Cdd:pfam03148 253 IEETEDAKNKLEWQLKKTLQEIAELEKNIEALEK-------AIRDKEAPLKLAQTRLEN---------------RTYrpn 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 373 ---CQDETQ--MISSLKtQIQSQESDLKSQeddLNRAKSELTRLQQEETQLEQSIQ 423
Cdd:pfam03148 311 velCRDEAQygLVDEVK-ELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
290-471 |
3.38e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.75 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 369
Cdd:pfam14988 25 NQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 370 RQKcqdetqmissLKTQIQSQESDLKSQEDDLN------RAKSELTRLQQEETqleqsiQAGKVQLETIIKSLKSTQDEI 443
Cdd:pfam14988 105 DRE----------AHLQFLKEKALLEKQLQELRilelgeRATRELKRKAQALK------LAAKQALSEFCRSIKRENRQL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953011266 444 NQARSKL-----------SQLQESHQEAHRTlEQYDEAL 471
Cdd:pfam14988 169 QKELLQLiqetqaleaikSKLENRKQRLKEE-QWYLEAL 206
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
287-466 |
3.39e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.32 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEV---QEL------------QNDLDRETSSLQELEAQKQDaqdR 351
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEKEES---K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 352 LDEMDQQKAKLRDMLsdvrQKCQDE-----TQM----------ISSLKTQIQsqesDLK-SQEDDLNraksELTRLQQEE 415
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEElnflsTYKdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 416 TQ-LEQSIQAGKVQLETII--KSLKSTQD--------------EINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQEsllqktrdnqvmlkEIEQFREFIDELEEEIPKLKAEVQQ 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-502 |
3.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDR--ETSSLQELEAQKQDAQDRLDEMDQQKA--KL 362
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNAEKEEELAEaeKL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 RDMLSDVRQKCQDETQMISSLKTQIQSqESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDE 442
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 443 INQARSKLSQLQESHQEAHRTLEQYDEALDGAHGASLTNLADLSEGVSLAERGGFGAMDD 502
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
287-357 |
3.53e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 287 KELDDISQEIAQLQREKysleQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 357
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
279-445 |
3.61e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.81 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 279 GSGEFTGVKELDDISQE-------IAQLQREKYSLEQDIREKEEAIRQKSNEV------QELQNDLDRETSSLQELEAQK 345
Cdd:pfam13166 299 ISSLLAQLPAVSDLASLlsafeldVEDIESEAEVLNSQLDGLRRALEAKRKDPfksielDSVDAKIESINDLVASINELI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 346 QDAQDRLDEMDQQKAKLRDMLsdvrqkcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQag 425
Cdd:pfam13166 379 AKHNEITDNFEEEKNKAKKKL---------RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIK-- 447
|
170 180
....*....|....*....|
gi 1953011266 426 kvQLETIIKSLKSTQDEINQ 445
Cdd:pfam13166 448 --ELEAQLRDHKPGADEINK 465
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
308-420 |
3.62e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.45 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 308 QDIREKEEaiRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqmissLKTQI 387
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110
....*....|....*....|....*....|...
gi 1953011266 388 QSQESDLKSQEDDLNRAKSELTRLQQEETQLEQ 420
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEK 110
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
181-240 |
3.82e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.62 E-value: 3.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 181 RFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAM 240
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
291-474 |
4.20e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 40.59 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREK-------YSLEQDIREKEEAIRQKSNEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:pfam15450 24 DLQAEVVSLRGHKercehatLSLLRELLQVRAHVQLQDSELKQLRQEVQQAARApeKEALEFPGPQNQNQMQALDKRLVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 362 LRDMLSDVRQK--CQDE-------------TQMISSLKTQIQSQESD----LKSQEDDLNRAKSELTRLQQEETQL--EQ 420
Cdd:pfam15450 104 VREALTQIRRKqaLQDSerkgaeqeanlrlTKLTGKLKQEEQGREAAcsalQKSQEEASQKVDHEVARMQAQVTKLgeEM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 421 S-------------IQAGKVQLETIIKSLKSTQ--------DEINQARSKLSQLQESH---------QEAHRTLEQYdEA 470
Cdd:pfam15450 184 SlrflkreaklcsfLQKSFLALEKRMKASESTRlkaesslrEELEGRWQKLQELTEERlralqgqreQEEGHLLEQC-RG 262
|
....
gi 1953011266 471 LDGA 474
Cdd:pfam15450 263 LDAA 266
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
315-455 |
4.22e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 315 EAIRQKSNEVQELqndldreTSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlKTQIQSQESDL 394
Cdd:TIGR00606 169 KALKQKFDEIFSA-------TRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIV 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 395 KSQEDDLNRAKSELTRLQQEETQLeqsiqagkVQLETIIKSLKSTQDEINQARSKLSQLQE 455
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKI--------MKLDNEIKALKSRKKQMEKDNSELELKME 293
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
291-421 |
4.23e-03 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 39.22 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 291 DISQEIAQLQREKYSLEQDIREKEEAiRQKSNEVQELQNDLDRETSSLQELEAQKQ-----DAQDRLDEMDQQKAklrdm 365
Cdd:pfam03280 76 SAEEKQQRLAALRAQLPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQRA----- 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953011266 366 lsdvrqkcqdetqmisslktQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQS 421
Cdd:pfam03280 150 --------------------AWQQRLDDYLAERQQINAAGLSEQERQAAIAQLRQQ 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
404-472 |
4.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953011266 404 AKSELTRLQQEETQLEQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQYDEALD 472
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
288-375 |
4.33e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.22 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAI---------RQK---------------SNEVQELQNdldretsSLQELEA 343
Cdd:pfam03148 266 QLKKTLQEIAELEKNIEALEKAIRDKEAPLklaqtrlenRTYrpnvelcrdeaqyglVDEVKELEE-------TIEALKQ 338
|
90 100 110
....*....|....*....|....*....|....*....
gi 1953011266 344 QKQDAQDRLDEMDQQKAKLRDMLSDV-------RQKCQD 375
Cdd:pfam03148 339 KLAEAEASLQALERTRLRLEEDIAVKanslfidREKCMG 377
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
288-496 |
4.37e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 368 DVRqKCQDETQMISSLktqiqsqESDLKSQEDDLNRAKSELTRLQQ--EETQLEQSIQAGKV-QLETII----------- 433
Cdd:pfam10174 549 AVR-TNPEINDRIRLL-------EQEVARYKEESGKAQAEVERLLGilREVENEKNDKDKKIaELESLTlrqmkeqnkkv 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953011266 434 KSLKSTQDEinQARSKLSQLQESHQE--------AHRTLEQYDEALD------GAHGASLTnladlSEGVSLAERGG 496
Cdd:pfam10174 621 ANIKHGQQE--MKKKGAQLLEEARRRednladnsQQLQLEELMGALEktrqelDATKARLS-----STQQSLAEKDG 690
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
282-432 |
4.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 282 EFTGVKELDdisQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQEL------------QNDLDRETSSLQ---ELEAQKQ 346
Cdd:TIGR00618 709 LETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMHQartvlkarteahFNNNEEVTAALQtgaELSHLAA 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 347 DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQE-ETQLEQSIQAG 425
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKyEECSKQLAQLT 865
|
....*..
gi 1953011266 426 KVQLETI 432
Cdd:TIGR00618 866 QEQAKII 872
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
287-467 |
5.16e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQ----------REKYSLEQDIREKEEAIRQKSNEV-----------QELQNDLDRETSSLQELEAQK 345
Cdd:PRK01156 346 SRYDDLNNQILELEgyemdynsylKSIESLKKKIEEYSKNIERMSAFIseilkiqeidpDAIKKELNEINVKLQDISSKV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 346 QDAQDRLDEMDQQKAKLR---DMLSDvRQKCQDETQMISSLKTQ--IQSQESDLKSQEDDLNRAKSELTRLQQEETQL-- 418
Cdd:PRK01156 426 SSLNQRIRALRENLDELSrnmEMLNG-QSVCPVCGTTLGEEKSNhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLkk 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953011266 419 -EQSIQAGKV-QLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQY 467
Cdd:PRK01156 505 rKEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
294-432 |
5.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 294 QEIAQLQREKYSLEQD---IREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV- 369
Cdd:PRK12705 43 QKEAEEKLEAALLEAKellLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELe 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 370 --RQKCQDETQMISSLkTQIQSQESDLKSQEDDLNRAKSELTRLQQEETQLEQSIQAGKVQLETI 432
Cdd:PRK12705 123 elEKQLDNELYRVAGL-TPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAM 186
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
287-472 |
5.36e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIrQKSNEVQELQNDLDREtsSLQELEAQKQDAQDRLDE----MDQQKAKL 362
Cdd:PTZ00440 1031 KLIKEKGKEIEEKVDQYISLLEKMKTKLSSF-HFNIDIKKYKNPKIKE--EIKLLEEKVEALLKKIDEnknkLIEIKNKS 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 363 RDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTRLQQ-EETQLE----------QSIQAGKVQLET 431
Cdd:PTZ00440 1108 HEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvNEIEIEyerilidhivEQINNEAKKSKT 1187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953011266 432 IIKSLKSTQDEINQARSKLSQLQESHqeaHRTLE---QYDEALD 472
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSKERNDH---LTTFEynaYYDKATA 1228
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
286-467 |
5.79e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 286 VKELDD---ISQEIAQLQREKYSLEQDIREKEEAIRQKSNE-VQELQNDLDRET-------SSLQELE----AQKQDAQD 350
Cdd:pfam10174 76 IQALQDelrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAkelfllrKTLEEMElrieTQKQTLGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 351 RldemDQQKAKLRDML------SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELTR---LQQEETQ---L 418
Cdd:pfam10174 156 R----DESIKKLLEMLqskglpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRrnqLQPDPAKtkaL 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953011266 419 EQSIQAGKVQLETIIKSLKSTQDEINQARSKLSQLQESHQEAHRTLEQY 467
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
285-361 |
6.84e-03 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 37.76 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 285 GVKELDDISQEIAQL---QREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA----QDRLDEMDQ 357
Cdd:pfam07321 64 LLKELEKVKQQVALLrenEADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEelrqQERQEEQEL 143
|
....
gi 1953011266 358 QKAK 361
Cdd:pfam07321 144 EEFA 147
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
305-365 |
7.10e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.39 E-value: 7.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953011266 305 SLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 365
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-372 |
8.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 287 KELDDISQEIAQLQReKYSlEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKL---- 362
Cdd:PRK03918 640 KRLEELRKELEELEK-KYS-EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekle 717
|
90
....*....|..
gi 1953011266 363 --RDMLSDVRQK 372
Cdd:PRK03918 718 kaLERVEELREK 729
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
285-372 |
8.63e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.56 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 285 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKSNEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQQKAKLR 363
Cdd:pfam03938 3 GYVDMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQ 82
|
....*....
gi 1953011266 364 DMLSDVRQK 372
Cdd:pfam03938 83 QELQKKQQE 91
|
|
| PI3K_P85_iSH2 |
pfam16454 |
Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain; This domain is found ... |
349-466 |
8.71e-03 |
|
Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain; This domain is found between the two SH2 domains in phosphatidylinositol 3-kinase regulatory subunit P85. It forms a complex with the adaptor-binding domain of phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha.
Pssm-ID: 465121 [Multi-domain] Cd Length: 161 Bit Score: 38.02 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 349 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDlnrAKSELTRLQQE--ETQLEQSIQA 424
Cdd:pfam16454 2 QEDEVVKEDDIEAVGKKLIEIHKQYLEKSREYDRLYEEYNktSQEIQMKRQALE---AFNEAIKMFEEqiKLQERFSKEA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1953011266 425 GKVQLETIIKS---LKSTQDEINQARSKLSQLQESHQEAHRTLEQ 466
Cdd:pfam16454 79 QPHEIERLLENyelLKSRLKELHDSKEQLEEDLKTQKEYNRELER 123
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
325-454 |
8.79e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 39.66 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953011266 325 QELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLrdmlsdvrQKCQDETQMISSLKTQIQSQESdLKS 396
Cdd:pfam15070 196 QHVKKELAKKLGQLQEelgelketLELKSQEAQSLQEQRDQYLAHL--------QQYVAAYQQLASEKEELHKQYL-LQT 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953011266 397 QEDDlnrakseltRLQQEETQleqsiqaGKVQLETIIKSLKSTQDEINQARSKLSQLQ 454
Cdd:pfam15070 267 QLMD---------RLQHEEVQ-------GKVAAEMARQELQETQERLEALTQQNQQLQ 308
|
|
| |
