|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
121-214 |
3.14e-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: 140.11 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 121 WAVRVEEKAKFDGIFESLLP-INGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 199
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 1622897437 200 VPSALPPSLIPPSKR 214
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
268-364 |
8.32e-37 |
|
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: 133.17 E-value: 8.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 268 NWVVPVADKMRFDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSkG 347
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 1622897437 348 IDPPQVLSPDMVPPSER 364
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
127-214 |
5.09e-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: 100.14 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 127 EKAKFDGIFESLLPINGLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPSAL 204
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDEL 87
|
90
....*....|
gi 1622897437 205 PPSLIPPSKR 214
Cdd:pfam12763 88 PDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
131-196 |
5.58e-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: 5.58e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 131 FDGIFESLLPIN-GLLSGDKVKPVLMNSKLPLDVLGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 196
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
279-345 |
6.48e-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: 6.48e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 279 FDEIFLKTDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVS 345
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
19-85 |
1.22e-20 |
|
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: 86.12 E-value: 1.22e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 19 YESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQS 85
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
13-103 |
3.90e-20 |
|
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: 85.79 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 13 PTGNSLYESYYKQVDPAYTGRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLVACAQSGHEVTLS 92
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 1622897437 93 NLNLSMPPPKF 103
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-566 |
5.76e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQAR 544
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180
....*....|....*....|..
gi 1622897437 545 SKLSQLHESRQEAHRSLEQYDQ 566
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEE 456
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-550 |
1.80e-17 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 84.95 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 381 TGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagRVQLETIIKSLKSTQDEI 540
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAEQALDELLKEA 192
|
170
....*....|
gi 1622897437 541 NQARSKLSQL 550
Cdd:COG4372 193 NRNAEKEEEL 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-591 |
3.31e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQD-------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:COG1196 368 LEAEAELAEaeeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 537 QDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 591
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-591 |
6.69e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622897437 544 RSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 591
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-591 |
6.75e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEI-AQLQR--------EKY-SLEQDIREKEeaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQ 455
Cdd:COG1196 191 LEDILGELeRQLEPlerqaekaERYrELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS 535
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 536 TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 591
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-571 |
6.88e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 471
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 472 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLH 551
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180
....*....|....*....|
gi 1622897437 552 ESRQEAHRSLEQYDQVLDGA 571
Cdd:COG1196 393 RAAAELAAQLEELEEAEEAL 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-563 |
6.25e-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: 79.33 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdqqkAKLRDML 463
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180
....*....|....*....|
gi 1622897437 544 RSKLSQLHESRQEAHRSLEQ 563
Cdd:TIGR02168 858 AAEIEELEELIEELESELEA 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-571 |
8.49e-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: 78.95 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE-------LEAQKQDAQDRLDEMDQQ 455
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisrLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS 535
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897437 536 TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGA 571
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-569 |
3.06e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 75.32 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 407 IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 486
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 487 QESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEahRSLEQYDQ 566
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA--LSEAEAEQ 183
|
...
gi 1622897437 567 VLD 569
Cdd:COG4372 184 ALD 186
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-550 |
3.56e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.60 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKSTQD----E 539
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKISSLKEKIEklesE 532
|
170
....*....|.
gi 1622897437 540 INQARSKLSQL 550
Cdd:TIGR04523 533 KKEKESKISDL 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-563 |
4.48e-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: 74.80 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDML 463
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 ------------------SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQ 525
Cdd:COG4942 111 ralyrlgrqpplalllspEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622897437 526 LETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-563 |
6.34e-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: 75.87 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 375 LGSGEFTGVKE-LDDISQEIAQLQR--------------EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE 439
Cdd:TIGR02169 284 LGEEEQLRVKEkIGELEAEIASLERsiaekereledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI-------QSQESDLKSQEDDLNRAKSELNRLQQEE 512
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 513 TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
404-562 |
7.30e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 404 EQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQ 483
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 484 IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLE 562
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-556 |
9.16e-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: 75.06 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQ------SQESDLKSQ----EDDLNRAKSELNRLQQE----ETQLEQSIQagrvQLETI 529
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQknksleSQISELKKQnnqlKDNIEKKQQEINEKTTEisntQTQLNQLKD----EQNKI 265
|
170 180
....*....|....*....|....*..
gi 1622897437 530 IKSLKSTQDEINQARSKLSQLHESRQE 556
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-576 |
9.29e-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: 73.64 E-value: 9.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQDRLDEMDQQK----- 456
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdflda 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897437 537 QDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASL 576
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-584 |
1.00e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL----NRLQQEETQLEQSIQAGRVQLETIIKSLKSTQD 538
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897437 539 EINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSE 584
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
385-573 |
1.42e-13 |
|
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: 71.11 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 DVR-----QKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 539
Cdd:COG1579 84 NVRnnkeyEALQKE---IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170 180 190
....*....|....*....|....*....|....
gi 1622897437 540 INQARSKLSQlhesrQEAHRSLEQYDQVLDGAHG 573
Cdd:COG1579 161 LEAEREELAA-----KIPPELLALYERIRKRKNG 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-588 |
1.90e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 S-------DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRVQLETIIKSL 533
Cdd:TIGR02168 813 TllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALL 892
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 534 KS----TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSL 588
Cdd:TIGR02168 893 RSeleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
385-562 |
4.55e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 dvRQKCQDETQMISSLKTQIQSQESDLKSQEddlnrakSELNRLQQEETQLEQSIQ---AGRVQLETIIKSLKSTQDEIN 541
Cdd:TIGR02169 790 --HSRIPEIQAELSKLEEEVSRIEARLREIE-------QKLNRLTLEKEYLEKEIQelqEQRIDLKEQIKSIEKEIENLN 860
|
170 180
....*....|....*....|.
gi 1622897437 542 QARSKLSQLHESRQEAHRSLE 562
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLE 881
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-556 |
5.91e-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: 72.75 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
170
....*....|...
gi 1622897437 544 RSKLSQLHESRQE 556
Cdd:TIGR04523 495 EKELKKLNEEKKE 507
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-568 |
9.84e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 393 IAQLQREKYSLE-----------QDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG4717 48 LERLEKEADELFkpqgrkpelnlKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 459 LRDMLSdvRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSI-QAGRVQLETIIKSLKSTQ 537
Cdd:COG4717 128 LPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 1622897437 538 DEINQARSKLSQLHESRQEAHRSLEQYDQVL 568
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-525 |
1.77e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKT--SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 461 DMLSDVRQKCQDETQM----ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQ 525
Cdd:COG4717 174 ELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-550 |
2.08e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRET--SSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDetqmISSLKTQIQSQESDLK-SQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 539
Cdd:COG4717 160 ELEEELEELEAE----LAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170
....*....|...
gi 1622897437 540 --INQARSKLSQL 550
Cdd:COG4717 236 leAAALEERLKEA 248
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-566 |
2.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRD-- 461
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEEle 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 -MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEI 540
Cdd:COG1196 407 eAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
170 180
....*....|....*....|....*.
gi 1622897437 541 NQARSKlsqlHESRQEAHRSLEQYDQ 566
Cdd:COG1196 487 AEAAAR----LLLLLEAEADYEGFLE 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
383-542 |
2.46e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 70.43 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQND--LDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDETQMI-SSLKTQI---QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:COG3206 298 AQIAALRAQLQQEAQRIlASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....*.
gi 1622897437 537 QDEINQ 542
Cdd:COG3206 378 RLAEAL 383
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-596 |
2.89e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.09 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDAQ--------------- 446
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSvsyldvllgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 447 --DRLDEMDQQKAKLRDMLSDVrqkcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRV 524
Cdd:COG3883 117 flDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 525 QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAERGGFGA 596
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-567 |
3.22e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.09 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR- 460
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERarALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 ---------DMLSDVRQKCQDETQMISSLKTQIQSQESD---LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLET 528
Cdd:COG3883 103 syldvllgsESFSDFLDRLSALSKIADADADLLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622897437 529 IIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQV 567
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-566 |
3.22e-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: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQ 471
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 472 DETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLH 551
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170
....*....|....*
gi 1622897437 552 ESRQEAHRSLEQYDQ 566
Cdd:TIGR02168 393 LQIASLNNEIERLEA 407
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-563 |
3.32e-12 |
|
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: 69.02 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SdvRQKCQDETQMISSLKTQIQSQESDLKSQED--DLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKS-------LK 534
Cdd:COG4942 100 E--AQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEleaeraeLE 177
|
170 180
....*....|....*....|....*....
gi 1622897437 535 STQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-563 |
7.78e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQdIREKEEAIRQKTSEVQELQ---------------NDLDREtssLQELEAQKQDAQDR 448
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEylraalrlwfaqrrlELLEAE---LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 449 LDEMDQQKAKLRDMLSDVRQKC-QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLE 527
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897437 528 TIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-571 |
1.04e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 388 DISQEIAQLQREKYSLeqDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:TIGR02168 217 ELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 468 QKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvqletiikslkSTQDEINQARSKL 547
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE--------------ELKEELESLEAEL 360
|
170 180
....*....|....*....|....
gi 1622897437 548 SQLHESRQEAHRSLEQYDQVLDGA 571
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETL 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-584 |
2.46e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKyslEQDIREKE---EAIRQKTSEVQELQNDLD--RETSSLQELEAqkQDAQDRLDEMDQQKAKL 459
Cdd:PRK02224 252 ELETLEAEIEDLRETI---AETEREREelaEEVRDLRERLEELEEERDdlLAEAGLDDADA--EAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 RDMLSDVRqkcqdetqmisslkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 539
Cdd:PRK02224 327 RDRLEECR--------------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897437 540 INQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGaSLTDL-ADLSE 584
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELRE-REAELeATLRT 437
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-521 |
3.67e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 380 FTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-ETSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 459 LRDMLSDVRQKCQDETQMISSLKTQIQSQ----ESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
385-532 |
3.87e-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: 67.02 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 465 DVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsiQAGRVQLETIIKS 532
Cdd:TIGR02169 466 KYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEER--------VRGGRAVEEVLKA 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-569 |
5.88e-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: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdml 463
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgrvqLETIIKSLKSTQDEINQa 543
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV----KELIIKNLDNTRESLET- 468
|
170 180
....*....|....*....|....*.
gi 1622897437 544 rsKLSQLHESRQEAHRSLEQYDQVLD 569
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQKQKELK 492
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
384-543 |
5.91e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.92 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLksQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
387-568 |
6.17e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.81 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQDIREKEEAI---RQKT------SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA 457
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 458 KLRDMLSDVRQkcqdeTQMISSLKTQIQSQESDLKSQED-------DLNRAKSELNRLQQE-ETQLEQSIQAGRVQLETI 529
Cdd:COG3206 251 SGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQlQQEAQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622897437 530 IKSLKSTQDEINQARSKLSQLHESRQEAhRSLEQ--------YDQVL 568
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAEL-RRLERevevarelYESLL 371
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
384-533 |
8.25e-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: 63.02 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKqDAQDRLDEMDQQKAKLRDmL 463
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISD-L 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAKSElnrLQQEETQLEQSIQAGRVQLETIIKSL 533
Cdd:COG1579 109 EDEILELMER---IEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKI 172
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
392-557 |
1.35e-10 |
|
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: 64.76 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSevqELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMlSDVRQKCQ 471
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELS---ELRRQIQRAELELQSTNSELEELQERLDL---LKAKASEA-EQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 472 DETQMISSLKTQIQSQESDLKSQEDD---LNRAKSELNRLQQEETQLEQsIQAGRVQLETIIKSLKSTQDEINQARSKLS 548
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
....*....
gi 1622897437 549 QLHESRQEA 557
Cdd:pfam05557 239 REEKYREEA 247
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
384-568 |
1.36e-10 |
|
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: 64.49 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKeeairqktsEVQELQNDLDRETSSLQELEAqkQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam06160 211 DQLEELKEGYREMEEEGYALEHLNVDK---------EIQQLEEQLEENLALLENLEL--DEAEEALEEIEERIDQLYDLL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 ---SDVRQKCQDETQMISSLKTQIQSQESDLKS-----------QEDDLNRAKS---ELNRLQQEETQLEQSIQAGRV-- 524
Cdd:pfam06160 280 ekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEelervqqsytlNENELERVRGlekQLEELEKRYDEIVERLEEKEVay 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622897437 525 -----QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 568
Cdd:pfam06160 360 selqeELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
384-557 |
1.61e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.65 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQR--EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----------- 450
Cdd:COG3206 182 EQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellq 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 451 -----EMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDD-LNRAKSELNRLQQEETQLEQSIQagrv 524
Cdd:COG3206 262 spviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLA---- 337
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897437 525 QLETIIKSLKSTQDEINQ-------ARSKLSQLHESRQEA 557
Cdd:COG3206 338 QLEARLAELPELEAELRRlerevevARELYESLLQRLEEA 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-563 |
2.55e-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: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQ-----KQDAQDRL----DE 451
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNkelkSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 452 MDQQKAKLRDMLSDVRQKcqdeTQMISSLKTQIQSQESDLKSQEDD-------LNRAKSELNRLQQEETQLEQSIQagrv 524
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQN----NKIISQLNEQISQLKKELTNSESEnsekqreLEEKQNEIEKLKKENQSYKQEIK---- 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622897437 525 QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-563 |
2.57e-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: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQ---DIREKEEAIRQKTSEVQE-------LQNDLDRETSSLQELEAQKQDAQDRLDEMD 453
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISElkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 454 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQ--EDDLNRAKSEL----NRLQQEETQLEQSIQAGRv 524
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeQDWNKELKSELknqeKKLEEIQNQISQNNKIIS- 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897437 525 QLETIIKSLKST-----------QDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:TIGR04523 339 QLNEQISQLKKEltnsesensekQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
391-591 |
3.58e-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: 62.99 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQDiREKEEAIRQKT---SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:pfam07888 50 QEAANRQREKEKERYK-RDREQWERQRReleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 468 QKCQDETQMISSLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEETQLEQSiqagRVQLETIIKSLKSTQDEINQARSKL 547
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQL----QAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622897437 548 SQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 591
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-573 |
4.17e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLD------RETSSLQE-------LEAQKQDAQDRL 449
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEkaeeyikLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 450 DEMDQQKAKLRDMLSDVRQKCQD------ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE-QSIQAG 522
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKL 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 523 RVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQydqvLDGAHG 573
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE----LKKAKG 436
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
385-568 |
5.49e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 62.55 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKE-EAIRQKTSEVQELQNDLDretssLQELEAQKQDAQDRLDEM----------- 452
Cdd:PRK04778 231 QLQELKAGYRELVEEGYHLDHLDIEKEiQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLydilerevkar 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 453 ---DQQKAKLRDMLSDVR---QKCQDETQMISslktqiQS---QESDLKSQEDdlnrAKSELNRLQQEETQLEQSIQAGR 523
Cdd:PRK04778 306 kyvEKNSDTLPDFLEHAKeqnKELKEEIDRVK------QSytlNESELESVRQ----LEKQLESLEKQYDEITERIAEQE 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 524 V-------QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 568
Cdd:PRK04778 376 IayselqeELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-566 |
9.37e-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: 62.35 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQ-------SQESDLKSQEDDLNRAKSELNRLQQEETQleQSIQAGRVQLETIIKSLKST 536
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEklesekkEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKK 583
|
170 180 190
....*....|....*....|....*....|
gi 1622897437 537 QDEINQarsKLSQLHESRQEAHRSLEQYDQ 566
Cdd:TIGR04523 584 QEEKQE---LIDQKEKEKKDLIKEIEEKEK 610
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-571 |
1.17e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 398 REKYSLEQDIREKEEAIRQktsEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDmLSDVRQKCQDetqmI 477
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEA---ELAELEEEL-------AEAEERLEALEAELDALQERREALQR-LAEYSWDEID----V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 478 SSLKTQIQSQESDLksqeDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLhESRQEA 557
Cdd:COG4913 664 ASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL-QDRLEA 738
|
170
....*....|....
gi 1622897437 558 HRSLEQYDQVLDGA 571
Cdd:COG4913 739 AEDLARLELRALLE 752
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
392-539 |
2.07e-09 |
|
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: 59.77 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE--------LEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREqlqeleeqLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQ-------KCQDETQMISSLKTQIQSQeSDLKSQEDDL-NRAKSELNRLQQEETQLEqSIQAGR----VQLETIIK 531
Cdd:pfam09787 128 EELRRskatlqsRIKDREAEIEKLRNQLTSK-SQSSSSQSELeNRLHQLTETLIQKQTMLE-ALSTEKnslvLQLERMEQ 205
|
....*...
gi 1622897437 532 SLKSTQDE 539
Cdd:pfam09787 206 QIKELQGE 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
385-563 |
2.79e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQL-----QREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQ-DRLDEMDQQKAK 458
Cdd:COG4913 270 RLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 459 LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQD 538
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180
....*....|....*....|....*
gi 1622897437 539 EINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAE 451
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
378-460 |
3.07e-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: 58.01 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 378 GEFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKA 457
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
...
gi 1622897437 458 KLR 460
Cdd:COG1579 160 ELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-584 |
3.17e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDIREKEEAIR---------QKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMD 453
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 454 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQSIQAGRVQleTIIK 531
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVER--ELRE 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 532 SLkstQDEINQARSKLSQLhesRQEAHRSLEQYDQVLDGAHGASLTDLADLSE 584
Cdd:COG4913 770 NL---EERIDALRARLNRA---EEELERAMRAFNREWPAETADLDADLESLPE 816
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
384-569 |
4.71e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 58.78 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLE---QDIREK-EEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ-Q 455
Cdd:pfam00038 61 RQLDTLTVERARLQLELDNLRlaaEDFRQKyEDELNLRTSaenDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQ--------ESDLKSQEDDLNRA----KSELNRLQQEET 513
Cdd:pfam00038 141 EEEVRELQAQVSDtqvnvemdaaRKLDLTSALAEIRAQYEEIaaknreeaEEWYQSKLEELQQAaarnGDALRSAKEEIT 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 514 QLEQSIQAGRVQLETIIKSLKSTQD-----------EINQARSKLS----QLHESRQEAHRSLEQYDQVLD 569
Cdd:pfam00038 221 ELRRTIQSLEIELQSLKKQKASLERqlaeteeryelQLADYQELISeleaELQETRQEMARQLREYQELLN 291
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
384-572 |
9.56e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDI---REKEEAIRQKT----SEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELkelAEKRDELNAQVkelrEEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 AKLRDMLSDVRQKCQDETQM---ISSLKTQIQSQESDLKsQEDDL----NRAKSELNRLQQEETQLEqsiqagrvQLETI 529
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLrkeIERLEWRQQTEVLSPE-EEKELvekiKELEKELEKAKKALEKNE--------KLKEL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897437 530 IKSLKSTQDEINQARSKLSQLHESRQEAHRSL----EQYDQV---LDGAH 572
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMielyKEADELrkeADELH 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-571 |
1.17e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQeIAQLQREKysleQDIREKEEAIRQKTSEVQ----ELQNDLDR-------------------ET------SS 434
Cdd:TIGR02169 157 KIIDEIAG-VAEFDRKK----EKALEELEEVEENIERLDliidEKRQQLERlrrerekaeryqallkekrEYegyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI------------------QSQESDLKSQED 496
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqlrvkekigelEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 497 DLNR-----------AKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYD 565
Cdd:TIGR02169 312 EKEReledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
....*.
gi 1622897437 566 QVLDGA 571
Cdd:TIGR02169 392 EKLEKL 397
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
394-582 |
1.22e-08 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 58.17 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 394 AQLQrekySLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlsdvrqkcqde 473
Cdd:PRK11637 47 DQLK----SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDEL-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 474 TQMISSLKTQIQSQESDLKSQEDDLNRaKSELNRLQ----QEETQLEQSIQA-----GRVQLETIIKsLKSTQDEINQAR 544
Cdd:PRK11637 109 NASIAKLEQQQAAQERLLAAQLDAAFR-QGEHTGLQlilsGEESQRGERILAyfgylNQARQETIAE-LKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622897437 545 SKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADL 582
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGL 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
383-557 |
1.41e-08 |
|
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: 58.49 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDI-------SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL--QELEAQKQDAQDRLDEMD 453
Cdd:TIGR04523 495 EKELKKLneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 454 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSiqagrvqLETIIKSL 533
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQEV 647
|
170 180
....*....|....*....|....
gi 1622897437 534 KSTQDEINQARSKLSQLHESRQEA 557
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKES 671
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
423-582 |
2.46e-08 |
|
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: 55.32 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 423 ELQnDLDREtssLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 502
Cdd:COG1579 11 DLQ-ELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 503 S--ELNRLQQEETQLEQSIQagrvQLEtiikslkstqDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLA 580
Cdd:COG1579 87 NnkEYEALQKEIESLKRRIS----DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
..
gi 1622897437 581 DL 582
Cdd:COG1579 153 EL 154
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
384-557 |
2.58e-08 |
|
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: 55.39 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSeVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam12795 44 KALDDAPAELRELRQELAALQAKAEAAPKEILASLS-LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISS---------------LKTQIQSQESDLKSQEDDL--NRAKSELNRLQQEETQLEQSiqagrvQL 526
Cdd:pfam12795 123 SEARQRLQQIRNRLNGpappgeplseaqrwaLQAELAALKAQIDMLEQELlsNNNRQDLLKARRDLLTLRIQ------RL 196
|
170 180 190
....*....|....*....|....*....|.
gi 1622897437 527 ETIIKSLKSTQDEINQARSKLSQLHESRQEA 557
Cdd:pfam12795 197 EQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-544 |
3.27e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREkySLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEqsiqagrvqletiiKSLKSTQDEINQAR 544
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE--------------ATLRTARERVEEAE 446
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-556 |
3.84e-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: 57.36 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEvQELQNDLDRETSSLQELEAQKQDAQDRLDEM--DQQKAKLR 460
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQQaaKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE---QSIQAGRVQLETIIKSLKSTQ 537
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGtnlQRRQQFEEQLVELSTEVQSLI 901
|
170
....*....|....*....
gi 1622897437 538 DEINQARSKLSQLHESRQE 556
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEK 920
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
387-563 |
4.58e-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: 56.44 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQdrlDEMDQQKAKLRDMLSDV 466
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AERKQLQAKLQQTEEEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 467 RQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKSTQDEINQARSK 546
Cdd:pfam07888 188 RSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERKVEGLGEE 259
|
170
....*....|....*..
gi 1622897437 547 LSQLHESRQEAHRSLEQ 563
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQ 276
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-571 |
4.73e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAI---RQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLeehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKC-----QDET--QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSL 533
Cdd:PRK02224 293 EERDDLLAEAglddaDAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622897437 534 KSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGA 571
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-562 |
6.43e-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: 56.61 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQDRLDEMdqqKAKLRDM 462
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-------DLKEQIKSIEKEIENL---NGKKEEL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQKCQDETQMISS---LKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQdE 539
Cdd:TIGR02169 867 EEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-E 945
|
170 180
....*....|....*....|...
gi 1622897437 540 INQARSKLSQLHESRQEAHRSLE 562
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIR 968
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-591 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 411 EEAIRqktsEVQELQNDLDRETSSLQELEAQK------QDAQDRLDEMDQQKAKLRDMLSDVRQkcQDETQMISSLKTQI 484
Cdd:COG4913 224 FEAAD----ALVEHFDDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 485 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgrvqletiikslkSTQDEINQARSKLSQLHESRQEAHRSLEQY 564
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180
....*....|....*....|....*..
gi 1622897437 565 DQVLDGAHGASLTDLADLSEGVSLAER 591
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAA 391
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-596 |
1.31e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 DVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELNRLQqeetqlEQSIQAgrvqletiiksLKSTQDEINQAR 544
Cdd:COG3096 582 ELRQQLE-----------QLRARIKELAARAPAWLAAQDALERLR------EQSGEA-----------LADSQEVTAAMQ 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 545 SKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAERggFGA 596
Cdd:COG3096 634 QLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAER--LGG 683
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-635 |
2.88e-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: 54.35 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQKAKL 459
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 RDMLSDVRQKCQDETQMISslktqiqsqesdlksqeddlnRAKSELNRLQQEETQLEQSIQAGRVQLETiIKSLKSTQD- 538
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVG---------------------QHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKDa 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 539 EINQARSKLSQLH----------ESRQEAHRSLEQ-YDQVLDGAHgASLTDLADLSEGVSLAERGgfgamddpFKNKALL 607
Cdd:pfam15921 619 KIRELEARVSDLElekvklvnagSERLRAVKDIKQeRDQLLNEVK-TSRNELNSLSEDYEVLKRN--------FRNKSEE 689
|
250 260 270
....*....|....*....|....*....|....*
gi 1622897437 608 FSNNTQEL-------HPDPFQTEDPFKSdpFKGAD 635
Cdd:pfam15921 690 METTTNKLkmqlksaQSELEQTRNTLKS--MEGSD 722
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
438-579 |
3.42e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 438 LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD--ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 516 EQSIQAGRVQLETIIKS--LKSTQDEINQARSKLSQL-------HESRQEAHRSLEQYDQVLDGAHGASLTDL 579
Cdd:COG3206 246 RAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQLQQEAQRILASL 318
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
405-581 |
3.42e-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: 54.03 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 405 QDIREKEEAIRQktsEVQELQNDLDRETSSLQEleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 484
Cdd:pfam01576 193 EERLKKEEKGRQ---ELEKAKRKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 485 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQY 564
Cdd:pfam01576 267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQ 346
|
170
....*....|....*..
gi 1622897437 565 DQVLDGAHGASLTDLAD 581
Cdd:pfam01576 347 LQEMRQKHTQALEELTE 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-568 |
3.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEmdQQKAKLRDML 463
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERF 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRvQLETIIKSLKST-----Q 537
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdLDADLESLP-EYLALLDRLEEDglpeyE 833
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897437 538 DEINQARSK---------LSQLHESRQEAHRSLEQYDQVL 568
Cdd:COG4913 834 ERFKELLNEnsiefvadlLSKLRRAIREIKERIDPLNDSL 873
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
379-575 |
3.55e-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: 53.81 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 379 EFTGVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS----LQELEAQKQDAQDRLDEMDQ 454
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqIEELQRQIEQATSSNEEVSK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 455 QKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQEsdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRVQLETII---- 530
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRS------------VRSKKEDLNEELTQIESRVSTLKATLEKLRakle 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622897437 531 KSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGAS 575
Cdd:COG5185 510 RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
385-572 |
3.67e-07 |
|
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: 51.68 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQktseVQELQNDLdretssLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEA----LNELGEQL------IEEGHPDAEEIQERLEELNQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 DVRQKCQD------ETQMISSLKTQIQSQESDLKSQE--DDLNRAKSELNRLQqeetQLEQSIQAGRVQLETIIKSLKS- 535
Cdd:cd00176 97 ERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKHK----ELEEELEAHEPRLKSLNELAEEl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622897437 536 ----TQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAH 572
Cdd:cd00176 173 leegHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
391-520 |
4.11e-07 |
|
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: 49.56 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQDIREKEEAIrqktsevQELQNDLDRETSSLQEleaqkqdAQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQL-------QKLQEDLEKQAEIARE-------AQQNYERELVLHAEDIKALQALREEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622897437 471 QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSelnRLQQEETQLEQSIQ 520
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIE 113
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
394-549 |
4.20e-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: 53.59 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 394 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQKQDAQDR------------------ 448
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKReaeaeealreqaelnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 449 ----------LDEMDQQKAKLRDMLSDVRQKcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS 518
Cdd:pfam05557 82 kkylealnkkLNEKESQLADAREVISCLKNE-------LSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190
....*....|....*....|....*....|.
gi 1622897437 519 IQagrvQLETIIKSLKSTQDEINQARSKLSQ 549
Cdd:pfam05557 155 RQ----NLEKQQSSLAEAEQRIKELEFEIQS 181
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
384-547 |
4.40e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQ-------ELQNDLDRET----------SSLQELEAQKQDAQ 446
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEelkeqneELEKQYKVKKktldllpdaeENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 447 DRLDEMDQQKAK-----------LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE--- 512
Cdd:pfam05667 415 QRLVELAGQWEKhrvplieeyraLKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrs 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622897437 513 --TQ--LE--QSIQAGRVQLETIIKSLKSTQDEINQARSKL 547
Cdd:pfam05667 495 ayTRriLEivKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-542 |
4.92e-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: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQKCQDETQMISSLKTQIQSQESD---------------------------------------------------- 490
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealenkieddeeearrrlkrlenkikelgpvnlaaieeyeelkeryd 1003
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622897437 491 -LKSQEDDLNRAKselnrlqqeeTQLEQSIQagrvQLETIIKS-LKSTQDEINQ 542
Cdd:TIGR02168 1004 fLTAQKEDLTEAK----------ETLEEAIE----EIDREARErFKDTFDQVNE 1043
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
391-568 |
5.62e-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: 53.42 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQDRLDE-------------- 451
Cdd:COG3096 917 KALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGEnsdlneklrarleq 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 452 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL------------NRAKSELNRLQQEETQLEQSi 519
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqadaeaeERARIRRDELHEELSQNRSR- 1074
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897437 520 qagRVQLETIIKSLKSTQDEINQARSKLSQ-LHESRQEAHRSLEQYDQVL 568
Cdd:COG3096 1075 ---RSQLEKQLTRCEAEMDSLQKRLRKAERdYKQEREQVVQAKAGWCAVL 1121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-557 |
6.86e-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: 53.20 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAqkqdaqdRLDEMDQQKAKL---- 459
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA-------RVSDLELEKVKLvnag 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 RDMLSDVRQKCQDETQMISSLKTqiqsqesdlksqeddlnrAKSELNRLQQEETQLEQSIQAGRVQLETIIK----SLKS 535
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKT------------------SRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKS 703
|
170 180
....*....|....*....|..
gi 1622897437 536 TQDEINQARSKLSQLHESRQEA 557
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHA 725
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-562 |
8.90e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKysLEQDIREKEEaIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE--LEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQKCQDEtqmissLKTQIQSQESDLKsQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQ 542
Cdd:PRK03918 579 LEELGFESVEE------LEERLKELEPFYN-EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
170 180
....*....|....*....|.
gi 1622897437 543 ARSKLSQ-LHESRQEAHRSLE 562
Cdd:PRK03918 652 LEKKYSEeEYEELREEYLELS 672
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
401-510 |
9.19e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 401 YSLEQDIR---------EKEEAIRQKTSEVQELQnDLDRETSSL----QELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:COG2433 376 LSIEEALEeliekelpeEEPEAEREKEHEERELT-EEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622897437 468 QKCQDE---TQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ 510
Cdd:COG2433 455 SEERREirkDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-583 |
1.01e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIR-------EKEEAIRQKTSEVQELQNdldretsSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEE-------ILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622897437 537 QDEINQARSKLSQLHE-------SRQEahrsLEQYDQVLDGAHGASLTDLADLS 583
Cdd:pfam01576 179 SKLKNKHEAMISDLEErlkkeekGRQE----LEKAKRKLEGESTDLQEQIAELQ 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
391-590 |
1.02e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKC 470
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 471 QdetqmisslktQIQSQESDLKSQEDDLNRAKSELNRLQqeetqlEQS--IQAGRVQLETIIKSLKSTQDEINQARSKLS 548
Cdd:PRK04863 589 E-----------QLQARIQRLAARAPAWLAAQDALARLR------EQSgeEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897437 549 QLHESRQEAHRSLEQYdqvlDGAHGASLTDLADLSEGVSLAE 590
Cdd:PRK04863 652 ARKQALDEEIERLSQP----GGSEDPRLNALAERFGGVLLSE 689
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
384-594 |
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 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 544 RSKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLAERGGF 594
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-567 |
1.62e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 410 KEEAIRQ--KTSE----VQELQNDLDRetsSLQELEAQKQDAQ------------------DRLDEMDQQKAKLRDMLSD 465
Cdd:TIGR02168 174 RKETERKleRTREnldrLEDILNELER---QLKSLERQAEKAErykelkaelrelelallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 466 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARS 545
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180
....*....|....*....|..
gi 1622897437 546 KLSqlhESRQEAHRSLEQYDQV 567
Cdd:TIGR02168 331 KLD---ELAEELAELEEKLEEL 349
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
384-529 |
1.65e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYS-----LEQDIREKEEAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEMDQ 454
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHklrneFEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 455 QKAKLRDMLSDVRQKCQDetqmISSLkTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 529
Cdd:PRK12704 129 KEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAI 198
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
387-549 |
1.75e-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: 51.68 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE----------LEAQKQDAQDRlDEMDQqk 456
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNrwrekvfalmVQLKAQDLEHR-DSVKQ-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 akLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:pfam07111 336 --LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
170
....*....|...
gi 1622897437 537 QDEINQARSKLSQ 549
Cdd:pfam07111 414 QIWLETTMTRVEQ 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-569 |
1.89e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 379 EFTGVKE-LDDISQEIAQLQRE---KYSLEQDIREKEEAIRQKTSEVQELQNDLDRET-SSLQELEaqkqdaqDRLDEMD 453
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELE-------ERLKELE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 454 QQKAKLRDmLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ------------EETQLEQSIQA 521
Cdd:PRK03918 599 PFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeelreEYLELSRELAG 677
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622897437 522 GRVQLETiiksLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 569
Cdd:PRK03918 678 LRAELEE----LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
403-591 |
1.90e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.44 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIrqktsevQELQNDLDRETSSLQELEAQKQDAQDRLDEMdQQKAKL----------RDMLSDvRQKCQD 472
Cdd:COG1842 28 LDQAIRDMEEDL-------VEARQALAQVIANQKRLERQLEELEAEAEKW-EEKARLalekgredlaREALER-KAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 473 EtqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRVQLETIIKSL--KSTQDEINQARSKLS 548
Cdd:COG1842 99 Q---AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSGIdsDDATSALERMEEKIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622897437 549 QLhESRQEAHRSLeqydqvldgAHGASLTD-LADLSEGVSLAER 591
Cdd:COG1842 176 EM-EARAEAAAEL---------AAGDSLDDeLAELEADSEVEDE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
396-557 |
2.13e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 396 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDR-------ETSSLQELEAQKQDAQDRLDEMDQQKAKLR-------- 460
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQleeleqei 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 ---------DMLSDVRQKC------QDETQMISSLKTQIQSQESDLKSQEDDLNRAkselnRLQQEETQLEQSIQAGRVQ 525
Cdd:COG4717 373 aallaeagvEDEEELRAALeqaeeyQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEE 447
|
170 180 190
....*....|....*....|....*....|....
gi 1622897437 526 LETIIKSLKSTQDEINQARS--KLSQLHESRQEA 557
Cdd:COG4717 448 LEELREELAELEAELEQLEEdgELAELLQELEEL 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-563 |
2.18e-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: 51.61 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 402 SLEQDIREKEEAI--------------RQKTSEVQELQNDLdretsslQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVR 467
Cdd:TIGR02169 643 TLEGELFEKSGAMtggsraprggilfsRSEPAELQRLRERL-------EGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 468 QKC---QDETQMI----SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQ-DE 539
Cdd:TIGR02169 716 RKIgeiEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPE 795
|
170 180
....*....|....*....|....
gi 1622897437 540 INQARSKLSQLHESRQEAHRSLEQ 563
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQ 819
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
374-578 |
2.64e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 374 SLGSGEFTGVKELDDISQEIAQLQRekysLEQDIREKEEAIRQKTSEvQELQNDLDR-ETSSLQELEA---QKQDAQDRL 449
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQLEELE-QEIAALLAEaGVEDEEELRAaleQAEEYQELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 450 DEMDQQKAKLRDMLSDVRQKCQDETQmiSSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQS--IQAGRVQLE 527
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELE 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 528 TIIKSLKSTQDEINQARSKLSQLHESRQEAHRslEQYDQVLDGA--HGASLTD 578
Cdd:COG4717 480 ELKAELRELAEEWAALKLALELLEEAREEYRE--ERLPPVLERAseYFSRLTD 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-563 |
2.79e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKT--SEVQELQNDLdrETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 MLSDVRQKCQDETQMISsLKTQIQSQESDLK-----------SQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETII 530
Cdd:PRK03918 544 LKKELEKLEELKKKLAE-LEKKLDELEEELAellkeleelgfESVEELEERLKELEPFYNEYLELKDAEK----ELEREE 618
|
170 180 190
....*....|....*....|....*....|...
gi 1622897437 531 KSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
384-549 |
2.92e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQR----------EKYSLEQdireKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMD 453
Cdd:PRK11281 94 AKLRQAQAELEALKDdndeetretlSTLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 454 QQKAKLRDMLSDVRqkcQDETQMISSLKTQIQSqESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQ-LETIIKS 532
Cdd:PRK11281 170 QRLQQIRNLLKGGK---VGGKALRPSQRVLLQA-EQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQrLEHQLQL 245
|
170
....*....|....*..
gi 1622897437 533 LkstQDEINQARSKLSQ 549
Cdd:PRK11281 246 L---QEAINSKRLTLSE 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
427-591 |
2.96e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 427 DLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL-NRAKSE- 504
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 505 ---------------------------LNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEA 557
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....
gi 1622897437 558 HRSLEQYDQVLDGAHGASLTDLADLSEGVSLAER 591
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
383-545 |
3.12e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLdemdQQKAKLRD 461
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYdELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI----EQFQKVIK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 MLSD------VRQKCQDETQMISSLKT---QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKS 532
Cdd:PHA02562 280 MYEKggvcptCTQQISEGPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
170
....*....|...
gi 1622897437 533 LKSTQDEINQARS 545
Cdd:PHA02562 360 AKKVKAAIEELQA 372
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
386-572 |
3.16e-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: 50.99 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLE---QDIREKEEAIRQKTSEvqelqnDLDRETSSLQELEAQKQDAQDRL-----DEMDQQKA 457
Cdd:pfam12128 349 LPSWQSELENLEERLKALTgkhQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQlavaeDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 458 KLRDMLSDVRQKCQDEtqmisslKTQIQSQESDLKSQEDDLNrAKSELnRLQQEETQLEqsIQAGRVQLETIIKSLKSTQ 537
Cdd:pfam12128 423 ELREQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQAT-ATPEL-LLQLENFDER--IERAREEQEAANAEVERLQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1622897437 538 DEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAH 572
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
387-556 |
3.46e-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: 50.51 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQR-------EKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL----DEMDQQ 455
Cdd:pfam05557 279 EDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQK--CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETiiKSL 533
Cdd:pfam05557 359 RAILESYDKELTMSnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL--ADP 436
|
170 180
....*....|....*....|...
gi 1622897437 534 KSTQDEINQARSKLSQLHESRQE 556
Cdd:pfam05557 437 SYSKEEVDSLRRKLETLELERQR 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
437-567 |
4.56e-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: 50.45 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 437 ELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 516
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 517 QSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLhesrqEAHRSLEQYDQV 567
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDL-----EARLSHSRIPEI 796
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
387-569 |
5.07e-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: 50.17 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-KQDAQDRlDEMDQQKAK-----LR 460
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQfERDLQAR-DEQGEEKRRqlvkqVR 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQEDDLNRAKSE----LNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAA-KKKLELDLKELEAQIDAANKGREEavkqLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
170 180 190
....*....|....*....|....*....|...
gi 1622897437 537 QDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 569
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
384-571 |
5.18e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETsslqELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----EAEDMLACEQHALLRKLQPEQDLQDVR 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQmissLKTQIQSQESDLKSQEDdlnRAKSELNRLQQEetQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:TIGR00618 632 LHLQQCSQELAL----KLTALHALQLTLTQERV---REHALSIRVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
170 180
....*....|....*....|....*...
gi 1622897437 544 RSKLSQLHESRQEAHRSLEQYDQVLDGA 571
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
377-569 |
5.22e-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: 50.21 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 377 SGEFTGVKELDDISQ-EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE---AQKQDAQDRL-DE 451
Cdd:pfam10174 379 AGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKERIIERLkEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 452 MDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQES---DLKSQEDDLN-RAKSELNRLQQEETQLEQSIQAGrVQLE 527
Cdd:pfam10174 459 REREDRERLEELESLKKENKDLKEKVSALQPELTEKESsliDLKEHASSLAsSGLKKDSKLKSLEIAVEQKKEEC-SKLE 537
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 528 TiikSLKSTQDEINQAR------SKLSQLHES----RQEAHRSLEQYDQVLD 569
Cdd:pfam10174 538 N---QLKKAHNAEEAVRtnpeinDRIRLLEQEvaryKEESGKAQAEVERLLG 586
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
386-502 |
5.47e-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: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREkysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSD 465
Cdd:COG4942 141 LKYLAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622897437 466 VRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK 502
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
383-511 |
5.71e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREkeeaIRQKTSEVQEL-QNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQ----LKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622897437 462 MLSDVRQKCQDetqmissLKTQIQSQESDLKS----QEDDLNRAKSELNRLQQE 511
Cdd:smart00787 240 KIEDLTNKKSE-------LNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-568 |
6.57e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQ-----------------NDLDRETSSLQE--------- 437
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikdlndklkknkdkiNKLNSDLSKINSeikndkeqk 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 438 --LEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:TIGR04523 120 nkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 516 EQSIqagrVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 568
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 ... |
386-569 |
6.71e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDIREKEeairqktSEVQELQNDL--------DRET------SSLQELEA-------QKQD 444
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALE-------SENAELQAELrtlqqakqDSEHkrkkleGQLQELQArlseserQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 445 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLksQEDdlNRAK----SELNRLQQEET----QLE 516
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL--QEE--TRQKlnlsTRLRQLEDERNslqeQLE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 517 QSIQAGRV---QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 569
Cdd:pfam01576 507 EEEEAKRNverQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
385-572 |
7.59e-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: 49.66 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYS---------LEQDIREKEEAIRQKTSEVQELQ-----------------NDLDRETSSLQEL 438
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGsdldrtvqqVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktNELKSEKLQIGTN 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 439 EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQ----IQSQESDLKSQEDDLNRAKSELNRLQQEETQ 514
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 515 LEQSIQAGRVqletiiKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAH 572
Cdd:TIGR00606 960 IENKIQDGKD------DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
384-557 |
8.37e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYS---LEQDIREKEEaiRQKTSEV-QELQNDLDRETSSL-QELEAQKQ--DAQDRLDEMDQQK 456
Cdd:COG1340 92 EELDELRKELAELNKAGGSidkLRKEIERLEW--RQQTEVLsPEEEKELVEKIKELeKELEKAKKalEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQSqesdLKSQEDDLNRaksELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRK---EADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
170 180
....*....|....*....|.
gi 1622897437 537 QDEINQARSKLSQLHESRQEA 557
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKE 263
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
403-555 |
9.80e-06 |
|
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: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQ 475
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLerslkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 476 MISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQagrvQLETIIKSL----KSTQDEINQARSKLSQL 550
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTEsLKQRKR----ELESEIKKLthdiKLKEEQIRELEIKVQEL 555
|
....*
gi 1622897437 551 HESRQ 555
Cdd:pfam09726 556 RKYKE 560
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
445-534 |
1.17e-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: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 445 AQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRV 524
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|
gi 1622897437 525 QLETIIKSLK 534
Cdd:COG4942 98 ELEAQKEELA 107
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
385-563 |
1.22e-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: 48.96 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQ-ELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGR---------VQ-LETIIKSL 533
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRrelddrnmeVQrLEALLKAM 438
|
170 180 190
....*....|....*....|....*....|
gi 1622897437 534 KStqdeinQARSKLSQLHESRQEAHRSLEQ 563
Cdd:pfam15921 439 KS------ECQGQMERQMAAIQGKNESLEK 462
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
450-566 |
1.24e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 450 DEMDQQKAKLRDMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 529
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622897437 530 IKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQ 566
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
393-563 |
1.30e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 393 IAQLQREKYSLEQDiREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-----QDAQD--------------RLDEMD 453
Cdd:PRK04863 920 LAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEmlaknsdlneklrqRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 454 QQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLN----RAKSEL-NRLQQEETQLEQSIQAGRVQLET 528
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAeERARARRDELHARLSANRSRRNQ 1078
|
170 180 190
....*....|....*....|....*....|....*
gi 1622897437 529 IIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
291-364 |
1.34e-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: 1.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 291 DGYVSGQEVKEIFMHSGLTQNLLAHIWALADTRQTGKLSKDQFALAMYFIQQKVSKGI-DPPQVLSPDMVPPSER 364
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
385-559 |
1.37e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.15 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIA-------QLQREKYSLEQDIREKEEAIRQKTSEVQELQN-------DLDRETSSLQELEAQkQDAQDR-- 448
Cdd:PRK11637 48 QLKSIQQDIAakeksvrQQQQQRASLLAQLKKQEEAISQASRKLRETQNtlnqlnkQIDELNASIAKLEQQ-QAAQERll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 449 ---LD-----------------EMDQQKAKLR---DMLSDVRQKCqdetqmISSLK---TQIQSQEsdlKSQEDDLNRAK 502
Cdd:PRK11637 127 aaqLDaafrqgehtglqlilsgEESQRGERILayfGYLNQARQET------IAELKqtrEELAAQK---AELEEKQSQQK 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 503 SELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHR 559
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAER 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-562 |
1.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQdaqdRLDEMDQQKAKLRDML 463
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS---------ELNRLQQEETQLEQSIQAGRVQLETIIKSLK 534
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180
....*....|....*....|....*...
gi 1622897437 535 STQDEINQARSKLSQLHESRQEAHRSLE 562
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLE 355
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-579 |
1.41e-05 |
|
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: 48.80 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQ-------LQREKYSLEQDIREK---------EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQ----- 443
Cdd:COG3096 793 ERDELAEQYAKasfdvqkLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDqlkeq 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 444 -----------------DAQDRLDEMDQQKAKLRDMLSDVRQKCqdetQMISSLKTQIQSQESDLKSQED---DLNRAKS 503
Cdd:COG3096 873 lqllnkllpqanlladeTLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLVAVLQSDPEQFEQlqaDYLQAKE 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 504 ELNRLQQEETQLEQSIQ-------AGRVQLetiiksLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHgASL 576
Cdd:COG3096 949 QQRRLKQQIFALSEVVQrrphfsyEDAVGL------LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYN-QVL 1021
|
...
gi 1622897437 577 TDL 579
Cdd:COG3096 1022 ASL 1024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-584 |
1.47e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 440 AQKQDAQDRLDEMDQQKAKLRDMLSDVR-------------------QKCQDETQMISSLKtQIQSQESDLKSQEDDLNR 500
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGELErqleplerqaekaeryrelKEELKELEAELLLL-KLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 501 AKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQL-------HESRQEAHRSLEQYDQVLDGAHG 573
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEE 330
|
170
....*....|.
gi 1622897437 574 ASLTDLADLSE 584
Cdd:COG1196 331 ELEELEEELEE 341
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
32-80 |
1.66e-05 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 44.29 E-value: 1.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622897437 32 GRVGASEAALFLKKSGLSDIILGKIWDLADPEGKGFLDKQGFYVALRLV 80
Cdd:pfam12763 24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-574 |
2.03e-05 |
|
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: 48.30 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQRE-KYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL-QELEAQKQDAQDRLDEMDQQ----- 455
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWykrdl 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 -------------KAKLRDM---LSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELnrlQQEETQLEQSI 519
Cdd:pfam12128 761 aslgvdpdviaklKREIRTLerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL---QQQLARLIADT 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 520 QAGRVQLETIIKSLKSTQDEINQA-------RSKLSQLHE---------SRQEAHRSLEQYDQVLDGAHGA 574
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENlrglrceMSKLATLKEdanseqaqgSIGERLAQLEDLKLKRDYLSES 908
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
482-552 |
2.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 482 TQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHE 552
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
386-539 |
2.20e-05 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 45.76 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLeqdiREKEEAIRQKTsevQELQNDLDRETSSLQELEAQKQDaQDRLDEMDQQKAKLRDMLSD 465
Cdd:pfam16043 9 LDQLQALILDLQEELEKL----SETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 466 VRQKCQDET-----QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEqsiqagrvQLETIIKSLKSTQDE 539
Cdd:pfam16043 81 VSRDQFDETleelnQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKE--------LLERRIKALQKLLQE 151
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
416-571 |
2.35e-05 |
|
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: 46.53 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 416 QKTSEVQELQNDLdretSSLQELEAQKQDAQD----------RLDEMDQQKAKLRDMLSDVRQKcQDETQMISSLKTQIQ 485
Cdd:pfam12795 14 AKKKLLQDLQQAL----SLLDKIDASKQRAAAyqkalddapaELRELRQELAALQAKAEAAPKE-ILASLSLEELEQRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 486 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRS-LEQY 564
Cdd:pfam12795 89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAqIDML 168
|
....*..
gi 1622897437 565 DQVLDGA 571
Cdd:pfam12795 169 EQELLSN 175
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
402-563 |
2.43e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.22 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 402 SLEQDIREKEeairqktSEVQELQNDLDRETSSLQEL-EAQKQDAQDRLDEMDQQKAKL-------RDMLSDVRQKCQDE 473
Cdd:pfam00038 22 FLEQQNKLLE-------TKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLqleldnlRLAAEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 474 TQMISSLKTQIQsqesDLKSQEDDLNRAKSEL-NRLQ--QEE------------TQLEQSIQAGRVQLE----------T 528
Cdd:pfam00038 95 LNLRTSAENDLV----GLRKDLDEATLARVDLeAKIEslKEElaflkknheeevRELQAQVSDTQVNVEmdaarkldltS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897437 529 IIKSLKSTQDEINQaRSKL-------SQLHESRQEAHRSLEQ 563
Cdd:pfam00038 171 ALAEIRAQYEEIAA-KNREeaeewyqSKLEELQQAAARNGDA 211
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
392-550 |
2.47e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYslEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK--QDAQDRLDEMDQQKAKL---------- 459
Cdd:COG5022 827 KREKKLRETE--EVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQrvELAERQLQELKIDVKSIsslklvnlel 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 --------RDMLSDVRQKCQDETQMISSLKTQIQsqESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIK 531
Cdd:COG5022 905 eseiielkKSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHEVESKLKETSE----EYEDLLK 978
|
170
....*....|....*....
gi 1622897437 532 SLKSTQDEINQARSKLSQL 550
Cdd:COG5022 979 KSTILVREGNKANSELKNF 997
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
435-553 |
2.62e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 435 LQELEAQKQDAQDRLDEMDQ----QKAKLRDMLSDVRQKCQdETQMISSLKTQIQSQESdlKSQEDDLNRAKSELNRLQQ 510
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElhekQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES--QSQEDLRNQLQNTVHELEA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622897437 511 EETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHES 553
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEA 199
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-569 |
3.01e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQ---DETQMISSLKTQIQSQESDLKSQEDDLNRAkselnrlqqeetqLEQSIQAGRVQLETIIKSLKSTQDEI 540
Cdd:TIGR04523 641 NKLKQEVKqikETIKEIRNKWPEIIKKIKESKTKIDDIIEL-------------MKDWLKELSLHYKKYITRMIRIKDLP 707
|
170 180
....*....|....*....|....*....
gi 1622897437 541 nqarsKLSQLHESRQEAHRSLEQYDQVLD 569
Cdd:TIGR04523 708 -----KLEEKYKEIEKELKKLDEFSKELE 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
474-568 |
3.01e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 474 TQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgrvqletIIKSLKSTQDEINQARSKLSQLHES 553
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKE 91
|
90
....*....|....*
gi 1622897437 554 RQEAHRSLEQYDQVL 568
Cdd:COG4942 92 IAELRAELEAQKEEL 106
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
397-517 |
3.06e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 44.14 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 397 QREKYSLEQDIREKEEAIRQKtsevqelQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQM 476
Cdd:pfam20492 5 EREKQELEERLKQYEEETKKA-------QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622897437 477 ISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE--ETQLEQ 517
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEleEAREEE 120
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
383-511 |
3.23e-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: 46.73 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLqrEKYSLeqDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLrdm 462
Cdd:pfam15905 225 LEYITELSCVSEQV--EKYKL--DIAQLEELLKEKNDEIESLKQSLEEKE---QELSKQIKDLNEKCKLLESEKEEL--- 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622897437 463 lsdvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQE 511
Cdd:pfam15905 295 --------------LREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
391-568 |
3.27e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQRekySLEQDIREKEEAI---RQK-TSEVQELQNDLD---RETSSL----QELEAQKQDAQDRL-------DEM 452
Cdd:pfam01576 327 QEVTELKK---ALEEETRSHEAQLqemRQKhTQALEELTEQLEqakRNKANLekakQALESENAELQAELrtlqqakQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 453 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQL--ETII 530
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQ 483
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622897437 531 K-----SLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVL 568
Cdd:pfam01576 484 KlnlstRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
384-575 |
3.54e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQ-------------------KC----------------QDETQMISSLKTQIQSQESDLKSQEDDLNRAKSelnrL 508
Cdd:PRK02224 429 AELEAtlrtarerveeaealleagKCpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED----L 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 509 QQEETQLEQSiqagRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHGAS 575
Cdd:PRK02224 505 VEAEDRIERL----EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
395-555 |
3.89e-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: 47.43 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 395 QLQREKYSLEQdIREKEEAIRQKtsEVQELQNDLDRETSS--LQELEAQKQDAQDRLDEMDQQKAKLrDMLSDVRQKCQD 472
Cdd:pfam17380 414 KIQQQKVEMEQ-IRAEQEEARQR--EVRRLEEERAREMERvrLEEQERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 473 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ---EETQLEQSIQAGRVQLEtiIKSLKSTQDEINQA---RSK 546
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKaiyEEERRREAEEERRKQQE--MEERRRIQEQMRKAteeRSR 567
|
....*....
gi 1622897437 547 LSQLHESRQ 555
Cdd:pfam17380 568 LEAMERERE 576
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
384-564 |
3.91e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEvQELQndldretssLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQ---------MEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ----QEETQLEQsiqagRVQLETIIKSLKSTQDE 539
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaEDEKLLDE-----KKQFEKIAEELKGKEQE 440
|
170 180
....*....|....*....|....*...
gi 1622897437 540 IN---QARSKLSQLHESRQEAHRSLEQY 564
Cdd:pfam05483 441 LIfllQAREKEIHDLEIQLTAIKTSEEH 468
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-568 |
4.45e-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: 47.27 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLS 464
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ-LALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 DV---RQKCQDETQMISSLKTQIQSQESDLK----------------SQEDDLNRAKSELNRLQ--QEETQLEQSIQAGR 523
Cdd:TIGR00618 712 HIeeyDREFNEIENASSSLGSDLAAREDALNqslkelmhqartvlkaRTEAHFNNNEEVTAALQtgAELSHLAAEIQFFN 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897437 524 VQLETIIKSLKSTQDEINQARSKLSQLHESRQE-AHRSLEQYDQVL 568
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRL 837
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
384-486 |
4.72e-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: 43.33 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKtseVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQREEELEKK---EQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|...
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQS 486
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLEE 105
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
386-552 |
4.78e-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: 47.04 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQR-----------EKYSLEQDI-------------REKEEAIRQKTSEVQE-LQNDLDretSSLQELEA 440
Cdd:pfam15921 80 LEEYSHQVKDLQRrlnesnelhekQKFYLRQSVidlqtklqemqmeRDAMADIRRRESQSQEdLRNQLQ---NTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 441 QKQDAQDRLDEMDQQKAKLRDM-------LSDVR-----------QKCQDETQM-----------ISSLKTQIQSQESDL 491
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMmlshegvLQEIRsilvdfeeasgKKIYEHDSMstmhfrslgsaISKILRELDTEISYL 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 492 KSQ----EDDLNRAKSELNR-----LQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHE 552
Cdd:pfam15921 237 KGRifpvEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
424-569 |
5.20e-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: 45.30 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 424 LQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKTQIQSQESDLKSQEDDLNRAKS 503
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRAL-------KAELESLEVYNRQLERLVASQEQEIASLER 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 504 ELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARskLSQLHESRQEAHRSL-EQYDQVLD 569
Cdd:pfam11932 84 QIEEIERTERELVPLMLKMLDRLEQFVALDLPFLLEERQAR--LARLRELMDDADVSLaEKYRRILE 148
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
404-528 |
7.06e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.00 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 404 EQDIREKEEAIRQKTSEVQELQN-----DLDRETSSLQ----ELEAQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDET 474
Cdd:COG3524 183 EEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELEAELAA-------LRSYLSPNSPQVRQLR 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 475 QMISSLKTQIQSQESDL--KSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLET 528
Cdd:COG3524 256 RRIAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
388-515 |
7.70e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 388 DISQEIAQLQREKYSLE---------QDIREKEEAIRQKTSEVQELQndldretSSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQ-------HSLEKLDTAIDELEEIMDEFNEQSKK 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 459 LRDMLSDVRQKCQDetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:PHA02562 339 LLELKNKISTNKQS----LITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
432-565 |
7.91e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.49 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 432 TSSLQELEAQKQDAQ---DRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK------ 502
Cdd:pfam00529 57 QAALDSAEAQLAKAQaqvARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapig 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 503 --------SELNRLQQEETQLEQSI-QAGRVQLE---TIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYD 565
Cdd:pfam00529 137 gisreslvTAGALVAQAQANLLATVaQLDQIYVQitqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
372-511 |
8.11e-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: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 372 SGSLGSGEFTGVKELDDISQEIAQLQREKYSLEQDIREK---EEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDR 448
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 449 LDEMdqqKAKLRDMLSDVRQKCQDETQMISSLKTQIQsQESDLKSQEDDLNRAKselNRLQQE 511
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLEALEEGKKRLQRELEALTQ-QLEEKAAAYDKLEKTK---NRLQQE 581
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
385-578 |
8.48e-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: 45.71 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSL---QELE--------AQKQDAQD---RLD 450
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAewkLELErvlpqlkvTIKADAKDwraHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 451 EMDQQKAKLRDMLSDVRQKcqdetqmisslktqiqsqesdLKSQEDDLNRAkseLNRLQQEETQLEQsiqagrvQLETII 530
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 531 KSLKSTQDEINQARSKLSQLHESRQEAHRSL----EQYDQV---LDgAHGASLTD 578
Cdd:pfam10498 275 QEYREAQDELSEVQEKYKQLSEGVTERTRELaeitEELEKVkqeME-ERGSSMTD 328
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
418-566 |
9.82e-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: 45.01 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 418 TSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQmisslktqiqSQESDLKSQEDD 497
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD----------RAKEKLKKLLQE 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 498 LNRAKSELNRLQQEETQLEQSIQAGRVQLETIikslkstQDEINQARSKLSQLHE-SRQEAHRSLEQYDQ 566
Cdd:smart00787 220 IMIKVKKLEELEEELQELESKIEDLTNKKSEL-------NTEIAEAEKKLEQCRGfTFKEIEKLKEQLKL 282
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-562 |
9.92e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIrQKTSEVQELQNDLDRetsslqeLEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIER-------LEERREDLEELIAERRETIEEKRER 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRvQLETIIKSLKSTQDEINQ 542
Cdd:PRK02224 539 AEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
170 180 190
....*....|....*....|....*....|
gi 1622897437 543 ARSKLSQLHE----------SRQEAHRSLE 562
Cdd:PRK02224 611 LREKREALAElnderrerlaEKRERKRELE 640
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
389-561 |
1.03e-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: 45.46 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 389 ISQEIAQLQREKYSLEQDIREKEEAIRQktsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKakLRDMLSD--- 465
Cdd:pfam04108 40 LSVQLANLEKVREGLEKVLNELKKDFKQ---LLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT--LLDFIDEdsv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 466 --VRQKCQdetQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQ-------------QEETQLEQSI----------- 519
Cdd:pfam04108 115 eiLRDALK---ELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSspsesisliptllKELESLEEEMasllesltnhy 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 520 ----QAGRV-----------------QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSL 561
Cdd:pfam04108 192 dqcvTAVKLteggraemlevlendarELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
390-557 |
1.07e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 390 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV-RQ 468
Cdd:pfam06008 39 KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALpSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 469 KCQDETQMISSLKTQIQSQesDLKSQ----EDDLNRAKSELNRLQqeetQLEQSIQAgrvQLETIiksLKSTQDEINQAR 544
Cdd:pfam06008 119 DLSRMLAEAQRMLGEIRSR--DFGTQlqnaEAELKAAQDLLSRIQ----TWFQSPQE---ENKAL---ANALRDSLAEYE 186
|
170
....*....|...
gi 1622897437 545 SKLSQLHESRQEA 557
Cdd:pfam06008 187 AKLSDLRELLREA 199
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-559 |
1.10e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDI-------------REKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM 452
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 453 DQQKAKLRDMLSDVRQ----------KCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ---SI 519
Cdd:PRK04863 389 EEEVDELKSQLADYQQaldvqqtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklsVA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897437 520 QAGRVQLETIIKSLKSTQDEI------NQARSKLSQLHESRQEAHR 559
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAEQ 514
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
433-552 |
1.10e-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: 42.63 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 433 SSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISslkTQIQSQESDLKSqeddLNRAKSELNRLQQEE 512
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKA----LQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622897437 513 TQLEQSIQAGRVQLETIIKSLKST----QDEINQARSKLSQLHE 552
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQkkelEKELSELEKRIEDLNE 117
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
414-566 |
1.10e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 414 IRQKTSEVQelqnDLDRETSSLQELEAQKQDAQDRLDEM-DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLK 492
Cdd:PHA02562 176 IRELNQQIQ----TLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 493 SQEDDLN-------RAKSELNRLQQEETQLEQsiqaGRV------QLETIIKSLKSTQDEINQARSKLSQLHESRQEAHR 559
Cdd:PHA02562 252 DPSAALNklntaaaKIKSKIEQFQKVIKMYEK----GGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
....*..
gi 1622897437 560 SLEQYDQ 566
Cdd:PHA02562 328 IMDEFNE 334
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
384-521 |
1.13e-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: 44.29 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndLDRETSSL-QELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEELaREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQKCQDETQMISSLKTQIQ---SQESDLKSQED--------DLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNllkARLKAAKAQEAvqtslgslSTSSATDSFERIEEKIEEREARADA 182
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
405-552 |
1.23e-04 |
|
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: 43.45 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 405 QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI 484
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 485 QSQESDLKSQE-DDLNRakselnRLQQEETQLEQSIQAGRvqLETIIKSLKSTQDEINQARSKLSQLHE 552
Cdd:cd16853 91 EYVQKNLTDEElADWKR------RQQIACIGGPPNICLDR--LENWITSLAESQLQTRQQIKKLEELQQ 151
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
391-580 |
1.29e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQD---IREKEEAIRQKTSEVQELQNDLDRE-TSSLQELEAQKQDA------QDRLDEMDQQKAKLR 460
Cdd:TIGR00618 462 QESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDETQMISSLKTQIQsqesdlksqeddlnrakselnRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEI 540
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQ---------------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897437 541 NQarsklsqlhESRQEAHRSLEQYDQVLDGAHGASLTDLA 580
Cdd:TIGR00618 601 EK---------LSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
400-557 |
1.31e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 400 KYSLEQDIREKEEAIRQKtseVQELQNDLDrETSSLQELEAQkqdaqdrlDEMDQQKaklRDMLSDVRQKcqdetqmiss 479
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLR---NEFEKELRER---------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 480 lKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLheSRQEA 557
Cdd:PRK12704 81 -RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEA 155
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
384-504 |
1.32e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQL-------QREKYSLEQDIREKEEAIRQKTSEVQELQNDLD-----------RETSSLQELEAQKQ-- 443
Cdd:PRK09039 53 SALDRLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAelagagaaaegRAGELAQELDSEKQvs 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 444 -DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDL------KSQEddLNRAKSE 504
Cdd:PRK09039 133 aRALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqRVQE--LNRYRSE 198
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
397-581 |
1.45e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 397 QREKYSLEQDIREKEEAIRQktsevQELQNdldreTSSLQEL-EAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDET- 474
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQR-----KSLEG-----NTQLQDLlQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTv 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 475 -QMISSLKTQiQSQESDLKSQEDDLN----------------------RAKSELNRLQQEETQLEQSIQA--GRVQLETI 529
Cdd:PRK11281 263 qEAQSQDEAA-RIQANPLVAQELEINlqlsqrllkateklntltqqnlRVKNWLDRLTQSERNIKEQISVlkGSLLLSRI 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897437 530 I-------KSLKSTQD-------------EINQARSKLSQLhesrqEAH-RSLEQYDQV-LDGAHGASLTDLAD 581
Cdd:PRK11281 342 LyqqqqalPSADLIEGladriadlrleqfEINQQRDALFQP-----DAYiDKLEAGHKSeVTDEVRDALLQLLD 410
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
383-538 |
1.48e-04 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 44.99 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVqELQNDLDRETSSLQELEAQK---QDAQDRLDEMDQQ---- 455
Cdd:pfam03999 142 LEELESFRKHLENLRNEKERRLEEVNELKKQIKLLMEEL-DLVPGTDFEEDLLCESEDNFclsRENIDKLRKLIKQleeq 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQKCQdetQMISSLKTQIQSQESDLK----SQEDDLNRAKSELNRLQQEETQLEQS-IQAGRVQLETII 530
Cdd:pfam03999 221 KAEREEKIDDLREKIL---ELWNRLQVPQEEQESFVRennsLSQDTIDALREELQRLEELKKKNIKKlIEDLRVEIEELW 297
|
....*....
gi 1622897437 531 -KSLKSTQD 538
Cdd:pfam03999 298 dKLFYSTEQ 306
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
421-566 |
1.50e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 43.96 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 421 VQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdETQMISSL---KTQ----IQSQESDLKS 493
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKH----ENDNLSSMlnrKERrlkdLEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 494 QEDDLNRAKSEL----NRLQQEETQLEQSIQAGRVQLETIIKSLK----STQDEINQARSKLSQLhesRQEAHRSLEQYD 565
Cdd:pfam17078 81 SYEELTESNKQLkkrlENSSASETTLEAELERLQIQYDALVDSQNeykdHYQQEINTLQESLEDL---KLENEKQLENYQ 157
|
.
gi 1622897437 566 Q 566
Cdd:pfam17078 158 Q 158
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
403-573 |
1.59e-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: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIRQKTSEVQELqnDLDRetsSLQELEAQKQDAQDRLDEMDQQKAKLRDMLsdvrqkcQDETQMISSLKT 482
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGS--DLDR---TVQQVNQEKQEKQHELDTVVSKIELNRKLI-------QDQQEQIQHLKS 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 483 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLE 562
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
170
....*....|.
gi 1622897437 563 QYDQVLDGAHG 573
Cdd:TIGR00606 945 DIKEKVKNIHG 955
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
419-614 |
1.69e-04 |
|
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: 44.28 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 419 SEVQELQNDLDRETSSlQELEAQKQDAQDRLDEMdQQKAKlrdmlsDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL 498
Cdd:cd22656 94 AEILELIDDLADATDD-EELEEAKKTIKALLDDL-LKEAK------KYQDKAAKVVDKLTDFENQTEKDQTALETLEKAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 499 NrakselNRLQQEETQLEQSiqagrvQLETIIKSLKSTQDEI-NQARSKLSQLHESRQEAHRSLeQYDQVLDGAHGASLT 577
Cdd:cd22656 166 K------DLLTDEGGAIARK------EIKDLQKELEKLNEEYaAKLKAKIDELKALIADDEAKL-AAALRLIADLTAADT 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622897437 578 DLADLSEGVSLAE------RGGFGAMDDPFKNKALLFSNNTQE 614
Cdd:cd22656 233 DLDNLLALIGPAIpaleklQGAWQAIATDLDSLKDLLEDDISK 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
453-533 |
1.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 453 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKS 532
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 1622897437 533 L 533
Cdd:COG3883 95 L 95
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
365-525 |
1.81e-04 |
|
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: 45.07 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 365 GTPGPDSSGSLGsgeftgvKEL--DDISQEIAQLQREKYSLeqdiREK-EEAIRQKTSEVQELqndLDRETSSLQELEAQ 441
Cdd:pfam05622 261 LSPSSDPGDNLA-------AEImpAEIREKLIRLQHENKML----RLGqEGSYRERLTELQQL---LEDANRRKNELETQ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 442 KQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDEtqmiSSLKtqiqsqeSDLKSQEDDLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:pfam05622 327 NRLANQRILELQQQVEELQKALQEQGSKAEDS----SLLK-------QKLEEHLEKLHEAQSELQKKKEQIEELEPKQDS 395
|
....
gi 1622897437 522 GRVQ 525
Cdd:pfam05622 396 NLAQ 399
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
403-550 |
1.94e-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: 43.56 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdmLSDVRQKCQDETQMISSLKT 482
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 483 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLET--IIKSLKSTQDEINQARSKLSQL 550
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAafLQADLKAAKADWNQLYEQAKSL 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
387-591 |
2.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR-----D 461
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARrdelhA 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 MLSDVRQKCqdetqmiSSLKTQIQSQESDLKSQEddlNRAKSELNRLQQEETQLEQSiqagRVQLETIIKSLKSTQDEIN 541
Cdd:PRK04863 1068 RLSANRSRR-------NQLEKQLTFCEAEMDNLT---KKLRKLERDYHEMREQVVNA----KAGWCAVLRLVKDNGVERR 1133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 542 QARSKLSQLheSRQEAhRSLEQYDQ------VLDGAHgasLTDLADLSEGVSLAER 591
Cdd:PRK04863 1134 LHRRELAYL--SADEL-RSMSDKALgalrlaVADNEH---LRDVLRLSEDPKRPER 1183
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-553 |
2.13e-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: 45.04 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQktsevQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ---QKAKLR 460
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGR-----LQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIQAGRvQLETIIKS 532
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielkkeiLEKKQEELKFVIKELQ-QLEGSSDR 472
|
170 180
....*....|....*....|.
gi 1622897437 533 LKSTQDEINQARSKLSQLHES 553
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKN 493
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
384-557 |
2.18e-04 |
|
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: 43.20 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNdlDRETSSLQELEAQK--QDAQDRLDEMDQQKAKLRD 461
Cdd:cd00176 54 ERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAE--ERRQRLEEALDLQQffRDADDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 MLsdvrqkcqdetqmISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRvqletiIKSLKSTQDEIN 541
Cdd:cd00176 132 ED-------------LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDA------DEEIEEKLEELN 192
|
170
....*....|....*.
gi 1622897437 542 QARSKLSQLHESRQEA 557
Cdd:cd00176 193 ERWEELLELAEERQKK 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
493-563 |
2.23e-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: 44.37 E-value: 2.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 493 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
402-526 |
2.38e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 402 SLEQDIREKEEAIRQK------TSEVQELQNDLDRETSSLQELEAQKQDAQDR-------LDEMDQQKAKLRDMLSDVRQ 468
Cdd:PRK10929 79 KLSAELRQQLNNERDEprsvppNMSTDALEQEILQVSSQLLEKSRQAQQEQDRareisdsLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 469 KCQDETQMISSLK----TQIQSQESDLKSQEDDLNRA------KSELNRLQQE-----ETQLEQSIQAGRVQL 526
Cdd:PRK10929 159 RLQTLGTPNTPLAqaqlTALQAESAALKALVDELELAqlsannRQELARLRSElakkrSQQLDAYLQALRNQL 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-573 |
2.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 381 TGVKELDDISQEIAQLQREKyslEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKA--- 457
Cdd:PRK02224 509 DRIERLEERREDLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 458 -------KLRDMLSDvRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL------NRL---QQEETQLEQSIQA 521
Cdd:PRK02224 586 eriesleRIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELeaefdeARIeeaREDKERAEEYLEQ 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 522 GRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEaHRSLEQYDQVLDGAHG 573
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEELRER-REALENRVEALEALYD 715
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
393-571 |
2.45e-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: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 393 IAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQK-------QDAQDRLDEMDQQKA----KLRD 461
Cdd:pfam01576 189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLakkeeelQAALARLEEETAQKNnalkKIRE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 M---LSDVRQKCQDETQMisslKTQIQSQESDLksqEDDLNRAKSELNRlQQEETQLEQSIQAGRvqlETIIKSLKSTQD 538
Cdd:pfam01576 269 LeaqISELQEDLESERAA----RNKAEKQRRDL---GEELEALKTELED-TLDTTAAQQELRSKR---EQEVTELKKALE 337
|
170 180 190
....*....|....*....|....*....|...
gi 1622897437 539 EinQARSKLSQLHESRQEAHRSLEQYDQVLDGA 571
Cdd:pfam01576 338 E--ETRSHEAQLQEMRQKHTQALEELTEQLEQA 368
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
385-484 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSL--EQDIREKEEAIRQKTsEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDM 462
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkkEQDEASFERLAELRD-ELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|..
gi 1622897437 463 LSDVRQKCQDETQMISSLKTQI 484
Cdd:COG0542 491 EKELAELEEELAELAPLLREEV 512
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
382-477 |
2.50e-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: 41.80 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 382 GVKELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQelEAQKQDAQDRLDEMDQQ-KAKLR 460
Cdd:smart00935 2 GVVDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQ 79
|
90
....*....|....*..
gi 1622897437 461 DMLSDVRQKCQDETQMI 477
Cdd:smart00935 80 KLQQDLQKRQQEELQKI 96
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
394-531 |
2.75e-04 |
|
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: 41.95 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 394 AQLQREKYslEQDIREKEEAIRQKTSEVQELQndldRETSSLQELEAQKQdAQDRLDEMDQQKAKLRDMLSDVRQKCQDE 473
Cdd:pfam05672 23 AREQRERE--EQERLEKEEEERLRKEELRRRA----EEERARREEEARRL-EEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 474 TQMIsslktQIQSQESDLKSQEDD----LNRAKselnRLQQEetqlEQSIQAGRVQLETIIK 531
Cdd:pfam05672 96 QERL-----QKQKEEAEAKAREEAerqrQEREK----IMQQE----EQERLERKKRIEEIMK 144
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
386-552 |
3.07e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ-------KQDAQDRLDEMDQQKAK 458
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlnitlqpQDDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 459 LrDMLSDvRQKCQ----DETQMISSLKTQIQSQESDLKSQ----------EDD----LNRAKSELNRLQQEETQLeQSIQ 520
Cdd:PRK10246 612 L-RLLSQ-RHELQgqiaAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEeaswLATRQQEAQSWQQRQNEL-TALQ 688
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897437 521 AGRVQLETIIKSLKSTQDEINQARS----KLSQLHE 552
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEETvaldNWRQVHE 724
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
387-555 |
3.16e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKySLEQDirekEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV 466
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 467 RQKcQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQqeeTQLEQ---SIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:PRK11281 114 TRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ---TQPERaqaALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170
....*....|..
gi 1622897437 544 RSKLSQLHESRQ 555
Cdd:PRK11281 190 RPSQRVLLQAEQ 201
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
390-571 |
3.17e-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: 44.43 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 390 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDqqkaklrdmlSDVRQK 469
Cdd:pfam10174 543 AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE----------SLTLRQ 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 470 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEEtQLEQSIQA---GRVQLETIIKSLKSTQDEINQARSK 546
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL-QLEELMGAlekTRQELDATKARLSSTQQSLAEKDGH 691
|
170 180
....*....|....*....|....*.
gi 1622897437 547 LSQL-HESRQEAHRSLEQYDQVLDGA 571
Cdd:pfam10174 692 LTNLrAERRKQLEEILEMKQEALLAA 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
390-533 |
3.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 390 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQK 469
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 470 CQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRL------------QQEE------TQ---LEQSIQagrvQLET 528
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEErydflsEQredLEEARE----TLEE 816
|
....*
gi 1622897437 529 IIKSL 533
Cdd:COG1196 817 AIEEI 821
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
381-549 |
3.43e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 381 TGVKELDDISQEIAQLQREKYSLEQ----DIREKEEAIRQKTS-------EVQELQNDLDRETSSLQELEAQKQDAQDR- 448
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETflekDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDGKDDy 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 449 --------------LDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQI--QSQESDLKSQEDDLNRAKSELNRLQ--- 509
Cdd:TIGR00606 972 lkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQvlq 1051
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897437 510 --QEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQ 549
Cdd:TIGR00606 1052 mkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
384-550 |
3.50e-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: 43.65 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslqELEAQKQDAQdRLDEMDQQKAklrdml 463
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-------QVEKYKLDIA-QLEELLKEKN------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 sdvrqkcqdetQMISSLKTQIQSQESDLKSQEDDLNrakselNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:pfam15905 257 -----------DEIESLKQSLEEKEQELSKQIKDLN------EKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE 319
|
....*..
gi 1622897437 544 RSKLSQL 550
Cdd:pfam15905 320 EQEHQKL 326
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
399-520 |
3.61e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 399 EKYSLEQDIREKEEAIRQKTSEVQELQNDldretsslqeleaQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMIS 478
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622897437 479 slktQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQ 520
Cdd:COG0542 472 ----EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
381-657 |
3.67e-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: 44.18 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 381 TGVKELDDISQEIAQLQrEKYSLEQDIREKEEAIrQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLR 460
Cdd:COG5185 286 NLIKQFENTKEKIAEYT-KSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 D------MLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRA-KSELNRLQQEETQLEQSIQAGRVQLETIIKSL 533
Cdd:COG5185 364 EnivgevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 534 KSTQDEINQAR-----SKLSQLHESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSL------AERGGFGAMDDPFK 602
Cdd:COG5185 444 NELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKlrakleRQLEGVRSKLDQVA 523
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 603 NKALLFSNNTQELHPDPFQTEDPFKSdpFKGADPFKGDPFQNDPFAEQQTTSTDP 657
Cdd:COG5185 524 ESLKDFMRARGYAHILALENLIPASE--LIQASNAKTDGQAANLRTAVIDELTQY 576
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-546 |
3.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQ------------REKY-SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRL 449
Cdd:PRK03918 275 IEELEEKVKELKELKekaeeyiklsefYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 450 DEMdQQKAKLrdmlsdvrqkcqdeTQMISSLKTQIQSQESDLKSQE-DDLNRAKSELNRLQQEETQLEQSIQAGRVQLET 528
Cdd:PRK03918 355 EEL-EERHEL--------------YEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
170
....*....|....*...
gi 1622897437 529 IIKSLKSTQDEINQARSK 546
Cdd:PRK03918 420 EIKELKKAIEELKKAKGK 437
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-562 |
3.78e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEI-----------AQLQREKYSLEQDIR------EKEEAIRQK--------TSEVQELQNDLDRETSSLQEL 438
Cdd:pfam01576 71 QELEEILHELesrleeeeersQQLQNEKKKMQQHIQdleeqlDEEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 439 EAQKQDAQDRLDEM------DQQKAKlrdMLSDVRQKcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEE 512
Cdd:pfam01576 151 SKERKLLEERISEFtsnlaeEEEKAK---SLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622897437 513 TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLhesrQEAHRSLE 562
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA----LKKIRELE 270
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
386-542 |
3.79e-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: 43.69 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDIREKEEAIR-----------------------------------QKTSEV-----QELQ 425
Cdd:pfam03148 139 LEQAWEQLRLLRAARHKLEKDLSDKKEALEidekclslnntspnisykpgptrippnsstpeeweKFTQDNieraeKERA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 426 N------DLD--RETSSlQELEAQKQDA----QDRLDEMDQQKAKLRDMLsdvrQKCQDEtqmISSLKTQIQSQESDLKS 493
Cdd:pfam03148 219 AsaqlreLIDsiLEQTA-NDLRAQADAVnfalRKRIEETEDAKNKLEWQL----KKTLQE---IAELEKNIEALEKAIRD 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 494 QEDDL--------NRAK---SEL------NRLQQEETQLEQSIQAGRVQL---ETIIKSLKSTQDEINQ 542
Cdd:pfam03148 291 KEAPLklaqtrleNRTYrpnVELcrdeaqYGLVDEVKELEETIEALKQKLaeaEASLQALERTRLRLEE 359
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
385-529 |
4.11e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLDRETSSLQE-----LEAQKQDAQDRLDEmdqqkAKl 459
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKE-----AK- 583
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 460 rdmlsdvrqkcQDETQMISSLKTQIQSQESDLKSQE-----DDLNRAKSELNRLQQEETQLEQSIQAG-RVQLETI 529
Cdd:PRK00409 584 -----------KEADEIIKELRQLQKGGYASVKAHEliearKRLNKANEKKEKKKKKQKEKQEELKVGdEVKYLSL 648
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
456-589 |
4.15e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.07 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQL--------- 526
Cdd:COG5283 2 QVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrq 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 527 -----ETIIKSLKSTQDEINQARSKLSQLhESRQEAHRSLEQYDQVLDGAHGASLTDLADLSEGVSLA 589
Cdd:COG5283 82 lsaaqRRLRSSLEQTNRQLERQQQRLARL-GARQDRLKAARARLQRLAGAGAAAAAIGAALAASVKPA 148
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
379-553 |
4.22e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 379 EFTGVKELDdiSQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ----KQDAQDRLDEMDQ 454
Cdd:pfam05483 398 KFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQltaiKTSEEHYLKEVED 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 455 QKAKL-RDMLSDVrqKCQDETQMISSLKTQIQSQESD----LKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 529
Cdd:pfam05483 476 LKTELeKEKLKNI--ELTAHCDKLLLENKELTQEASDmtleLKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV 553
|
170 180
....*....|....*....|....
gi 1622897437 530 IKSLKSTQDEInqaRSKLSQLHES 553
Cdd:pfam05483 554 REEFIQKGDEV---KCKLDKSEEN 574
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
380-534 |
4.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 380 FTGVKELDDISQEIAQLQREKYSL---EQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQK 456
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 457 aklrdmlsdVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEqSIQAGRVQLETIIKSLK 534
Cdd:PRK03918 664 ---------LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVK 731
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
394-556 |
4.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 394 AQLQREKYSLEQDIREKEEAirqkTSEVQELQNDLDRETSSLQE--------------LEAQKQDAQDRLDEMDQQKAKL 459
Cdd:pfam01576 412 GQLQELQARLSESERQRAEL----AEKLSKLQSELESVSSLLNEaegkniklskdvssLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 RdmlSDVRQKCQDETQMISSLKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDE 539
Cdd:pfam01576 488 S---TRLRQLEDERNSLQEQLEEEEEAKRN-VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
170
....*....|....*..
gi 1622897437 540 INQARSKLSQLHESRQE 556
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQ 580
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
429-556 |
4.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 429 DRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRL 508
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622897437 509 QQEETQLEQSIQAGRVQLETIIKSLKStqdeINQARSKLSQLhESRQE 556
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERL-EWRQQ 126
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
392-555 |
5.18e-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: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETS-------SLQELEAQKQDAQDRLDEMDQQKAKlrdmls 464
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAqknnalkKIRELEAQISELQEDLESERAARNK------ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 465 dVRQKCQDETQMISSLKTQIQ-SQESDLKSQEDDLNRAK--SELNRLQQEETQL-EQSIQAGRVQLETIIKSLkstQDEI 540
Cdd:pfam01576 290 -AEKQRRDLGEELEALKTELEdTLDTTAAQQELRSKREQevTELKKALEEETRShEAQLQEMRQKHTQALEEL---TEQL 365
|
170
....*....|....*
gi 1622897437 541 NQARSKLSQLHESRQ 555
Cdd:pfam01576 366 EQAKRNKANLEKAKQ 380
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-563 |
5.43e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-----------DLDRETSSLQELEAQKQ--------- 443
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpFSERQIKNFHTLVIERQedeaktaaq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 444 ---DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE---DDLNRAKSELNRLQQEETQLEQ 517
Cdd:TIGR00606 413 lcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEK 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622897437 518 SIQAGRVQLEtiIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:TIGR00606 493 NSLTETLKKE--VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
434-564 |
5.93e-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: 40.85 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 434 SLQELEAQKQ--DAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlktQIQSQESDLKsqedDLNRAKSELNRLQQE 511
Cdd:pfam07321 9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRLYA---EIQGKLVLLK----ELEKVKQQVALLREN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 512 ETQLEQSIQAGRVQLETIIKSLKSTQDEINQAR---SKLSQLHESRQEAHRSLEQY 564
Cdd:pfam07321 82 EADLEKQVAEARQQLEAEREALRQARQALAEARravEKFAELVRLVQAEELRQQER 137
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
387-563 |
6.03e-04 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 42.89 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdretssLQELEAQKQDAQDRldeMDQQKAK-LRDMLSD 465
Cdd:pfam05816 109 DELLKDNAMLDQMYEKNLEYFKELEKYIAAGELKLEELDAEL------LPELEAKAAASGDP---EDAQALRdLRQALFR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 466 VRQKCQD-ETQM-------------------------------ISSLKTQ------IQSQESDLKSQE------DDLNRA 501
Cdd:pfam05816 180 LEQRIHDlELQRavsiqtapqirlvqnnnqeliekiqsaitttIPLWKNQlvvalaLKRQKLALEAQKavndttNELLLK 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 502 KSELNRLQQEETQlEQSiQAGRVQLETIIK---SLKSTQDEINQARsklSQLHESRQEAHRSLEQ 563
Cdd:pfam05816 260 NAEMLKTQSIETA-KEA-ERGIVDIETLKKtnqTLIATIDETLQIQ---EEGREKRREAEAELEQ 319
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
384-521 |
6.46e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQEL----QNDLDRET-SSLQELEAQKQDAQDRLDEMDQQKAK 458
Cdd:COG1842 37 EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAlekgREDLAREAlERKAELEAQAEALEAQLAQLEEQVEK 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 459 LRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQE----DDLNRAKSELNRLQQEETQLEQSIQA 521
Cdd:COG1842 117 LKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEalsgIDSDDATSALERMEEKIEEMEARAEA 183
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-561 |
6.66e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQeLEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-LQADRHQEHIRARDSLIQSLATRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQ-------EDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKST 536
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
170 180
....*....|....*....|....*
gi 1622897437 537 QDEINQARSKLSQLHESRQEAHRSL 561
Cdd:TIGR00606 460 IKELQQLEGSSDRILELDQELRKAE 484
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
410-557 |
7.23e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 410 KEEAIRQKTSEVQELQNDLDRET----SSLQELE---AQKQDAQDRLDE-MDQQKAKLrdmlsdvrqkcqdetqmisslk 481
Cdd:pfam12072 51 KKEALLEAKEEIHKLRAEAERELkerrNELQRQErrlLQKEETLDRKDEsLEKKEESL---------------------- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 482 tqiQSQESDLKSQEDDLNRAKSELNRLQQEETQ-LEQSIQAGRVQLETIIksLKSTQDEINQARSKLsqLHESRQEA 557
Cdd:pfam12072 109 ---EKKEKELEAQQQQLEEKEEELEELIEEQRQeLERISGLTSEEAKEIL--LDEVEEELRHEAAVM--IKEIEEEA 178
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
381-562 |
7.27e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 381 TGVKELDDISQ--EIAQLQRE------KYSLEQDIREK----EEAIRQKTSEVQELQNDLDRETSS-------------- 434
Cdd:pfam01576 699 TQLEELEDELQatEDAKLRLEvnmqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAELEDERKQraqavaakkkleld 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 435 LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQ 514
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 515 LEQSiqagRVQLETIIKSLKS----TQDEINQARSKLSQLHESRQEAHRSLE 562
Cdd:pfam01576 859 AQQE----RDELADEIASGASgksaLQDEKRRLEARIAQLEEELEEEQSNTE 906
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
389-494 |
7.34e-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: 42.66 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 389 ISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDE--MDQQKAKLRD--MLS 464
Cdd:pfam17060 145 INRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHHEHggNNSIKTATKHefIIS 224
|
90 100 110
....*....|....*....|....*....|
gi 1622897437 465 DVRQKCQDETQMISSLKTQIQSQESDLKSQ 494
Cdd:pfam17060 225 ELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
392-556 |
7.87e-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: 41.57 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRetsslQELEAQKQDAQdRLDEMDQQ--------KAKLRDML 463
Cdd:pfam15665 47 EELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE-----RELKAEAEHRQ-RVVELSREveeakrafEEKLESFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKS-ELNRLQQEetqLEQSIQAGRVQLETIIKSLKSTQDEINQ 542
Cdd:pfam15665 121 QLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAQSASSLaEQEKLEEL---HKAELESLRKEVEDLRKEKKKLAEEYEQ 197
|
170
....*....|....
gi 1622897437 543 ARSKLSQLHESRQE 556
Cdd:pfam15665 198 KLSKAQAFYERELE 211
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
479-555 |
8.12e-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: 40.76 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 479 SLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKL-----SQLHES 553
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALqqiktQFAHEV 135
|
..
gi 1622897437 554 RQ 555
Cdd:pfam11559 136 KK 137
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
475-563 |
8.78e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 475 QMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ----SIQAGRVQLETIIKSLKSTQDEINQARSKLSQL 550
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90 100
....*....|....*....|
gi 1622897437 551 -------HESrQEAHRSLEQ 563
Cdd:PRK00409 600 gyasvkaHEL-IEARKRLNK 618
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
401-543 |
8.98e-04 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 40.59 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 401 YSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDA-QDRLDEMDQqkakLRDMLSD--VRQKCQDETQMI 477
Cdd:pfam16789 3 YPLEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVrKHKKAKMQQ----LRDEMDRgtTSDKILQMKRYI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897437 478 SSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS--------TQDEINQA 543
Cdd:pfam16789 79 KVVKERLKQEEKKVQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKeeedqeerEQDEIGSA 152
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
434-563 |
9.11e-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: 41.52 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 434 SLQELEAQK-------------QDAQDRLDEMDQQKAKLRdmlsDVRQKCQDETQMISSLKTQIQS--QESDLKSQEDDL 498
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAA----AYQKALDDAPAELRELRQELAAlqAKAEAAPKEILA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 499 NRAKSEL-NRLQQEETQLeQSIQAGRVQLETiikSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:pfam12795 77 SLSLEELeQRLLQTSAQL-QELQNQLAQLNS---QLIELQTRPERAQQQLSEARQRLQQIRNRLNG 138
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
371-556 |
9.14e-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: 41.52 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 371 SSGSLGSGEFTGVKE-LDDISQEIAQLQREKYSLEQDIR-EKEEAIRQKTSEVQELQNDLDretSSLQELEAQKQDAqdr 448
Cdd:cd07651 46 SRKSLGGSEEGGLKNsLDTLRLETESMAKSHLKFAKQIRqDLEEKLAAFASSYTQKRKKIQ---SHMEKLLKKKQDQ--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 449 ldEMDQQKAklrdmlsdvRQKCQDETQMISSLktqiQSQESDLKSQEDDLNRAKseLNRLQQeetqleqSIQAGRVQLET 528
Cdd:cd07651 120 --EKYLEKA---------REKYEADCSKINSY----TLQSQLTWGKELEKNNAK--LNKAQS-------SINSSRRDYQN 175
|
170 180 190
....*....|....*....|....*....|..
gi 1622897437 529 IIKSLKSTQDEINQ----ARSKLSQLHESRQE 556
Cdd:cd07651 176 AVKALRELNEIWNRewkaALDDFQDLEEERIQ 207
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
384-553 |
9.27e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIR---------EKE-EAIRQKTSEVQELQNDLDRetsSLQELEAQKQ---------- 443
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDrvkqsytlnESElESVRQLEKQLESLEKQYDE---ITERIAEQEIayselqeele 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 444 DAQDRLDEMDQQKAKLRDMLSDVRqkcQDET---QMISSLKTQIQS-----QESDL----KSQEDDLNRAKSELNRLqqe 511
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLR---KDELearEKLERYRNKLHEikrylEKSNLpglpEDYLEMFFEVSDEIEAL--- 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622897437 512 ETQLEQsiqaGRVQLETIIKSLKSTQDEINQARSKLSQLHES 553
Cdd:PRK04778 461 AEELEE----KPINMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
384-563 |
9.94e-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: 41.86 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEV---QEL------------QNDLDRETSSLQELEAQKQDaqdR 448
Cdd:pfam15397 6 TSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLlqqYEKfgtiisileysnKKQLQQAKAELQEWEEKEES---K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 449 LDEMDQQKAKLRDMLsdvrQKCQDE-----TQM----------ISSLKTQIQsqesDLK-SQEDDLNraksELNRLQQEE 512
Cdd:pfam15397 83 LNKLEQQLEQLNAKI----QKTQEElnflsTYKdkeypvkavqIANLVRQLQ----QLKdSQQDELD----ELEEMRRMV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 513 TQ-LEQSIQAGRVQLETII--KSLKSTQD--------------EINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:pfam15397 151 LEsLSRKIQKKKEKILSSLaeKTLSPYQEsllqktrdnqvmlkEIEQFREFIDELEEEIPKLKAEVQQ 218
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
403-511 |
1.04e-03 |
|
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: 41.55 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLkt 482
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL-- 202
|
90 100
....*....|....*....|....*....
gi 1622897437 483 qiqsqESDLKSQEDDLNRAKSELNRLQQE 511
Cdd:pfam00261 203 -----EKEVDRLEDELEAEKEKYKAISEE 226
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
370-542 |
1.12e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.36 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 370 DSSGSLGSGEFTGVKELDDISQE-------IAQLQREKYSLEQDIREKEEAIRQK------TSEVQELQNDLDRETSSLQ 436
Cdd:pfam13166 293 EKVESAISSLLAQLPAVSDLASLlsafeldVEDIESEAEVLNSQLDGLRRALEAKrkdpfkSIELDSVDAKIESINDLVA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 437 ELEAQKQDAQDRLDEMDQQKAKLRDMLsdvrqkcqdETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 516
Cdd:pfam13166 373 SINELIAKHNEITDNFEEEKNKAKKKL---------RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLR 443
|
170 180
....*....|....*....|....*.
gi 1622897437 517 QSIQagrvQLETIIKSLKSTQDEINQ 542
Cdd:pfam13166 444 EEIK----ELEAQLRDHKPGADEINK 465
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
384-566 |
1.17e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 41.75 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQ-LQR------EKYSLEQDIREKEEAIRQKTSEVQELQNdldretsslqeleAQKQDAQDRLDEMDQQK 456
Cdd:COG5325 77 DEIDELSKKVNQdLQRcekilkTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQVLQAK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 aKLRDMLSDVR--QKCQDETQMISSLKTQIQSQESDLKSQEDDlnrAKSELNRLQQEETQLEQSIQagrvQLETIIKSLK 534
Cdd:COG5325 144 -FLRNKNNDQHplEEEEDEESLSSLGSQQTLQQQGLSNEELEY---QQILITERDEEIKNLARGIY----ELNEIFRDLG 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622897437 535 STQDE----INQARSKLSQLHESRQEAHRSLEQYDQ 566
Cdd:COG5325 216 SLVGEqgelVDRIDFNIENTSDNLKNANKELEKAPA 251
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
386-591 |
1.29e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQ--REKYsleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQ--KQDAQDRLDEmDQQK----A 457
Cdd:COG0497 147 LDAFAGLEELLEeyREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEAAalQPGEEEELEE-ERRRlsnaE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 458 KLRDMLSDVRQKCQDETQMISSLktqiqsqesdlksqeddLNRAKSELNRLQQEETQLE---QSIQAGRVQLETIIKSLK 534
Cdd:COG0497 223 KLREALQEALEALSGGEGGALDL-----------------LGQALRALERLAEYDPSLAelaERLESALIELEEAASELR 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 535 STQD--EINQARskLSQLhESRQEAHRSLEQydqvldgAHGASLTDLADLSEgvSLAER 591
Cdd:COG0497 286 RYLDslEFDPER--LEEV-EERLALLRRLAR-------KYGVTVEELLAYAE--ELRAE 332
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
385-486 |
1.42e-03 |
|
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: 39.54 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIR----------QKTSE-VQELQ---NDLDRETSSLQELEAQKQDAQDRLD 450
Cdd:pfam07926 9 EIKRLKEEAADAEAQLQKLQEDLEKQAEIAReaqqnyerelVLHAEdIKALQalrEELNELKAEIAELKAEAESAKAELE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622897437 451 EM----DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQS 486
Cdd:pfam07926 89 ESeeswEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
456-564 |
1.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 456 KAKLRDMLSDVRQKCQDETQMISSLK----TQIQSQESDLKSQ-EDDLNRAKSEL----NRLQQEETQLE---QSIQAGR 523
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKkealLEAKEEIHKLRNEfEKELRERRNELqkleKRLLQKEENLDrklELLEKRE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622897437 524 VQLETIIKSLKSTQDEINQARSKLSQLHESRQEAhrsLEQY 564
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQE---LERI 147
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
388-584 |
1.47e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 388 DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdretSSLQELEAQ-----KQDAQDRLDEMDQQKAKLRDM 462
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLLPRlnllaDETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 463 LSDVRQkcQDETqmISSLKTQ---IQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAgRVQL--ETIIKSLKSTQ 537
Cdd:PRK04863 910 KRFVQQ--HGNA--LAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR-RAHFsyEDAAEMLAKNS 984
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 538 DEINQARSKLSQLHESRQEAHRSLE-------QYDQV---LDGAHGASLTDLADLSE 584
Cdd:PRK04863 985 DLNEKLRQRLEQAEQERTRAREQLRqaqaqlaQYNQVlasLKSSYDAKRQMLQELKQ 1041
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
396-563 |
1.52e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 396 LQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQ-KCQDET 474
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 475 QMiSSLKTQIqsqESDLKSQEDDLNRAKSELNR--------LQQEETQLEQSIqAGRVQLETIIKSLKSTQDEINQARS- 545
Cdd:pfam01576 721 NM-QALKAQF---ERDLQARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAV-AAKKKLELDLKELEAQIDAANKGREe 795
|
170 180
....*....|....*....|.
gi 1622897437 546 ---KLSQLHESRQEAHRSLEQ 563
Cdd:pfam01576 796 avkQLKKLQAQMKDLQRELEE 816
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
412-520 |
1.54e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.17 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 412 EAIRQKTSEVQELQNDLDRETSSL----QELEAQKQDAQDRLDEmdqQKAKLRDMLsdvrqkCQDETQMISSLKTQIQSQ 487
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLisiiQEVEENAADVEAQIKA---AFDELRNAL------NKRKKQLLEDLEEQKENK 73
|
90 100 110
....*....|....*....|....*....|...
gi 1622897437 488 ESDLKSQeddlnrakseLNRLQQEETQLEQSIQ 520
Cdd:smart00502 74 LKVLEQQ----------LESLTQKQEKLSHAIN 96
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
390-517 |
1.67e-03 |
|
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: 41.13 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 390 SQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQD--------------RLDEMDQQ 455
Cdd:pfam14915 150 SQQLSKAESKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDkvnkyigkqesleeRLAQLQSE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 456 KAKLRDMLSDVRQK----------CQDETQMISSlKTQIQSQESDLKSQEddlnRAK---SELNRLQQEETQLEQ 517
Cdd:pfam14915 230 NMLLRQQLEDAQNKadakektvidIQDQFQDIVK-KLQAESEKQVLLLEE----RNKeliNECNHLKERLYQYEK 299
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-517 |
1.80e-03 |
|
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: 41.44 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIA---QLQREKYSLE-----QDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEM--- 452
Cdd:pfam13868 130 EEIDEFNEEQAewkELEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrak 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 453 ---DQQKAKLRD-MLSDVRQKCQDETQMISSLKTQIQSQEsdlKSQEDDLNRAKSELNRL---QQEETQLEQ 517
Cdd:pfam13868 210 lyqEEQERKERQkEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQ 278
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
495-569 |
1.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 495 EDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLD 569
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-591 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLdRETSSLQELEAQKQDAQDRLDEMDQQKAKLR--- 460
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQDEESDLERLKEEIEKSSKQRAMLAgat 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 -------DMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQ----EDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETI 529
Cdd:TIGR00606 663 avysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlaPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 530 IKslkstqdEINQARSKLSQLHESRQEAHRSLEQYDQVLdGAHGASLTDLADLSEGVSLAER 591
Cdd:TIGR00606 743 EK-------EIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESAKVCLTDVTIMER 796
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
164-337 |
1.95e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.39 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 164 LGRVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEPVPsalppslippskrkktvfpgavpvlpaspppkdslrstpshg 243
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADT------------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 244 svsslNSTGSLSPKHSLK-QTQPTVNWVVPVADKMrFDEIflktDLDLDGYVSGQEVKEIFMHSGLTQNLLAHIWALADT 322
Cdd:COG5126 45 -----DGDGRISREEFVAgMESLFEATVEPFARAA-FDLL----DTDGDGKISADEFRRLLTALGVSEEEADELFARLDT 114
|
170
....*....|....*
gi 1622897437 323 RQTGKLSKDQFALAM 337
Cdd:COG5126 115 DGDGKISFEEFVAAV 129
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
403-563 |
1.95e-03 |
|
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: 40.43 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIRQKTSEVQELqndLDRETSSLQELEAQKQDAQDRldemdQQKAKLrdMLSdvrqkcQDETQMISSLKT 482
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQT---IARQKQLERRLEQQTEQAKKL-----EEKAQA--ALT------KGNEELAREALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 483 QIQSQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS--TQDEINQARSKLSQlhesrQEAHRS 560
Cdd:pfam04012 91 EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLST-----SSATDS 165
|
...
gi 1622897437 561 LEQ 563
Cdd:pfam04012 166 FER 168
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
403-550 |
1.97e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 403 LEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVrqkcqdeTQMISSLKT 482
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 483 QIQSQESDLKSQEDDLNRAKSELNRLQQEetqleqsIQAGRVQLETIIKSLKSTQDEINQARSKLSQL 550
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQ-------IAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
390-555 |
1.99e-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: 41.88 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 390 SQEIAQLQRekysLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQD---AQDRLDEMDQQKAKLRDMLSDV 466
Cdd:TIGR00618 337 QSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 467 ---RQKCQDETQMISSLKTQIQSQESDLKSQE-------DDLNRAKSELNRLQQEETQLEQSIQagrvQLETIIKSLKst 536
Cdd:TIGR00618 413 dtrTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQET-- 486
|
170
....*....|....*....
gi 1622897437 537 qdEINQARSKLSQLHESRQ 555
Cdd:TIGR00618 487 --RKKAVVLARLLELQEEP 503
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-547 |
2.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQ-------LQREKYSLEQDIREKEEAI--------------RQKTSEVQELQNDLDRETSSLQ------- 436
Cdd:pfam01576 862 ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQksesarq 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 437 ELEAQKQDAQDRLDEMDQQ-KAKLRDMLSDVRQK-CQDETQMISSLKTQIQS------QESDLKS---QEDDLNR----- 500
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTvKSKFKSSIAALEAKiAQLEEQLEQESRERQAAnklvrrTEKKLKEvllQVEDERRhadqy 1021
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 501 ---AKSELNRLQQEETQLE------QSIQAGR----VQLETIIKSLKSTQDEINQARSKL 547
Cdd:pfam01576 1022 kdqAEKGNSRMKQLKRQLEeaeeeaSRANAARrklqRELDDATESNESMNREVSTLKSKL 1081
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
418-555 |
2.21e-03 |
|
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: 40.07 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 418 TSEVQELQNDLDRETSSLQELeaqKQDAQDRLDEMDQQKAKLRDMLSDVRQkcqdetQMISSLKtqiQSQE-SD----LK 492
Cdd:pfam15272 3 TSEYLELLDKLDKNNRALHLL---NKDVRERDEHYQLQETSYKKKYLQTRN------ELINELK---QSKKlYDnyykLY 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 493 SQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLkstQDEINQARSKLSQLHESRQ 555
Cdd:pfam15272 71 SKYQQLKKISNESLDLQSTITNLESQLVDQAIDKDREIHNL---NEKILSLELRNQELETKRE 130
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
384-563 |
2.24e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQRE----KYSLEQ----DIREKE----EAIRQKTSEVQELQNDLdreTSSLQELEAQKQDAQDRLD- 450
Cdd:COG0497 172 KELEELRADEAERAREldllRFQLEEleaaALQPGEeeelEEERRRLSNAEKLREAL---QEALEALSGGEGGALDLLGq 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 451 ---------EMDQQKAKLRDMLSDVRQKCQDetqmissLKTQIQSQESDLKSQEDDLNRA---KSELNRLQQ------EE 512
Cdd:COG0497 249 alralerlaEYDPSLAELAERLESALIELEE-------AASELRRYLDSLEFDPERLEEVeerLALLRRLARkygvtvEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 513 -TQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLS----QLHESRQEAHRSLEQ 563
Cdd:COG0497 322 lLAYAEELRAELAELENSDERLEELEAELAEAEAELLeaaeKLSAARKKAAKKLEK 377
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
435-567 |
2.53e-03 |
|
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: 40.40 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 435 LQELEAQKQDAQDRLDEMDQQKAKLRDmlsdVRQKCQDEtqmISSLKTQIQSQESDLKSQEDDLNRAkseLNRLQQEETQ 514
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEK----RAEKAEAE---VAALNRRIQLLEEELERTEERLAEA---LEKLEEAEKA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622897437 515 LEQSIQAGRVqLETiikslKSTQDEiNQARSKLSQLHESRQEAHRSLEQYDQV 567
Cdd:pfam00261 73 ADESERGRKV-LEN-----RALKDE-EKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
384-515 |
2.57e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.09 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQrekysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQEL--EAQKQDA-----QDRLDEMDQQK 456
Cdd:cd21116 91 GAKQQLLQGLEALQ-------SQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDatKAQAQVAvlnalKNQLNSLAEQI 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 457 AKLRDMLSDVRQKCQDETQMISSLKTQIQ--SQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:cd21116 164 DAAIDALEKLSNDWQTLDSDIKELITDLEdaESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
384-509 |
2.88e-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: 40.35 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQR---EKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQdaqdrldEMDQQKAKLR 460
Cdd:pfam02841 183 QSKEAVEEAILQTDQaltAKEKAIEAERAKAEAAEAEQELLREKQKEEE------QMMEAQER-------SYQEHVKQLI 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 461 DMLSDVRQKCQDETQMISSLKTQIQ---SQESdLKSQEDDLNRaksELNRLQ 509
Cdd:pfam02841 250 EKMEAEREQLLAEQERMLEHKLQEQeelLKEG-FKTEAESLQK---EIQDLK 297
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
384-449 |
3.28e-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: 38.71 E-value: 3.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEI----AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRL 449
Cdd:pfam03938 33 AELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQ------QELQKKQQELLQPI 96
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
419-552 |
3.42e-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: 41.19 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 419 SEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSlKTQIQSQESDLKSQE 495
Cdd:TIGR00606 166 SEGKALKQKFDeifSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIVKSYE 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 496 DDLNRAKSELNRLQQEETQLeqsiqagrVQLETIIKSLKSTQDEINQARSKLSQLHE 552
Cdd:TIGR00606 245 NELDPLKNRLKEIEHNLSKI--------MKLDNEIKALKSRKKQMEKDNSELELKME 293
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
383-472 |
3.44e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 38.13 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 383 VKELDDISQEIAQLQREKYSLEQDIREKEEAIRqktsEVQELQNDLD------------RETSSLQELEAQKQDAQDRLD 450
Cdd:PRK09343 13 LAQLQQLQQQLERLLQQKSQIDLELREINKALE----ELEKLPDDTPiykivgnllvkvDKTKVEKELKERKELLELRSR 88
|
90 100
....*....|....*....|..
gi 1622897437 451 EMDQQKAKLRDMLSDVRQKCQD 472
Cdd:PRK09343 89 TLEKQEKKLREKLKELQAKINE 110
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
386-530 |
3.45e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 39.43 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKaklrdmlsd 465
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARY--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 466 vrqkcqdETQMISSLktqiqsqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRVQLETII 530
Cdd:pfam02321 139 -------EAGLISLL----------------DVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
384-552 |
3.48e-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: 40.45 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQRekySLEQDIREKEEAIRQKTSEVQELQNDLDRETsslQELEAQKQDAQDRLDEMDQQKAKLRDML 463
Cdd:pfam04108 171 KELESLEEEMASLLE---SLTNHYDQCVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQKLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 S---DVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAK-------SELNRLQQEETQLEQSIQAGRVQLETIIKSL 533
Cdd:pfam04108 245 EqknSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKetiedylSELEDLREFYEGFPSAYGSLLLEVERRREWA 324
|
170
....*....|....*....
gi 1622897437 534 KSTQDEINQARSKLSQLHE 552
Cdd:pfam04108 325 EKMKKILRKLAEELDRLQE 343
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
405-520 |
3.57e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 405 QDIREKEEAIRQKTSEVQELQND-----LDR---ETSS-LQELEAQKQDAQDRLDEMDQQKAKLRDMLSDV--------- 466
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADavnfaLRKrieETEDaKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKeaplklaqt 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 467 ----RQK------CQDETQ--MISSLKtQIQSQESDLKSQeddLNRAKSELNRLQQEETQLEQSIQ 520
Cdd:pfam03148 301 rlenRTYrpnvelCRDEAQygLVDEVK-ELEETIEALKQK---LAEAEASLQALERTRLRLEEDIA 362
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
386-471 |
3.59e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 38.40 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKYSLEQDIRE----KEEAIRQKTSEVQELQNDLD-RETSSLQELEAQKqdaQDRLDEMDQQKAKLR 460
Cdd:smart00502 9 LTKLRKKAAELEDALKQLISIIQEveenAADVEAQIKAAFDELRNALNkRKKQLLEDLEEQK---ENKLKVLEQQLESLT 85
|
90
....*....|.
gi 1622897437 461 DMLSDVRQKCQ 471
Cdd:smart00502 86 QKQEKLSHAIN 96
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
407-568 |
3.75e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 407 IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRldemdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQS 486
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR----------KQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 487 QESDLKSQEDDLN-------RAKSELNRLQQEE-------------TQLEQS---IQAGRVQLETIIKSLKSTQDEINQA 543
Cdd:PHA02562 246 LVMDIEDPSAALNklntaaaKIKSKIEQFQKVIkmyekggvcptctQQISEGpdrITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180
....*....|....*....|....*...
gi 1622897437 544 RSKLSQLHESRQEAH---RSLEQYDQVL 568
Cdd:PHA02562 326 EEIMDEFNEQSKKLLelkNKISTNKQSL 353
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
384-454 |
3.76e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 384 KELDDISQEIAQLQREKysleQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQ 454
Cdd:COG0542 440 ERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
406-468 |
3.80e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 3.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 406 DIREKEEAIRQKTSEVQELQNDLD---RETSSLQELEAQKQDAQDRLDEMDQQ---KAKLRDMLSDVRQ 468
Cdd:COG3167 40 LISPQLEELEELEAEEAQLKQELEkkqAKAANLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDISQ 108
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
462-564 |
3.83e-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: 40.19 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 462 MLSDVRQKCQDET-QMISSLKTQIQSQESDLKSQEDDL------NRAKSELNRLQQEEtqleQSIQAgrvQLETIIKSLK 534
Cdd:pfam05816 33 MLDNVRTKDLGEVgDLLNELRRTLKDFDPDELGEEKKLgflplfKKAGNKIEKYFAKY----QTAGA---QIDKIVVELE 105
|
90 100 110
....*....|....*....|....*....|
gi 1622897437 535 STQDEINQARSKLSQLHESRQEAHRSLEQY 564
Cdd:pfam05816 106 KGQDELLKDNAMLDQMYEKNLEYFKELEKY 135
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
419-549 |
3.87e-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: 39.70 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 419 SEVQELQNDLDRETSSLQEleaQKQDAQDRLDEmdqqkakLRDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDL 498
Cdd:cd21116 73 SYYPDLIELADNLIKGDQG---AKQQLLQGLEA-------LQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 499 NRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQ 549
Cdd:cd21116 143 QAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLED 193
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
384-565 |
4.00e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQrEKYSL----EQDIREKEEAIRQKTSEVQELQNDLDRETSS-------LQELEAQKQDAQDRLDEM 452
Cdd:pfam06160 305 EQNKELKEELERVQ-QSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAyselqeeLEEILEQLEEIEEEQEEF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 453 DQQKAKLRDMLSDVRQKCQDETQMISSLKTQIQSqeSDL----KSQEDDLNRAKSELNRLQQeetQLEQS---IQAGRVQ 525
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVEK--SNLpglpESYLDYFFDVSDEIEDLAD---ELNEVplnMDEVNRL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 526 LETIIKSL----KSTQDEINQA-------------RSKLSQLHESRQEAHRSLEQYD 565
Cdd:pfam06160 459 LDEAQDDVdtlyEKTEELIDNAtlaeqliqyanryRSSNPEVAEALTEAELLFRNYD 515
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-584 |
4.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 422 QELQNDLDRETSSLQELEAQKQDAQDRLDEmdqQKAKLRDMLSDVRQkcqdetqmISSLKTQIQSQESDLKSQEDDLNRA 501
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 502 KSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSL---EQYDQVLDGAHGASLTd 578
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKR- 315
|
....*.
gi 1622897437 579 LADLSE 584
Cdd:PRK03918 316 LSRLEE 321
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
394-527 |
4.21e-03 |
|
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: 37.95 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 394 AQLQREKysleQDIREKEEAIRQ---KTSEVQELQNDLDRETSSLQELEAQkqdaQDRLDEMDQQKAKLRDMLSDvRQKC 470
Cdd:pfam18595 2 STLAEEK----EELAELERKARElqaKIDALQVVEKDLRSCIKLLEEIEAE----LAKLEEAKKKLKELRDALEE-KEIE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 471 QDETQMisslktqiqsQESDLKSQeddLNRAKSELNRLQQeetQLEQSIQAGRVQLE 527
Cdd:pfam18595 73 LRELER----------REERLQRQ---LENAQEKLERLRE---QAEEKREAAQARLE 113
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
385-558 |
4.34e-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: 40.40 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDREtsslQELEAQ-KQD---AQDRLDEMDQQKAklr 460
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA----QTEEAQaKQDselAKLRVEEMEQGIA--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 dmlsdvrqkcqDETQMISslKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL--EQSIQAGRVQlETIIKSlKSTQD 538
Cdd:pfam05701 116 -----------DEASVAA--KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvsERDIAIKRAE-EAVSAS-KEIEK 180
|
170 180
....*....|....*....|
gi 1622897437 539 EINQARSKLSQLHESRQEAH 558
Cdd:pfam05701 181 TVEELTIELIATKESLESAH 200
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
385-565 |
4.40e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQE---LEAQKQDAQDRLDEMDQQKAKL-- 459
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSMELEKNNYYke 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 --------------------RDMLSDVRQkCQDETQMISSLKTQIQSQE------SDLKSQEDDLNRAKSELNRLQQEET 513
Cdd:PRK01156 278 leerhmkiindpvyknrnyiNDYFKYKND-IENKKQILSNIDAEINKYHaiikklSVLQKDYNDYIKKKSRYDDLNNQIL 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 514 QLE----------QSIQAGRVQLETIIKSLKSTQDEINQ----ARSKLSQLHESRQEAHRSLEQYD 565
Cdd:PRK01156 357 ELEgyemdynsylKSIESLKKKIEEYSKNIERMSAFISEilkiQEIDPDAIKKELNEINVKLQDIS 422
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
384-563 |
4.53e-03 |
|
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: 39.90 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSeVQELQNDL-DRETSSLQELEAQKQDAQ------DRLDEMDQQK 456
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIeEREQKRQEEYEEKLQEREqmdeivERIQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 457 AKLRDMLsdvRQKCQDETQMISSLKTQIQSQEsDLKSQEDDLnRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSL--- 533
Cdd:pfam13868 118 AEEKLEK---QRQLREEIDEFNEEQAEWKELE-KEEEREEDE-RILEYLKEKAEREEEREAEREEIEEEKEREIARLraq 192
|
170 180 190
....*....|....*....|....*....|....
gi 1622897437 534 ----KSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:pfam13868 193 qekaQDEKAERDELRAKLYQEEQERKERQKEREE 226
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
394-461 |
4.68e-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: 38.49 E-value: 4.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897437 394 AQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSslqelEAQKQDAQDRLDEMDQQKAKLRD 461
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAEERLAMLEEQRRMKEE 118
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
391-564 |
4.81e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELE----AQKQDAQDRldemDQQKAKLRDML--- 463
Cdd:pfam10174 95 QDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMElrieTQKQTLGAR----DESIKKLLEMLqsk 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 464 ---SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL---NRLQQEETQ---LEQSIQAGRVQLETIIKSLK 534
Cdd:pfam10174 171 glpKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaLQTVIEMKDTKISSLERNIR 250
|
170 180 190
....*....|....*....|....*....|
gi 1622897437 535 STQDEINQARSKLSQLHESRQEAHRSLEQY 564
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-563 |
5.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIRE-------------------KEEAIRQKTSEVQELQNDldretssLQELEAQKQD 444
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelteehRKELLEEYTAELKRIEKE-------LKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 445 AQDRLDEMDQQKAKLRDMLSdvrqkcqdetqmISSLKTQIQSQESDLKS-QEDDLNRAKSELNRLQQEETQLEQSIQAgr 523
Cdd:PRK03918 478 LRKELRELEKVLKKESELIK------------LKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKS-- 543
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622897437 524 vqLETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:PRK03918 544 --LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
392-515 |
5.08e-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: 38.58 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 392 EIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETS-----SLQELEAQKQ---DAQDRLDEMDQQKAKLRDML 463
Cdd:pfam09486 23 ELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTggspfSAADYLACRAyrdVLEGRVGAAEAALAAARQAL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622897437 464 SDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQL 515
Cdd:pfam09486 103 DAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAADEEAEEAAL 154
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
397-563 |
5.42e-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: 40.01 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 397 QREKYSLEQDIREKEEAI---RQKTSEVQELQNDLDRETSSLQELEAQ-------------KQDAQDRLDEMDQQK--AK 458
Cdd:pfam05701 218 EQDKLNWEKELKQAEEELqrlNQQLLSAKDLKSKLETASALLLDLKAElaaymesklkeeaDGEGNEKKTSTSIQAalAS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 459 LRDMLSDVR---QKCQDETQMISSLKTQIQSqesdlksqedDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKS 535
Cdd:pfam05701 298 AKKELEEVKaniEKAKDEVNCLRVAAASLRS----------ELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIAL 367
|
170 180
....*....|....*....|....*...
gi 1622897437 536 TQDEINQARSKLSQLHESRQEAHRSLEQ 563
Cdd:pfam05701 368 VQAKEKEAREKMVELPKQLQQAAQEAEE 395
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
391-564 |
5.51e-03 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 39.88 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 391 QEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELqndldretssLQELEAQKQDAQDRLDEMDQQK-AKLRD-MLSDVRQ 468
Cdd:COG3853 25 PEVPEQAAGMVDPEEAEVDLSKLSAEADAFVEAL----------AAQIDLSDVNAILQYGAKAQRKlAAFSNrMLDRVKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 469 KCQDET-QMISSLKTQIQsqESDLKSQEDD---------LNRAKSELNRLQQEEtqleQSIQAgrvQLETIIKSLKSTQD 538
Cdd:COG3853 95 KDLGEVgDSLSELRRTLE--DLDPSELDDLkkkgllgklFPKGGNKLEKYFAKY----QSAQT---QIDKISVALEKGQD 165
|
170 180
....*....|....*....|....*.
gi 1622897437 539 EINQARSKLSQLHESRQEAHRSLEQY 564
Cdd:COG3853 166 ELLKDNAMLDQLYEKNWEYFKELNQY 191
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
384-553 |
5.95e-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: 39.32 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 384 KELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQN-DLDRETSSLQEL--EAQKQDAQDRLDEMDQQKAKLR 460
Cdd:pfam06008 75 AESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsDLSRMLAEAQRMlgEIRSRDFGTQLQNAEAELKAAQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 461 DMLSDVR---QKCQDETQmisSLKTQIQSQESD----LKSQEDDLNRAKS------ELNRLQQEE-TQLEQSIQAGRVQL 526
Cdd:pfam06008 155 DLLSRIQtwfQSPQEENK---ALANALRDSLAEyeakLSDLRELLREAAAktrdanRLNLANQANlREFQRKKEEVSEQK 231
|
170 180
....*....|....*....|....*..
gi 1622897437 527 ETIIKSLKSTQDEINQARSKLSQLHES 553
Cdd:pfam06008 232 NQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
486-552 |
6.00e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.77 E-value: 6.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897437 486 SQESDLKSQEDDLNRAKSELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHE 552
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQE 67
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
386-563 |
6.20e-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: 38.40 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQrekyslEQDIREKEEAIRQKTSEVQELQNDLDretsslQELEAQKQDAQDRLDEMdqqKAKLRDMLSD 465
Cdd:pfam01442 6 LDELSTYAEELQ------EQLGPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEEL---QAKLGQNVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 466 VRQKCQDETQMI-SSLKTQIQSQESDLKSQEDDL-NRAKSELNRLQqeeTQLEQSIQAGRVQLETIIKSLKSTQDEI--- 540
Cdd:pfam01442 71 LRQRLEPYTEELrKRLNADAEELQEKLAPYGEELrERLEQNVDALR---ARLAPYAEELRQKLAERLEELKESLAPYaee 147
|
170 180
....*....|....*....|....*
gi 1622897437 541 --NQARSKLSQLHESRQEAHRSLEQ 563
Cdd:pfam01442 148 vqAQLSQRLQELREKLEPQAEDLRE 172
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
411-585 |
6.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 411 EEAIRQKTSEVQELQNdLDRETSSLQELEAQKQDAQD-RLDEMDQQKAKLRDMLSDVRqkcqDETQmisslktqiqsqeS 489
Cdd:pfam12128 247 QQEFNTLESAELRLSH-LHFGYKSDETLIASRQEERQeTSAELNQLLRTLDDQWKEKR----DELN-------------G 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 490 DLKSQEDDLNRAKSELNRLqqeETQLEQSIQAGrvqletiIKSLKSTQDEINQARSKLSQL---HESRQEAHRSLEQYDQ 566
Cdd:pfam12128 309 ELSAADAAVAKDRSELEAL---EDQHGAFLDAD-------IETAAADQEQLPSWQSELENLeerLKALTGKHQDVTAKYN 378
|
170 180
....*....|....*....|
gi 1622897437 567 VLDGAHGASL-TDLADLSEG 585
Cdd:pfam12128 379 RRRSKIKEQNnRDIAGIKDK 398
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
395-581 |
6.42e-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: 38.97 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 395 QLQREKYSLEQDIREKEEAIRQKTSEvqelqndldretSSLQELEAQKQDAQDRLDEMDQQKAKLrdmlSDVRQKCQDET 474
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG------------DDLESVEALLKKHEALEAELAAHEERV----EALNELGEQLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 475 QMISSLKTQIQSQESDLKSQEDDLNRAKSE-LNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHES 553
Cdd:cd00176 68 EEGHPDAEEIQERLEELNQRWEELRELAEErRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK 147
|
170 180
....*....|....*....|....*...
gi 1622897437 554 RQEAHRSLEQYDQVLDgahgaSLTDLAD 581
Cdd:cd00176 148 HKELEEELEAHEPRLK-----SLNELAE 170
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
402-462 |
6.68e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.39 E-value: 6.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 402 SLEQDIREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLD----EMDQQKAKLRDM 462
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEEKLRKL 65
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
385-572 |
6.85e-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: 39.94 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 385 ELDDISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQndlDREtsslQELEAQKQDAQDRLDEMD---QQKAKL-- 459
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELS---ARE----SDLEQDYQAASDHLNLVQtalRQQEKIer 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 460 -RDMLSDVRQKCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQ----EET---QLEQSIQA---GRVQLET 528
Cdd:COG3096 352 yQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQaldvQQTraiQYQQAVQAlekARALCGL 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622897437 529 IIKSLKSTQDEINQARSKLSQLHESRqeahRSLEQYDQVLDGAH 572
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEV----LELEQKLSVADAAR 471
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
448-556 |
6.94e-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: 38.04 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 448 RLDEMDQQKAKLRDMLSDVRQKCQDETQ-------------MISSLKTQIQSQESDLKSQEDDLN------------RAK 502
Cdd:pfam17098 12 RLAEKEQEIQELKAQLQDLKQSLQPPSSqlrsllldpavnlEFLRLKKELEEKKKKLKEAQLELAawkftpdsttgkRLM 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 503 SELNRLQQEETQLEQSIQAGRVQ-LETIIKSLKSTQDEINQARSKLSQLHESRQE 556
Cdd:pfam17098 92 AKCRLLQQENEELGRQLSEGRIAkLEIELALQKKVVEELKKSLEELDEFLIELDE 146
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
480-584 |
7.11e-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: 39.54 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 480 LKTQIQSQESDLKSQEDDLNRAKSELNRLQqeetQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLSQLHESRQEAH- 558
Cdd:COG0845 59 LQAALAQAQAQLAAAQAQLELAKAELERYK----ALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTi 134
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622897437 559 ----------RSLEQYDQVldgAHGASLTDLADLSE 584
Cdd:COG0845 135 rapfdgvvgeRNVEPGQLV---SAGTPLFTIADLDP 167
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
372-564 |
7.45e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 372 SGSLGSGEFTGVKELDDisqeiaqLQREKYSLEQDIrekeEAIRQKTSEVQELQND---LDRETS----SLQELEAQKQD 444
Cdd:PLN02939 214 GATEGLCVHSLSKELDV-------LKEENMLLKDDI----QFLKAELIEVAETEERvfkLEKERSlldaSLRELESKFIV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 445 AQDRLDEMDQQKAklrDMLSDVRQKCQDetqMISSLKTQIQS------QESDLKSQEDDLNRAKSELNR----------L 508
Cdd:PLN02939 283 AQEDVSKLSPLQY---DCWWEKVENLQD---LLDRATNQVEKaalvldQNQDLRDKVDKLEASLKEANVskfssykvelL 356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622897437 509 QQEETQLEQSIQAGRVQLETIIKSLkstQDEINQARSKLSQLHESRQEahRSLEQY 564
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHSYIQLY---QESIKEFQDTLSKLKEESKK--RSLEHP 407
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
387-517 |
7.68e-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: 37.66 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 387 DDISQEIAQLQREKYSLEQdirEKEEAIRQKTS---EVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQkaklrdml 463
Cdd:pfam10473 20 DSLKDKVENLERELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKE-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622897437 464 sdvrqkCQDETQMISSLKTQIQSQESDLKSQEDDLNRAKSEL-NRLQQEETQLEQ 517
Cdd:pfam10473 89 ------LQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESkTAVEMLQTQLKE 137
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
394-516 |
7.83e-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: 39.40 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 394 AQLQREKYSLEQD-IREKEEAIRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQD 472
Cdd:pfam17097 121 ASLEDEVSQLEDDtLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECWELLNELERLRDQRITVEEQTSN 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622897437 473 ETQMISSLKTQIQSQESDLKSQEDDLNRAKSELNRLQQEETQLE 516
Cdd:pfam17097 201 EKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLE 244
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
386-517 |
8.22e-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: 37.16 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 386 LDDISQEIAQLQREKysleqdirekeeairqktsevqelqndldretsslQELEAQKQDAQDRLDEMDQQKAKLRDML-- 463
Cdd:pfam05103 27 LDQVAEDYEALIREN-----------------------------------AELKEKIEELEEKLAHYKNLEETLQNTLil 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897437 464 -----SDVRQKCQDETQMISSlKTQIQSQESdLKSQEDDLNRAKSELNRLQQEETQLEQ 517
Cdd:pfam05103 72 aqetaEEVKANAQKEAELIIK-EAEAKAERI-VDDANNEVKKINDEIEELKRQRRQFRT 128
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
354-548 |
8.83e-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: 39.64 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 354 LSPDMVPPSErgtPGPDSSGSLGSGEFTGVKELDDISQEI-AQLQRekySLEQDI--REKEEAIRQKtsEVQELqndLDR 430
Cdd:pfam10168 471 LLIDAVPPSP---PLLCSKEDVTVDEPLRGLQEDSFEDHIkSILQR---SVSNPIlsADKLSSPSPQ--ECLQL---LSR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 431 ETSSLQELEAQKQDA-----QDRLDEMDQQKAK-LRDMlsdvrQKCQDETQMISSLKTQIQSQESDLK-SQEDDLNRAKS 503
Cdd:pfam10168 540 ATQVFREEYLKKHDLareeiQKRVKLLKLQKEQqLQEL-----QSLEEERKSLSERAEKLAEKYEEIKdKQEKLMRRCKK 614
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622897437 504 ELNRLQQEETQLEQSIQAGRVQLETIIKSLKSTQDEINQARSKLS 548
Cdd:pfam10168 615 VLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKKKMN 659
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
451-569 |
8.97e-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: 38.01 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 451 EMDQQKAKLRDMLSDVRQKCQDETQMIsslktqIQSQESdlksqeddlNRAKSELNRLQ-QEETQLEQSIQAGRVQLETI 529
Cdd:cd16855 9 QLEELRQRTQETENDLRNLQQKQESFV------IQYQES---------QKIQAQLQQLQqQPQNERIELEQQLQQQKEQL 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622897437 530 IKSLKSTQDEINQARSKLSQLHesrQEAHRSLEQ-YDQVLD 569
Cdd:cd16855 74 EQLLNAKAQELLQLRMELADKF---KKTIQLLSKlQSRVLD 111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
361-574 |
9.05e-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: 39.57 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 361 PSER-----GTPGPDSSGSLGSGEFTGVKELD-DISQEIAQLQREKYSLEQDIREKEEAIRQKTSEVQELQNDLDRETSS 434
Cdd:TIGR00618 162 SKEKkellmNLFPLDQYTQLALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 435 LQELEaqkqdaqdRLDEMDQQKAKLRDMLSDVRQKCQdetqmisslktQIQSQESDLKSQEDDLNRAKSELnRLQQEETQ 514
Cdd:TIGR00618 242 HAYLT--------QKREAQEEQLKKQQLLKQLRARIE-----------ELRAQEAVLEETQERINRARKAA-PLAAHIKA 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 515 LEQSIQagrvQLETIIKSLKSTQDEINQARSKLSQLHESRQeahrSLEQYDQVLDGAHGA 574
Cdd:TIGR00618 302 VTQIEQ----QAQRIHTELQSKMRSRAKLLMKRAAHVKQQS----SIEEQRRLLQTLHSQ 353
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
405-517 |
9.41e-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: 37.29 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 405 QDIREKEEaiRQKTSEVQELQNDLDRETSSLQELEAQKQDAQDRLDEMDQQKAKLRDMLSDVRQKCQdetqmissLKTQI 484
Cdd:TIGR02473 8 LDLREKEE--EQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQ--------LDQRI 77
|
90 100 110
....*....|....*....|....*....|...
gi 1622897437 485 QSQESDLKSQEDDLNRAKSELNRLQQEETQLEQ 517
Cdd:TIGR02473 78 QQQQQELALLQQEVEAKRERLLEARRELKALEK 110
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
446-591 |
9.50e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897437 446 QDRLDEMDQQKAKLRDMLSDVRQKCQDETQMISSLKtqiqsqesdlksqeDDLNRAKSELNRLQQEETQLEQSIQAGRVQ 525
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897437 526 LETIIKSLKSTQDEINQARSKLSQLHESRQEAHRSLEQYDQVLDGAHG---ASLTDLADLSE--GVSLAER 591
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKrdrESQAKIADLGRrlNVALAQR 188
|
|
| |
