|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2-695 |
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: 1107.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 2 KRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFV 81
Cdd:pfam09726 1 KRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQGLAFSVFFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 82 CVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGY 161
Cdd:pfam09726 81 CIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 162 PVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAaaaaaaSKSIHDVDSPAVAQNGS 241
Cdd:pfam09726 161 PVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQERETSET------AKGLSEVDPLALNQNGH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 242 AGGKKPSSNTLPELEYREKERGK----NESKKQHNHNQNhhsstsssILPSVDNKAQEMEYMENHVNSKRLSSSDLLGST 317
Cdd:pfam09726 235 SLNKKDSTLQLPELEYREKKNSGtssgSDSKKSHNHNIH--------NLNHVDSKLQEKEYMENHSNSKRLNISTSPGSE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 318 ENLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPsssassssKGDRKQKYGGGKNSASH 397
Cdd:pfam09726 307 EDLLVRESVSSKSSSSSSSSNKNYKNASGGSANSSNSSPRSHSHNSGSVTSSSSS--------KNSKKQKGPGGKSGARH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 398 RDPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQ 477
Cdd:pfam09726 379 KDPAENCIPNNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 478 AKQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTLDI 557
Cdd:pfam09726 459 AKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 558 KVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKD 637
Cdd:pfam09726 539 KLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQKD 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207114191 638 QEIKDLKQKIAEVMAVMPSvvysadTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPL 695
Cdd:pfam09726 619 QEIKDLKQKIAEVMAVMPS------TSRITPVTPHYSSKFMDTSPSMRDPNASVYPPL 670
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-649 |
5.89e-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: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 407 NNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLgslgtseRSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTL 486
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 487 GQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRG------ECTESLRRRISELEAECK-------KL 553
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkEELKALREALDELRAELTllneeaaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 554 TLDIKVKEDQIRELELKVQELHKYKEnekDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFS----ALGDAKRQLEIA 629
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEEL 899
|
250 260
....*....|....*....|
gi 1207114191 630 QGQILQKDQEIKDLKQKIAE 649
Cdd:TIGR02168 900 SEELRELESKRSELRRELEE 919
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
407-645 |
3.25e-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: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 407 NNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLgtsersiRSELGQLRQENELLQNKLHNavqaKQKDKQTL 486
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-------ESKIQNQEKLNQQKDEQIKK----LQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 487 GQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAvalaaatrgecTESLRRRISELEAECKKLTLDIkvkEDQIRE 566
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-----------RESLETQLKVLSRSINKIKQNL---EQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 567 LELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQL------EIAQGQILQKDQEI 640
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkENLEKEIDEKNKEI 570
|
....*
gi 1207114191 641 KDLKQ 645
Cdd:TIGR04523 571 EELKQ 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
418-649 |
3.32e-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: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 418 RLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQkdkqtlgQLEKRLKAEQ 497
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-------RLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 498 EARaaaekllaeekkrkkleeataaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELH-K 576
Cdd:COG1196 309 ERR------------------------------------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEeE 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207114191 577 YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 649
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-649 |
4.08e-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: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 414 EALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAvqakqkdKQTLGQLEKRL 493
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 494 KAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAEckkltldIKVKEDQIRELELKVQE 573
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-------EELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207114191 574 LHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 649
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
421-684 |
5.77e-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: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 421 QDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKAEQEAR 500
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 501 AAAEKLLAEEKKRKKLEEATAARAVALAAATRGEcTESLRRRISELEAECKKLTLDIKVKEDQIRELElkvqelhkyKEN 580
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALR---------AEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 581 EKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSVVYS 660
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
250 260
....*....|....*....|....*
gi 1207114191 661 ADTGSMT-PVTPHYSSKFMDTSPSG 684
Cdd:COG4942 250 ALKGKLPwPVSGRVVRRFGERDGGG 274
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-652 |
6.17e-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: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 416 LVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKdkqtlgqLEKRLKA 495
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 496 EQEARAAAEKLLAEEKKRKKLEEATAARAValaaatrgECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELH 575
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELA--------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 576 --------KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAkrQLEIAQGQILQKDQEIKDLKQKI 647
Cdd:TIGR02168 379 eqletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEEL 456
|
....*
gi 1207114191 648 AEVMA 652
Cdd:TIGR02168 457 ERLEE 461
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
537-652 |
3.33e-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: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 537 ESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKEnekdtevlmsaLSAMQDKTQHLENSLS-AETRIkLDL 615
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-----------YEALQKEIESLKRRISdLEDEI-LEL 115
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207114191 616 FSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMA 652
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 |
3.60e-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: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 29 FLYLKFLVVWALVLLA-DFVLEFRFEYLWPFWLFI------RSVYDSFryqGLAFSVFFVCVAFTSDiICLLFIPVQ-WL 100
Cdd:TIGR03462 1 YLYLGVLLVWALPVLAlLWVFRGPFLRLRALALALlialptFLVWDNL---AIRRGVWTYNPRYILG-IRLGDLPIEeFL 76
|
90
....*....|...
gi 1207114191 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 ... |
407-649 |
3.96e-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: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 407 NNQLSKPEALV-RLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQT 485
Cdd:TIGR04523 327 QNQISQNNKIIsQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 486 LGQLEKRLKAEQEARaaaekllaeekkrkkleeataaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIR 565
Cdd:TIGR04523 407 NQQKDEQIKKLQQEK------------------------------------ELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 566 ELELKVQELHKYKENEKDTevlMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEiaqgqilqkdQEIKDLKQ 645
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQ---LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE----------EKVKDLTK 517
|
....
gi 1207114191 646 KIAE 649
Cdd:TIGR04523 518 KISS 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-649 |
4.64e-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: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 414 EALVRLEQDVKKLKADLQASR----QTEQDLRSQLgslgTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQL 489
Cdd:COG1196 274 LELEELELELEEAQAEEYELLaelaRLEQDIARLE----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 490 EKRLKAEQEARAAAEKLLAEEKKRKKLEEATAaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIRELEL 569
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEEL---------------EELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 570 KVQELHKYKENEKDtevlmsALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 649
Cdd:COG1196 415 RLERLEEELEELEE------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-493 |
6.92e-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: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 414 EALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRL 493
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
416-650 |
7.40e-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: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 416 LVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHnavqakqKDKQTLGQLEKRLKA 495
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 496 EQEARAAAEKllaeekkrkkleeataaravalaaATRGECTESLRRRISELEAECKKLTLD-------IKVKEDQIRELE 568
Cdd:TIGR02169 791 SRIPEIQAEL------------------------SKLEEEVSRIEARLREIEQKLNRLTLEkeylekeIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 569 LKVQELHKYKEN-EKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKI 647
Cdd:TIGR02169 847 EQIKSIEKEIENlNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
...
gi 1207114191 648 AEV 650
Cdd:TIGR02169 927 EAL 929
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
540-649 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 540 RRRISELEAECKKLTLDIKVKEDQIRELELKVQELHK----------YKENEKDTEVLMSALSAMQDKTQHLENSLSAET 609
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207114191 610 RIKldlfSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 649
Cdd:COG4913 689 ALE----EQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
414-641 |
1.79e-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: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 414 EALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSiRSELGQLRQenelLQNKLHNAVQAKQKDKQTLGQLEKRL 493
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 494 KAEQEARAAAEKLLAEekkrkkleeataaravalaaatrgectESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQE 573
Cdd:COG3206 250 GSGPDALPELLQSPVI---------------------------QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207114191 574 LHKYKENEKDTEV--LMSALSAMQDKTQHLENSLsAETRIKLDLFSA----LGDAKRQLEIAQG---QILQKDQEIK 641
Cdd:COG3206 303 LRAQLQQEAQRILasLEAELEALQAREASLQAQL-AQLEARLAELPEleaeLRRLEREVEVARElyeSLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
536-652 |
3.49e-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: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 536 TESLRRRISELEAECKKLTL---DIKVKEDQIRELELKVQELHK--------YKENEKDTEVLMSALSAMQDKTQHLENS 604
Cdd:COG4913 663 VASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEeldelkgeIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207114191 605 LSAETRIKLD-LFSALGDAKRQLEIA---QGQILQKDQEIKDLKQKIAEVMA 652
Cdd:COG4913 743 ARLELRALLEeRFAAALGDAVERELRenlEERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-646 |
3.55e-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: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 414 EALVRLEQDVKKLkADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQEneLLQNKLHNAVQAKQKDKQTLGQLEKRL 493
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 494 KAEQEARAAAEKLLAEEKkrkkleeataaravalaaatrGECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVqe 573
Cdd:COG4913 319 DALREELDELEAQIRGNG---------------------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPL-- 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207114191 574 lhkyKENEKDtevlmsaLSAMQDKTQHLENSLSAETRiklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQK 646
Cdd:COG4913 376 ----PASAEE-------FAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
416-654 |
6.74e-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: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 416 LVRLEQDVKKLKADLQASRQTEQD----LRSQLgSLGTSERS-IRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLE 490
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDkieeLEKQL-VLANSELTeARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 491 KRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAE------CKKLTLDIKVKEDQI 564
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKneslekVSSLTAQLESTKEML 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 565 RELelkVQELHKYKENEKDTEVLMSALSA-MQDKTQHLE--NSLSAETRIKLDLF-----------SALGDAKRQLEIAQ 630
Cdd:pfam15921 478 RKV---VEELTAKKMTLESSERTVSDLTAsLQEKERAIEatNAEITKLRSRVDLKlqelqhlknegDHLRNVQTECEALK 554
|
250 260
....*....|....*....|....
gi 1207114191 631 GQILQKDQEIKDLKQKIAEVMAVM 654
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLV 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
536-650 |
7.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 536 TESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSaetriklDL 615
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS-------RL 319
|
90 100 110
....*....|....*....|....*....|....*
gi 1207114191 616 FSALGDAKRQLEiaqgQILQKDQEIKDLKQKIAEV 650
Cdd:PRK03918 320 EEEINGIEERIK----ELEEKEERLEELKKKLKEL 350
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
539-608 |
8.21e-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: 8.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207114191 539 LRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHK--YKENEKDTEVlmsalSAMQDKTQHLENSLSAE 608
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREI-----SRLDREIERLERELEEE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-494 |
9.36e-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: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 414 EALVRLEQ---DVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLgqLE 490
Cdd:COG4913 675 AELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LE 752
|
....
gi 1207114191 491 KRLK 494
Cdd:COG4913 753 ERFA 756
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-649 |
9.76e-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: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 416 LVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKA 495
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114191 496 EQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGEcTESLRRRISELEAECKKLTldikvkeDQIRELELKVQELh 575
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEE-LRELESKRSELRRELEELR-------EKLAQLELRLEGL- 934
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207114191 576 kykenekdtevlmsalsamQDKTQHLENSLSAETRIKLDlfsalgDAKRQLEIAQGQILQKDQEIKDLKQKIAE 649
Cdd:TIGR02168 935 -------------------EVRIDNLQERLSEEYSLTLE------EAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| |
