|
Name |
Accession |
Description |
Interval |
E-value |
| PTB_Rab6GAP |
cd01211 |
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ... |
72-200 |
2.44e-81 |
|
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.
Pssm-ID: 269922 Cd Length: 129 Bit Score: 259.49 E-value: 2.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 72 VVFNKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGTVRLLDPQTNTEIANYPIYKILFCVRGHDG 151
Cdd:cd01211 1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1386635304 152 TPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQ 200
Cdd:cd01211 81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
490-699 |
2.70e-70 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 232.58 E-value: 2.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 490 VRSGVPEALRGEVWQLLAGCHNNDH--LVEKYRILITKESPQD----SAITRDINRTFPAHDYFKDTGGDGQDSLYKICK 563
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLKETAPDDksivHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 564 AYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLReLFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLD 642
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386635304 643 ISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLL 699
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
496-699 |
4.70e-66 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 219.43 E-value: 4.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 496 EALRGEVWQllagchnndhlvekyrilitkespqdSAITRDINRTFPAHDYFKDtgGDGQDSLYKICKAYSVYDEEIGYC 575
Cdd:pfam00566 1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 576 QGQSFLAAVLLL-HMPEEQAFSVLVKIMFDYGLRELFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQW 654
Cdd:pfam00566 53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386635304 655 FLTLFTAKFPLYMVFHIIDLLLCEGISV-IFNVALGLLKTSKDDLL 699
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
462-707 |
1.03e-49 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 183.85 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 462 EKILETWGELL-SKWHLNLSVRPKQLSSLVRSGVPEALRGEVWQLLAG-------CHNNDHLVEKYRILITKESPQD-SA 532
Cdd:COG5210 180 LAADKLWISYLdPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGigfdldkNPGLYERLLNLHREAKIPTQEIiSQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 533 ITRDINRTFPAHDYFKDTGGDGQDSLYKICKAYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLRELF 611
Cdd:COG5210 260 IEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 612 KQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLL 691
Cdd:COG5210 340 LKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAIL 419
|
250
....*....|....*.
gi 1386635304 692 KTSKDDLLLTDFEGAL 707
Cdd:COG5210 420 KLLRDKLLKLDSDELL 435
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
234-364 |
1.01e-34 |
|
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.
Pssm-ID: 463599 Cd Length: 149 Bit Score: 129.63 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 234 FSAVPKDK----DRQCFKLRQGIDKKIVICVQQTANKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 305
Cdd:pfam12473 2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635304 306 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 364
Cdd:pfam12473 72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
|
|
| PTB |
smart00462 |
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
70-203 |
4.00e-28 |
|
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.
Pssm-ID: 214675 Cd Length: 134 Bit Score: 110.10 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 70 DSVVFNKLTYLGCASVNAPRSEVEALR-MMSILRSQCQISLDVTLSVPNVSEGTVRLLDPQTNTEIANYPIYKILFCVRG 148
Cdd:smart00462 1 GSGVSFRVKYLGSVEVPEARGLQVVQEaIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386635304 149 HDGtpeSDCFAFTESHYNAELFRIHVFRCEI--QEAVSRILYSFATAFRRSAKQTPL 203
Cdd:smart00462 81 PDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKARSE 134
|
|
| PTB |
cd00934 |
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ... |
76-194 |
1.08e-17 |
|
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.
Pssm-ID: 269911 Cd Length: 120 Bit Score: 79.86 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 76 KLTYLGCASVNAPR----SEVEALRMMSILRSQCQISLDVTLsvpNVSEGTVRLLDPQTNTEIANYPIYKILFCVRGHDg 151
Cdd:cd00934 4 QVKYLGSVEVGSSRgvdvVEEALKALAAALKSSKRKPGPVLL---EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1386635304 152 tpESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAF 194
Cdd:cd00934 80 --NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
716-959 |
3.96e-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: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 716 KRYRSEENAKRLMELAcntkISQKKLKKFEKEYHTMREQQAQQEDPIERFERE-----------NRRLQEANMRLEQEND 784
Cdd:TIGR02168 213 ERYKELKAELRELELA----LLVLRLEELREELEELQEELKEAEEELEELTAElqeleekleelRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 785 DL------AHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLK---EMCRRELDKAESEIK 855
Cdd:TIGR02168 289 ELyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 856 KNSSIIGDYKQICSQLSER---LEKQQTANKVEIEKIRQKVDDCDRCRDFF--NKEGRVKGISSAK----GVSDEDTDEE 926
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLqqEIEELLKKLEEAElkelQAELEELEEE 448
|
250 260 270
....*....|....*....|....*....|...
gi 1386635304 927 KETLKNQLREMELELAQTKLQLVEAECKIQDLE 959
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
713-974 |
3.54e-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: 67.39 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 713 QLPKRYRSEENAKRLMELacntkisQKKLKKFEKEYHTMReqqaqqedpIERFERENRRLQEANMRLEQENDDLAHELVT 792
Cdd:TIGR02168 201 QLKSLERQAEKAERYKEL-------KAELRELELALLVLR---------LEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 793 SKIA---LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKemcrRELDKAESEIKKNSSIIGDYKQICS 869
Cdd:TIGR02168 265 LEEKleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE----RQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 870 QLSERLEKQQtankVEIEKIRQKVDDcdRCRDFFNKEGRVkgissakgvsdEDTDEEKETLKNQLREMELELAQTKLQLV 949
Cdd:TIGR02168 341 ELEEKLEELK----EELESLEAELEE--LEAELEELESRL-----------EELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260
....*....|....*....|....*
gi 1386635304 950 EAECKIQDLEHHLGLALSEVQAAKK 974
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
738-973 |
1.60e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 738 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELvtskIALRKDLDNAEEKADALNKELLM 817
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 818 TKQKLIDAE----DEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQIcsqlsERLEKQQTANKVEIEKIRQkv 893
Cdd:COG1196 349 AEEELEEAEaelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-----EELEEAEEALLERLERLEE-- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 894 ddcdrcrdffNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREmELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAK 973
Cdd:COG1196 422 ----------ELEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-970 |
6.12e-09 |
|
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: 60.07 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 705 GALKFFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnd 784
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 785 dlaHELVTSKIA-LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMC---RRELDKAESEIKKNSSI 860
Cdd:TIGR02168 742 ---VEQLEERIAqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 861 IGDYKQICSQLS----------ERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEgrVKGISSAKGVSDEDTD---EEK 927
Cdd:TIGR02168 819 AANLRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALAllrSEL 896
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1386635304 928 ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQ 970
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
721-841 |
9.39e-09 |
|
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: 54.54 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMELacntkisQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnddlAHELVTSKIALRKD 800
Cdd:pfam20492 2 EEAEREKQEL-------EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQK----RQEAEEEKERLEES 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1386635304 801 LDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKE 841
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQE 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
692-959 |
3.27e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 692 KTSKDDLLLTDFEGALKFFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQED--------PIE 763
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltglTPE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 764 RFERENRRLQEANMRLEQENDDLAHEL--VTSKIALRKD----LDNAEEKADALNKEL-------LMTK--QKLIDAEDE 828
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIgeLKKEIKELKKaieeLKKAKGKCPVCGRELteehrkeLLEEytAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 829 KRRLEEESAQLkemcRRELDKAESEIKKNSSIIgDYKQICSQLSERLEKqqtANKVEIEKIRQKVDDCDRCRDFFNK-EG 907
Cdd:PRK03918 468 LKEIEEKERKL----RKELRELEKVLKKESELI-KLKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKlKG 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386635304 908 RVKGI-SSAKgvSDEDTDEEKETLKNQLREMELELAQTKLQLV--------EAECKIQDLE 959
Cdd:PRK03918 540 EIKSLkKELE--KLEELKKKLAELEKKLDELEEELAELLKELEelgfesveELEERLKELE 598
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
722-974 |
3.51e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEdpIERFERENRRLQEANMRLEQENDDLAHELvtskIALRKDL 801
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEELRLEL----EELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 802 DNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTA 881
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 882 NKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAK-------GVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECK 954
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260
....*....|....*....|
gi 1386635304 955 IQDLEHHLGLALSEVQAAKK 974
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
739-898 |
4.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 739 KKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDdlAHELVTSKIALRKDLDNAEEKADALNKELlmt 818
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERL--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 819 kQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKnssiigDYKQICSQLsERLEKQQTANKVEIEKIRQKVDDCDR 898
Cdd:COG4717 156 -EELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEEL-EELQQRLAELEEELEEAQEELEELEE 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
784-959 |
2.00e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 784 DDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSSIIGD 863
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 864 -----YKQIC--SQLSERLEKQQTAnkveiekirqkvddcdrcrDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLRE 936
Cdd:COG3883 91 raralYRSGGsvSYLDVLLGSESFS-------------------DFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180
....*....|....*....|...
gi 1386635304 937 MELELAQTKLQLVEAECKIQDLE 959
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE 174
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
717-853 |
2.70e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 717 RYRSEENAKRLMELacntkisQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEAN----MRLEQENDDLAHELVT 792
Cdd:pfam15709 337 RLRAERAEMRRLEV-------ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIrlrkQRLEEERQRQEEEERK 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386635304 793 SKIALRKDLDNAEEKADALNKELLMTKQK-----LIDAEDEKRRLEEESAQLKEMCRRELDKAESE 853
Cdd:pfam15709 410 QRLQLQAAQERARQQQEEFRRKLQELQRKkqqeeAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE 475
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
734-985 |
3.01e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 734 TKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLahelvTSKIALRKdldnaeEKADALNK 813
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-----TKKISSLK------EKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 814 ELLMTKQKLIDAEDEKRRLEEESAqlKEMCRRELDKAESEIKK----NSSIIGDYKQIcSQLSERLEKQQTANKVEIEKI 889
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEElkqtQKSLKKKQEEK-QELIDQKEKEKKDLIKEIEEK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 890 RQKVDDCDRCRDFFNKEGrvKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHhlglALSEV 969
Cdd:TIGR04523 609 EKKISSLEKELEKAKKEN--EKLSSII----KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT----KIDDI 678
|
250
....*....|....*.
gi 1386635304 970 QAAKKTWFNRTLSSIK 985
Cdd:TIGR04523 679 IELMKDWLKELSLHYK 694
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
721-959 |
3.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLE--QENDDLAHELVTSKIALR 798
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 799 KDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELdkaeSEIKKNSSIIGDYKQICSQLsERLEKQ 878
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-EKRL----EELEERHELYEEAKAKKEEL-ERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 879 QTANkvEIEKIRQKVDDCDRCRDFFNKE--------GRVKGIS-----------SAKGV----SDEDTDEEKETLknqLR 935
Cdd:PRK03918 381 LTGL--TPEKLEKELEELEKAKEEIEEEiskitariGELKKEIkelkkaieelkKAKGKcpvcGRELTEEHRKEL---LE 455
|
250 260
....*....|....*....|....
gi 1386635304 936 EMELELAQTKLQLVEAECKIQDLE 959
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLR 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
711-895 |
3.57e-06 |
|
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: 50.89 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 711 RVQLpKRYRSEENAKRLMELACNTKI----SQKKLKKFEKEYHTMR-EQQAQQEDPIERFE----RENRRLQEANM---- 777
Cdd:pfam17380 382 RLQM-ERQQKNERVRQELEAARKVKIleeeRQRKIQQQKVEMEQIRaEQEEARQREVRRLEeeraREMERVRLEEQerqq 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 778 ---RLEQENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE-----SAQLKEMCRREldk 849
Cdd:pfam17380 461 qveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeerqKAIYEEERRRE--- 537
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1386635304 850 AESEIKKNSSiIGDYKQICSQLSERLEKQQTANKVEIEK--IRQKVDD 895
Cdd:pfam17380 538 AEEERRKQQE-MEERRRIQEQMRKATEERSRLEAMERERemMRQIVES 584
|
|
| PID |
pfam00640 |
Phosphotyrosine interaction domain (PTB/PID); |
79-194 |
3.96e-06 |
|
Phosphotyrosine interaction domain (PTB/PID);
Pssm-ID: 395515 Cd Length: 133 Bit Score: 47.36 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 79 YLGCASVNAPRSEVEALRMM----SILR-SQCQISLDVTLSVP---------NVSEGTVRLLDPQTNTEIANYPIYKILF 144
Cdd:pfam00640 5 YLGSVEVPEERAPDKNTRMQqareAIRRvKAAKINKIRGLSGEtgpgtkvdlFISTDGLKLLNPDTQELIHDHPLVSISF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1386635304 145 CVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 194
Cdd:pfam00640 85 CADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
735-974 |
4.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 735 KISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMR---LEQENDDLAHELVTSKIALRKDLDNAEEKADAL 811
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEELAELLKELEELGFESVEELEER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 812 NKELLMTKQKLIDAEDEKRRLEEESAQLKEmCRRELDKAESEIKKnssIIGDYKQICSQLSerlEKQQTANKVEIEKIRQ 891
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKK-LEEELDKAFEELAE---TEKRLEELRKELE---ELEKKYSEEEYEELRE 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 892 KvddcdrcrdFFNKEGRVKGIssakgvsdedtDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEhHLGLALSEVQA 971
Cdd:PRK03918 667 E---------YLELSRELAGL-----------RAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEE 725
|
...
gi 1386635304 972 AKK 974
Cdd:PRK03918 726 LRE 728
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
700-959 |
5.73e-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: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 700 LTDFEGALKFFRVQLPKRYRSEENakRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRL 779
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 780 EQENDDLAhelvtskialrKDLDNAEEKADALNKELlmtkqklidaEDEKRRLEEEsaQLKEMcRRELDKAESEIKKNSS 859
Cdd:TIGR02169 757 KSELKELE-----------ARIEELEEDLHKLEEAL----------NDLEARLSHS--RIPEI-QAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 860 IIGDYKQIcsqLSERLEKQQTANKvEIEKIRQKVDDCDRCRDFFNKEgrvkgissakgvsdedtdeeKETLKNQLREMEL 939
Cdd:TIGR02169 813 RLREIEQK---LNRLTLEKEYLEK-EIQELQEQRIDLKEQIKSIEKE--------------------IENLNGKKEELEE 868
|
250 260
....*....|....*....|
gi 1386635304 940 ELAQTKLQLVEAECKIQDLE 959
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLK 888
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
750-962 |
1.13e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 750 TMREQQAQQEDPIERFERENRRLQEANMRleqENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK 829
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQARNQNSMYMR---QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 830 RRLEEESAQLKEMCRR---ELDKAESEIkknssiigdykQICSQLSERLEKQQTANKVEIEKIRQKVDdcDRCRDFFNKE 906
Cdd:pfam15921 366 DQFSQESGNLDDQLQKllaDLHKREKEL-----------SLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386635304 907 GRVKGISSA---------KGVSDEDTDEEK--------ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHL 962
Cdd:pfam15921 433 ALLKAMKSEcqgqmerqmAAIQGKNESLEKvssltaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
731-970 |
1.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 731 ACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFErenrRLQEANMRLE--QENDDLAHELVTSKialRKDLDNAEEKA 808
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIErlEERREDLEELIAER---RETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 809 DALNKEllmtKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQtankvEIEK 888
Cdd:PRK02224 540 EELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED-----EIER 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 889 IRQKVDDCDRCRDffNKEGRVKGISSAKGVSDEDTDEEK-ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALS 967
Cdd:PRK02224 611 LREKREALAELND--ERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
...
gi 1386635304 968 EVQ 970
Cdd:PRK02224 689 ELE 691
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
714-962 |
1.70e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 714 LPKRYRSEENAKRLMElacntkisqKKLKKFEKEYHTMREQ----QAQQEDPIERFERENRRLQEANMRLEQENddlahe 789
Cdd:pfam01576 192 LEERLKKEEKGRQELE---------KAKRKLEGESTDLQEQiaelQAQIAELRAQLAKKEEELQAALARLEEET------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 790 lvTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE---------------SAQLKEMCRRE-----LDK 849
Cdd:pfam01576 257 --AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElealkteledtldttAAQQELRSKREqevteLKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 850 A-ESEIKKNSSIIGDYKQICSQ----LSERLEkQQTANKVEIEKIRQKVDdcdrcRDFFNKEGRVKGISSAKGvsdeDTD 924
Cdd:pfam01576 335 AlEEETRSHEAQLQEMRQKHTQaleeLTEQLE-QAKRNKANLEKAKQALE-----SENAELQAELRTLQQAKQ----DSE 404
|
250 260 270
....*....|....*....|....*....|....*...
gi 1386635304 925 EEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHL 962
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
738-959 |
1.96e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 738 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHElvtskialrkdLDNAEEKADALNKELLM 817
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ-----------RKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 818 TKQKLIDAEDEKRRLEEESAQL-KEMCRRELDKAESEIkknssiigdyKQICSQLSERLEKQQTaNKVEIEKIRQKVDDC 896
Cdd:COG4372 148 REEELKELEEQLESLQEELAALeQELQALSEAEAEQAL----------DELLKEANRNAEKEEE-LAEAEKLIESLPREL 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386635304 897 DRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 959
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
719-945 |
2.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 719 RSEENAKRLMELACNTKISQKK----LKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSK 794
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 795 iALRKDLDNAEEKADALNKEllmTKQKLIDAEDEKRRLEEESAQLKEMCRRELDK---AESEIKKNSSIIGDYKQICSQL 871
Cdd:PTZ00121 1706 -ELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkkiAHLKKEEEKKAEEIRKEKEAVI 1781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635304 872 SERLEKQQTANKVEIEKIRQKVDDcdrcrDFFN-KEGRVKG---ISSAKGVSDEDTDEEKETlKNQLREMELELAQTK 945
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFD-----NFANiIEGGKEGnlvINDSKEMEDSAIKEVADS-KNMQLEEADAFEKHK 1853
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
722-985 |
3.13e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENAK-RLMELACNTKISQKKLKKFEKEYHTMR-EQQAQQEDPI------ERFERENRRLQEANMRLEQENDDLAHELVTS 793
Cdd:pfam05483 481 EKEKlKNIELTAHCDKLLLENKELTQEASDMTlELKKHQEDIInckkqeERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 794 KIALRKDLDNAEEKADALNKELLMTKQKLIDAEDE----KRRLEEESAQLKemcrrELDKAESEIKKNSSiiGDYKQIcs 869
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnlKKQIENKNKNIE-----ELHQENKALKKKGS--AENKQL-- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 870 qlsERLEKQQTANKVEIEKIRQKVDDcdrCRDFFNKEGRVKGISS---------AKGVSDEDTDEEKET---LKNQLREM 937
Cdd:pfam05483 632 ---NAYEIKVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEeklleevekAKAIADEAVKLQKEIdkrCQHKIAEM 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1386635304 938 ELELAQTKLQLVEAeckIQDLEHHLGLALS--EVQAAKKTWFNRTLSSIK 985
Cdd:pfam05483 706 VALMEKHKHQYDKI---IEERDSELGLYKNkeQEQSSAKAALEIELSNIK 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
738-960 |
3.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 738 QKKLKKFEKEYHTMREQQAQQEDPIERFERE----NRRLQEANMRLEQENDDLAHELVTSKIA--------LRK---DLD 802
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEldalQERREALQRLAEYSWDEIDVASAEREIAeleaelerLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 803 NAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKK-----NSSIIGDYKQIC-----SQLS 872
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERFAAALgdaveRELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 873 ERLEKQQTANKVEIEKIRQKVddcDRCRDFFNKegRVKGISSAKGVSDEDTDEEKETLkNQLREMELELAQTKLQLVEAE 952
Cdd:COG4913 769 ENLEERIDALRARLNRAEEEL---ERAMRAFNR--EWPAETADLDADLESLPEYLALL-DRLEEDGLPEYEERFKELLNE 842
|
....*...
gi 1386635304 953 CKIQDLEH 960
Cdd:COG4913 843 NSIEFVAD 850
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
738-895 |
4.24e-05 |
|
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: 46.07 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 738 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEAnmrLEQENDDLAHelvtskiaLRKDLDNA--EEKADALNKEL 815
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKK--------YEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 816 LMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDD 895
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEE----ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
722-959 |
6.31e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENA-KRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKiALRKD 800
Cdd:PRK03918 161 ENAyKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 801 LDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQT 880
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386635304 881 ANKVEIEKIRQKVDDCDrcrdffNKEGRVKGISSAKgvsdEDTDEEKETLKNQLREMElELAQTKLQLVEAECKIQDLE 959
Cdd:PRK03918 318 RLEEEINGIEERIKELE------EKEERLEELKKKL----KELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLT 385
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
722-889 |
9.94e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENAKRLMELACNTKISQKKlKKFEKEYHTMREQQAQQEdpierferenRRLQEANMRLEQENDDLAHElvtskialRKDL 801
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKLE----------KRLLQKEENLDRKLELLEKR--------EEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 802 DNAEEKADALNKELLMTKQKLIDAEDEKR-RLEEESAQLKEMCRRE-LDKAESEIKKNSSIIgdYKQICSQLSERLEKQq 879
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLqELERISGLTAEEAKEIlLEKVEEEARHEAAVL--IKEIEEEAKEEADKK- 189
|
170
....*....|
gi 1386635304 880 tANKVEIEKI 889
Cdd:PRK12704 190 -AKEILAQAI 198
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
767-985 |
1.11e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 767 RENRRLQEANMRLEQENDDLAH---ELVTSKIALRKDLDNAEEKADALNK----------ELLMTKQKL-IDAEDEKRRL 832
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAEliiDLEELKLQELKLKEQAKKALEYYQLkekleleeeyLLYLDYLKLnEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 833 EEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEK----IRQKVDDCDRCRDFFNKEGR 908
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllklERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635304 909 V-KGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKKTWFNRTLSSIK 985
Cdd:pfam02463 326 AeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
738-898 |
1.33e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 738 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQenddlahelVTSKIALRKDLDNAEEKADALNKELLM 817
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE---------YLKEKAEREEEREAEREEIEEEKEREI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 818 TK--QKLIDAEDEKRRLEE------ESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKI 889
Cdd:pfam13868 187 ARlrAQQEKAQDEKAERDElraklyQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
....*....
gi 1386635304 890 RQKVDDCDR 898
Cdd:pfam13868 267 LRKQAEDEE 275
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
722-959 |
1.73e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENAKrlMELACNTKISQKKLKKFEKEYHTMREQQAQQEDP--IERFERENRrLQEANMRLEqENDDLAHELVTSKIALRK 799
Cdd:pfam05483 207 ENAR--LEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLllIQITEKENK-MKDLTFLLE-ESRDKANQLEEKTKLQDE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 800 DLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEE----------ESAQLKEMCRRELDKAESeikKNSSIIGDYKQICS 869
Cdd:pfam05483 283 NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKA---AHSFVVTEFEATTC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 870 QLSE-------RLEKQQTANKVEIEKIRQKVDDCDRCRDFF-NKEGRVKGISSAKGVSDEDTDEEK--ETLKNQLREMEL 939
Cdd:pfam05483 360 SLEEllrteqqRLEKNEDQLKIITMELQKKSSELEEMTKFKnNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQ 439
|
250 260
....*....|....*....|
gi 1386635304 940 ELAQTkLQLVEAEckIQDLE 959
Cdd:pfam05483 440 ELIFL-LQAREKE--IHDLE 456
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
721-895 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERE----NRRLQEANMRLEQENDDLAHELVTSKIA 796
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 797 LR-----------KDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKknssiigdyk 865
Cdd:COG3883 99 GGsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK-LAELEALKAELE---------- 167
|
170 180 190
....*....|....*....|....*....|
gi 1386635304 866 qicSQLSErLEKQQTANKVEIEKIRQKVDD 895
Cdd:COG3883 168 ---AAKAE-LEAQQAEQEALLAQLSAEEAA 193
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
711-839 |
2.03e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 711 RVQLPKRYRSEENAKRLMELacntKISQKKLKKFEKEYH-TMRE-QQAQQEDPIERFERENRRLQEANMRLEQENDDLAH 788
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQL----QAAQERARQQQEEFRrKLQElQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1386635304 789 ELVTSKIALRKDLDNAEEKAdalnkellmtkqkLIDAEdEKRRLEEESAQL 839
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEEKA-------------RLEAE-ERRQKEEEAARL 507
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
721-856 |
2.16e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMElacNTKISQKKLKKFEKEYHTMREQQAQQEdpierferenrrlQEAnmRLEQENDDLAHElvtskiALRKD 800
Cdd:PRK09510 86 QQQAEELQQ---KQAAEQERLKQLEKERLAAQEQKKQAE-------------EAA--KQAALKQKQAEE------AAAKA 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1386635304 801 LDNAEEKADALNKELLMTKQKlidAEDEKRRLEEESAQlkemcrrelDKAESEIKK 856
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKK---AAAEAKKKAEAEAA---------KKAAAEAKK 185
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
771-955 |
2.35e-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: 43.76 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 771 RLQEanmrLEQENDDLAHELVTskiaLRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKA 850
Cdd:COG1579 11 DLQE----LDSELDRLEHRLKE----LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA----RIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 851 ESEIKKnssiIGDYKQIcSQLSERLEKQQTANKVEIEKIRQKVDDCDrcrdffNKEGRVKGISSAKGVSDEDTDEEKETL 930
Cdd:COG1579 79 EEQLGN----VRNNKEY-EALQKEIESLKRRISDLEDEILELMERIE------ELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|....*
gi 1386635304 931 KNQLREMELELAQTKLQLVEAECKI 955
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
752-895 |
2.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 752 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVtskiALRKDLDNAE-EKADALNKELLmtkqkliDAEDEKR 830
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNGgDRLEQLEREIE-------RLERELE 355
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635304 831 RLEEESAQLKEMCRR---ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDD 895
Cdd:COG4913 356 ERERRRARLEALLAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
719-975 |
2.61e-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: 45.01 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 719 RSEENAKRLMELACNTKIsqKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALR 798
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKI--QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 799 ---KDLDNAEEKADALNKELLMTKQKLIDAEDEKRrlEEESAQLKEMCR---RELDKAESEIKKNSSIIGDYKQICSQLS 872
Cdd:TIGR04523 271 ekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKnqeKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 873 ERLEKQQTANKVEIEKIRQKVDdcdrcrdffnkegRVKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAE 952
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQN-------------EIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
250 260
....*....|....*....|...
gi 1386635304 953 CKIQDLEHHLGLALSEVQAAKKT 975
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKET 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
756-983 |
2.64e-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: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 756 AQQEDPIERFERENRRLQEanmRLEQENDDLAhELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE 835
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQ---EIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 836 SAQLkemcRRELDKAESEIKK------------------NSSIIGD-------YKQICSQLSERLEKQQtANKVEIEKIR 890
Cdd:COG4942 92 IAEL----RAELEAQKEELAEllralyrlgrqpplalllSPEDFLDavrrlqyLKYLAPARREQAEELR-ADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 891 QKVddcdrcrdffnkEGRVKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDL---EHHLGLALS 967
Cdd:COG4942 167 AEL------------EAERAELEALL----AELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIA 230
|
250
....*....|....*.
gi 1386635304 968 EVQAAKKTWFNRTLSS 983
Cdd:COG4942 231 RLEAEAAAAAERTPAA 246
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
738-847 |
2.86e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 43.54 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 738 QKKLKKFEKEYHTMREQQAQqedpiERFER--ENRRLQEANMRLEQENDDLA-HELVTSKIALRKdldNAEEKADALNKE 814
Cdd:pfam13904 75 QKEEREKEEQEAELRKRLAK-----EKYQEwlQRKARQQTKKREESHKQKAAeSASKSLAKPERK---VSQEEAKEVLQE 146
|
90 100 110
....*....|....*....|....*....|...
gi 1386635304 815 LLMTKQKLIDAEDEKRRLEEESAQLKEMCRREL 847
Cdd:pfam13904 147 WERKKLEQQQRKREEEQREQLKKEEEEQERKQL 179
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
767-948 |
3.19e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 767 RENRRLQEAnMRLEQENDDLAHELVTSKIAL--------RKDLDNAEEKADALNKELLMTKQKLidaEDEKRRLEEesaq 838
Cdd:PRK04863 240 RENRMTLEA-IRVTQSDRDLFKHLITESTNYvaadymrhANERRVHLEEALELRRELYTSRRQL---AAEQYRLVE---- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 839 lkemCRRELDkaesEIKKNSSIIG-DYkqicSQLSERLEKQQTANKVEiEKIRQKVDDCDRcrdffnKEGRvkgISSAKG 917
Cdd:PRK04863 312 ----MARELA----ELNEAESDLEqDY----QAASDHLNLVQTALRQQ-EKIERYQADLEE------LEER---LEEQNE 369
|
170 180 190
....*....|....*....|....*....|.
gi 1386635304 918 VSdEDTDEEKETLKNQLREMELELAQTKLQL 948
Cdd:PRK04863 370 VV-EEADEQQEENEARAEAAEEEVDELKSQL 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
753-960 |
4.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 753 EQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIAL-RKDLDNAEEKADALNKELLMTKQKLIDAEDEKRR 831
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 832 LEEESAQL----KEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEkqqtANKVEIEKIRQKVDDcdrcrdffnkeg 907
Cdd:COG4913 328 LEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLP----ASAEEFAALRAEAAA------------ 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1386635304 908 rvkgissakgvSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEH 960
Cdd:COG4913 392 -----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
721-991 |
4.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSK---IAL 797
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREeelKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 798 RKDLDNAEEKADALNKELlmtkqKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEK 877
Cdd:COG4372 156 EEQLESLQEELAALEQEL-----QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 878 QQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQD 957
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250 260 270
....*....|....*....|....*....|....
gi 1386635304 958 LEHHLGLALSEVQAAKKTWFNRTLSSIKTATGVQ 991
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
699-959 |
5.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 699 LLTDFEGALKFFRVQLpKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEanmr 778
Cdd:PRK02224 181 VLSDQRGSLDQLKAQI-EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 779 LEQENDDlahelvtskiaLRKDLDNAEEKADALnkellmtKQKLIDAEDEKRRLEEESAQLKEMCrrELDKAESEIkkns 858
Cdd:PRK02224 256 LEAEIED-----------LRETIAETEREREEL-------AEEVRDLRERLEELEEERDDLLAEA--GLDDADAEA---- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 859 siigdykqicsqLSERLEKQQTankvEIEKIRQKVDDCDRCRDFFNKEgrvkgissAKGVSDE--DTDEEKETLKNQLRE 936
Cdd:PRK02224 312 ------------VEARREELED----RDEELRDRLEECRVAAQAHNEE--------AESLREDadDLEERAEELREEAAE 367
|
250 260
....*....|....*....|...
gi 1386635304 937 MELELAQTKLQLVEAECKIQDLE 959
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELE 390
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
773-895 |
5.41e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 773 QEANMRLEQENDDLaHELVTSKIALRKDLDNAEEKADALNKEllmtkqklidAEDEKRRLEEESAQLKEMCRRELDKAES 852
Cdd:PRK00409 505 EEAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKE----------AEKLKEELEEKKEKLQEEEDKLLEEAEK 573
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1386635304 853 EIKKnssIIGDYK----QICSQLSERLEKQQTANKV-EIEKIRQKVDD 895
Cdd:PRK00409 574 EAQQ---AIKEAKkeadEIIKELRQLQKGGYASVKAhELIEARKRLNK 618
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
691-961 |
5.63e-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: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 691 LKTSKDdlLLTDFeGALKFFRVQLpkryrsEENAKRLMELAcnTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENR 770
Cdd:TIGR00606 781 EESAKV--CLTDV-TIMERFQMEL------KDVERKIAQQA--AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 771 RLQEANMRLEQENDDLAHELVTSKIALRKDLDNA---EEKADALNKELLMTKQKLIDAEDE-------KRRLEEESAQLK 840
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQdspletfLEKDQQEKEELI 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 841 EMCRRELDKAESEI----KKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAK 916
Cdd:TIGR00606 930 SSKETSNKKAQDKVndikEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1386635304 917 GVSDEDTDEEKETL---KNQLREMELELAQTKLQLVEAECKIQDLEHH 961
Cdd:TIGR00606 1010 QKIQERWLQDNLTLrkrENELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
|
| PTB_LDLRAP-mammal-like |
cd13159 |
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ... |
76-177 |
6.96e-04 |
|
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges.
Pssm-ID: 269981 Cd Length: 123 Bit Score: 40.39 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 76 KLTYLGCASVNAPRSE---VEALR-MMSILRSQCQISLDVTLsvpNVSEGTVRLLDPQTNTEIANYPIYKILFCV--RGH 149
Cdd:cd13159 6 YLKYLGSTLVEKPKGEgatAEAVKtIIAMAKASGKKLQKVTL---TVSPKGIKVTDSATNETILEVSIYRISYCTadANH 82
|
90 100
....*....|....*....|....*...
gi 1386635304 150 DgtpesDCFAFTESHYNAELFRIHVFRC 177
Cdd:cd13159 83 D-----KVFAFIATNQDNEKLECHAFLC 105
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
762-861 |
7.58e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 762 IERFERENRRLQEANMRLEQENDDLAHELVTskiALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKE 841
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLA---ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|
gi 1386635304 842 McRRELDKAESEIKKNSSII 861
Cdd:COG0542 490 L-EKELAELEEELAELAPLL 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
722-974 |
7.60e-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: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQeanmrleQENDDLA------HELVTSKI 795
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ-------QELDDLLvdldhqRQLVSNLE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 796 ALRKDLDN--AEEK--------------ADALNKE--LLMTKQKLIDAEDEKRRLEEESAQLK----------------- 840
Cdd:pfam01576 601 KKQKKFDQmlAEEKaisaryaeerdraeAEAREKEtrALSLARALEEALEAKEELERTNKQLRaemedlvsskddvgknv 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 841 ---EMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEkirqkvddcdrcRDFFNKegrvkgissakg 917
Cdd:pfam01576 681 helERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE------------RDLQAR------------ 736
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386635304 918 vsDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKK 974
Cdd:pfam01576 737 --DEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK 791
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
792-989 |
7.76e-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: 43.51 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 792 TSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDYKQICSQL 871
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 872 SERLEKQQTANKVEIEKIRQKVDDcdrcrdffnkegrvkgiSSAKGVSDEdtdEEKETLKNQLREMELELAQTKLQLVEA 951
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEE-----------------AEEELAEAE---AEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1386635304 952 ECKIQDLEHHLGLALSEVQ------AAKKTWFNRTLSSIKTATG 989
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLEslerriAATERRLEDLEEQIEELSE 852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
719-959 |
8.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 719 RSEENAKRLMELACNTKISQKKLKKFEK--EYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIA 796
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 797 lrKDLDNAEE--KADALNKELLMTKQKLIDAEDEKRRLEEEsaqlKEMCRRELDKA-ESEIKKNSSIIGDYKQICSQLSE 873
Cdd:PTZ00121 1537 --DEAKKAEEkkKADELKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 874 RLEKQQTAnKVEIEKIRqkvddcdrcrdffnKEGRVKGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAEC 953
Cdd:PTZ00121 1611 EAKKAEEA-KIKAEELK--------------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
....*.
gi 1386635304 954 KIQDLE 959
Cdd:PTZ00121 1676 KAEEAK 1681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-881 |
8.52e-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: 43.51 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 700 LTDFEGALKFFRVQLPKRYRSEENAKRLMELAcntkisQKKLKKFEKEYHTMREQQAQQ-------EDPIERFERENRRL 772
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEEL------EEQLETLRSKVAQLELQIASLnneierlEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 773 QEANMRLEQENDDLAHELVTSKIA--------LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCR 844
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEeleeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
170 180 190
....*....|....*....|....*....|....*....
gi 1386635304 845 RE--LDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTA 881
Cdd:TIGR02168 500 NLegFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAA 538
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
722-948 |
8.96e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 722 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEdpIERFERENRRLQEANMRLEQENDDLA--------HELVTS 793
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE--INKSINEYNKIESARADLEDIKIKINelkdkhdkYEEIKN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 794 KIAlRKDLDNAEEKADALNKelLMTKQKLIDAEDEKRRLEEESAQLKEMCRReLDKAESEIKKNSSIIGDY-KQICSQLS 872
Cdd:PRK01156 554 RYK-SLKLEDLDSKRTSWLN--ALAVISLIDIETNRSRSNEIKKQLNDLESR-LQEIEIGFPDDKSYIDKSiREIENEAN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635304 873 --ERLEKQQTANKVEIEKIRQKVDDcdrcrdfFNKEgrvkgISSAKGVSDedtdeEKETLKNQLREMELELAQTKLQL 948
Cdd:PRK01156 630 nlNNKYNEIQENKILIEKLRGKIDN-------YKKQ-----IAEIDSIIP-----DLKEITSRINDIEDNLKKSRKAL 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
721-898 |
1.12e-03 |
|
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: 42.44 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIerfERENRRLQEANMRLEQENDDLAhELVTSKIALRKD 800
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAALEAELA-ELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 801 LD--------------------------NAEEKADALN-----KELLMTKQKLIDA-EDEKRRLEEESAQLKEMcRRELD 848
Cdd:COG4942 99 LEaqkeelaellralyrlgrqpplalllSPEDFLDAVRrlqylKYLAPARREQAEElRADLAELAALRAELEAE-RAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1386635304 849 KAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDR 898
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
756-952 |
1.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 756 AQQEDPIERFERENRRLQEANMRLEQENDDLAHelvtskiaLRKDLDNAEEKADALNKelLMTKQKLIDAEDEKRRLEEE 835
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQ--------QRSQLEQAKEGLSALNR--LLPRLNLLADETLADRVEEI 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 836 SAQLKEmcrreLDKAESEIKKNSSIIGDYKQICSQLS------ERLEKQQTANKVEIEKIRQKVD---DCDRCRDFFNKE 906
Cdd:PRK04863 900 REQLDE-----AEEAKRFVQQHGNALAQLEPIVSVLQsdpeqfEQLKQDYQQAQQTQRDAKQQAFaltEVVQRRAHFSYE 974
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386635304 907 GRVKGISsakgvsdeDTDEEKETLKNQLREMELELAQTKLQLVEAE 952
Cdd:PRK04863 975 DAAEMLA--------KNSDLNEKLRQRLEQAEQERTRAREQLRQAQ 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
770-979 |
1.35e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 770 RRLQEANMRLEqENDDLAHELVTSKIALRKDLDNAEE----KADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrr 845
Cdd:COG1196 179 RKLEATEENLE-RLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEA---- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 846 ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDffnKEGRVKGISSAKGVSDEDTDE 925
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEE 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1386635304 926 EKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKKTWFNR 979
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
743-895 |
1.45e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.53 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 743 KFEKEYHTMREQQAQQEDPIERFERENrrLQEANMRLEQENDDL---------AHELVTSKIA-LRKDLDNAEEKADALN 812
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLELDE--AEEALEEIEERIDQLydllekevdAKKYVEKNLPeIEDYLEHAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 813 KELLMTKQKLIDAEDEK---RRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQtankveiEKI 889
Cdd:pfam06160 312 EELERVQQSYTLNENELervRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE-IEEEQ-------EEF 383
|
....*.
gi 1386635304 890 RQKVDD 895
Cdd:pfam06160 384 KESLQS 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
708-946 |
1.48e-03 |
|
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: 42.42 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 708 KFFRVQLPKRYRSEENAKRLMElacntkiSQKKLKKFEKEYHTMREQQA-----QQEDPIERfERENRRLQEANMRLEQE 782
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVE-------RRRKLEEAEKARQAEMDRQAaiyaeQERMAMER-ERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 783 ---NDDLAHELVTSKIALRKDLDNaEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKnss 859
Cdd:pfam17380 364 rirQEEIAMEISRMRELERLQMER-QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR--- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 860 iigdYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSA--KGVSDEDTDEEKETL-----KN 932
Cdd:pfam17380 440 ----LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEqrRKILEKELEERKQAMieeerKR 515
|
250
....*....|....
gi 1386635304 933 QLREMELELAQTKL 946
Cdd:pfam17380 516 KLLEKEMEERQKAI 529
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
803-986 |
1.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 803 NAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQL---KEMCRRELDKAESEIkknssiigDYKQICSQLsERLEKQQ 879
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerREALQRLAEYSWDEI--------DVASAEREI-AELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 880 ---TANKVEIEKIRQKVDDCdrcrdffnkEGRVKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKI- 955
Cdd:COG4913 678 erlDASSDDLAALEEQLEEL---------EAELEELEEEL----DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAr 744
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386635304 956 ----QDLEHHLG-LALSEVQAAKKTWFNRTLSSIKT 986
Cdd:COG4913 745 lelrALLEERFAaALGDAVERELRENLEERIDALRA 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
798-959 |
1.84e-03 |
|
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: 42.36 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 798 RKDLDNAEEK---ADALNKELLMTKQKLidaEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIgdyKQICSQLSEr 874
Cdd:TIGR02169 176 LEELEEVEENierLDLIIDEKRQQLERL---RREREKAERYQALLKEKREYEGYELLKEKEALERQK---EAIERQLAS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 875 LEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGissakgvsdedtDEEKETLKNQLREMELELAQTKLQLVEAECK 954
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------------EEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
....*
gi 1386635304 955 IQDLE 959
Cdd:TIGR02169 317 LEDAE 321
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
796-974 |
1.85e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 796 ALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK----------RRLEEESAQLKEMcRRELDKAESEIKKNSSiigdyk 865
Cdd:pfam12795 41 AYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleQRLLQTSAQLQEL-QNQLAQLNSQLIELQT------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 866 qicsqLSERLEKQQTANKVEIEKIRQKVDdcdrcrdffNKEGRVKGISSAKGVSDEdTDEEKETLKNQLREMEL------ 939
Cdd:pfam12795 114 -----RPERAQQQLSEARQRLQQIRNRLN---------GPAPPGEPLSEAQRWALQ-AELAALKAQIDMLEQELlsnnnr 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386635304 940 -ELAQTKLQLVEAecKIQDLEHHLgLALSEVQAAKK 974
Cdd:pfam12795 179 qDLLKARRDLLTL--RIQRLEQQL-QALQELLNEKR 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
716-898 |
1.97e-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: 42.35 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 716 KRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnddlAHELVTSKI 795
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA----LALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 796 ALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEM-------------------------CRRELDKA 850
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltleeaealenkieddeeeARRRLKRL 977
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1386635304 851 ESEIKK----NSSIIGDYKqicsQLSERLE--KQQTANKVE-IEKIRQKVDDCDR 898
Cdd:TIGR02168 978 ENKIKElgpvNLAAIEEYE----ELKERYDflTAQKEDLTEaKETLEEAIEEIDR 1028
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
709-895 |
2.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 709 FFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQedpiERFERENRRLQEANMRLEQENddlah 788
Cdd:PRK12705 20 VLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQR----QEARREREELQREEERLVQKE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 789 elvtskialrKDLDNAEEKADALNKELLMTKQKLIDAEDEkrrLEEESAQLKEMCRRELDKAESEIKknssiigdyKQIC 868
Cdd:PRK12705 91 ----------EQLDARAEKLDNLENQLEEREKALSARELE---LEELEKQLDNELYRVAGLTPEQAR---------KLLL 148
|
170 180
....*....|....*....|....*..
gi 1386635304 869 SQLSERLEKQQTankVEIEKIRQKVDD 895
Cdd:PRK12705 149 KLLDAELEEEKA---QRVKKIEEEADL 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
743-880 |
2.42e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 743 KFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQE----NDDLAheLVTSKIALRKDLDNAEEKADALNKELlmt 818
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLN--LVQTALRQQEKIERYQEDLEELTERL--- 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386635304 819 kqklidaeDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQicsqlseRLEKQQT 880
Cdd:COG3096 364 --------EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ-------ALDVQQT 410
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
702-965 |
3.13e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 702 DFEGALKFFRVQLPKRYRS-EENAKRLMELACNTKISQK----------KLKKFEKEYHTMREQQAQQEDPIERFERE-- 768
Cdd:pfam12128 416 DLQALESELREQLEAGKLEfNEEEYRLKSRLGELKLRLNqatatpelllQLENFDERIERAREEQEAANAEVERLQSElr 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 769 ---------NRRLQEANMRLEQ---ENDDLAHEL-------------------------VTSKIALRKDLD---NAEEKA 808
Cdd:pfam12128 496 qarkrrdqaSEALRQASRRLEErqsALDELELQLfpqagtllhflrkeapdweqsigkvISPELLHRTDLDpevWDGSVG 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 809 DALNKELLMTKQKLIDAEdekrrleeESAQLKEMCRRELDKAESEIKKNSSIIgdykqicsqlsERLEKQQTANKVEIEK 888
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVP--------EWAASEEELRERLDKAEEALQSAREKQ-----------AAAEEQLVQANGELEK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 889 IRQKVDDCDRCrdFFNKEGRVKGISsakgvsdedtdEEKETLK---NQLREMELELAQTKLQLVEAECKIQDLEHHLGLA 965
Cdd:pfam12128 637 ASREETFARTA--LKNARLDLRRLF-----------DEKQSEKdkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLE 703
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
735-893 |
3.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 735 KISQKKLKKFEKEYHTMREQQAQQEDPIERferENRRLQEANMRLEQENDDlahelvtskiaLRKDLDNAEEKADALNKE 814
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEE-----------LEAELEEKDERIERLERE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 815 LLMTKQKL---IDAEDEKRRLEEESAQLkemcRRELDKAESEIKKnssiigdykqicsqLSERLEKQQTANKVEI--EKI 889
Cdd:COG2433 450 LSEARSEErreIRKDREISRLDREIERL----ERELEEERERIEE--------------LKRKLERLKELWKLEHsgELV 511
|
....
gi 1386635304 890 RQKV 893
Cdd:COG2433 512 PVKV 515
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
745-853 |
3.59e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 745 EKEYHTMREQQAQQedpI---ERFERENRRLQE--------ANMRLEQENDDLAHELVTSKI-------ALRKDLDNAEE 806
Cdd:COG1842 36 EEDLVEARQALAQV---IanqKRLERQLEELEAeaekweekARLALEKGREDLAREALERKAeleaqaeALEAQLAQLEE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1386635304 807 KADALNKELLMTKQKLIDAEDEKRRL--EEESAQLKEMCRRELDKAESE 853
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSGIDSD 161
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
719-931 |
4.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 719 RSEENAKRLMELACNTKI---SQKKLKKFEKEYHTMREQQAQQEDPIERFErENRRLQEANMRLEQEN-DDLAHELVTSK 794
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAE-EKKKADEAKKAEEKKKaDEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 795 IA--LRKDLDNAEEKADALNKELLMTKQKlidaeDEKRRLEEESAqlkemcRRELDKAESEIKKNSSIIGDYKQICSQLS 872
Cdd:PTZ00121 1316 KAdeAKKKAEEAKKKADAAKKKAEEAKKA-----AEAAKAEAEAA------ADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386635304 873 ERLEKQQTAN--KVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLK 931
Cdd:PTZ00121 1385 KKAEEKKKADeaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
687-854 |
4.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 687 ALGLLKTSKDDLLLTDFEGAlkffrVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQedpIERFE 766
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRI-----EELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ---AEEYQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 767 RENRRLQEANMRLEQENDDLAHELVTSkialrkDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcRRE 846
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEAL------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGE 470
|
....*...
gi 1386635304 847 LDKAESEI 854
Cdd:COG4717 471 LAELLQEL 478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
711-940 |
4.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 711 RVQLPKRYRSEENAKRLMEL--ACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDlAH 788
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-AE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 789 ELVTSKIALRKDLDNAEEKADALNKEllmtkqklidaEDEKRRLEeesaQLKEMCRRELDKAESEIKKNSSIIGDYKQIC 868
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAE----ELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386635304 869 SQLSERLEKQQTANKVEIEKirQKVDDCDRCRDFFNKEGRvkgiSSAKGVSDEDTDEEKETlknqlREMELE 940
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEK--KKIAHLKKEEEKKAEEIR----KEKEAVIEEELDEEDEK-----RRMEVD 1797
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
716-965 |
5.02e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.22 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 716 KRYRSE---ENAKRLM-ELACNTKISQ----KKLKKFEKEYHTMREQQAQQedpIERFERENRRLQEANMRLEQENDDLA 787
Cdd:pfam03148 15 QRNDAErlrQESRRLRnETDAKTKWDQydsnRRLGERIQDITFWKSELEKE---LEELDEEIELLLEEKRRLEKALEALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 788 H-ELVTSK-IALRK-----DL--DNAEEkadALNKEL--------LMtKQKLIDAEDEKRRLEEesaqLKEMCRREL-DK 849
Cdd:pfam03148 92 EpLHIAQEcLTLREkrqgiDLvhDEVEK---ELLKEVeliegiqeLL-QRTLEQAWEQLRLLRA----ARHKLEKDLsDK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 850 AES--------EIKKNSSIIGDY-------KQICS------------QLSERlEKQQTAN-KVEIEKIRQKVDD-----C 896
Cdd:pfam03148 164 KEAleidekclSLNNTSPNISYKpgptripPNSSTpeewekftqdniERAEK-ERAASAQlRELIDSILEQTANdlraqA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386635304 897 DRCRDFFNKegRVkgissakgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLA 965
Cdd:pfam03148 243 DAVNFALRK--RI-----------EETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLA 298
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
742-894 |
5.29e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 742 KKFEKEYHTMREQQAQQEDPIERFERENrrLQEANMRLEQENDDL---------AHELVTSKIA-LRKDLDNAEEKADAL 811
Cdd:PRK04778 252 LDIEKEIQDLKEQIDENLALLEELDLDE--AEEKNEEIQERIDQLydilerevkARKYVEKNSDtLPDFLEHAKEQNKEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 812 NKELLMTKQKLIDAEDEK---RRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQtankveiEK 888
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE-IEKEQ-------EK 401
|
....*.
gi 1386635304 889 IRQKVD 894
Cdd:PRK04778 402 LSEMLQ 407
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
744-959 |
7.60e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 744 FEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLahelvtskialrkdldnaEEKADALNKELLMTKQKLI 823
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL------------------REEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 824 DAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSsiigDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDff 903
Cdd:PRK02224 381 DRREEIEELEEEIEELRE----RFGDAPVDLGNAE----DFLEELREERDELREREAELEATLRTARERVEEAEALLE-- 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635304 904 nkEGR-------VKGISSAKGVSD-----EDTDEEKETLKNQLREMELELAQTKlQLVEAECKIQDLE 959
Cdd:PRK02224 451 --AGKcpecgqpVEGSPHVETIEEdrervEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLE 515
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
735-954 |
7.90e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 735 KISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALrKDLDNAEEKADALNKE 814
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESAKVCLTD 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 815 LLMTKQKLIDAEDEKRRLEEESAQL---------------KEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQ 879
Cdd:TIGR00606 791 VTIMERFQMELKDVERKIAQQAAKLqgsdldrtvqqvnqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 880 TaNKVEI-----------EKIRQKVDDCDRC-RDFFNKEGRVKGISSAKgvsdEDTDEEKETLKNQlREMELELAQTKLQ 947
Cdd:TIGR00606 871 S-EKLQIgtnlqrrqqfeEQLVELSTEVQSLiREIKDAKEQDSPLETFL----EKDQQEKEELISS-KETSNKKAQDKVN 944
|
....*..
gi 1386635304 948 LVEAECK 954
Cdd:TIGR00606 945 DIKEKVK 951
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
801-892 |
8.45e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 801 LDNAEEKADALNKE-LLMTKQKLI----DAEDE-KRRLEEESAQLKEMCRRE--LDKAESEIKKNSSIIGDYKQICSQLS 872
Cdd:PRK12704 44 LEEAKKEAEAIKKEaLLEAKEEIHklrnEFEKElRERRNELQKLEKRLLQKEenLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100
....*....|....*....|
gi 1386635304 873 ERLEKQQTankvEIEKIRQK 892
Cdd:PRK12704 124 QELEKKEE----ELEELIEE 139
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
670-982 |
8.69e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 670 HIIDLLLCEGISVIFNVALGLLKTSKDDLLLTDFEGALKFFRVQLPKRYRSEENAKRLMELACNTKISQ-----KKLKKF 744
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKLKAQ 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 745 EKEyhtMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALRKDLDNAEEKADALN----------KE 814
Cdd:pfam02463 800 EEE---LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITkeellqelllKE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 815 LLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVD 894
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 895 DCDRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREmELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKK 974
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE-RLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNK 1035
|
....*...
gi 1386635304 975 TWFNRTLS 982
Cdd:pfam02463 1036 VFFYLELG 1043
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
711-988 |
8.78e-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: 39.95 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 711 RVQLPKRYRSEEnakrlMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFEREnRRLQEANMRLEQEnddlAHEL 790
Cdd:TIGR00618 196 AELLTLRSQLLT-----LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQL----LKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 791 VTSkialrkdldnaEEKADALNKELLMTkQKLIDAEDEKRRLEEESAQLKEmCRRELDKAESEIK----KNSSIIGDYKQ 866
Cdd:TIGR00618 266 RAR-----------IEELRAQEAVLEET-QERINRARKAAPLAAHIKAVTQ-IEQQAQRIHTELQskmrSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 867 ICSQLSERLEKQQTANKVEIEkirqkvddCDRCRDFFNKEGRVKGISSA---------KGVSDEDTDEEKETLKNQLREM 937
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQ--------EIHIRDAHEVATSIREISCQqhtltqhihTLQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1386635304 938 ELELAQTKLQLVEAEckiQDLEHHLGLALSEVQAAKKTWFNRTLSSIKTAT 988
Cdd:TIGR00618 405 LQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
721-974 |
8.88e-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: 40.16 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 721 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQ----EDPIERFERENRRLQEANMRLEQENDDLAHELvtskia 796
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQAleelTEQLEQAKRNKANLEKAKQALESENAELQAEL------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 797 lrkdldnaeekadalnKELLMTKQkliDAEDEKRRLEeesAQLKEMCRReldKAESEIKKNssiigdykqicsQLSERLE 876
Cdd:pfam01576 394 ----------------RTLQQAKQ---DSEHKRKKLE---GQLQELQAR---LSESERQRA------------ELAEKLS 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 877 KQQTankvEIEKIRQKVDDCDRcrdffnkegrvKGISSAKGVSD-----EDTDE-------EKETLKNQLREMELELAQT 944
Cdd:pfam01576 437 KLQS----ELESVSSLLNEAEG-----------KNIKLSKDVSSlesqlQDTQEllqeetrQKLNLSTRLRQLEDERNSL 501
|
250 260 270
....*....|....*....|....*....|
gi 1386635304 945 KLQLVEAECKIQDLEHHLGLALSEVQAAKK 974
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
797-959 |
9.74e-03 |
|
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: 40.00 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 797 LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKemcrrelDKAESEIKKNSSIIGDYKQICSQLSERLE 876
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 877 kQQTANKVEIEKIRQKVDDCDRCRDFFNKE-GRVKGISSAKGVSDEDTDEEKETLKNQLREMELE-------LAQTKLQL 948
Cdd:TIGR04523 118 -QKNKLEVELNKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEklniqknIDKIKNKL 196
|
170
....*....|.
gi 1386635304 949 VEAECKIQDLE 959
Cdd:TIGR04523 197 LKLELLLSNLK 207
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
750-892 |
9.78e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.55 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635304 750 TMREQQAQQEDPIERFERENRRLQEANMRLEQENDdlahelvtskialRKDLDNAEEKADALNKELLMTKQKLIDA-EDE 828
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQ-------------RRLQQEQLERAEKMREELELEQQRRFEEiRLR 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386635304 829 KRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQK 892
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL-QRKKQQEEAERAEAEKQRQK 455
|
|
| |
