|
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 |
5.66e-39 |
|
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: 139.33 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 24 WAVRVEEKAKFDGIFESLLP-INGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 102
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 1622897435 103 VPSALPPSLIPPSKR 117
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
171-267 |
1.45e-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: 132.79 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 171 NWVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSkG 250
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 1622897435 251 IDPPQVLSPDMVPPSER 267
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
34-99 |
5.53e-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: 5.53e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 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 |
5.96e-25 |
|
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: 99.76 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 30 EKAKFDGIFESLLPINGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPSAL 107
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDEL 87
|
90
....*....|
gi 1622897435 108 PPSLIPPSKR 117
Cdd:pfam12763 88 PDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
182-248 |
6.42e-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: 6.42e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 182 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVS 248
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
284-453 |
6.77e-19 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 89.58 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 284 TGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRVQLETIIKSLKSTQDEI 443
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAEQALDELLKEA 192
|
170
....*....|
gi 1622897435 444 NQARSKLSQL 453
Cdd:COG4372 193 NRNAEKEEEL 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-469 |
1.78e-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: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQAR 447
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|..
gi 1622897435 448 SKLSQLHESRQEAHRSLEQYDQ 469
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEE 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-494 |
9.94e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 9.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQD-------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:COG1196 368 LEAEAELAEaeeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 440 QDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 494
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-494 |
1.75e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 358
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS 438
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 439 TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 494
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-494 |
2.08e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622897435 447 RSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 494
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
295-474 |
2.55e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 374
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 375 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLH 454
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180
....*....|....*....|
gi 1622897435 455 ESRQEAHRSLEQYDQVLDGA 474
Cdd:COG1196 393 RAAAELAAQLEELEEAEEAL 412
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
310-472 |
1.81e-15 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 79.18 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 310 IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 389
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 390 QESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEahRSLEQYDQ 469
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQ 183
|
...
gi 1622897435 470 VLD 472
Cdd:COG4372 184 ALD 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-466 |
2.34e-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: 80.87 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdqqkAKLRDML 366
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180
....*....|....*....|
gi 1622897435 447 RSKLSQLHESRQEAHRSLEQ 466
Cdd:TIGR02168 858 AAEIEELEELIEELESELEA 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-474 |
3.26e-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: 80.49 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQ 358
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisrLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS 438
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897435 439 TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGA 474
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-453 |
8.58e-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: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKSTQD----E 442
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEklesE 532
|
170
....*....|.
gi 1622897435 443 INQARSKLSQL 453
Cdd:TIGR04523 533 KKEKESKISDL 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-466 |
1.08e-14 |
|
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: 76.73 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 366
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 ------------------SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQ 428
Cdd:COG4942 111 ralyrlgrqpplalllspEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622897435 429 LETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
288-476 |
1.30e-14 |
|
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: 74.19 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DVR-----QKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 442
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180 190
....*....|....*....|....*....|....
gi 1622897435 443 INQARSKLSQlhesrQEAHRSLEQYDQVLDGAHG 476
Cdd:COG1579 161 LEAEREELAA-----KIPPELLALYERIRKRKNG 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-459 |
1.83e-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: 77.37 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELNRLQQE----ETQLEQSIQagrvQLETI 432
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEisntQTQLNQLKD----EQNKI 265
|
170 180
....*....|....*....|....*..
gi 1622897435 433 IKSLKSTQDEINQARSKLSQLHESRQE 459
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-479 |
2.23e-14 |
|
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: 75.57 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 359
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897435 440 QDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASL 479
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-466 |
2.60e-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: 77.42 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 278 LGSGEFTGVKE-LDDISQEIAQLQR--------------EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE 342
Cdd:TIGR02169 284 LGEEEQLRVKEkIGELEAEIASLERsiaekereledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 343 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI-------QSQESDLKSQEDDLNRAKSELNRLQQEE 415
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 416 TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
307-465 |
3.10e-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: 77.02 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 307 EQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQ 386
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 387 IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLE 465
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-487 |
3.28e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL----NRLQQEETQLEQSIQAGRVQLETIIKSLKSTQD 441
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897435 442 EINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSE 487
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-491 |
6.03e-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: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 S-------DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRVQLETIIKSL 436
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALL 892
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 437 KS----TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSL 491
Cdd:TIGR02168 893 RSeleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
296-471 |
9.93e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 296 IAQLQREKYSLE-----------QDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 362 LRDM--LSDVRQKCQDETQMISSLKTQIQsqesDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRVQLETIIKSLKS 438
Cdd:COG4717 128 LPLYqeLEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1622897435 439 TQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 471
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-459 |
1.96e-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: 74.29 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|...
gi 1622897435 447 RSKLSQLHESRQE 459
Cdd:TIGR04523 495 EKELKKLNEEKKE 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-465 |
1.98e-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: 74.33 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKE---EAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQD---RLDEMDQQK 359
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLeQEIENVKSELKEleaRIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLSDVRQKCQDEtqMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQ---AGRVQLETIIKSL 436
Cdd:TIGR02169 775 HKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQelqEQRIDLKEQIKSI 852
|
170 180
....*....|....*....|....*....
gi 1622897435 437 KSTQDEINQARSKLSQLHESRQEAHRSLE 465
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLE 881
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
286-428 |
2.65e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKT--SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 364 DMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQ 428
Cdd:COG4717 174 ELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
286-453 |
2.75e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDetqmISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 442
Cdd:COG4717 160 ELEEELEELEAE----LAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170
....*....|...
gi 1622897435 443 --INQARSKLSQL 453
Cdd:COG4717 236 leAAALEERLKEA 248
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
286-445 |
5.45e-13 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 72.74 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDETQMI-SSLKTQI---QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....*.
gi 1622897435 440 QDEINQ 445
Cdd:COG3206 378 RLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-469 |
7.75e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD-- 364
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEEle 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 -MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEI 443
Cdd:COG1196 407 eAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
170 180
....*....|....*....|....*.
gi 1622897435 444 NQARSKlsqlHESRQEAHRSLEQYDQ 469
Cdd:COG1196 487 AEAAAR----LLLLLEAEADYEGFLE 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-466 |
8.93e-13 |
|
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: 70.95 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SdvRQKCQDETQMISSLKTQIQSQESDLKSQED------------DLNRA-KSELNRLQQEETQLEQSIQagrvQLETII 433
Cdd:COG4942 100 E--AQKEELAELLRALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPArREQAEELRADLAELAALRA----ELEAER 173
|
170 180 190
....*....|....*....|....*....|...
gi 1622897435 434 KSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-469 |
1.53e-12 |
|
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: 71.63 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 374
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 375 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLH 454
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170
....*....|....*
gi 1622897435 455 ESRQEAHRSLEQYDQ 469
Cdd:TIGR02168 393 LQIASLNNEIERLEA 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-499 |
1.56e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 70.24 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQ--------------- 349
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSvsyldvllgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 350 --DRLDEMDQQKAKLRDMLSDVrqkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRV 427
Cdd:COG3883 117 flDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 428 QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAERGGFGA 499
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-470 |
1.69e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.86 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 363
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 ---------DMLSDVRQKCQDETQMISSLKTQIQSQESD---LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLET 431
Cdd:COG3883 103 syldvllgsESFSDFLDRLSALSKIADADADLLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622897435 432 IIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQV 470
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-466 |
3.29e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKTSEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 351
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 352 LDEMDQQKAKLRDMLSDVRQKC-QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLE 430
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897435 431 TIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
291-474 |
3.76e-12 |
|
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: 70.47 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 291 DISQEIAQLQREKYSLeqDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 370
Cdd:TIGR02168 217 ELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 371 QKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvqletiikslkSTQDEINQARSKL 450
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE--------------ELKEELESLEAEL 360
|
170 180
....*....|....*....|....
gi 1622897435 451 SQLHESRQEAHRSLEQYDQVLDGA 474
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETL 384
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-446 |
5.08e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 68.39 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLksQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-471 |
7.97e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 68.89 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKT------SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 360
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 361 KLRDMLSDVRQkcqdeTQMISSLKTQIQSQESDLKSQED-------DLNRAKSELNRLQQeetQLEQSIQAGRVQLETII 433
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRA---QLQQEAQRILASLEAEL 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897435 434 KSLKST----QDEINQARSKLSQLHESRQEAhRSLEQ--------YDQVL 471
Cdd:COG3206 323 EALQAReaslQAQLAQLEARLAELPELEAEL-RRLERevevarelYESLL 371
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
288-487 |
1.01e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKTSEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 362
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 363 RDMLSDVRqkcqdetqmisslkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 442
Cdd:PRK02224 327 RDRLEECR--------------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897435 443 INQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGaSLTDL-ADLSE 487
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELRE-REAELeATLRT 437
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
287-436 |
1.06e-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: 65.72 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 366
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSElnrLQQEETQLEQSIQAGRVQLETIIKSL 436
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-472 |
1.53e-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: 68.12 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdml 366
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgrvqLETIIKSLKSTQDEINQa 446
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV----KELIIKNLDNTRESLET- 468
|
170 180
....*....|....*....|....*.
gi 1622897435 447 rsKLSQLHESRQEAHRSLEQYDQVLD 472
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQKQKELK 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
288-435 |
1.83e-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: 68.17 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 368 DVRQKCQDETQMISSLktqiqsqesdlksqEDDLNRAKSELNRLQQEETQLEQSiQAGRVQLETIIKS 435
Cdd:TIGR02169 466 KYEQELYDLKEEYDRV--------------EKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-424 |
1.95e-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: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 283 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 362 LRDMLSDVRQKCQDETQMISSLKTQIQSQ----ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 424
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
287-471 |
2.51e-11 |
|
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: 67.19 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKeeairqktsEVQELQNDLDRETSSLQELEAqkQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDK---------EIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 ---SDVRQKCQDETQMISSLKTQIQSQESDLKS-----------QEDDLNRAKS---ELNRLQQEETQLEQSIQAGRV-- 427
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEelervqqsytlNENELERVRGlekQLEELEKRYDEIVERLEEKEVay 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622897435 428 -----QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 471
Cdd:pfam06160 360 selqeELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
287-460 |
2.82e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.35 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQR--EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----------- 353
Cdd:COG3206 182 EQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellq 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 354 -----EMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDD-LNRAKSELNRLQQEETQLEQSIQagrv 427
Cdd:COG3206 262 spviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLA---- 337
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897435 428 QLETIIKSLKSTQDEINQ-------ARSKLSQLHESRQEA 460
Cdd:COG3206 338 QLEARLAELPELEAELRRlerevevARELYESLLQRLEEA 377
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
295-460 |
4.22e-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: 66.69 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSevqELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 374
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELS---ELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 375 DETQMISSLKTQIQSQESDLKSQEDD---LNRAKSELNRLQQEETQLEQsIQAGRVQLETIIKSLKSTQDEINQARSKLS 451
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 1622897435 452 QLHESRQEA 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 |
4.95e-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: 66.58 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKTSEVQE-------LQNDLDRETSSLQELEAQKQDAQDRLDEMD 356
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISElkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 357 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQ--EDDLNRAKSEL----NRLQQEETQLEQSIQAGRv 427
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELknqeKKLEEIQNQISQNNKIIS- 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897435 428 QLETIIKSLKST-----------QDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:TIGR04523 339 QLNEQISQLKKEltnsesensekQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-466 |
5.25e-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: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQ-----KQDAQDRL----DE 354
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNkelkSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 355 MDQQKAKLRDMLSDVRQKcqdeTQMISSLKTQIQSQESDLKSQEDD-------LNRAKSELNRLQQEETQLEQSIQagrv 427
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQN----NKIISQLNEQISQLKKELTNSESEnsekqreLEEKQNEIEKLKKENQSYKQEIK---- 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622897435 428 QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
288-471 |
8.04e-11 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 65.63 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKTSEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 355
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 356 ---DQQKAKLRDMLSDVR---QKCQDETQMISslktqiQS---QESDLKSQEDdlnrAKSELNRLQQEETQLEQSIQAGR 426
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKeqnKELKEEIDRVK------QSytlNESELESVRQ----LEKQLESLEKQYDEITERIAEQE 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 427 V-------QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 471
Cdd:PRK04778 376 IayselqeELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
286-476 |
9.58e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLD------RETSSLQE-------LEAQKQDAQDRL 352
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEkaeeyikLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 353 DEMDQQKAKLRDMLSDVRQKCQD------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE-QSIQAG 425
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKL 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 426 RVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQydqvLDGAHG 476
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE----LKKAKG 436
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
294-494 |
2.05e-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: 64.15 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQREKYSLEQDiREKEEAIRQKT---SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 370
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 371 QKCQDETQMISSLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEETQLEQSiqagRVQLETIIKSLKSTQDEINQARSKL 450
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL----QAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622897435 451 SQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 494
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-469 |
2.74e-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: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNRLQQEETQleQSIQAGRVQLETIIKSLKST 439
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKK 583
|
170 180 190
....*....|....*....|....*....|
gi 1622897435 440 QDEINQarsKLSQLHESRQEAHRSLEQYDQ 469
Cdd:TIGR04523 584 QEEKQE---LIDQKEKEKKDLIKEIEEKEK 610
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
301-474 |
4.77e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 301 REKYSLEQDIREKEEAIRQktsEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDmLSDVRQKCQDetqmI 380
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEEL-------AEAEERLEALEAELDALQERREALQR-LAEYSWDEID----V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 381 SSLKTQIQSQESDLksqeDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLhESRQEA 460
Cdd:COG4913 664 ASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL-QDRLEA 738
|
170
....*....|....
gi 1622897435 461 HRSLEQYDQVLDGA 474
Cdd:COG4913 739 AEDLARLELRALLE 752
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
287-472 |
5.63e-10 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 61.47 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLE---QDIREK-EEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ-Q 358
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRlaaEDFRQKyEDELNLRTSaenDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQ--------ESDLKSQEDDLNRA----KSELNRLQQEET 416
Cdd:pfam00038 141 EEEVRELQAQVSDtqvnvemdaaRKLDLTSALAEIRAQYEEIaaknreeaEEWYQSKLEELQQAaarnGDALRSAKEEIT 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 417 QLEQSIQAGRVQLETIIKSLKSTQD-----------EINQARSKLS----QLHESRQEAHRSLEQYDQVLD 472
Cdd:pfam00038 221 ELRRTIQSLEIELQSLKKQKASLERqlaeteeryelQLADYQELISeleaELQETRQEMARQLREYQELLN 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
281-363 |
6.44e-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: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 281 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 360
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 1622897435 361 KLR 363
Cdd:COG1579 160 ELE 162
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
295-442 |
7.85e-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: 60.93 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQ-------KCQDETQMISSLKTQIQSQeSDLKSQEDDL-NRAKSELNRLQQEETQLEqSIQAGR----VQLETIIK 434
Cdd:pfam09787 128 EELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELeNRLHQLTETLIQKQTMLE-ALSTEKnslvLQLERMEQ 205
|
....*...
gi 1622897435 435 SLKSTQDE 442
Cdd:pfam09787 206 QIKELQGE 213
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
287-475 |
1.16e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 60.31 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDI---REKEEAIRQKT----SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELkelAEKRDELNAQVkelrEEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLSDVRQKCQDETQM---ISSLKTQIQSQESDLKsQEDDL----NRAKSELNRLQQEETQLEqsiqagrvQLETI 432
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLrkeIERLEWRQQTEVLSPE-EEKELvekiKELEKELEKAKKALEKNE--------KLKEL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897435 433 IKSLKSTQDEINQARSKLSQLHESRQEAHRSL----EQYDQV---LDGAH 475
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMielyKEADELrkeADELH 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-487 |
1.31e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDIREKEEAIR---------QKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMD 356
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 357 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQSIQAGRVQleTIIK 434
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVER--ELRE 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 435 SLkstQDEINQARSKLSQLhesRQEAHRSLEQYDQVLDGAHGASLTDLADLSE 487
Cdd:COG4913 770 NL---EERIDALRARLNRA---EEELERAMRAFNREWPAETADLDADLESLPE 816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
288-466 |
1.48e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQL-----QREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQ-DRLDEMDQQKAK 361
Cdd:COG4913 270 RLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 362 LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQD 441
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180
....*....|....*....|....*
gi 1622897435 442 EINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAE 451
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
326-485 |
3.08e-09 |
|
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: 58.40 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 326 ELQnDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 405
Cdd:COG1579 11 DLQ-ELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 406 S--ELNRLQQEETQLEQSIQagrvQLEtiikslkstqDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLA 483
Cdd:COG1579 87 NnkEYEALQKEIESLKRRIS----DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
..
gi 1622897435 484 DL 485
Cdd:COG1579 153 EL 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-474 |
3.67e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQeIAQLQREKysleQDIREKEEAIRQKTSEVQ----ELQNDLDR-------------------ET------SS 337
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 338 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI------------------QSQESDLKSQED 399
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 400 DLNR-----------AKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYD 468
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
....*.
gi 1622897435 469 QVLDGA 474
Cdd:TIGR02169 392 EKLEKL 397
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
286-460 |
4.36e-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: 60.03 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 356
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 357 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSiqagrvqLETIIKSL 436
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170 180
....*....|....*....|....
gi 1622897435 437 KSTQDEINQARSKLSQLHESRQEA 460
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKES 671
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
287-460 |
4.61e-09 |
|
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: 57.70 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSeVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam12795 44 KALDDAPAELRELRQELAALQAKAEAAPKEILASLS-LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISS---------------LKTQIQSQESDLKSQEDDL--NRAKSELNRLQQEETQLEQSiqagrvQL 429
Cdd:pfam12795 123 SEARQRLQQIRNRLNGpappgeplseaqrwaLQAELAALKAQIDMLEQELlsNNNRQDLLKARRDLLTLRIQ------RL 196
|
170 180 190
....*....|....*....|....*....|.
gi 1622897435 430 ETIIKSLKSTQDEINQARSKLSQLHESRQEA 460
Cdd:pfam12795 197 EQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
297-482 |
7.06e-09 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 58.94 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 297 AQLQrekySLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 376
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 377 TQMISSLKTQIQSQESDLKSQEDDLNRaKSELNRLQ----QEETQLEQSIQA-----GRVQLETIIKsLKSTQDEINQAR 447
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETIAE-LKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622897435 448 SKLSQLHESRQEAHRSLEQYDQVLDGAHGA---SLTDL 482
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLEQARNErkkTLTGL 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
288-447 |
1.81e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREkySLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEqsiqagrvqletiiKSLKSTQDEINQAR 447
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE--------------ATLRTARERVEEAE 446
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
286-459 |
2.18e-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: 58.13 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEvQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR 363
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQQaaKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRVQLETIIKSLKSTQ 440
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlQRRQQFEEQLVELSTEVQSLI 901
|
170
....*....|....*....
gi 1622897435 441 DEINQARSKLSQLHESRQE 459
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEK 920
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
287-474 |
2.48e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKyslEQDIREKEEAI------RQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 360
Cdd:PRK02224 213 SELAELDEEIERYEEQR---EQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 361 KLRDMLSDVRQKC-----QDET--QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETII 433
Cdd:PRK02224 290 ELEEERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622897435 434 KSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGA 474
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
290-466 |
2.52e-08 |
|
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: 57.21 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 369
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 370 RQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKSTQDEINQARSK 449
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERKVEGLGEE 259
|
170
....*....|....*..
gi 1622897435 450 LSQLHESRQEAHRSLEQ 466
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQ 276
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-465 |
3.08e-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: 57.77 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMdqqKAKLRDM 365
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENL---NGKKEEL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQdE 442
Cdd:TIGR02169 867 EEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-E 945
|
170 180
....*....|....*....|...
gi 1622897435 443 INQARSKLSQLHESRQEAHRSLE 465
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIR 968
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-487 |
3.17e-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: 56.70 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 343 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI 422
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 423 QAGRVQLETIIKSL--KSTQDEINQ-ARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSE 487
Cdd:COG4942 100 EAQKEELAELLRALyrLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
288-475 |
4.18e-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: 54.37 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DVRQKCQD------ETQMISSLKTQIQSQESDLKSQE--DDLNRAKSELNRLQqeetQLEQSIQAGRVQLETIIKSLKS- 438
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHK----ELEEELEAHEPRLKSLNELAEEl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622897435 439 ----TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAH 475
Cdd:cd00176 173 leegHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-499 |
6.20e-08 |
|
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: 56.50 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELNRLQqeetqlEQSIQAgrvqletiiksLKSTQDEINQAR 447
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLR------EQSGEA-----------LADSQEVTAAMQ 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 448 SKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAERggFGA 499
Cdd:COG3096 634 QLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAER--LGG 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
314-494 |
6.21e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 314 EEAIRqktsEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQMISSLKTQI 387
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 388 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgrvqletiikslkSTQDEINQARSKLSQLHESRQEAHRSLEQY 467
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180
....*....|....*....|....*..
gi 1622897435 468 DQVLDGAHGASLTDLADLSEGVSLAER 494
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAA 391
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
294-423 |
8.71e-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: 51.49 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQREKYSLEQDIREKEEAIrqktsevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 373
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622897435 374 QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSelnRLQQEETQLEQSIQ 423
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIE 113
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-482 |
9.72e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 341 LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD--ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 419 EQSIQAGRVQLETIIKS--LKSTQDEINQARSKLSQL-------HESRQEAHRSLEQYDQVLDGAHGASLTDL 482
Cdd:COG3206 246 RAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQLQQEAQRILASL 318
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
297-452 |
1.33e-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: 55.13 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 297 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 351
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 352 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS 421
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190
....*....|....*....|....*....|.
gi 1622897435 422 IQagrvQLETIIKSLKSTQDEINQARSKLSQ 452
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEIQS 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-445 |
1.41e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQKCQDETQMISSLKTQIQSQESD---------------------------------------------------- 393
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealenkieddeeearrrlkrlenkikelgpvnlaaieeyeelkeryd 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 394 -LKSQEDDLNRAKselnrlqqeeTQLEQSIQagrvQLETIIKS-LKSTQDEINQ 445
Cdd:TIGR02168 1004 fLTAQKEDLTEAK----------ETLEEAIE----EIDREARErFKDTFDQVNE 1043
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-471 |
1.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 366
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRvQLETIIKSLKST-----Q 440
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdLDADLESLP-EYLALLDRLEEDglpeyE 833
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897435 441 DEINQARSK---------LSQLHESRQEAHRSLEQYDQVL 471
Cdd:COG4913 834 ERFKELLNEnsiefvadlLSKLRRAIREIKERIDPLNDSL 873
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
282-478 |
1.64e-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: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 282 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 357
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 358 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQEsdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRVQLETII---- 433
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRakle 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622897435 434 KSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGAS 478
Cdd:COG5185 510 RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
308-484 |
1.78e-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: 55.18 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 308 QDIREKEEAIRQktsEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 387
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 388 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQY 467
Cdd:pfam01576 267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQ 346
|
170
....*....|....*..
gi 1622897435 468 DQVLDGAHGASLTDLAD 484
Cdd:pfam01576 347 LQEMRQKHTQALEELTE 363
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-538 |
2.20e-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: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 362
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 363 RDMLSDVRQKCQDETQMISslktqiqsqesdlksqeddlnRAKSELNRLQQEETQLEQSIQAGRVQLETiIKSLKSTQD- 441
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVG---------------------QHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKDa 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 442 EINQARSKLSQLH----------ESRQEAHRSLEQ-YDQVLDGAHgASLTDLADLSEGVSLAERGgfgamddpFKNKALL 510
Cdd:pfam15921 619 KIRELEARVSDLElekvklvnagSERLRAVKDIKQeRDQLLNEVK-TSRNELNSLSEDYEVLKRN--------FRNKSEE 689
|
250 260 270
....*....|....*....|....*....|....*
gi 1622897435 511 FSNNTQEL-------HPDPFQTEDPFKSdpFKGAD 538
Cdd:pfam15921 690 METTTNKLkmqlksaQSELEQTRNTLKS--MEGSD 722
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
294-494 |
2.21e-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: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 354
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 355 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL------------NRAKSELNRLQQE-------E 415
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEElsqnrsrR 1075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 416 TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQ--------------------LHESR---QEAH--RSLEqyDQV 470
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQakagwcavlrlardndverrLHRRElayLSADelRSMS--DKA 1153
|
250 260
....*....|....*....|....*....
gi 1622897435 471 LDGAHGA-----SLTDLADLSEGVSLAER 494
Cdd:COG3096 1154 LGALRLAvadneHLRDALRLSEDPRRPER 1182
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
287-450 |
2.28e-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: 54.26 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 349
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 350 DRLDEMDQQ--KAK---------LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE--- 415
Cdd:pfam05667 415 QRLVELAGQweKHRvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622897435 416 --TQ--LE--QSIQAGRVQLETIIKSLKSTQDEINQARSKL 450
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-497 |
2.35e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 447 RSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAERGGF 497
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
286-465 |
2.66e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQKCQDEtqmissLKTQIQSQESDLKsQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQ 445
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPFYN-EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
170 180
....*....|....*....|.
gi 1622897435 446 ARSKLSQ-LHESRQEAHRSLE 465
Cdd:PRK03918 652 LEKKYSEeEYEELREEYLELS 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
299-460 |
2.87e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 299 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 363
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 ---------DMLSDVRQKC------QDETQMISSLKTQIQSQESDLKSQEDDLNRAkselnRLQQEETQLEQSIQAGRVQ 428
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEE 447
|
170 180 190
....*....|....*....|....*....|....
gi 1622897435 429 LETIIKSLKSTQDEINQARS--KLSQLHESRQEA 460
Cdd:COG4717 448 LEELREELAELEAELEQLEEdgELAELLQELEEL 481
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
305-494 |
2.93e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 52.13 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 305 SLEQDIREKEEAIRQktsEVQELQNDLDRETSSL-------QELEAQKQDAQDRLDEMdQQKAKL----------RDMLS 367
Cdd:COG1842 16 ALLDKAEDPEKMLDQ---AIRDMEEDLVEARQALaqvianqKRLERQLEELEAEAEKW-EEKARLalekgredlaREALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DvRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRVQLETIIKSL--KSTQDEI 443
Cdd:COG1842 92 R-KAELEAQ---AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSGIdsDDATSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 444 NQARSKLSQLhESRQEAHRSLeqydqvldgAHGASLTD-LADLSEGVSLAER 494
Cdd:COG1842 168 ERMEEKIEEM-EARAEAAAEL---------AAGDSLDDeLAELEADSEVEDE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
277-481 |
3.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 277 SLGSGEFTGVKELDDISQEIAQLQRekysLEQDIREKEEAIRQKTSEvQELQNDLDR-ETSSLQELEA---QKQDAQDRL 352
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 353 DEMDQQKAKLRDMLSDVRQKCQDETQmiSSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS--IQAGRVQLE 430
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELE 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 431 TIIKSLKSTQDEINQARSKLSQLHESRQEAHRslEQYDQVLDGA--HGASLTD 481
Cdd:COG4717 480 ELKAELRELAEEWAALKLALELLEEAREEYRE--ERLPPVLERAseYFSRLTD 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
282-497 |
3.55e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 282 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKTSEVQELQNDLDRET-SSLQELEaqkqdaqDRLDEMD 356
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELE-------ERLKELE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 357 QQKAKLRDmLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ------------EETQLEQSIQA 424
Cdd:PRK03918 599 PFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeelreEYLELSRELAG 677
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 425 GRVQLETiiksLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDgahgasltDLADLSEGV----SLAERGGF 497
Cdd:PRK03918 678 LRAELEE----LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE--------RVEELREKVkkykALLKERAL 742
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-486 |
4.38e-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: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKTSEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 440 QDEINQARSKLSQLHE-------SRQEahrsLEQYDQVLDGAHGASLTDLADLS 486
Cdd:pfam01576 179 SKLKNKHEAMISDLEErlkkeekGRQE----LEKAKRKLEGESTDLQEQIAELQ 228
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
304-413 |
5.18e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.32 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 304 YSLEQDIR---------EKEEAIRQKTSEVQELQnDLDRETSSL----QELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 370
Cdd:COG2433 376 LSIEEALEeliekelpeEEPEAEREKEHEERELT-EEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622897435 371 QKCQDE---TQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ 413
Cdd:COG2433 455 SEERREirkDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
294-493 |
5.39e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 373
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 374 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELNRLQqeetqlEQS--IQAGRVQLETIIKSLKSTQDEINQARSKLS 451
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLR------EQSgeEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897435 452 QLHESRQEAHRSLEQYdqvlDGAHGASLTDLADLSEGVSLAE 493
Cdd:PRK04863 652 ARKQALDEEIERLSQP----GGSEDPRLNALAERFGGVLLSE 689
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
287-460 |
5.70e-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: 53.58 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAqkqdaqdRLDEMDQQKAKL---- 362
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA-------RVSDLELEKVKLvnag 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 363 RDMLSDVRQKCQDETQMISSLKTqiqsqesdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRVQLETIIK----SLKS 438
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKT------------------SRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKS 703
|
170 180
....*....|....*....|..
gi 1622897435 439 TQDEINQARSKLSQLHESRQEA 460
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHA 725
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-470 |
6.26e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 313 KEEAIRQ--KTSE----VQELQNDLDRetsSLQELEAQKQDAQ------------------DRLDEMDQQKAKLRDMLSD 368
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELER---QLKSLERQAEKAErykelkaelrelelallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 369 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARS 448
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180
....*....|....*....|..
gi 1622897435 449 KLSqlhESRQEAHRSLEQYDQV 470
Cdd:TIGR02168 331 KLD---ELAEELAELEEKLEEL 349
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-466 |
8.26e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKT--SEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 364
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 MLSDVRQKCQDETQMISsLKTQIQSQESDLK-----------SQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETII 433
Cdd:PRK03918 544 LKKELEKLEELKKKLAE-LEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDAEK----ELEREE 618
|
170 180 190
....*....|....*....|....*....|...
gi 1622897435 434 KSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-466 |
9.72e-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: 52.76 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 305 SLEQDIREKEEAI--------------RQKTSEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 370
Cdd:TIGR02169 643 TLEGELFEKSGAMtggsraprggilfsRSEPAELQRLRERL-------EGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 371 QKC---QDETQMI----SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQ-DE 442
Cdd:TIGR02169 716 RKIgeiEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPE 795
|
170 180
....*....|....*....|....
gi 1622897435 443 INQARSKLSQLHESRQEAHRSLEQ 466
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQ 819
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
287-432 |
1.24e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 357
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 358 QKAKLRDMLSDVRQKCQDetqmISSLkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 432
Cdd:PRK12704 129 KEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAI 198
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
287-452 |
1.25e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 356
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 357 QQKAKLRDMLSDVRqkcQDETQMISSLKTQIQSqESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQ-LETIIKS 435
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQrLEHQLQL 245
|
170
....*....|....*..
gi 1622897435 436 LkstQDEINQARSKLSQ 452
Cdd:PRK11281 246 L---QEAINSKRLTLSE 259
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
290-459 |
1.28e-06 |
|
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: 52.05 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 358
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQK--CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETiiKSL 436
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL--ADP 436
|
170 180
....*....|....*....|...
gi 1622897435 437 KSTQDEINQARSKLSQLHESRQE 459
Cdd:pfam05557 437 SYSKEEVDSLRRKLETLELERQR 459
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
290-452 |
1.29e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.06 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE----------LEAQKQDAQDRlDEMDQqk 359
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNrwrekvfalmVQLKAQDLEHR-DSVKQ-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 akLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:pfam07111 336 --LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
170
....*....|...
gi 1622897435 440 QDEINQARSKLSQ 452
Cdd:pfam07111 414 QIWLETTMTRVEQ 426
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
289-475 |
1.41e-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: 52.15 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKTSEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 360
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 361 KLRDMLSDVRQKCQDEtqmisslKTQIQSQESDLKSQEDDLNrAKSELnRLQQEETQLEqsIQAGRVQLETIIKSLKSTQ 440
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQAT-ATPEL-LLQLENFDER--IERAREEQEAANAEVERLQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1622897435 441 DEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAH 475
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
358-466 |
1.42e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 358 QKAKLRdmLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE----ETQLEQS---IQAGRVQLE 430
Cdd:COG4372 9 GKARLS--LFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseLEQLEEELE 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622897435 431 TIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
287-460 |
1.54e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYS---LEQDIREKEEaiRQKTSEV-QELQNDLDRETSSL-QELEAQKQ--DAQDRLDEMDQQK 359
Cdd:COG1340 92 EELDELRKELAELNKAGGSidkLRKEIERLEW--RQQTEVLsPEEEKELVEKIKELeKELEKAKKalEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQSqesdLKSQEDDLNRaksELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRK---EADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
170 180
....*....|....*....|.
gi 1622897435 440 QDEINQARSKLSQLHESRQEA 460
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKE 263
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
287-474 |
1.84e-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: 51.89 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslqELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----EAEDMLACEQHALLRKLQPEQDLQDVR 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQmissLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEetQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:TIGR00618 632 LHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSIRVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
170 180
....*....|....*....|....*...
gi 1622897435 447 RSKLSQLHESRQEAHRSLEQYDQVLDGA 474
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-494 |
1.86e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 330 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL-NRAKSE- 407
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 408 ---------------------------LNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEA 460
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....
gi 1622897435 461 HRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 494
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-471 |
2.15e-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: 51.56 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQ-----------------NDLDRETSSLQE--------- 340
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikdlndklkknkdkiNKLNSDLSKINSeikndkeqk 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 341 --LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:TIGR04523 120 nkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 419 EQSIqagrVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 471
Cdd:TIGR04523 200 ELLL----SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-472 |
2.21e-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: 51.71 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 363
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQEDDLNRAKSE----LNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190
....*....|....*....|....*....|...
gi 1622897435 440 QDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 472
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
289-472 |
2.22e-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: 51.33 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDIREKEeairqktSEVQELQNDL--------DRET------SSLQELEA-------QKQD 347
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALE-------SENAELQAELrtlqqakqDSEHkrkkleGQLQELQArlseserQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 348 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLksQEDdlNRAK----SELNRLQQEET----QLE 419
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL--QEE--TRQKlnlsTRLRQLEDERNslqeQLE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 420 QSIQAGRV---QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 472
Cdd:pfam01576 507 EEEEAKRNverQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
280-472 |
2.42e-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: 51.36 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 280 SGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE---AQKQDAQDRL-DE 354
Cdd:pfam10174 379 AGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKERIIERLkEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 355 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQES---DLKSQEDDLN-RAKSELNRLQQEETQLEQSIQAGrVQLE 430
Cdd:pfam10174 459 REREDRERLEELESLKKENKDLKEKVSALQPELTEKESsliDLKEHASSLAsSGLKKDSKLKSLEIAVEQKKEEC-SKLE 537
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 431 TiikSLKSTQDEINQAR------SKLSQLHES----RQEAHRSLEQYDQVLD 472
Cdd:pfam10174 538 N---QLKKAHNAEEAVRtnpeinDRIRLLEQEvaryKEESGKAQAEVERLLG 586
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
286-448 |
2.61e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdQQKAKLRD 364
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYdELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI----EQFQKVIK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 MLSD------VRQKCQDETQMISSLKT---QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKS 435
Cdd:PHA02562 280 MYEKggvcptCTQQISEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
170
....*....|...
gi 1622897435 436 LKSTQDEINQARS 448
Cdd:PHA02562 360 AKKVKAAIEELQA 372
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
286-414 |
2.65e-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: 50.02 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREkeeaIRQKTSEVQEL-QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 364
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQ----LKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 365 MLSDVRQKCQDetqmissLKTQIQSQESDLKS----QEDDLNRAKSELNRLQQE 414
Cdd:smart00787 240 KIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-405 |
2.67e-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: 50.53 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREkysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 368
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622897435 369 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 405
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
340-470 |
2.67e-06 |
|
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: 51.22 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 340 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 419
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 420 QSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLhesrqEAHRSLEQYDQV 470
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDL-----EARLSHSRIPEI 796
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
305-466 |
3.23e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 305 SLEQDIREKEeairqktSEVQELQNDLDRETSSLQEL-EAQKQDAQDRLDEMDQQKAKL-------RDMLSDVRQKCQDE 376
Cdd:pfam00038 22 FLEQQNKLLE-------TKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLqleldnlRLAAEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 377 TQMISSLKTQIQsqesDLKSQEDDLNRAKSEL-NRLQ--QEE------------TQLEQSIQAGRVQLE----------T 431
Cdd:pfam00038 95 LNLRTSAENDLV----GLRKDLDEATLARVDLeAKIEslKEElaflkknheeevRELQAQVSDTQVNVEmdaarkldltS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897435 432 IIKSLKSTQDEINQaRSKL-------SQLHESRQEAHRSLEQ 466
Cdd:pfam00038 171 ALAEIRAQYEEIAA-KNREeaeewyqSKLEELQQAAARNGDA 211
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
288-475 |
4.45e-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: 50.43 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYS---------LEQDIREKEEAIRQKTSEVQELQ-----------------NDLDRETSSLQEL 341
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGsdldrtvqqVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktNELKSEKLQIGTN 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 342 EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQ----IQSQESDLKSQEDDLNRAKSELNRLQQEETQ 417
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 418 LEQSIQAGRVqletiiKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAH 475
Cdd:TIGR00606 960 IENKIQDGKD------DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-487 |
5.29e-06 |
|
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: 50.34 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQ-------LQREKYSLEQDIREK---------EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQ----- 346
Cdd:COG3096 793 ERDELAEQYAKasfdvqkLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeq 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 347 -----------------DAQDRLDEMDQQKAKLRDMLSDVRQKCqdetQMISSLKTQIQSQESDLKSQED---DLNRAKS 406
Cdd:COG3096 873 lqllnkllpqanlladeTLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLVAVLQSDPEQFEQlqaDYLQAKE 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 407 ELNRLQQEETQLEQSIQ-------AGRVQLetiiksLKSTQDEINQARSKLSQLHESRQEAHRSLEQ-------YDQV-- 470
Cdd:COG3096 949 QQRRLKQQIFALSEVVQrrphfsyEDAVGL------LGENSDLNEKLRARLEQAEEARREAREQLRQaqaqysqYNQVla 1022
|
250
....*....|....*...
gi 1622897435 471 -LDGAHGASLTDLADLSE 487
Cdd:COG3096 1023 sLKSSRDAKQQTLQELEQ 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-465 |
5.67e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQdaqdRLDEMDQQKAKLRDML 366
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS---------ELNRLQQEETQLEQSIQAGRVQLETIIKSLK 437
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180
....*....|....*....|....*...
gi 1622897435 438 STQDEINQARSKLSQLHESRQEAHRSLE 465
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLE 355
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-487 |
5.76e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 343 AQKQDAQDRLDEMDQQKAKLRDMLSDVR-------------------QKCQDETQMISSLKtQIQSQESDLKSQEDDLNR 403
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGELErqleplerqaekaeryrelKEELKELEAELLLL-KLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 404 AKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQL-------HESRQEAHRSLEQYDQVLDGAHG 476
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEE 330
|
170
....*....|.
gi 1622897435 477 ASLTDLADLSE 487
Cdd:COG1196 331 ELEELEEELEE 341
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
319-474 |
6.02e-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: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 319 QKTSEVQELQNDLdretSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQMISSLKTQIQ 388
Cdd:pfam12795 14 AKKKLLQDLQQAL----SLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLEELEQRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 389 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRS-LEQY 467
Cdd:pfam12795 89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAqIDML 168
|
....*..
gi 1622897435 468 DQVLDGA 474
Cdd:pfam12795 169 EQELLSN 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
348-437 |
6.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 348 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRV 427
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|
gi 1622897435 428 QLETIIKSLK 437
Cdd:COG4942 98 ELEAQKEELA 107
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
289-442 |
6.29e-06 |
|
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: 47.30 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLeqdiREKEEAIRQKTsevQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 368
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 369 VRQKCQDET-----QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEqsiqagrvQLETIIKSLKSTQDE 442
Cdd:pfam16043 81 VSRDQFDETleelnQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKE--------LLERRIKALQKLLQE 151
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
296-447 |
7.10e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 296 IAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 356
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 357 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN------------RAKSELNRLQQE-------ETQ 417
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgaeeRARARRDELHARlsanrsrRNQ 1078
|
170 180 190
....*....|....*....|....*....|
gi 1622897435 418 LEQSIQAGRVQLETIIKSLKSTQDEINQAR 447
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
300-420 |
7.13e-06 |
|
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: 46.06 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 300 QREKYSLEQDIREKEEAIRQKtsevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQM 379
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622897435 380 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQ 420
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
288-462 |
8.35e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.92 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 351
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 352 ---LD-----------------EMDQQKAKLR---DMLSDVRQKCqdetqmISSLK---TQIQSQEsdlKSQEDDLNRAK 405
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQET------IAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 406 SELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHR 462
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
286-477 |
9.88e-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: 49.45 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 358
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 -------------KAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSI 422
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 423 QAGRVQLETIIKSLKSTQDEINQA-------RSKLSQLHE---------SRQEAHRSLEQYDQVLDGAHGA 477
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENlrglrceMSKLATLKEdanseqaqgSIGERLAQLEDLKLKRDYLSES 908
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-472 |
9.99e-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: 49.25 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQ---DETQMISSLKTQIQSQESDLKSQEDDLNRAkselnrlqqeetqLEQSIQAGRVQLETIIKSLKSTQDEI 443
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDIIEL-------------MKDWLKELSLHYKKYITRMIRIKDLP 707
|
170 180
....*....|....*....|....*....
gi 1622897435 444 nqarsKLSQLHESRQEAHRSLEQYDQVLD 472
Cdd:TIGR04523 708 -----KLEEKYKEIEKELKKLDEFSKELE 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
288-466 |
1.01e-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: 49.35 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGR---------VQ-LETIIKSL 436
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRrelddrnmeVQrLEALLKAM 438
|
170 180 190
....*....|....*....|....*....|
gi 1622897435 437 KStqdeinQARSKLSQLHESRQEAHRSLEQ 466
Cdd:pfam15921 439 KS------ECQGQMERQMAAIQGKNESLEK 462
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
385-469 |
1.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 385 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSL 464
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
....*
gi 1622897435 465 EQYDQ 469
Cdd:COG4372 104 ESLQE 108
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
306-458 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 306 LEQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQ 378
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 379 MISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQagrvQLETIIKSL----KSTQDEINQARSKLSQL 453
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKR----ELESEIKKLthdiKLKEEQIRELEIKVQEL 555
|
....*
gi 1622897435 454 HESRQ 458
Cdd:pfam09726 556 RKYKE 560
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
294-471 |
1.22e-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: 49.02 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQRekySLEQDIREKEEAI---RQK-TSEVQELQNDLD---RETSSL----QELEAQKQDAQDRL-------DEM 355
Cdd:pfam01576 327 QEVTELKK---ALEEETRSHEAQLqemRQKhTQALEELTEQLEqakRNKANLekakQALESENAELQAELrtlqqakQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 356 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQL--ETII 433
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQ 483
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622897435 434 K-----SLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 471
Cdd:pfam01576 484 KlnlstRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
287-391 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKtseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKK---EQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|....*
gi 1622897435 367 SDVRQKcqdetqmISSLKTQIQSQE 391
Cdd:pfam13863 83 KKLTAQ-------IEELKSEISKLE 100
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
194-267 |
1.44e-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: 44.67 E-value: 1.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 194 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 267
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
288-471 |
1.45e-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: 48.81 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 367
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ-LALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 DV---RQKCQDETQMISSLKTQIQSQESDLK----------------SQEDDLNRAKSELNRLQ--QEETQLEQSIQAGR 426
Cdd:TIGR00618 712 HIeeyDREFNEIENASSSLGSDLAAREDALNqslkelmhqartvlkaRTEAHFNNNEEVTAALQtgAELSHLAAEIQFFN 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897435 427 VQLETIIKSLKSTQDEINQARSKLSQLHESRQE-AHRSLEQYDQVL 471
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRL 837
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
377-471 |
1.48e-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: 48.22 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 377 TQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgrvqletIIKSLKSTQDEINQARSKLSQLHES 456
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKE 91
|
90
....*....|....*
gi 1622897435 457 RQEAHRSLEQYDQVL 471
Cdd:COG4942 92 IAELRAELEAQKEEL 106
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
295-453 |
1.63e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYslEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK--QDAQDRLDEMDQQKAKL---------- 362
Cdd:COG5022 827 KREKKLRETE--EVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQrvELAERQLQELKIDVKSIsslklvnlel 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 363 --------RDMLSDVRQKCQDETQMISSLKTQIQsqESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIK 434
Cdd:COG5022 905 eseiielkKSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHEVESKLKETSE----EYEDLLK 978
|
170
....*....|....*....
gi 1622897435 435 SLKSTQDEINQARSKLSQL 453
Cdd:COG5022 979 KSTILVREGNKANSELKNF 997
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
385-455 |
1.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 385 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHE 455
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
287-478 |
1.74e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQ-------------------KC----------------QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSelnrL 411
Cdd:PRK02224 429 AELEAtlrtarerveeaealleagKCpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED----L 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 412 QQEETQLEQSiqagRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGAS 478
Cdd:PRK02224 505 VEAEDRIERL----EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
287-467 |
1.78e-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: 48.56 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ----QEETQLEQsiqagRVQLETIIKSLKSTQDE 442
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 1622897435 443 IN---QARSKLSQLHESRQEAHRSLEQY 467
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
292-464 |
1.88e-05 |
|
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: 47.77 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 292 ISQEIAQLQREKYSLEQDIREKEEAIRQktsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 368
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVLNELKKDFKQ---LLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 369 --VRQKCQdetQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ-------------QEETQLEQSI----------- 422
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMasllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 423 ----QAGRV-----------------QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSL 464
Cdd:pfam04108 192 dqcvTAVKLteggraemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
338-456 |
2.32e-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: 48.19 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 338 LQELEAQKQDAQDRLDEMDQ----QKAKLRDMLSDVRQKCQdETQMISSLKTQIQSQESdlKSQEDDLNRAKSELNRLQQ 413
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElhekQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES--QSQEDLRNQLQNTVHELEA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622897435 414 EETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHES 456
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEA 199
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
286-414 |
2.36e-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: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 365
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622897435 366 lsdvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 414
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
327-472 |
2.44e-05 |
|
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: 46.46 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 327 LQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKS 406
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRAL-------KAELESLEVYNRQLERLVASQEQEIASLER 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 407 ELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARskLSQLHESRQEAHRSL-EQYDQVLD 472
Cdd:pfam11932 84 QIEEIERTERELVPLMLKMLDRLEQFVALDLPFLLEERQAR--LARLRELMDDADVSLaEKYRRILE 148
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
336-455 |
3.08e-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: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 336 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISslkTQIQSQESDLKSqeddLNRAKSELNRLQQEE 415
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622897435 416 TQLEQSIQAGRVQLETIIKSLKST----QDEINQARSKLSQLHE 455
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNE 117
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
293-460 |
3.55e-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: 46.25 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 293 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV-RQ 371
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALpSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 372 KCQDETQMISSLKTQIQSQesDLKSQ----EDDLNRAKSELNRLQqeetQLEQSIQAgrvQLETIiksLKSTQDEINQAR 447
Cdd:pfam06008 119 DLSRMLAEAQRMLGEIRSR--DFGTQlqnaEAELKAAQDLLSRIQ----TWFQSPQE---ENKAL---ANALRDSLAEYE 186
|
170
....*....|...
gi 1622897435 448 SKLSQLHESRQEA 460
Cdd:pfam06008 187 AKLSDLRELLREA 199
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
289-455 |
3.67e-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: 47.42 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQR-----------EKYSLEQDI-------------REKEEAIRQKTSEVQE-LQNDLDretSSLQELEA 343
Cdd:pfam15921 80 LEEYSHQVKDLQRrlnesnelhekQKFYLRQSVidlqtklqemqmeRDAMADIRRRESQSQEdLRNQLQ---NTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 344 QKQDAQDRLDEMDQQKAKLRDM-------LSDVR-----------QKCQDETQM-----------ISSLKTQIQSQESDL 394
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMmlshegvLQEIRsilvdfeeasgKKIYEHDSMstmhfrslgsaISKILRELDTEISYL 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 395 KSQ----EDDLNRAKSELNR-----LQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHE 455
Cdd:pfam15921 237 KGRifpvEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
307-431 |
3.72e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.77 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 307 EQDIREKEEAIRQKTSEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSD----VRQKc 373
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPnspqVRQL- 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 374 qdETQmISSLKTQIQSQESDL--KSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLET 431
Cdd:COG3524 255 --RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
287-460 |
3.97e-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: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNdlDRETSSLQELEAQK--QDAQDRLDEMDQQKAKLRD 364
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAE--ERRQRLEEALDLQQffRDADDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 MlsdvrqkcqdetQMISSLkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRvqletiIKSLKSTQDEIN 444
Cdd:cd00176 132 E------------DLGKDL-ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDA------DEEIEEKLEELN 192
|
170
....*....|....*.
gi 1622897435 445 QARSKLSQLHESRQEA 460
Cdd:cd00176 193 ERWEELLELAEERQKK 208
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
300-484 |
4.01e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 300 QREKYSLEQDIREKEEAIRQktsevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 377
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 378 -QMISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELNRLQQEETQLEQSIQA--GRVQLETI 432
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 433 I-------KSLKSTQD-------------EINQARSKLSQLhesrqEAH-RSLEQYDQV-LDGAHGASLTDLAD 484
Cdd:PRK11281 342 LyqqqqalPSADLIEGladriadlrleqfEINQQRDALFQP-----DAYiDKLEAGHKSeVTDEVRDALLQLLD 410
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
335-468 |
4.10e-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: 46.65 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 335 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK------ 405
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapig 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 406 --------SELNRLQQEETQLEQSI-QAGRVQLE---TIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYD 468
Cdd:pfam00529 137 gisreslvTAGALVAQAQANLLATVaQLDQIYVQitqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
294-483 |
4.16e-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: 47.27 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQREKYSLEQD---IREKEEAIRQKTSEVQELQNDLDRE-TSSLQELEAQKQDA------QDRLDEMDQQKAKLR 363
Cdd:TIGR00618 462 QESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDETQMISSLKTQIQsqesdlksqeddlnrakselnRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEI 443
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQ---------------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897435 444 NQarsklsqlhESRQEAHRSLEQYDQVLDGAHGASLTDLA 483
Cdd:TIGR00618 601 EK---------LSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
287-449 |
4.19e-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: 45.44 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQED--------DLNRAKSELNRLQ--QEETQLEQSIQAGRVQLETI 432
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNllkARLKAAKAQEAvqtslgslSTSSATDSFERIEekIEEREARADAAAELASAVDL 192
|
170
....*....|....*..
gi 1622897435 433 IKSLKstQDEINQARSK 449
Cdd:pfam04012 193 DAKLE--QAGIQMEVSE 207
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
288-481 |
4.31e-05 |
|
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: 46.48 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL---QELE--------AQKQDAQD---RLD 353
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAewkLELErvlpqlkvTIKADAKDwraHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 354 EMDQQKAKLRDMLSDVRQKcqdetqmisslktqiqsqesdLKSQEDDLNRAkseLNRLQQEETQLEQsiqagrvQLETII 433
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 434 KSLKSTQDEINQARSKLSQLHESRQEAHRSL----EQYDQV---LDgAHGASLTD 481
Cdd:pfam10498 275 QEYREAQDELSEVQEKYKQLSEGVTERTRELaeitEELEKVkqeME-ERGSSMTD 328
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
275-414 |
4.36e-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: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 275 SGSLGSGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDR 351
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 352 LDEMdqqKAKLRDMLSDVRQKCQDETQMISSLKTQIQsQESDLKSQEDDLNRAKselNRLQQE 414
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLEALEEGKKRLQRELEALTQ-QLEEKAAAYDKLEKTK---NRLQQE 581
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
298-458 |
4.49e-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: 47.04 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 298 QLQREKYSLEQdIREKEEAIRQKtsEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLrDMLSDVRQKCQD 375
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 376 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ---EETQLEQSIQAGRVQLEtiIKSLKSTQDEINQA---RSK 449
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKaiyEEERRREAEEERRKQQE--MEERRRIQEQMRKAteeRSR 567
|
....*....
gi 1622897435 450 LSQLHESRQ 458
Cdd:pfam17380 568 LEAMERERE 576
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
324-469 |
4.51e-05 |
|
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: 45.50 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 324 VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdETQMISSL---KTQ----IQSQESDLKS 396
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKH----ENDNLSSMlnrKERrlkdLEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 397 QEDDLNRAKSEL----NRLQQEETQLEQSIQAGRVQLETIIKSLK----STQDEINQARSKLSQLhesRQEAHRSLEQYD 468
Cdd:pfam17078 81 SYEELTESNKQLkkrlENSSASETTLEAELERLQIQYDALVDSQNeykdHYQQEINTLQESLEDL---KLENEKQLENYQ 157
|
.
gi 1622897435 469 Q 469
Cdd:pfam17078 158 Q 158
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
322-517 |
4.53e-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: 46.21 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 322 SEVQELQNDLDRETSSlQELEAQKQDAQDRLDEMdQQKAKlrdmlsDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL 401
Cdd:cd22656 94 AEILELIDDLADATDD-EELEEAKKTIKALLDDL-LKEAK------KYQDKAAKVVDKLTDFENQTEKDQTALETLEKAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 402 NrakselNRLQQEETQLEQSiqagrvQLETIIKSLKSTQDEI-NQARSKLSQLHESRQEAHRSLeQYDQVLDGAHGASLT 480
Cdd:cd22656 166 K------DLLTDEGGAIARK------EIKDLQKELEKLNEEYaAKLKAKIDELKALIADDEAKL-AAALRLIADLTAADT 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622897435 481 DLADLSEGVSLAE------RGGFGAMDDPFKNKALLFSNNTQE 517
Cdd:cd22656 233 DLDNLLALIGPAIpaleklQGAWQAIATDLDSLKDLLEDDISK 275
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
321-469 |
4.78e-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: 46.16 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 321 TSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmisslktqiqSQESDLKSQEDD 400
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQE 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 401 LNRAKSELNRLQQEETQLEQSIQAGRVQLETIikslkstQDEINQARSKLSQLHE-SRQEAHRSLEQYDQ 469
Cdd:smart00787 220 IMIKVKKLEELEEELQELESKIEDLTNKKSEL-------NTEIAEAEKKLEQCRGfTFKEIEKLKEQLKL 282
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
285-445 |
4.92e-05 |
|
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: 46.39 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 285 GVKEL-----DDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKTSEV 324
Cdd:pfam03148 130 GIQELlqrtlEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 325 -----QELQN--DLdRET--SSLQ----ELEAQKQDA----QDRLDEMDQQKAKLRDMLsdvrQKCQDEtqmISSLKTQI 387
Cdd:pfam03148 210 ieraeKERAAsaQL-RELidSILEqtanDLRAQADAVnfalRKRIEETEDAKNKLEWQL----KKTLQE---IAELEKNI 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 388 QSQESDLKSQEDDL--------NRAK---SEL------NRLQQEETQLEQSIQAGRVQL---ETIIKSLKSTQDEINQ 445
Cdd:pfam03148 282 EALEKAIRDKEAPLklaqtrleNRTYrpnVELcrdeaqYGLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
286-465 |
5.01e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKTSEVQELQNDLDRetsslqeLEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERREDLEELIAERRETIEEKRER 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRvQLETIIKSLKSTQDEINQ 445
Cdd:PRK02224 539 AEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
170 180 190
....*....|....*....|....*....|
gi 1622897435 446 ARSKLSQLHE----------SRQEAHRSLE 465
Cdd:PRK02224 611 LREKREALAElnderrerlaEKRERKRELE 640
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
286-441 |
5.89e-05 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 46.53 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 358
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQKCQdetQMISSLKTQIQSQESDLK----SQEDDLNRAKSELNRLQQEETQLEQS-IQAGRVQLETII 433
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
....*....
gi 1622897435 434 -KSLKSTQD 441
Cdd:pfam03999 298 dKLFYSTEQ 306
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
289-462 |
6.44e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 355
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 356 DQQKAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ---SI 422
Cdd:PRK04863 389 EEEVDELKSQLADYQQaldvqqtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsVA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897435 423 QAGRVQLETIIKSLKSTQDEI------NQARSKLSQLHESRQEAHR 462
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAEQ 514
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
291-418 |
6.47e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 291 DISQEIAQLQREKYSLE---------QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEaqkqdaqDRLDEMDQQKAK 361
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE-------EIMDEFNEQSKK 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 362 LRDMLSDVRQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:PHA02562 339 LLELKNKISTNKQS----LITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
308-455 |
6.79e-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: 44.60 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 308 QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 387
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 388 QSQESDLKSQE-DDLNRakselnRLQQEETQLEQSIQAGRvqLETIIKSLKSTQDEINQARSKLSQLHE 455
Cdd:cd16853 91 EYVQKNLTDEElADWKR------RQQIACIGGPPNICLDR--LENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
268-428 |
7.22e-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: 46.22 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 268 GTPGPDSSGSLGsgeftgvKEL--DDISQEIAQLQREKYSLeqdiREK-EEAIRQKTSEVQELqndLDRETSSLQELEAQ 344
Cdd:pfam05622 261 LSPSSDPGDNLA-------AEImpAEIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 345 KQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDEtqmiSSLKtqiqsqeSDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 424
Cdd:pfam05622 327 NRLANQRILELQQQVEELQKALQEQGSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDS 395
|
....
gi 1622897435 425 GRVQ 428
Cdd:pfam05622 396 NLAQ 399
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
297-434 |
7.89e-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: 43.49 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 297 AQLQREKYslEQDIREKEEAIRQKTSEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 376
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 377 TQMIsslktQIQSQESDLKSQEDD----LNRAKselnRLQQEetqlEQSIQAGRVQLETIIK 434
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
303-460 |
8.64e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 303 KYSLEQDIREKEEAIRQKtseVQELQNDLDrETSSLQELEAQkqdaqdrlDEMDQQKaklRDMLSDVRQKcqdetqmiss 382
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLR---NEFEKELRER---------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 383 lKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLheSRQEA 460
Cdd:PRK12704 81 -RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEA 155
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
296-474 |
9.05e-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: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 296 IAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-------QDAQDRLDEMDQQKA----KLRD 364
Cdd:pfam01576 189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLakkeeelQAALARLEEETAQKNnalkKIRE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 M---LSDVRQKCQDETQMisslKTQIQSQESDLksqEDDLNRAKSELNRlQQEETQLEQSIQAGRvqlETIIKSLKSTQD 441
Cdd:pfam01576 269 LeaqISELQEDLESERAA----RNKAEKQRRDL---GEELEALKTELED-TLDTTAAQQELRSKR---EQEVTELKKALE 337
|
170 180 190
....*....|....*....|....*....|...
gi 1622897435 442 EinQARSKLSQLHESRQEAHRSLEQYDQVLDGA 474
Cdd:pfam01576 338 E--ETRSHEAQLQEMRQKHTQALEELTEQLEQA 368
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
317-469 |
9.20e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 317 IRQKTSEVQelqnDLDRETSSLQELEAQKQDAQDRLDEM-DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLK 395
Cdd:PHA02562 176 IRELNQQIQ----TLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 396 SQEDDLN-------RAKSELNRLQQEETQLEQsiqaGRV------QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHR 462
Cdd:PHA02562 252 DPSAALNklntaaaKIKSKIEQFQKVIKMYEK----GGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
....*..
gi 1622897435 463 SLEQYDQ 469
Cdd:PHA02562 328 IMDEFNE 334
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
287-407 |
9.60e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKTSEVQELQNDLD-----------RETSSLQELEAQKQ-- 346
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 347 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDL------KSQEddLNRAKSE 407
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
306-476 |
9.77e-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: 46.19 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 306 LEQDIREKEEAIRQKTSEVQELqnDLDRetsSLQELEAQKQDAQDRLDEMDQQKAKLRDMLsdvrqkcQDETQMISSLKT 385
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGS--DLDR---TVQQVNQEKQEKQHELDTVVSKIELNRKLI-------QDQQEQIQHLKS 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 386 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLE 465
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
170
....*....|.
gi 1622897435 466 QYDQVLDGAHG 476
Cdd:TIGR00606 945 DIKEKVKNIHG 955
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
306-453 |
1.00e-04 |
|
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: 44.71 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 306 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVRQKCQDETQMISSLKT 385
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 386 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLET--IIKSLKSTQDEINQARSKLSQL 453
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAafLQADLKAAKADWNQLYEQAKSL 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
290-494 |
1.09e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 364
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 MLSDVRQKCqdetqmiSSLKTQIQSQESDLKSQEddlNRAKSELNRLQQEETQLEQSiqagRVQLETIIKSLKSTQDEIN 444
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA----KAGWCAVLRLVKDNGVERR 1133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 445 QARSKLSQLheSRQEAhRSLEQYDQ------VLDGAHgasLTDLADLSEGVSLAER 494
Cdd:PRK04863 1134 LHRRELAYL--SADEL-RSMSDKALgalrlaVADNEH---LRDVLRLSEDPKRPER 1183
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
285-380 |
1.09e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 42.96 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 285 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 363
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 1622897435 364 DMLSDVRQKCQDETQMI 380
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
286-449 |
1.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL 352
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 353 DEMdQQKAKLrdmlsdvrqkcqdeTQMISSLKTQIQSQESDLKSQE-DDLNRAKSELNRLQQEETQLEQSIQAGRVQLET 431
Cdd:PRK03918 355 EEL-EERHEL--------------YEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
170
....*....|....*...
gi 1622897435 432 IIKSLKSTQDEINQARSK 449
Cdd:PRK03918 420 EIKELKKAIEELKKAKGK 437
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
337-467 |
1.14e-04 |
|
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: 43.16 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 337 SLQELEAQKQ--DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlktQIQSQESDLKsqedDLNRAKSELNRLQQE 414
Cdd:pfam07321 9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRLYA---EIQGKLVLLK----ELEKVKQQVALLREN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 415 ETQLEQSIQAGRVQLETIIKSLKSTQDEINQAR---SKLSQLHESRQEAHRSLEQY 467
Cdd:pfam07321 82 EADLEKQVAEARQQLEAEREALRQARQALAEARravEKFAELVRLVQAEELRQQER 137
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-466 |
1.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 396 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
284-476 |
1.23e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 284 TGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA--- 360
Cdd:PRK02224 509 DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 361 -------KLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL------NRL---QQEETQLEQSIQA 424
Cdd:PRK02224 586 eriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeARIeeaREDKERAEEYLEQ 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 425 GRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEaHRSLEQYDQVLDGAHG 476
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEELRER-REALENRVEALEALYD 715
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-456 |
1.27e-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: 45.81 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQktsevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 363
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGR-----LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIQAGRvQLETIIKS 435
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielkkeiLEKKQEELKFVIKELQ-QLEGSSDR 472
|
170 180
....*....|....*....|.
gi 1622897435 436 LKSTQDEINQARSKLSQLHES 456
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKN 493
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
356-436 |
1.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 356 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKS 435
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 1622897435 436 L 436
Cdd:COG3883 95 L 95
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
293-436 |
1.37e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 293 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 372
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 373 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRL------------QQEE------TQ---LEQSIQagrvQLET 431
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEErydflsEQredLEEARE----TLEE 816
|
....*
gi 1622897435 432 IIKSL 436
Cdd:COG1196 817 AIEEI 821
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
290-482 |
1.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKySLEQDirekEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 369
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 370 RQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQqeeTQLEQ---SIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ---TQPERaqaALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622897435 447 RSKLSQLHESRQ---EAHRSLEQydQVLDGAhgASLTDL 482
Cdd:PRK11281 190 RPSQRVLLQAEQallNAQNDLQR--KSLEGN--TQLQDL 224
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
305-429 |
1.44e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 305 SLEQDIREKEEAIRQK------TSEVQELQNDLDRETSSLQELEAQKQDAQDR-------LDEMDQQKAKLRDMLSDVRQ 371
Cdd:PRK10929 79 KLSAELRQQLNNERDEprsvppNMSTDALEQEILQVSSQLLEKSRQAQQEQDRareisdsLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 372 KCQ----DETQMISSLKTQIQSQESDLKSQEDDLNRA------KSELNRLQQE-----ETQLEQSIQAGRVQL 429
Cdd:PRK10929 159 RLQtlgtPNTPLAQAQLTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQALRNQL 231
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
313-460 |
1.45e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 313 KEEAIRQKTSEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqmisslk 384
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 385 tqiQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRVQLETIIksLKSTQDEINQARSKLsqLHESRQEA 460
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLERISGLTSEEAKEIL--LDEVEEELRHEAAVM--IKEIEEEA 178
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
287-420 |
1.48e-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: 44.91 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 355
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 356 ---DQQKAKLRD-MLSDVRQKCQDETQMISSLKTQIQSQEsdlKSQEDDLNRAKSELNRL---QQEETQLEQ 420
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQ 278
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-465 |
1.48e-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: 45.55 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------TSEVQELQNDLDRETSSLQEL 341
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 342 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 415
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897435 416 TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLhesrQEAHRSLE 465
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA----LKKIRELE 270
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
290-466 |
1.58e-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: 44.81 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdretssLQELEAQKQDAQDRldeMDQQKAK-LRDMLSD 368
Cdd:pfam05816 109 DELLKDNAMLDQMYEKNLEYFKELEKYIAAGELKLEELDAEL------LPELEAKAAASGDP---EDAQALRdLRQALFR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 369 VRQKCQD-ETQM-------------------------------ISSLKTQ------IQSQESDLKSQE------DDLNRA 404
Cdd:pfam05816 180 LEQRIHDlELQRavsiqtapqirlvqnnnqeliekiqsaitttIPLWKNQlvvalaLKRQKLALEAQKavndttNELLLK 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 405 KSELNRLQQEETQlEQSiQAGRVQLETIIK---SLKSTQDEINQARsklSQLHESRQEAHRSLEQ 466
Cdd:pfam05816 260 NAEMLKTQSIETA-KEA-ERGIVDIETLKKtnqTLIATIDETLQIQ---EEGREKRREAEAELEQ 319
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
287-456 |
1.69e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIR---------EKE-EAIRQKTSEVQELQNDLDRetsSLQELEAQKQ---------- 346
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDrvkqsytlnESElESVRQLEKQLESLEKQYDE---ITERIAEQEIayselqeele 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 347 DAQDRLDEMDQQKAKLRDMLSDVRqkcQDET---QMISSLKTQIQS-----QESDL----KSQEDDLNRAKSELNRLqqe 414
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLR---KDELearEKLERYRNKLHEikrylEKSNLpglpEDYLEMFFEVSDEIEAL--- 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897435 415 ETQLEQsiqaGRVQLETIIKSLKSTQDEINQARSKLSQLHES 456
Cdd:PRK04778 461 AEELEE----KPINMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
289-455 |
1.72e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 361
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 362 LrDMLSDvRQKCQ----DETQMISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELNRLQQEETQLeQSIQ 423
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897435 424 AGRVQLETIIKSLKSTQDEINQARS----KLSQLHE 455
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvaldNWRQVHE 724
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
284-560 |
1.80e-04 |
|
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: 44.95 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 284 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 363
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 D------MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRA-KSELNRLQQEETQLEQSIQAGRVQLETIIKSL 436
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 437 KSTQDEINQAR-----SKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSL------AERGGFGAMDDPFK 505
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKlrakleRQLEGVRSKLDQVA 523
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 506 NKALLFSNNTQELHPDPFQTEDPFKSdpFKGADPFKGDPFQNDPFAEQQTTSTDP 560
Cdd:COG5185 524 ESLKDFMRARGYAHILALENLIPASE--LIQASNAKTDGQAANLRTAVIDELTQY 576
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
332-459 |
1.81e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 332 DRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 411
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622897435 412 QQEETQLEQSIQAGRVQLETIIKSLKStqdeINQARSKLSQLhESRQE 459
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERL-EWRQQ 126
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
288-387 |
1.84e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSL--EQDIREKEEAIRQKTsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 365
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkkEQDEASFERLAELRD-ELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|..
gi 1622897435 366 LSDVRQKCQDETQMISSLKTQI 387
Cdd:COG0542 491 EKELAELEEELAELAPLLREEV 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
282-456 |
1.84e-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: 45.10 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 282 EFTGVKELDdiSQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ----KQDAQDRLDEMDQ 357
Cdd:pfam05483 398 KFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQltaiKTSEEHYLKEVED 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 358 QKAKL-RDMLSDVrqKCQDETQMISSLKTQIQSQESD----LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 432
Cdd:pfam05483 476 LKTELeKEKLKNI--ELTAHCDKLLLENKELTQEASDmtleLKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV 553
|
170 180
....*....|....*....|....
gi 1622897435 433 IKSLKSTQDEInqaRSKLSQLHES 456
Cdd:pfam05483 554 REEFIQKGDEV---KCKLDKSEEN 574
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
293-474 |
1.86e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 293 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQK 372
Cdd:pfam10174 543 AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQ 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 373 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEEtQLEQSIQA---GRVQLETIIKSLKSTQDEINQARSK 449
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL-QLEELMGAlekTRQELDATKARLSSTQQSLAEKDGH 691
|
170 180
....*....|....*....|....*.
gi 1622897435 450 LSQL-HESRQEAHRSLEQYDQVLDGA 474
Cdd:pfam10174 692 LTNLrAERRKQLEEILEMKQEALLAA 717
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
284-452 |
1.93e-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: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 284 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKTS-------EVQELQNDLDRETSSLQELEAQKQDAQDR- 351
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 352 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI--QSQESDLKSQEDDLNRAKSELNRLQ--- 412
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQvlq 1051
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897435 413 --QEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQ 452
Cdd:TIGR00606 1052 mkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
337-466 |
1.94e-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: 43.83 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 337 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQMISSLKTQIQS--QESDLKSQEDDL 401
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 402 NRAKSEL-NRLQQEETQLeQSIQAGRVQLETiikSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQNQLAQLNS---QLIELQTRPERAQQQLSEARQRLQQIRNRLNG 138
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
287-466 |
1.96e-04 |
|
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: 43.79 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEV---QEL------------QNDLDRETSSLQELEAQKQDaqdR 351
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEKEES---K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 352 LDEMDQQKAKLRDMLsdvrQKCQDE-----TQM----------ISSLKTQIQsqesDLK-SQEDDLNraksELNRLQQEE 415
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEElnflsTYKdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 416 TQ-LEQSIQAGRVQLETII--KSLKSTQD--------------EINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQEsllqktrdnqvmlkEIEQFREFIDELEEEIPKLKAEVQQ 218
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-459 |
2.17e-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: 45.17 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKE-----------EAIRQKTS---EVQELQNDLDRETSSLQE------------ 340
Cdd:pfam01576 384 SENAELQAELRTLQQAKQDSEHKRKKLEgqlqelqarlsESERQRAElaeKLSKLQSELESVSSLLNEaegkniklskdv 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 341 --LEAQKQDAQDRLDEMDQQKAKLRdmlSDVRQKCQDETQMISSLKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:pfam01576 464 ssLESQLQDTQELLQEETRQKLNLS---TRLRQLEDERNSLQEQLEEEEEAKRN-VERQLSTLQAQLSDMKKKLEEDAGT 539
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622897435 419 EQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQE 459
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
295-458 |
2.31e-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: 44.78 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETS-------SLQELEAQKQDAQDRLDEMDQQKAKlrdmls 367
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAqknnalkKIRELEAQISELQEDLESERAARNK------ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 368 dVRQKCQDETQMISSLKTQIQ-SQESDLKSQEDDLNRAK--SELNRLQQEETQL-EQSIQAGRVQLETIIKSLkstQDEI 443
Cdd:pfam01576 290 -AEKQRRDLGEELEALKTELEdTLDTTAAQQELRSKREQevTELKKALEEETRShEAQLQEMRQKHTQALEEL---TEQL 365
|
170
....*....|....*
gi 1622897435 444 NQARSKLSQLHESRQ 458
Cdd:pfam01576 366 EQAKRNKANLEKAKQ 380
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
287-466 |
2.36e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.28 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQEL----QNDLDRET-SSLQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAlekgREDLAREAlERKAELEAQAEALEAQLAQLEEQVEK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 362 LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE----DDLNRAKSELNRLQQEETQLEQSIQAgrvqletiikslk 437
Cdd:COG1842 117 LKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA------------- 183
|
170 180 190
....*....|....*....|....*....|..
gi 1622897435 438 stQDEINQARS---KLSQLhESRQEAHRSLEQ 466
Cdd:COG1842 184 --AAELAAGDSlddELAEL-EADSEVEDELAA 212
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
287-453 |
2.41e-04 |
|
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: 44.03 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 366
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 sdvrqkcqdetQMISSLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*..
gi 1622897435 447 RSKLSQL 453
Cdd:pfam15905 320 EQEHQKL 326
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
302-423 |
2.50e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 302 EKYSLEQDIREKEEAIRQKTSEVQELQNDldretsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMIS 381
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622897435 382 slktQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQ 423
Cdd:COG0542 472 ----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
288-432 |
2.55e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEmdqqkAKl 362
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKE-----AK- 583
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 363 rdmlsdvrqkcQDETQMISSLKTQIQSQESDLKSQE-----DDLNRAKSELNRLQQEETQLEQSIQAG-RVQLETI 432
Cdd:PRK00409 584 -----------KEADEIIKELRQLQKGGYASVKAHEliearKRLNKANEKKEKKKKKQKEKQEELKVGdEVKYLSL 648
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
295-459 |
2.74e-04 |
|
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: 43.11 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDL-DRE-------TSSLQELEAQKQDAQDRLDEmdqqkaKLRDML 366
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVeERElkaeaehRQRVVELSREVEEAKRAFEE------KLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS-ELNRLQQEetqLEQSIQAGRVQLETIIKSLKSTQDEINQ 445
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVEDLRKEKKKLAEEYEQ 197
|
170
....*....|....
gi 1622897435 446 ARSKLSQLHESRQE 459
Cdd:pfam15665 198 KLSKAQAFYERELE 211
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
315-423 |
2.96e-04 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 41.48 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 315 EAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQMISSLKTQIQSQ 390
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLisiiQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKENK 73
|
90 100 110
....*....|....*....|....*....|...
gi 1622897435 391 ESDLKSQeddlnrakseLNRLQQEETQLEQSIQ 423
Cdd:smart00502 74 LKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
382-458 |
2.98e-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: 41.92 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 382 SLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKL-----SQLHES 456
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALqqiktQFAHEV 135
|
..
gi 1622897435 457 RQ 458
Cdd:pfam11559 136 KK 137
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
284-465 |
3.03e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 284 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKTSEVQELQNDLDRETSS-------------- 337
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 338 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ 417
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 418 LEQSiqagRVQLETIIKSLKS----TQDEINQARSKLSQLHESRQEAHRSLE 465
Cdd:pfam01576 859 AQQE----RDELADEIASGASgksaLQDEKRRLEARIAQLEEELEEEQSNTE 906
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
274-459 |
3.06e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 43.06 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 274 SSGSLGSGEFTGVKE-LDDISQEIAQLQREKYSLEQDIR-EKEEAIRQKTSEVQELQNDLDretSSLQELEAQKQDAqdr 351
Cdd:cd07651 46 SRKSLGGSEEGGLKNsLDTLRLETESMAKSHLKFAKQIRqDLEEKLAAFASSYTQKRKKIQ---SHMEKLLKKKQDQ--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 352 ldEMDQQKAklrdmlsdvRQKCQDETQMISSLktqiQSQESDLKSQEDDLNRAKseLNRLQQeetqleqSIQAGRVQLET 431
Cdd:cd07651 120 --EKYLEKA---------REKYEADCSKINSY----TLQSQLTWGKELEKNNAK--LNKAQS-------SINSSRRDYQN 175
|
170 180 190
....*....|....*....|....*....|..
gi 1622897435 432 IIKSLKSTQDEINQ----ARSKLSQLHESRQE 459
Cdd:cd07651 176 AVKALRELNEIWNRewkaALDDFQDLEEERIQ 207
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
304-446 |
3.23e-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: 42.13 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 304 YSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQqkakLRDMLSD--VRQKCQDETQMI 380
Cdd:pfam16789 3 YPLEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVrKHKKAKMQQ----LRDEMDRgtTSDKILQMKRYI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 381 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS--------TQDEINQA 446
Cdd:pfam16789 79 KVVKERLKQEEKKVQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKeeedqeerEQDEIGSA 152
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-466 |
3.29e-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: 44.65 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-----------DLDRETSSLQELEAQKQ--------- 346
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 347 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE---DDLNRAKSELNRLQQEETQLEQ 420
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897435 421 SIQAGRVQLEtiIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:TIGR00606 493 NSLTETLKKE--VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
288-389 |
3.35e-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: 41.47 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIR----------QKTSE-VQELQ---NDLDRETSSLQELEAQKQDAQDRLD 353
Cdd:pfam07926 9 EIKRLKEEAADAEAQLQKLQEDLEKQAEIAReaqqnyerelVLHAEdIKALQalrEELNELKAEIAELKAEAESAKAELE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622897435 354 EM----DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 389
Cdd:pfam07926 89 ESeeswEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
287-466 |
3.48e-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: 43.75 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSeVQELQNDL-DRETSSLQELEAQKQDAQ------DRLDEMDQQK 359
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIeEREQKRQEEYEEKLQEREqmdeivERIQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLsdvRQKCQDETQMISSLKTQIQSQEsDLKSQEDDLnRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSL--- 436
Cdd:pfam13868 118 AEEKLEK---QRQLREEIDEFNEEQAEWKELE-KEEEREEDE-RILEYLKEKAEREEEREAEREEIEEEKEREIARLraq 192
|
170 180 190
....*....|....*....|....*....|....
gi 1622897435 437 ----KSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:pfam13868 193 qekaQDEKAERDELRAKLYQEEQERKERQKEREE 226
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
359-492 |
3.87e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.07 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQL--------- 429
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrq 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 430 -----ETIIKSLKSTQDEINQARSKLSQLhESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLA 492
Cdd:COG5283 82 lsaaqRRLRSSLEQTNRQLERQQQRLARL-GARQDRLKAARARLQRLAGAGAAAAAIGAALAASVKPA 148
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
289-494 |
4.04e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 360
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 361 KLRDMLSDVRQKCQDETQMISSLktqiqsqesdlksqeddLNRAKSELNRLQQEETQLE---QSIQAGRVQLETIIKSLK 437
Cdd:COG0497 223 KLREALQEALEALSGGEGGALDL-----------------LGQALRALERLAEYDPSLAelaERLESALIELEEAASELR 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 438 STQD--EINQARskLSQLhESRQEAHRSLEQydqvldgAHGASLTDLADLSEgvSLAER 494
Cdd:COG0497 286 RYLDslEFDPER--LEEV-EERLALLRRLAR-------KYGVTVEELLAYAE--ELRAE 332
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
287-469 |
4.37e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 42.91 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKTSEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 359
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 aKLRDMLSDVR--QKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELNRLQQEETQLEQSIQagrvQLETIIKSLK 437
Cdd:COG5325 144 -FLRNKNNDQHplEEEEDEESLSSLGSQQTLQQQGLSNEELEY---QQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897435 438 STQDE----INQARSKLSQLHESRQEAHRSLEQYDQ 469
Cdd:COG5325 216 SLVGEqgelVDRIDFNIENTSDNLKNANKELEKAPA 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-464 |
4.39e-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: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQ-------EDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 439
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
170 180
....*....|....*....|....*
gi 1622897435 440 QDEINQARSKLSQLHESRQEAHRSL 464
Cdd:TIGR00606 460 IKELQQLEGSSDRILELDQELRKAE 484
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
306-414 |
5.45e-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: 42.32 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 306 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLkt 385
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 1622897435 386 qiqsqESDLKSQEDDLNRAKSELNRLQQE 414
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
293-420 |
5.47e-04 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 43.05 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 293 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQD--------------RLDEMDQQ 358
Cdd:pfam14915 150 SQQLSKAESKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDkvnkyigkqesleeRLAQLQSE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 359 KAKLRDMLSDVRQK----------CQDETQMISSlKTQIQSQESDLKSQEddlnRAK---SELNRLQQEETQLEQ 420
Cdd:pfam14915 230 NMLLRQQLEDAQNKadakektvidIQDQFQDIVK-KLQAESEKQVLLLEE----RNKeliNECNHLKERLYQYEK 299
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
297-430 |
6.06e-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: 40.26 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 297 AQLQREKysleQDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDvRQKC 373
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEE-KEIE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 374 QDETQMisslktqiqsQESDLKSQeddLNRAKSELNRLQQeetQLEQSIQAGRVQLE 430
Cdd:pfam18595 73 LRELER----------REERLQRQ---LENAQEKLERLRE---QAEEKREAAQARLE 113
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
288-450 |
6.18e-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: 43.63 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKTSEVQELQNDLDRETSSLQ------- 339
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 340 ELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDVRQK-CQDETQMISSLKTQIQS------QESDLKS---QEDDLNR----- 403
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFKSSIAALEAKiAQLEEQLEQESRERQAAnklvrrTEKKLKEvllQVEDERRhadqy 1021
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 404 ---AKSELNRLQQEETQLE------QSIQAGR----VQLETIIKSLKSTQDEINQARSKL 450
Cdd:pfam01576 1022 kdqAEKGNSRMKQLKRQLEeaeeeaSRANAARrklqRELDDATESNESMNREVSTLKSKL 1081
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
378-466 |
6.23e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 378 QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ----SIQAGRVQLETIIKSLKSTQDEINQARSKLSQL 453
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90 100
....*....|....*....|
gi 1622897435 454 -------HESrQEAHRSLEQ 466
Cdd:PRK00409 600 gyasvkaHEL-IEARKRLNK 618
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
306-466 |
6.40e-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: 41.97 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 306 LEQDIREKEEAIRQKTSEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQMISSLKT 385
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 386 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS--TQDEINQARSKLSQlhesrQEAHRS 463
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLST-----SSATDS 165
|
...
gi 1622897435 464 LEQ 466
Cdd:pfam04012 166 FER 168
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
289-433 |
6.63e-04 |
|
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: 41.35 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 368
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 369 vrqkcqdETQMISSLktqiqsqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRVQLETII 433
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
299-466 |
6.84e-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: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 299 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ-KCQDET 377
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 378 QMiSSLKTQIqsqESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIqAGRVQLETIIKSLKSTQDEINQARS- 448
Cdd:pfam01576 721 NM-QALKAQF---ERDLQARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGREe 795
|
170 180
....*....|....*....|.
gi 1622897435 449 ---KLSQLHESRQEAHRSLEQ 466
Cdd:pfam01576 796 avkQLKKLQAQMKDLQRELEE 816
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
291-487 |
7.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 291 DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 365
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 366 LSDVRQkcQDETqmISSLKTQ---IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgRVQL--ETIIKSLKSTQ 440
Cdd:PRK04863 910 KRFVQQ--HGNA--LAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR-RAHFsyEDAAEMLAKNS 984
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 441 DEINQARSKLSQLHESRQEAHRSLE-------QYDQV---LDGAHGASLTDLADLSE 487
Cdd:PRK04863 985 DLNEKLRQRLEQAEQERTRAREQLRqaqaqlaQYNQVlasLKSSYDAKRQMLQELKQ 1041
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
293-458 |
7.49e-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: 43.42 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 293 SQEIAQLQRekysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 369
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 370 ---RQKCQDETQMISSLKTQIQSQESDLKSQE-------DDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKst 439
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQET-- 486
|
170
....*....|....*....
gi 1622897435 440 qdEINQARSKLSQLHESRQ 458
Cdd:TIGR00618 487 --RKKAVVLARLLELQEEP 503
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
338-470 |
7.75e-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: 41.94 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 338 LQELEAQKQDAQDRLDEMDQQKAKLRDmlsdVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAkseLNRLQQEETQ 417
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEK----RAEKAEAE---VAALNRRIQLLEEELERTEERLAEA---LEKLEEAEKA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 418 LEQSIQAGRVqLETiikslKSTQDEiNQARSKLSQLHESRQEAHRSLEQYDQV 470
Cdd:pfam00261 73 ADESERGRKV-LEN-----RALKDE-EKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
287-483 |
7.76e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQRE----KYSLEQ----DIREKE----EAIRQKTSEVQELQNDLdreTSSLQELEAQKQDAQDRLD- 353
Cdd:COG0497 172 KELEELRADEAERAREldllRFQLEEleaaALQPGEeeelEEERRRLSNAEKLREAL---QEALEALSGGEGGALDLLGq 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 354 ---------EMDQQKAKLRDMLSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRA---KSELNRLQQ------EE 415
Cdd:COG0497 249 alralerlaEYDPSLAELAERLESALIELEE-------AASELRRYLDSLEFDPERLEEVeerLALLRRLARkygvtvEE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 416 -TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLS----QLHESRQEAHRSLEQydQVLdgahgASLTDLA 483
Cdd:COG0497 322 lLAYAEELRAELAELENSDERLEELEAELAEAEAELLeaaeKLSAARKKAAKKLEK--AVT-----AELADLG 387
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
321-458 |
8.08e-04 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 41.22 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 321 TSEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetQMISSLKtqiQSQE-SD----LK 395
Cdd:pfam15272 3 TSEYLELLDKLDKNNRALHLL---NKDVRERDEHYQLQETSYKKKYLQTRN------ELINELK---QSKKlYDnyykLY 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897435 396 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLkstQDEINQARSKLSQLHESRQ 458
Cdd:pfam15272 71 SKYQQLKKISNESLDLQSTITNLESQLVDQAIDKDREIHNL---NEKILSLELRNQELETKRE 130
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
287-455 |
8.45e-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: 42.37 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQRekySLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLRDML 366
Cdd:pfam04108 171 KELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQKLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 367 S---DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK-------SELNRLQQEETQLEQS-----IQAGR----- 426
Cdd:pfam04108 245 EqknSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKetiedylSELEDLREFYEGFPSAygsllLEVERrrewa 324
|
170 180
....*....|....*....|....*....
gi 1622897435 427 VQLETIIKSLkstqdeinqaRSKLSQLHE 455
Cdd:pfam04108 325 EKMKKILRKL----------AEELDRLQE 343
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
292-397 |
8.63e-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: 42.27 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 292 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 367
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 1622897435 368 DVRQKCQDETQMISSLKTQIQSQESDLKSQ 397
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
287-468 |
8.72e-04 |
|
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: 42.92 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQrEKYSL----EQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEM 355
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAyselqeeLEEILEQLEEIEEEQEEF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 356 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqeSDL----KSQEDDLNRAKSELNRLQQeetQLEQS---IQAGRVQ 428
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEVplnMDEVNRL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 429 LETIIKSL----KSTQDEINQA-------------RSKLSQLHESRQEAHRSLEQYD 468
Cdd:pfam06160 459 LDEAQDDVdtlyEKTEELIDNAtlaeqliqyanryRSSNPEVAEALTEAELLFRNYD 515
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
273-445 |
8.99e-04 |
|
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: 42.74 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 273 DSSGSLGSGEFTGVKELDDISQE-------IAQLQREKYSLEQDIREKEEAIRQK------TSEVQELQNDLDRETSSLQ 339
Cdd:pfam13166 293 EKVESAISSLLAQLPAVSDLASLlsafeldVEDIESEAEVLNSQLDGLRRALEAKrkdpfkSIELDSVDAKIESINDLVA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 340 ELEAQKQDAQDRLDEMDQQKAKLRDMLsdvrqkcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 419
Cdd:pfam13166 373 SINELIAKHNEITDNFEEEKNKAKKKL---------RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLR 443
|
170 180
....*....|....*....|....*.
gi 1622897435 420 QSIQagrvQLETIIKSLKSTQDEINQ 445
Cdd:pfam13166 444 EEIK----ELEAQLRDHKPGADEINK 465
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
308-423 |
9.08e-04 |
|
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: 42.54 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 308 QDIREKEEAIRQKTSEVQELQND-----LDR---ETSS-LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV--------- 369
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADavnfaLRKrieETEDaKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKeaplklaqt 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 370 ----RQK------CQDETQ--MISSLKtQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQ 423
Cdd:pfam03148 301 rlenRTYrpnvelCRDEAQygLVDEVK-ELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
289-374 |
9.49e-04 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.94 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDIRE----KEEAIRQKTSEVQELQNDLD-RETSSLQELEAQKqdaQDRLDEMDQQKAKLR 363
Cdd:smart00502 9 LTKLRKKAAELEDALKQLISIIQEveenAADVEAQIKAAFDELRNALNkRKKQLLEDLEEQK---ENKLKVLEQQLESLT 85
|
90
....*....|.
gi 1622897435 364 DMLSDVRQKCQ 374
Cdd:smart00502 86 QKQEKLSHAIN 96
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
359-467 |
1.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 359 KAKLRDMLSDVRQKCQDETQMISSLK----TQIQSQESDLKSQ-EDDLNRAKSEL----NRLQQEETQLE---QSIQAGR 426
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKkealLEAKEEIHKLRNEfEKELRERRNELqkleKRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622897435 427 VQLETIIKSLKSTQDEINQARSKLSQLHESRQEAhrsLEQY 467
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERI 147
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-494 |
1.13e-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: 42.73 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 363
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQDEESDLERLKEEIEKSSKQRAMLAgat 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 -------DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQ----EDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 432
Cdd:TIGR00606 663 avysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlaPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 433 IKslkstqdEINQARSKLSQLHESRQEAHRSLEQYDQVLdGAHGASLTDLADLSEGVSLAER 494
Cdd:TIGR00606 743 EK-------EIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESAKVCLTDVTIMER 796
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
287-418 |
1.14e-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: 41.24 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQrekysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 359
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 360 AKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
287-352 |
1.40e-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: 39.87 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRL 352
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
298-484 |
1.45e-03 |
|
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: 40.89 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 298 QLQREKYSLEQDIREKEEAIRQKTSEvqelqndldretSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlSDVRQKCQDET 377
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG------------DDLESVEALLKKHEALEAELAAHEERV----EALNELGEQLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 378 QMISSLKTQIQSQESDLKSQEDDLN-RAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHES 456
Cdd:cd00176 68 EEGHPDAEEIQERLEELNQRWEELReLAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK 147
|
170 180
....*....|....*....|....*...
gi 1622897435 457 RQEAHRSLEQYDQVLDgahgaSLTDLAD 484
Cdd:cd00176 148 HKELEEELEAHEPRLK-----SLNELAE 170
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
287-412 |
1.45e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.50 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQR---EKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQdaqdrldEMDQQKAKLR 363
Cdd:pfam02841 183 QSKEAVEEAILQTDQaltAKEKAIEAERAKAEAAEAEQELLREKQKEEE------QMMEAQER-------SYQEHVKQLI 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 364 DMLSDVRQKCQDETQMISSLKTQIQ---SQESdLKSQEDDLNRaksELNRLQ 412
Cdd:pfam02841 250 EKMEAEREQLLAEQERMLEHKLQEQeelLKEG-FKTEAESLQK---EIQDLK 297
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-466 |
1.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIRE-------------------KEEAIRQKTSEVQELQNDldretssLQELEAQKQD 347
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelteehRKELLEEYTAELKRIEKE-------LKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 348 AQDRLDEMDQQKAKLRDMLSdvrqkcqdetqmISSLKTQIQSQESDLKS-QEDDLNRAKSELNRLQQEETQLEQSIQAgr 426
Cdd:PRK03918 478 LRKELRELEKVLKKESELIK------------LKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKS-- 543
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897435 427 vqLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:PRK03918 544 --LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
398-472 |
1.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 398 EDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 472
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
306-453 |
1.50e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 306 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKT 385
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 386 QIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQAGRVQLETIIKSLKSTQDEINQARSKLSQL 453
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQ-------IAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
286-375 |
1.51e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 39.28 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLD------------RETSSLQELEAQKQDAQDRLD 353
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALE----ELEKLPDDTPiykivgnllvkvDKTKVEKELKERKELLELRSR 88
|
90 100
....*....|....*....|..
gi 1622897435 354 EMDQQKAKLRDMLSDVRQKCQD 375
Cdd:PRK09343 89 TLEKQEKKLREKLKELQAKINE 110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
325-487 |
1.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 325 QELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLSDVRQkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA 404
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 405 KSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSL---EQYDQVLDGAHGASLTd 481
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKR- 315
|
....*.
gi 1622897435 482 LADLSE 487
Cdd:PRK03918 316 LSRLEE 321
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
297-364 |
1.76e-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: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897435 297 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 364
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
288-461 |
1.85e-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: 41.94 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 363
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 dmlsdvrqkcqDETQMISslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRVQlETIIKSlKSTQD 441
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSAS-KEIEK 180
|
170 180
....*....|....*....|
gi 1622897435 442 EINQARSKLSQLHESRQEAH 461
Cdd:pfam05701 181 TVEELTIELIATKESLESAH 200
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
365-467 |
1.86e-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: 41.35 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 365 MLSDVRQKCQDET-QMISSLKTQIQSQESDLKSQEDDL------NRAKSELNRLQQEEtqleQSIQAgrvQLETIIKSLK 437
Cdd:pfam05816 33 MLDNVRTKDLGEVgDLLNELRRTLKDFDPDELGEEKKLgflplfKKAGNKIEKYFAKY----QTAGA---QIDKIVVELE 105
|
90 100 110
....*....|....*....|....*....|
gi 1622897435 438 STQDEINQARSKLSQLHESRQEAHRSLEQY 467
Cdd:pfam05816 106 KGQDELLKDNAMLDQMYEKNLEYFKELEKY 135
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
322-452 |
1.96e-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: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 322 SEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL 401
Cdd:cd21116 73 SYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 402 NRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQ 452
Cdd:cd21116 143 QAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLED 193
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
295-418 |
1.97e-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: 39.73 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 295 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 366
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622897435 367 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
289-466 |
2.00e-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: 39.94 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQrekyslEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 368
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 369 VRQKCQDETQMI-SSLKTQIQSQESDLKSQEDDL-NRAKSELNRLQqeeTQLEQSIQAGRVQLETIIKSLKSTQDEI--- 443
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAPYaee 147
|
170 180
....*....|....*....|....*
gi 1622897435 444 --NQARSKLSQLHESRQEAHRSLEQ 466
Cdd:pfam01442 148 vqAQLSQRLQELREKLEPQAEDLRE 172
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
287-456 |
2.02e-03 |
|
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: 40.86 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLR 363
Cdd:pfam06008 75 AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQNAEAELKAAQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 364 DMLSDVR---QKCQDETQmisSLKTQIQSQESD----LKSQEDDLNRAKS------ELNRLQQEE-TQLEQSIQAGRVQL 429
Cdd:pfam06008 155 DLLSRIQtwfQSPQEENK---ALANALRDSLAEyeakLSDLRELLREAAAktrdanRLNLANQANlREFQRKKEEVSEQK 231
|
170 180
....*....|....*....|....*..
gi 1622897435 430 ETIIKSLKSTQDEINQARSKLSQLHES 456
Cdd:pfam06008 232 NQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
305-365 |
2.16e-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: 37.93 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 305 SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 365
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
389-455 |
2.18e-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: 37.93 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 389 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHE 455
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQE 67
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
351-465 |
2.19e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 39.59 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 351 RLDEMDQQKAKLRDMLSDVRQKCQDETQ-------------MISSLKTQIQSQESDLKSQEDDLN------------RAK 405
Cdd:pfam17098 12 RLAEKEQEIQELKAQLQDLKQSLQPPSSqlrsllldpavnlEFLRLKKELEEKKKKLKEAQLELAawkftpdsttgkRLM 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 406 SELNRLQQEETQLEQSIQAGRVQ-LETIIKSLKSTQDEInqaRSKLSQLHESRQEAHRSLE 465
Cdd:pfam17098 92 AKCRLLQQENEELGRQLSEGRIAkLEIELALQKKVVEEL---KKSLEELDEFLIELDEELE 149
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
322-455 |
2.20e-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: 41.96 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 322 SEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQE 398
Cdd:TIGR00606 166 SEGKALKQKFDeifSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIVKSYE 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897435 399 DDLNRAKSELNRLQQEETQLeqsiqagrVQLETIIKSLKSTQDEINQARSKLSQLHE 455
Cdd:TIGR00606 245 NELDPLKNRLKEIEHNLSKI--------MKLDNEIKALKSRKKQMEKDNSELELKME 293
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
288-468 |
2.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE---LEAQKQDAQDRLDEMDQQKAKL-- 362
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSMELEKNNYYke 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 363 --------------------RDMLSDVRQkCQDETQMISSLKTQIQSQE------SDLKSQEDDLNRAKSELNRLQQEET 416
Cdd:PRK01156 278 leerhmkiindpvyknrnyiNDYFKYKND-IENKKQILSNIDAEINKYHaiikklSVLQKDYNDYIKKKSRYDDLNNQIL 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 417 QLE----------QSIQAGRVQLETIIKSLKSTQDEINQ----ARSKLSQLHESRQEAHRSLEQYD 468
Cdd:PRK01156 357 ELEgyemdynsylKSIESLKKKIEEYSKNIERMSAFISEilkiQEIDPDAIKKELNEINVKLQDIS 422
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
308-420 |
2.40e-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: 39.22 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 308 QDIREKEEaiRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqmissLKTQI 387
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110
....*....|....*....|....*....|...
gi 1622897435 388 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ 420
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEK 110
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
354-472 |
2.49e-03 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 39.94 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 354 EMDQQKAKLRDMLSDVRQKCQDETQMIsslktqIQSQESdlksqeddlNRAKSELNRLQ-QEETQLEQSIQAGRVQLETI 432
Cdd:cd16855 9 QLEELRQRTQETENDLRNLQQKQESFV------IQYQES---------QKIQAQLQQLQqQPQNERIELEQQLQQQKEQL 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622897435 433 IKSLKSTQDEINQARSKLSQLHesrQEAHRSLEQ-YDQVLD 472
Cdd:cd16855 74 EQLLNAKAQELLQLRMELADKF---KKTIQLLSKlQSRVLD 111
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
288-467 |
2.56e-03 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 41.03 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDIS------QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndldretssLQELEAQKQDAQDRLDEMDQQK-A 360
Cdd:COG3853 13 TLEDLLappapvPEVPEQAAGMVDPEEAEVDLSKLSAEADAFVEAL----------AAQIDLSDVNAILQYGAKAQRKlA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 361 KLRD-MLSDVRQKCQDET-QMISSLKTQIQsqESDLKSQEDD---------LNRAKSELNRLQQEEtqleQSIQAgrvQL 429
Cdd:COG3853 83 AFSNrMLDRVKTKDLGEVgDSLSELRRTLE--DLDPSELDDLkkkgllgklFPKGGNKLEKYFAKY----QSAQT---QI 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622897435 430 ETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQY 467
Cdd:COG3853 154 DKISVALEKGQDELLKDNAMLDQLYEKNWEYFKELNQY 191
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
286-467 |
2.58e-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: 41.35 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 286 VKELDD---ISQEIAQLQREKYSLEQDIREKEEAIRQKTSE-VQELQNDLDRET-------SSLQELE----AQKQDAQD 350
Cdd:pfam10174 76 IQALQDelrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAkelfllrKTLEEMElrieTQKQTLGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 351 RldemDQQKAKLRDML------SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL---NRLQQEETQ---L 418
Cdd:pfam10174 156 R----DESIKKLLEMLqskglpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaL 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622897435 419 EQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQY 467
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
290-420 |
2.58e-03 |
|
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: 38.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQdirEKEEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 366
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897435 367 sdvrqkCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL-NRLQQEETQLEQ 420
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
309-371 |
2.68e-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: 2.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 309 DIREKEEAIRQKTSEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 371
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
287-357 |
2.76e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 287 KELDDISQEIAQLQREKysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 357
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
300-466 |
2.77e-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: 41.17 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 300 QREKYSLEQDIREKEEAI---RQKTSEVQELQNDLDRETSSLQELEAQ-------------KQDAQDRLDEMDQQK--AK 361
Cdd:pfam05701 218 EQDKLNWEKELKQAEEELqrlNQQLLSAKDLKSKLETASALLLDLKAElaaymesklkeeaDGEGNEKKTSTSIQAalAS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 362 LRDMLSDVR---QKCQDETQMISSLKTQIQSqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS 438
Cdd:pfam05701 298 AKKELEEVKaniEKAKDEVNCLRVAAASLRS----------ELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIAL 367
|
170 180
....*....|....*....|....*...
gi 1622897435 439 TQDEINQARSKLSQLHESRQEAHRSLEQ 466
Cdd:pfam05701 368 VQAKEKEAREKMVELPKQLQQAAQEAEE 395
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
264-477 |
2.89e-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: 41.49 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 264 PSER-----GTPGPDSSGSLGSGEFTGVKELD-DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS 337
Cdd:TIGR00618 162 SKEKkellmNLFPLDQYTQLALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 338 LQELEaqkqdaqdRLDEMDQQKAKLRDMLSDVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELnRLQQEETQ 417
Cdd:TIGR00618 242 HAYLT--------QKREAQEEQLKKQQLLKQLRARIE-----------ELRAQEAVLEETQERINRARKAA-PLAAHIKA 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 418 LEQSIQagrvQLETIIKSLKSTQDEINQARSKLSQLHESRQeahrSLEQYDQVLDGAHGA 477
Cdd:TIGR00618 302 VTQIEQ----QAQRIHTELQSKMRSRAKLLMKRAAHVKQQS----SIEEQRRLLQTLHSQ 353
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
310-471 |
3.04e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 310 IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRldemdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQS 389
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR----------KQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 390 QESDLKSQEDDLN-------RAKSELNRLQQEE-------------TQLEQS---IQAGRVQLETIIKSLKSTQDEINQA 446
Cdd:PHA02562 246 LVMDIEDPSAALNklntaaaKIKSKIEQFQKVIkmyekggvcptctQQISEGpdrITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180
....*....|....*....|....*...
gi 1622897435 447 RSKLSQLHESRQEAH---RSLEQYDQVL 471
Cdd:PHA02562 326 EEIMDEFNEQSKKLLelkNKISTNKQSL 353
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-475 |
3.06e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQndlDREtsslQELEAQKQDAQDRLDEMD---QQKAKL-- 362
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELS---ARE----SDLEQDYQAASDHLNLVQtalRQQEKIer 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 363 -RDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ----EET---QLEQSIQA---GRVQLET 431
Cdd:COG3096 352 yQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQaldvQQTraiQYQQAVQAlekARALCGL 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622897435 432 IIKSLKSTQDEINQARSKLSQLHESRqeahRSLEQYDQVLDGAH 475
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEV----LELEQKLSVADAAR 471
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
314-488 |
3.12e-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: 41.36 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 314 EEAIRQKTSEVQELQNdLDRETSSLQELEAQKQDAQD-RLDEMDQQKAKLRDMLSDVRqkcqDETQmisslktqiqsqeS 392
Cdd:pfam12128 247 QQEFNTLESAELRLSH-LHFGYKSDETLIASRQEERQeTSAELNQLLRTLDDQWKEKR----DELN-------------G 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 393 DLKSQEDDLNRAKSELNRLqqeETQLEQSIQAGrvqletiIKSLKSTQDEINQARSKLSQL---HESRQEAHRSLEQYDQ 469
Cdd:pfam12128 309 ELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAADQEQLPSWQSELENLeerLKALTGKHQDVTAKYN 378
|
170 180
....*....|....*....|
gi 1622897435 470 VLDGAHGASL-TDLADLSEG 488
Cdd:pfam12128 379 RRRSKIKEQNnRDIAGIKDK 398
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
339-472 |
3.14e-03 |
|
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: 38.32 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 339 QELEAQKQDAQDRLDEMDQQKAKLRDMlsdvRQKCQDETQMIsslktqiqsqESDLKSQEDDLNRAKselnRLQQEETQL 418
Cdd:pfam13863 13 LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKF----------DKFLKENDAKRRRAL----KKAEEETKL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 419 eqsiqagRVQLETIIKSLKSTQDEINQARSKLsqlhesrQEAHRSLEQYDQVLD 472
Cdd:pfam13863 75 -------KKEKEKEIKKLTAQIEELKSEISKL-------EEKLEEYKPYEDFLE 114
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
289-420 |
3.17e-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: 38.70 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKysleqdirekeeairqktsevqelqndldretsslQELEAQKQDAQDRLDEMDQQKAKLRDML-- 366
Cdd:pfam05103 27 LDQVAEDYEALIREN-----------------------------------AELKEKIEELEEKLAHYKNLEETLQNTLil 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897435 367 -----SDVRQKCQDETQMISSlKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQLEQ 420
Cdd:pfam05103 72 aqetaEEVKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
67-240 |
3.41e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.62 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 67 LGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEPVPsalppslippskrkktvfpgavpvlpaspppkdslrstpshg 146
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADT------------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 147 svsslNSTGSLSPKHSLKQTQPTVNWVVPVADKMRFDEIflktDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTR 226
Cdd:COG5126 45 -----DGDGRISREEFVAGMESLFEATVEPFARAAFDLL----DTDGDGKISADEFRRLLTALGVSEEEADELFARLDTD 115
|
170
....*....|....
gi 1622897435 227 QTGKLSKDQFALAM 240
Cdd:COG5126 116 GDGKISFEEFVAAV 129
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
287-419 |
3.90e-03 |
|
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: 39.98 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 287 KELDDISQEIAQLQ-------REKYSlEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 359
Cdd:pfam12795 51 AELRELRQELAALQakaeaapKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDML-------SDVRQKCQDETQM-ISSLKTQIQSQE-------------------------------SDLKSQEDD 400
Cdd:pfam12795 130 QQIRNRLngpappgEPLSEAQRWALQAeLAALKAQIDMLEqellsnnnrqdllkarrdlltlriqrleqqlQALQELLNE 209
|
170
....*....|....*....
gi 1622897435 401 LNRAKSELNRLQQEETQLE 419
Cdd:pfam12795 210 KRLQEAEQAVAQTEQLAEE 228
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
288-375 |
4.69e-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: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLEQDIREKEEAI---------RQKTSEVqEL-----QNDLDRETSSLQE----LEAQKQDAQ 349
Cdd:pfam03148 266 QLKKTLQEIAELEKNIEALEKAIRDKEAPLklaqtrlenRTYRPNV-ELcrdeaQYGLVDEVKELEEtieaLKQKLAEAE 344
|
90 100 110
....*....|....*....|....*....|...
gi 1622897435 350 DRLDEMDQQKAKLRDMLSDV-------RQKCQD 375
Cdd:pfam03148 345 ASLQALERTRLRLEEDIAVKanslfidREKCMG 377
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
297-419 |
5.22e-03 |
|
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.
Pssm-ID: 407241 [Multi-domain] Cd Length: 360 Bit Score: 40.17 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 297 AQLQREKYSLEQD-IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD 375
Cdd:pfam17097 121 ASLEDEVSQLEDDtLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECWELLNELERLRDQRITVEEQTSN 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622897435 376 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 419
Cdd:pfam17097 201 EKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLE 244
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
383-487 |
5.44e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.93 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 383 LKTQIQSQESDLKSQEDDLNRAKSELNRLQqeetQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAH- 461
Cdd:COG0845 59 LQAALAQAQAQLAAAQAQLELAKAELERYK----ALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTi 134
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622897435 462 ----------RSLEQYDQVldgAHGASLTDLADLSE 487
Cdd:COG0845 135 rapfdgvvgeRNVEPGQLV---SAGTPLFTIADLDP 167
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
328-474 |
5.64e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 328 QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD-------------ETqmISSLKTQIQSQESDL 394
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrksllanrfsfgPA--LDELEKQLENLEEEF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 395 kSQEDDLN------RAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKST-QDEINQAR-------------------S 448
Cdd:PRK04778 182 -SQFVELTesgdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKagyrelveegyhldhldieK 256
|
170 180
....*....|....*....|....*.
gi 1622897435 449 KLSQLHESRQEAHRSLEQYDqvLDGA 474
Cdd:PRK04778 257 EIQDLKEQIDENLALLEELD--LDEA 280
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
275-467 |
6.16e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 275 SGSLGSGEFTGVKELDDisqeiaqLQREKYSLEQDIrekeEAIRQKTSEVQELQND---LDRETS----SLQELEAQKQD 347
Cdd:PLN02939 214 GATEGLCVHSLSKELDV-------LKEENMLLKDDI----QFLKAELIEVAETEERvfkLEKERSlldaSLRELESKFIV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 348 AQDRLDEMDQQKAklrDMLSDVRQKCQDetqMISSLKTQIQS------QESDLKSQEDDLNRAKSELNR----------L 411
Cdd:PLN02939 283 AQEDVSKLSPLQY---DCWWEKVENLQD---LLDRATNQVEKaalvldQNQDLRDKVDKLEASLKEANVskfssykvelL 356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 412 QQEETQLEQSIQAGRVQLETIIKSLkstQDEINQARSKLSQLHESRQEahRSLEQY 467
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHSYIQLY---QESIKEFQDTLSKLKEESKK--RSLEHP 407
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
288-477 |
6.59e-03 |
|
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: 39.62 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREkysleqdIREKEEAIRQKTSEVQELQNDlDRETSSLQELEAQKQ-------DA-QDRLDEMDQQK 359
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETE-SSCSTPLRRNESFSSlhgcvqlDAlQEKLRGLEEEN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 360 AKLRDMLSDVRQKCQD----ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLeqsiQAGRVQLETIIKS 435
Cdd:pfam04849 181 LKLRSEASHLKTETDTyeekEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSL----LAQIVDLQHKCKE 256
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897435 436 LKSTQDEINQarsklsQLHESRqEAHRSL--------EQYDQVLDGAHGA 477
Cdd:pfam04849 257 LGIENEELQQ------HLQASK-EAQRQLtselqelqDRYAECLGMLHEA 299
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
257-451 |
6.87e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 40.03 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 257 LSPDMVPPSErgtPGPDSSGSLGSGEFTGVKELDDISQEI-AQLQRekySLEQDI--REKEEAIRQKtsEVQELqndLDR 333
Cdd:pfam10168 471 LLIDAVPPSP---PLLCSKEDVTVDEPLRGLQEDSFEDHIkSILQR---SVSNPIlsADKLSSPSPQ--ECLQL---LSR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 334 ETSSLQELEAQKQDA-----QDRLDEMDQQKAK-LRDMlsdvrQKCQDETQMISSLKTQIQSQESDLK-SQEDDLNRAKS 406
Cdd:pfam10168 540 ATQVFREEYLKKHDLareeiQKRVKLLKLQKEQqLQEL-----QSLEEERKSLSERAEKLAEKYEEIKdKQEKLMRRCKK 614
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622897435 407 ELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLS 451
Cdd:pfam10168 615 VLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKKKMN 659
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
337-487 |
6.89e-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: 39.68 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 337 SLQELEAQKQDAQDRLDEMdqqkaklRDMLSDVrQKCQDETQ-MISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 415
Cdd:pfam04108 1 SLSSAQDLCRWANELLTDA-------RSLLEEL-VVLLAKIAfLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 416 TQLEQsiqagrvQLETIIKSLKST---------------------QDEINQARSKLSQLHESRQEAHRSLEQYDQVLDga 474
Cdd:pfam04108 73 DAALE-------RLEETLDKLRNTpvepalppgeekqktlldfidEDSVEILRDALKELIDELQAAQESLDSDLKRFD-- 143
|
170
....*....|...
gi 1622897435 475 hgaslTDLADLSE 487
Cdd:pfam04108 144 -----DDLRDLQK 151
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
291-466 |
7.21e-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: 39.82 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 291 DISQEIAQLQREK-------YSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAK 361
Cdd:pfam15450 24 DLQAEVVSLRGHKercehatLSLLRELLQVRAHVQLQDSELKQLRQEVQQAARApeKEALEFPGPQNQNQMQALDKRLVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 362 LRDMLSDVRQK--CQDE-------------TQMISSLKTQIQSQESD----LKSQEDDLNRAKSELNRLQQEETQL--EQ 420
Cdd:pfam15450 104 VREALTQIRRKqaLQDSerkgaeqeanlrlTKLTGKLKQEEQGREAAcsalQKSQEEASQKVDHEVARMQAQVTKLgeEM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 421 S-------------IQAGRVQLETIIKSLKSTQ--------DEINQARSKLSQLHESR---------QEAHRSLEQ 466
Cdd:pfam15450 184 SlrflkreaklcsfLQKSFLALEKRMKASESTRlkaesslrEELEGRWQKLQELTEERlralqgqreQEEGHLLEQ 259
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
349-494 |
7.34e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 349 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKtqiqsqesdlksqeDDLNRAKSELNRLQQEETQLEQSIQAGRVQ 428
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897435 429 LETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHG---ASLTDLADLSE--GVSLAER 494
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKrdrESQAKIADLGRrlNVALAQR 188
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
318-463 |
7.62e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 318 RQKTSEVQELQNDLDRETSSLQE-LEAQKQDAQDRLDEMDQQKAKLRdmlsdvRQKCQDETQMISSLKTQIQSQESDLKS 396
Cdd:PRK12705 29 QRLAKEAERILQEAQKEAEEKLEaALLEAKELLLRERNQQRQEARRE------REELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897435 397 QEDDLNRAKSELNR----LQQEETQLEQSIQ--AG---RVQLETIIKSLKSTQDEINQARSKLsQLHESRQEAHRS 463
Cdd:PRK12705 103 LENQLEEREKALSAreleLEELEKQLDNELYrvAGltpEQARKLLLKLLDAELEEEKAQRVKK-IEEEADLEAERK 177
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
289-366 |
7.96e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.13 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 289 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQDRLD---EMDQQKAKLRD 364
Cdd:pfam00038 226 IQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETrQEMARQLREYQELLNvklALDIEIATYRK 305
|
..
gi 1622897435 365 ML 366
Cdd:pfam00038 306 LL 307
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
290-431 |
8.10e-03 |
|
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: 39.04 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 290 DDISQEIAQLQREKYSLEQ----------------------DIREKEEAIRQKTSEVQELQNDLDRETSSL--------Q 339
Cdd:pfam09755 110 NDLSRKLTQLRQEKVELEQtleqeqeyqvnklmrkiekleaETLNKQTNLEQLRREKVELENTLEQEQEALvnrlwkrmD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 340 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELNRLQQEETQL- 418
Cdd:pfam09755 190 KLEAEKRLLQEKLDQPVSAPPSPRDSTSE-GDTAQNLTAHIQYLRKEVERLRRQLATAQQE---HTEKMAQYAQEERHIr 265
|
170
....*....|....
gi 1622897435 419 EQSIQAGR-VQLET 431
Cdd:pfam09755 266 EENLRLQRkLQLEM 279
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
317-444 |
8.73e-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: 38.78 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 317 IRQKTSEVQELQNDLDRETSSLQELeaqKQDAQDrldeMDQQKA-KLRDMLsdvrQKcQDETQMISSL-----KTQIQSQ 390
Cdd:pfam15397 1 IRNRRTSLEELKKHEDFLTKLNLEL---IKAIQD----TEDSTAlKVRKLL----QQ-YEKFGTIISIleysnKKQLQQA 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622897435 391 ESDLKSQEDdlnRAKSELNRLQQEETQLEQSIQagrvqletiikslkSTQDEIN 444
Cdd:pfam15397 69 KAELQEWEE---KEESKLNKLEQQLEQLNAKIQ--------------KTQEELN 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
339-460 |
8.89e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 36.53 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 339 QELEAQKQDAQDRLDEMDQQKAKLRDmlsdvrqkcQDETQMISSlktqIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 418
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSS---------EDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622897435 419 eqsIQAGRVQLETIikslKSTQDEINQARSKLSQLHESRQEA 460
Cdd:pfam00435 68 ---IDEGHYASEEI----QERLEELNERWEQLLELAAERKQK 102
|
|
| DUF5082 |
pfam16888 |
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized. |
294-411 |
8.92e-03 |
|
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized.
Pssm-ID: 407125 [Multi-domain] Cd Length: 122 Bit Score: 36.89 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 294 QEIAQLQREKYSLEQDIREKEEAiRQKTSEVQElqndldretsslqELEAQKQDAQDRLDEMD----QQKAKLRDMLSDV 369
Cdd:pfam16888 10 AQIAQLRSEIAALEEKIERLKEA-KTKLDAEKE-------------SLHDKKTKLQGPLNSSEswngSNENNYDGIRSNL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622897435 370 RQKCQ---DET-QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 411
Cdd:pfam16888 76 ETSYQnyvDELdELIDAIEEEITRLENQINEAQGVIDTLQSQLNSL 121
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
293-466 |
8.92e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 39.64 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 293 SQEIAQLQREKYSLeqDIREKEEAIRQK--TSEVQELQNDLDRETSSLQEL-EAQKQDAQDRLDEmdqqkaklrdmLSDV 369
Cdd:pfam14817 259 AREKTAIQEETESL--DVRADAEALRFRyeSNHLLDVSSDESSDLPSVRQLlERQWAHVQQFLNE-----------LAET 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 370 RQKCQDETQMISSLKTQIQSQESDL--KSQEDDLNRAKSELNRlqqeetqleqsiQAGRVQletiiKSLKSTQDEINQar 447
Cdd:pfam14817 326 RSRCQQLQARLQGLKDEAELESLGIgdTSQNDSLLRQVLELEL------------QAAGLA-----ASRDTLRSECQQ-- 386
|
170
....*....|....*....
gi 1622897435 448 skLSQLHESRQEAHRSLEQ 466
Cdd:pfam14817 387 --LNKLARERQEALRSLQK 403
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
288-370 |
8.98e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 38.26 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 288 ELDDISQEIAQLQREKYSLE---QDIR--------EKEEAIRQKTSEVQELQndldretsslQELEAQKQDAQDRLDEMD 356
Cdd:pfam06785 105 ELSQKEEELRRLTEENQQLQiqlQQISqdfaefrlESEEQLAEKQLLINEYQ----------QTIEEQRSVLEKRQDQIE 174
|
90
....*....|....
gi 1622897435 357 QQKAKLRDMLSDVR 370
Cdd:pfam06785 175 NLESKVRDLNYEIK 188
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
338-452 |
9.22e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 36.79 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897435 338 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR------QKCQDETQMISSLKT-QIQSQESDLKsqeDDLNRAKSELN- 409
Cdd:COG1382 9 VQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEkaleelEKLPDDAEVYKSVGNlLVKTDKEEVI---KELEEKKETLEl 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622897435 410 RLQQEETQLEqsiqagRVQletiiKSLKSTQDEINQARSKLSQ 452
Cdd:COG1382 86 RLKTLEKQEE------RLQ-----KQLEELQEKLQEALSGAGG 117
|
|
| |
