|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2-697 |
0e+00 |
|
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: 1106.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 2 KRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFV 81
Cdd:pfam09726 1 KRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQGLAFSVFFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 82 CVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGY 161
Cdd:pfam09726 81 CIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 162 PVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAaaaaaaaaSKSIHDVDSPAVAQN 241
Cdd:pfam09726 161 PVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQERETSET--------AKGLSEVDPLALNQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 242 GSAGGKKPSSNTLPELEYREKERGK----NESKKQHNHNQNhhsstsssILPSVDNKAQEMEYMENHVNSKRLSSSDLLG 317
Cdd:pfam09726 233 GHSLNKKDSTLQLPELEYREKKNSGtssgSDSKKSHNHNIH--------NLNHVDSKLQEKEYMENHSNSKRLNISTSPG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 318 STENLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPsssassssKGDRKQKYGGGKNSA 397
Cdd:pfam09726 305 SEEDLLVRESVSSKSSSSSSSSNKNYKNASGGSANSSNSSPRSHSHNSGSVTSSSSS--------KNSKKQKGPGGKSGA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 398 SHRDPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNA 477
Cdd:pfam09726 377 RHKDPAENCIPNNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 478 VQAKQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTL 557
Cdd:pfam09726 457 VSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTH 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 558 DIKVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQ 637
Cdd:pfam09726 537 DIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 638 KDQEIKDLKQKIAEVMAVMPSvvysadTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPL 697
Cdd:pfam09726 617 KDQEIKDLKQKIAEVMAVMPS------TSRITPVTPHYSSKFMDTSPSMRDPNASVYPPL 670
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
409-651 |
5.91e-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: 53.14 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 409 NNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLgslgtseRSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTL 488
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 489 GQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRG------ECTESLRRRISELEAECK-------KL 555
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkEELKALREALDELRAELTllneeaaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 556 TLDIKVKEDQIRELELKVQELHKYKEnekDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFS----ALGDAKRQLEIA 631
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEEL 899
|
250 260
....*....|....*....|
gi 112807178 632 QGQILQKDQEIKDLKQKIAE 651
Cdd:TIGR02168 900 SEELRELESKRSELRRELEE 919
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
409-647 |
3.27e-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: 50.40 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 409 NNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLgtsersiRSELGQLRQENELLQNKLHNavqaKQKDKQTL 488
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-------ESKIQNQEKLNQQKDEQIKK----LQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 489 GQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAvalaaatrgecTESLRRRISELEAECKKLTLDIkvkEDQIRE 568
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-----------RESLETQLKVLSRSINKIKQNL---EQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 569 LELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQL------EIAQGQILQKDQEI 642
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkENLEKEIDEKNKEI 570
|
....*
gi 112807178 643 KDLKQ 647
Cdd:TIGR04523 571 EELKQ 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
420-651 |
3.33e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 420 RLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQkdkqtlgQLEKRLKAEQ 499
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-------RLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 500 EARaaaekllaeekkrkkleeataaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELH-K 578
Cdd:COG1196 309 ERR------------------------------------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEeE 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112807178 579 YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 651
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
416-651 |
4.09e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 416 EALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAvqakqkdKQTLGQLEKRL 495
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 496 KAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAEckkltldIKVKEDQIRELELKVQE 575
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-------EELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112807178 576 LHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 651
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
423-686 |
5.79e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 423 QDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKAEQEAR 502
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 503 AAAEKLLAEEKKRKKLEEATAARAVALAAATRGEcTESLRRRISELEAECKKLTLDIKVKEDQIRELElkvqelhkyKEN 582
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALR---------AEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 583 EKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSVVYS 662
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
250 260
....*....|....*....|....*
gi 112807178 663 ADTGSMT-PVTPHYSSKFMDTSPSG 686
Cdd:COG4942 250 ALKGKLPwPVSGRVVRRFGERDGGG 274
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-654 |
6.19e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 418 LVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKdkqtlgqLEKRLKA 497
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 498 EQEARAAAEKLLAEEKKRKKLEEATAARAValaaatrgECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELH 577
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELA--------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 578 --------KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAkrQLEIAQGQILQKDQEIKDLKQKI 649
Cdd:TIGR02168 379 eqletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEEL 456
|
....*
gi 112807178 650 AEVMA 654
Cdd:TIGR02168 457 ERLEE 461
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
539-654 |
3.35e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 539 ESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKEnekdtevlmsaLSAMQDKTQHLENSLS-AETRIkLDL 617
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-----------YEALQKEIESLKRRISdLEDEI-LEL 115
|
90 100 110
....*....|....*....|....*....|....*..
gi 112807178 618 FSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMA 654
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
|
| CarR_dom_SF |
TIGR03462 |
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as ... |
29-113 |
3.61e-04 |
|
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.
Pssm-ID: 274590 Cd Length: 89 Bit Score: 39.89 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 29 FLYLKFLVVWALVLLA-DFVLEFRFEYLWPFWLFI------RSVYDSFryqGLAFSVFFVCVAFTSDiICLLFIPVQ-WL 100
Cdd:TIGR03462 1 YLYLGVLLVWALPVLAlLWVFRGPFLRLRALALALlialptFLVWDNL---AIRRGVWTYNPRYILG-IRLGDLPIEeFL 76
|
90
....*....|...
gi 112807178 101 FFAASTYVWVQYV 113
Cdd:TIGR03462 77 FFLLTPLLTVLWL 89
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
409-651 |
3.97e-04 |
|
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: 43.86 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 409 NNQLSKPEALV-RLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQT 487
Cdd:TIGR04523 327 QNQISQNNKIIsQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 488 LGQLEKRLKAEQEARaaaekllaeekkrkkleeataaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIR 567
Cdd:TIGR04523 407 NQQKDEQIKKLQQEK------------------------------------ELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 568 ELELKVQELHKYKENEKDTevlMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEiaqgqilqkdQEIKDLKQ 647
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQ---LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE----------EKVKDLTK 517
|
....
gi 112807178 648 KIAE 651
Cdd:TIGR04523 518 KISS 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
416-651 |
4.65e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 416 EALVRLEQDVKKLKADLQASR----QTEQDLRSQLgslgTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQL 491
Cdd:COG1196 274 LELEELELELEEAQAEEYELLaelaRLEQDIARLE----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 492 EKRLKAEQEARAAAEKLLAEEKKRKKLEEATAaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIRELEL 571
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEEL---------------EELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 572 KVQELHKYKENEKDtevlmsALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 651
Cdd:COG1196 415 RLERLEEELEELEE------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-495 |
6.94e-04 |
|
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: 43.12 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 416 EALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRL 495
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-652 |
7.42e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 418 LVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHnavqakqKDKQTLGQLEKRLKA 497
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 498 EQEARAAAEKllaeekkrkkleeataaravalaaATRGECTESLRRRISELEAECKKLTLD-------IKVKEDQIRELE 570
Cdd:TIGR02169 791 SRIPEIQAEL------------------------SKLEEEVSRIEARLREIEQKLNRLTLEkeylekeIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 571 LKVQELHKYKEN-EKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKI 649
Cdd:TIGR02169 847 EQIKSIEKEIENlNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
...
gi 112807178 650 AEV 652
Cdd:TIGR02169 927 EAL 929
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-651 |
1.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 542 RRRISELEAECKKLTLDIKVKEDQIRELELKVQELHK----------YKENEKDTEVLMSALSAMQDKTQHLENSLSAET 611
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 112807178 612 RIKldlfSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 651
Cdd:COG4913 689 ALE----EQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
416-643 |
1.80e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 416 EALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSiRSELGQLRQenelLQNKLHNAVQAKQKDKQTLGQLEKRL 495
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 496 KAEQEARAAAEKLLAEekkrkkleeataaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQE 575
Cdd:COG3206 250 GSGPDALPELLQSPVI---------------------------QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112807178 576 LHKYKENEKDTEV--LMSALSAMQDKTQHLENSLsAETRIKLDLFSA----LGDAKRQLEIAQG---QILQKDQEIK 643
Cdd:COG3206 303 LRAQLQQEAQRILasLEAELEALQAREASLQAQL-AQLEARLAELPEleaeLRRLEREVEVARElyeSLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
538-654 |
3.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 538 TESLRRRISELEAECKKLTL---DIKVKEDQIRELELKVQELHK--------YKENEKDTEVLMSALSAMQDKTQHLENS 606
Cdd:COG4913 663 VASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEeldelkgeIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 112807178 607 LSAETRIKLD-LFSALGDAKRQLEIA---QGQILQKDQEIKDLKQKIAEVMA 654
Cdd:COG4913 743 ARLELRALLEeRFAAALGDAVERELRenlEERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
416-648 |
3.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 416 EALVRLEQDVKKLkADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQEneLLQNKLHNAVQAKQKDKQTLGQLEKRL 495
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 496 KAEQEARAAAEKLLAEEKkrkkleeataaravalaaatrGECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVqe 575
Cdd:COG4913 319 DALREELDELEAQIRGNG---------------------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPL-- 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112807178 576 lhkyKENEKDtevlmsaLSAMQDKTQHLENSLSAETRiklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQK 648
Cdd:COG4913 376 ----PASAEE-------FAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
418-656 |
6.77e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 418 LVRLEQDVKKLKADLQASRQTEQD----LRSQLgSLGTSERS-IRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLE 492
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDkieeLEKQL-VLANSELTeARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 493 KRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAE------CKKLTLDIKVKEDQI 566
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKneslekVSSLTAQLESTKEML 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 567 RELelkVQELHKYKENEKDTEVLMSALSA-MQDKTQHLE--NSLSAETRIKLDLF-----------SALGDAKRQLEIAQ 632
Cdd:pfam15921 478 RKV---VEELTAKKMTLESSERTVSDLTAsLQEKERAIEatNAEITKLRSRVDLKlqelqhlknegDHLRNVQTECEALK 554
|
250 260
....*....|....*....|....
gi 112807178 633 GQILQKDQEIKDLKQKIAEVMAVM 656
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLV 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
538-652 |
7.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 538 TESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSaetriklDL 617
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS-------RL 319
|
90 100 110
....*....|....*....|....*....|....*
gi 112807178 618 FSALGDAKRQLEiaqgQILQKDQEIKDLKQKIAEV 652
Cdd:PRK03918 320 EEEINGIEERIK----ELEEKEERLEELKKKLKEL 350
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
541-610 |
8.24e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 8.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112807178 541 LRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHK--YKENEKDTEVlmsalSAMQDKTQHLENSLSAE 610
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREI-----SRLDREIERLERELEEE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
416-496 |
9.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 416 EALVRLEQ---DVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLgqLE 492
Cdd:COG4913 675 AELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LE 752
|
....
gi 112807178 493 KRLK 496
Cdd:COG4913 753 ERFA 756
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-651 |
9.79e-03 |
|
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: 39.27 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 418 LVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKA 497
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112807178 498 EQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGEcTESLRRRISELEAECKKLTldikvkeDQIRELELKVQELh 577
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEE-LRELESKRSELRRELEELR-------EKLAQLELRLEGL- 934
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112807178 578 kykenekdtevlmsalsamQDKTQHLENSLSAETRIKLDlfsalgDAKRQLEIAQGQILQKDQEIKDLKQKIAE 651
Cdd:TIGR02168 935 -------------------EVRIDNLQERLSEEYSLTLE------EAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| |
