|
Name |
Accession |
Description |
Interval |
E-value |
| PTB_Rab6GAP |
cd01211 |
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ... |
140-268 |
3.82e-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: 3.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 140 VVFNKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGTVRLLDPQTNTEIANYPIYKILFCVRGHDG 219
Cdd:cd01211 1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1386635396 220 TPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQ 268
Cdd:cd01211 81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
558-767 |
1.08e-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: 234.51 E-value: 1.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 558 VRSGVPEALRGEVWQLLAGCHNNDH--LVEKYRILITKESPQD----SAITRDINRTFPAHDYFKDTGGDGQDSLYKICK 631
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLKETAPDDksivHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 632 AYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLReLFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLD 710
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386635396 711 ISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLL 767
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 ... |
564-767 |
1.32e-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: 221.36 E-value: 1.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 564 EALRGEVWQllagchnndhlvekyrilitkespqdSAITRDINRTFPAHDYFKDtgGDGQDSLYKICKAYSVYDEEIGYC 643
Cdd:pfam00566 1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 644 QGQSFLAAVLLL-HMPEEQAFSVLVKIMFDYGLRELFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQW 722
Cdd:pfam00566 53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386635396 723 FLTLFTAKFPLYMVFHIIDLLLCEGISV-IFNVALGLLKTSKDDLL 767
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
530-775 |
1.36e-49 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 183.85 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 530 EKILETWGELL-SKWHLNLSVRPKQLSSLVRSGVPEALRGEVWQLLAG-------CHNNDHLVEKYRILITKESPQD-SA 600
Cdd:COG5210 180 LAADKLWISYLdPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGigfdldkNPGLYERLLNLHREAKIPTQEIiSQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 601 ITRDINRTFPAHDYFKDTGGDGQDSLYKICKAYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLRELF 679
Cdd:COG5210 260 IEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 680 KQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLL 759
Cdd:COG5210 340 LKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAIL 419
|
250
....*....|....*.
gi 1386635396 760 KTSKDDLLLTDFEGAL 775
Cdd:COG5210 420 KLLRDKLLKLDSDELL 435
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
302-432 |
1.60e-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: 129.24 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 302 FSAVPKDK----DRQCFKLRQGIDKKIVICVQQTANKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 373
Cdd:pfam12473 2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635396 374 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 432
Cdd:pfam12473 72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
|
|
| PTB |
smart00462 |
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
138-271 |
3.40e-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: 110.48 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 138 DSVVFNKLTYLGCASVNAPRSEVEALR-MMSILRSQCQISLDVTLSVPNVSEGTVRLLDPQTNTEIANYPIYKILFCVRG 216
Cdd:smart00462 1 GSGVSFRVKYLGSVEVPEARGLQVVQEaIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386635396 217 HDGtpeSDCFAFTESHYNAELFRIHVFRCEI--QEAVSRILYSFATAFRRSAKQTPL 271
Cdd:smart00462 81 PDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKARSE 134
|
|
| PTB |
cd00934 |
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ... |
144-262 |
8.26e-18 |
|
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: 80.25 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 144 KLTYLGCASVNAPR----SEVEALRMMSILRSQCQISLDVTLsvpNVSEGTVRLLDPQTNTEIANYPIYKILFCVRGHDg 219
Cdd:cd00934 4 QVKYLGSVEVGSSRgvdvVEEALKALAAALKSSKRKPGPVLL---EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1386635396 220 tpESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAF 262
Cdd:cd00934 80 --NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
784-1027 |
4.38e-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: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 784 KRYRSEENAKRLMELAcntkISQKKLKKFEKEYHTMREQQAQQEDPIERFERE-----------NRRLQEANMRLEQEND 852
Cdd:TIGR02168 213 ERYKELKAELRELELA----LLVLRLEELREELEELQEELKEAEEELEELTAElqeleekleelRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 853 DL------AHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLK---EMCRRELDKAESEIK 923
Cdd:TIGR02168 289 ELyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 924 KNSSIIGDYKQICSQLSER---LEKQQTANKVEIEKIRQKVDDCDRCRDFF--NKEGRVKGISSAK----GVSDEDTDEE 994
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLqqEIEELLKKLEEAElkelQAELEELEEE 448
|
250 260 270
....*....|....*....|....*....|...
gi 1386635396 995 KETLKNQLREMELELAQTKLQLVEAECKIQDLE 1027
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
781-1042 |
3.98e-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: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 781 QLPKRYRSEENAKRLMELacntkisQKKLKKFEKEYHTMReqqaqqedpIERFERENRRLQEANMRLEQENDDLAHELVT 860
Cdd:TIGR02168 201 QLKSLERQAEKAERYKEL-------KAELRELELALLVLR---------LEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 861 SKIA---LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKemcrRELDKAESEIKKNSSIIGDYKQICS 937
Cdd:TIGR02168 265 LEEKleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE----RQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 938 QLSERLEKQQtankVEIEKIRQKVDDcdRCRDFFNKEGRVkgissakgvsdEDTDEEKETLKNQLREMELELAQTKLQLV 1017
Cdd:TIGR02168 341 ELEEKLEELK----EELESLEAELEE--LEAELEELESRL-----------EELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260
....*....|....*....|....*
gi 1386635396 1018 EAECKIQDLEHHLGLALSEVQAAKK 1042
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
806-1041 |
1.49e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 806 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELvtskIALRKDLDNAEEKADALNKELLM 885
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 886 TKQKLIDAE----DEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQIcsqlsERLEKQQTANKVEIEKIRQkv 961
Cdd:COG1196 349 AEEELEEAEaelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-----EELEEAEEALLERLERLEE-- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 962 ddcdrcrdffNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREmELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAK 1041
Cdd:COG1196 422 ----------ELEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
789-909 |
5.47e-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: 55.31 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMELacntkisQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnddlAHELVTSKIALRKD 868
Cdd:pfam20492 2 EEAEREKQEL-------EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQK----RQEAEEEKERLEES 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1386635396 869 LDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKE 909
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQE 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
773-1038 |
6.73e-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: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 773 GALKFFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnd 852
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 853 dlaHELVTSKIA-LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMC---RRELDKAESEIKKNSSI 928
Cdd:TIGR02168 742 ---VEQLEERIAqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 929 IGDYKQICSQLS----------ERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEgrVKGISSAKGVSDEDTD---EEK 995
Cdd:TIGR02168 819 AANLRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALAllrSEL 896
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1386635396 996 ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQ 1038
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
760-1027 |
2.55e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 760 KTSKDDLLLTDFEGALKFFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQED--------PIE 831
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltglTPE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 832 RFERENRRLQEANMRLEQENDDLAHEL--VTSKIALRKD----LDNAEEKADALNKEL-------LMTK--QKLIDAEDE 896
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIgeLKKEIKELKKaieeLKKAKGKCPVCGRELteehrkeLLEEytAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 897 KRRLEEESAQLkemcRRELDKAESEIKKNSSIIgDYKQICSQLSERLEKqqtANKVEIEKIRQKVDDCDRCRDFFNK-EG 975
Cdd:PRK03918 468 LKEIEEKERKL----RKELRELEKVLKKESELI-KLKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKlKG 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386635396 976 RVKGI-SSAKgvSDEDTDEEKETLKNQLREMELELAQTKLQLV--------EAECKIQDLE 1027
Cdd:PRK03918 540 EIKSLkKELE--KLEELKKKLAELEKKLDELEEELAELLKELEelgfesveELEERLKELE 598
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
790-1042 |
3.36e-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: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEdpIERFERENRRLQEANMRLEQENDDLAHELvtskIALRKDL 869
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEELRLEL----EELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 870 DNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTA 949
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 950 NKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAK-------GVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECK 1022
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260
....*....|....*....|
gi 1386635396 1023 IQDLEHHLGLALSEVQAAKK 1042
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
807-966 |
3.48e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 807 KKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDdlAHELVTSKIALRKDLDNAEEKADALNKELlmt 886
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERL--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 887 kQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKnssiigDYKQICSQLsERLEKQQTANKVEIEKIRQKVDDCDR 966
Cdd:COG4717 156 -EELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEEL-EELQQRLAELEEELEEAQEELEELEE 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
789-1027 |
2.51e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLE--QENDDLAHELVTSKIALR 866
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 867 KDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELdkaeSEIKKNSSIIGDYKQICSQLsERLEKQ 946
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-EKRL----EELEERHELYEEAKAKKEEL-ERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 947 QTANkvEIEKIRQKVDDCDRCRDFFNKE--------GRVKGIS-----------SAKGV----SDEDTDEEKETLknqLR 1003
Cdd:PRK03918 381 LTGL--TPEKLEKELEELEKAKEEIEEEiskitariGELKKEIkelkkaieelkKAKGKcpvcGRELTEEHRKEL---LE 455
|
250 260
....*....|....*....|....
gi 1386635396 1004 EMELELAQTKLQLVEAECKIQDLE 1027
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLR 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
779-963 |
2.68e-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: 51.66 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 779 RVQLpKRYRSEENAKRLMELACNTKI----SQKKLKKFEKEYHTMR-EQQAQQEDPIERFE----RENRRLQEANM---- 845
Cdd:pfam17380 382 RLQM-ERQQKNERVRQELEAARKVKIleeeRQRKIQQQKVEMEQIRaEQEEARQREVRRLEeeraREMERVRLEEQerqq 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 846 ---RLEQENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE-----SAQLKEMCRREldk 917
Cdd:pfam17380 461 qveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeerqKAIYEEERRRE--- 537
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1386635396 918 AESEIKKNSSiIGDYKQICSQLSERLEKQQTANKVEIEK--IRQKVDD 963
Cdd:pfam17380 538 AEEERRKQQE-MEERRRIQEQMRKATEERSRLEAMERERemMRQIVES 584
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
785-921 |
2.73e-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: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 785 RYRSEENAKRLMELacntkisQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEAN----MRLEQENDDLAHELVT 860
Cdd:pfam15709 337 RLRAERAEMRRLEV-------ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIrlrkQRLEEERQRQEEEERK 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386635396 861 SKIALRKDLDNAEEKADALNKELLMTKQK-----LIDAEDEKRRLEEESAQLKEMCRRELDKAESE 921
Cdd:pfam15709 410 QRLQLQAAQERARQQQEEFRRKLQELQRKkqqeeAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
803-1042 |
3.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 803 KISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMR---LEQENDDLAHELVTSKIALRKDLDNAEEKADAL 879
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEELAELLKELEELGFESVEELEER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 880 NKELLMTKQKLIDAEDEKRRLEEESAQLKEmCRRELDKAESEIKKnssIIGDYKQICSQLSerlEKQQTANKVEIEKIRQ 959
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKK-LEEELDKAFEELAE---TEKRLEELRKELE---ELEKKYSEEEYEELRE 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 960 KvddcdrcrdFFNKEGRVKGIssakgvsdedtDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEhHLGLALSEVQA 1039
Cdd:PRK03918 667 E---------YLELSRELAGL-----------RAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEE 725
|
...
gi 1386635396 1040 AKK 1042
Cdd:PRK03918 726 LRE 728
|
|
| PID |
pfam00640 |
Phosphotyrosine interaction domain (PTB/PID); |
147-262 |
4.10e-06 |
|
Phosphotyrosine interaction domain (PTB/PID);
Pssm-ID: 395515 Cd Length: 133 Bit Score: 47.36 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 147 YLGCASVNAPRSEVEALRMM----SILR-SQCQISLDVTLSVP---------NVSEGTVRLLDPQTNTEIANYPIYKILF 212
Cdd:pfam00640 5 YLGSVEVPEERAPDKNTRMQqareAIRRvKAAKINKIRGLSGEtgpgtkvdlFISTDGLKLLNPDTQELIHDHPLVSISF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1386635396 213 CVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 262
Cdd:pfam00640 85 CADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
852-1027 |
4.28e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 852 DDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSSIIGD 931
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 932 -----YKQIC--SQLSERLEKQQTAnkveiekirqkvddcdrcrDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLRE 1004
Cdd:COG3883 91 raralYRSGGsvSYLDVLLGSESFS-------------------DFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180
....*....|....*....|...
gi 1386635396 1005 MELELAQTKLQLVEAECKIQDLE 1027
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
802-1053 |
4.67e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 802 TKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLahelvTSKIALRKdldnaeEKADALNK 881
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-----TKKISSLK------EKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 882 ELLMTKQKLIDAEDEKRRLEEESAqlKEMCRRELDKAESEIKK----NSSIIGDYKQIcSQLSERLEKQQTANKVEIEKI 957
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEElkqtQKSLKKKQEEK-QELIDQKEKEKKDLIKEIEEK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 958 RQKVDDCDRCRDFFNKEGrvKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHhlglALSEV 1037
Cdd:TIGR04523 609 EKKISSLEKELEKAKKEN--EKLSSII----KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT----KIDDI 678
|
250
....*....|....*.
gi 1386635396 1038 QAAKKTWFNRTLSSIK 1053
Cdd:TIGR04523 679 IELMKDWLKELSLHYK 694
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
768-1027 |
6.43e-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: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 768 LTDFEGALKFFRVQLPKRYRSEENakRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRL 847
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 848 EQENDDLAhelvtskialrKDLDNAEEKADALNKELlmtkqklidaEDEKRRLEEEsaQLKEMcRRELDKAESEIKKNSS 927
Cdd:TIGR02169 757 KSELKELE-----------ARIEELEEDLHKLEEAL----------NDLEARLSHS--RIPEI-QAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 928 IIGDYKQIcsqLSERLEKQQTANKvEIEKIRQKVDDCDRCRDFFNKEgrvkgissakgvsdedtdeeKETLKNQLREMEL 1007
Cdd:TIGR02169 813 RLREIEQK---LNRLTLEKEYLEK-EIQELQEQRIDLKEQIKSIEKE--------------------IENLNGKKEELEE 868
|
250 260
....*....|....*....|
gi 1386635396 1008 ELAQTKLQLVEAECKIQDLE 1027
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLK 888
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
818-1030 |
1.84e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 818 TMREQQAQQEDPIERFERENRRLQEANMRleqENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK 897
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQARNQNSMYMR---QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 898 RRLEEESAQLKEMCRR---ELDKAESEIkknssiigdykQICSQLSERLEKQQTANKVEIEKIRQKVDdcDRCRDFFNKE 974
Cdd:pfam15921 366 DQFSQESGNLDDQLQKllaDLHKREKEL-----------SLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386635396 975 GRVKGISSA---------KGVSDEDTDEEK--------ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHL 1030
Cdd:pfam15921 433 ALLKAMKSEcqgqmerqmAAIQGKNESLEKvssltaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
799-1038 |
1.93e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 799 ACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFErenrRLQEANMRLE--QENDDLAHELVTSKialRKDLDNAEEKA 876
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIErlEERREDLEELIAER---RETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 877 DALNKEllmtKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQtankvEIEK 956
Cdd:PRK02224 540 EELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED-----EIER 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 957 IRQKVDDCDRCRDffNKEGRVKGISSAKGVSDEDTDEEK-ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALS 1035
Cdd:PRK02224 611 LREKREALAELND--ERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
...
gi 1386635396 1036 EVQ 1038
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 ... |
782-1030 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 782 LPKRYRSEENAKRLMElacntkisqKKLKKFEKEYHTMREQ----QAQQEDPIERFERENRRLQEANMRLEQENddlahe 857
Cdd:pfam01576 192 LEERLKKEEKGRQELE---------KAKRKLEGESTDLQEQiaelQAQIAELRAQLAKKEEELQAALARLEEET------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 858 lvTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE---------------SAQLKEMCRRE-----LDK 917
Cdd:pfam01576 257 --AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElealkteledtldttAAQQELRSKREqevteLKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 918 A-ESEIKKNSSIIGDYKQICSQ----LSERLEkQQTANKVEIEKIRQKVDdcdrcRDFFNKEGRVKGISSAKGvsdeDTD 992
Cdd:pfam01576 335 AlEEETRSHEAQLQEMRQKHTQaleeLTEQLE-QAKRNKANLEKAKQALE-----SENAELQAELRTLQQAKQ----DSE 404
|
250 260 270
....*....|....*....|....*....|....*...
gi 1386635396 993 EEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHL 1030
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
806-1027 |
2.35e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 806 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHElvtskialrkdLDNAEEKADALNKELLM 885
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ-----------RKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 886 TKQKLIDAEDEKRRLEEESAQL-KEMCRRELDKAESEIkknssiigdyKQICSQLSERLEKQQTaNKVEIEKIRQKVDDC 964
Cdd:COG4372 148 REEELKELEEQLESLQEELAALeQELQALSEAEAEQAL----------DELLKEANRNAEKEEE-LAEAEKLIESLPREL 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386635396 965 DRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 1027
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-1013 |
2.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 787 RSEENAKRLMELACNTKISQKK----LKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSK 862
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 863 iALRKDLDNAEEKADALNKEllmTKQKLIDAEDEKRRLEEESAQLKEMCRRELDK---AESEIKKNSSIIGDYKQICSQL 939
Cdd:PTZ00121 1706 -ELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkkiAHLKKEEEKKAEEIRKEKEAVI 1781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635396 940 SERLEKQQTANKVEIEKIRQKVDDcdrcrDFFN-KEGRVKG---ISSAKGVSDEDTDEEKETlKNQLREMELELAQTK 1013
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFD-----NFANiIEGGKEGnlvINDSKEMEDSAIKEVADS-KNMQLEEADAFEKHK 1853
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
806-1028 |
3.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 806 QKKLKKFEKEYHTMREQQAQQEDPIERF---------ERENRRLQEANMRLEQENDDLAhelvtskiALRKDLDNAEEKA 876
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLA--------ALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 877 DALNKELlmtkqklIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKK-----NSSIIGDYKQIC-----SQLSERLEKQ 946
Cdd:COG4913 702 EELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERFAAALgdaveRELRENLEER 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 947 QTANKVEIEKIRQKVddcDRCRDFFNKegRVKGISSAKGVSDEDTDEEKETLkNQLREMELELAQTKLQLVEAECKIQDL 1026
Cdd:COG4913 775 IDALRARLNRAEEEL---ERAMRAFNR--EWPAETADLDADLESLPEYLALL-DRLEEDGLPEYEERFKELLNENSIEFV 848
|
..
gi 1386635396 1027 EH 1028
Cdd:COG4913 849 AD 850
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
806-963 |
3.71e-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: 46.46 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 806 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEAnmrLEQENDDLAHelvtskiaLRKDLDNA--EEKADALNKEL 883
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKK--------YEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 884 LMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDD 963
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEE----ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
790-1053 |
3.98e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENAK-RLMELACNTKISQKKLKKFEKEYHTMR-EQQAQQEDPI------ERFERENRRLQEANMRLEQENDDLAHELVTS 861
Cdd:pfam05483 481 EKEKlKNIELTAHCDKLLLENKELTQEASDMTlELKKHQEDIInckkqeERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 862 KIALRKDLDNAEEKADALNKELLMTKQKLIDAEDE----KRRLEEESAQLKemcrrELDKAESEIKKNSSiiGDYKQIcs 937
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnlKKQIENKNKNIE-----ELHQENKALKKKGS--AENKQL-- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 938 qlsERLEKQQTANKVEIEKIRQKVDDcdrCRDFFNKEGRVKGISS---------AKGVSDEDTDEEKET---LKNQLREM 1005
Cdd:pfam05483 632 ---NAYEIKVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEeklleevekAKAIADEAVKLQKEIdkrCQHKIAEM 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1386635396 1006 ELELAQTKLQLVEAeckIQDLEHHLGLALS--EVQAAKKTWFNRTLSSIK 1053
Cdd:pfam05483 706 VALMEKHKHQYDKI---IEERDSELGLYKNkeQEQSSAKAALEIELSNIK 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
790-1027 |
5.72e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENA-KRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKiALRKD 868
Cdd:PRK03918 161 ENAyKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 869 LDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQT 948
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386635396 949 ANKVEIEKIRQKVDDCDrcrdffNKEGRVKGISSAKgvsdEDTDEEKETLKNQLREMElELAQTKLQLVEAECKIQDLE 1027
Cdd:PRK03918 318 RLEEEINGIEERIKELE------EKEERLEELKKKL----KELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLT 385
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
806-966 |
6.84e-05 |
|
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: 46.45 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 806 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQenddlahelVTSKIALRKDLDNAEEKADALNKELLM 885
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE---------YLKEKAEREEEREAEREEIEEEKEREI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 886 TK--QKLIDAEDEKRRLEE------ESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKI 957
Cdd:pfam13868 187 ARlrAQQEKAQDEKAERDElraklyQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
....*....
gi 1386635396 958 RQKVDDCDR 966
Cdd:pfam13868 267 LRKQAEDEE 275
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
790-957 |
9.55e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENAKRLMELACNTKISQKKlKKFEKEYHTMREQQAQQEdpierferenRRLQEANMRLEQENDDLAHElvtskialRKDL 869
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKLE----------KRLLQKEENLDRKLELLEKR--------EEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 870 DNAEEKADALNKELLMTKQKLIDAEDEKR-RLEEESAQLKEMCRRE-LDKAESEIKKNSSIIgdYKQICSQLSERLEKQq 947
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLqELERISGLTAEEAKEIlLEKVEEEARHEAAVL--IKEIEEEAKEEADKK- 189
|
170
....*....|
gi 1386635396 948 tANKVEIEKI 957
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 ... |
835-1053 |
1.22e-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: 46.12 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 835 RENRRLQEANMRLEQENDDLAH---ELVTSKIALRKDLDNAEEKADALNK----------ELLMTKQKL-IDAEDEKRRL 900
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAEliiDLEELKLQELKLKEQAKKALEYYQLkekleleeeyLLYLDYLKLnEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 901 EEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEK----IRQKVDDCDRCRDFFNKEGR 976
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllklERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635396 977 V-KGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKKTWFNRTLSSIK 1053
Cdd:pfam02463 326 AeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
839-1023 |
2.05e-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: 44.15 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 839 RLQEanmrLEQENDDLAHELVTskiaLRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKA 918
Cdd:COG1579 11 DLQE----LDSELDRLEHRLKE----LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA----RIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 919 ESEIKKnssiIGDYKQIcSQLSERLEKQQTANKVEIEKIRQKVDDCDrcrdffNKEGRVKGISSAKGVSDEDTDEEKETL 998
Cdd:COG1579 79 EEQLGN----VRNNKEY-EALQKEIESLKRRISDLEDEILELMERIE------ELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|....*
gi 1386635396 999 KNQLREMELELAQTKLQLVEAECKI 1023
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKI 172
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
790-1027 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENAKrlMELACNTKISQKKLKKFEKEYHTMREQQAQQEDP--IERFERENRrLQEANMRLEqENDDLAHELVTSKIALRK 867
Cdd:pfam05483 207 ENAR--LEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLllIQITEKENK-MKDLTFLLE-ESRDKANQLEEKTKLQDE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 868 DLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEE----------ESAQLKEMCRRELDKAESeikKNSSIIGDYKQICS 937
Cdd:pfam05483 283 NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKA---AHSFVVTEFEATTC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 938 QLSE-------RLEKQQTANKVEIEKIRQKVDDCDRCRDFF-NKEGRVKGISSAKGVSDEDTDEEK--ETLKNQLREMEL 1007
Cdd:pfam05483 360 SLEEllrteqqRLEKNEDQLKIITMELQKKSSELEEMTKFKnNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQ 439
|
250 260
....*....|....*....|
gi 1386635396 1008 ELAQTkLQLVEAEckIQDLE 1027
Cdd:pfam05483 440 ELIFL-LQAREKE--IHDLE 456
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
779-907 |
2.10e-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: 45.33 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 779 RVQLPKRYRSEENAKRLMELacntKISQKKLKKFEKEYH-TMRE-QQAQQEDPIERFERENRRLQEANMRLEQENDDLAH 856
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQL----QAAQERARQQQEEFRrKLQElQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1386635396 857 ELVTSKIALRKDLDNAEEKAdalnkellmtkqkLIDAEdEKRRLEEESAQL 907
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEEKA-------------RLEAE-ERRQKEEEAARL 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
820-963 |
2.30e-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: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 820 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVtskiALRKDLDNAE-EKADALNKELLmtkqkliDAEDEKR 898
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNGgDRLEQLEREIE-------RLERELE 355
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635396 899 RLEEESAQLKEMCRR---ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDD 963
Cdd:COG4913 356 ERERRRARLEALLAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
806-915 |
2.59e-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: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 806 QKKLKKFEKEYHTMREQQAQqedpiERFER--ENRRLQEANMRLEQENDDLA-HELVTSKIALRKdldNAEEKADALNKE 882
Cdd:pfam13904 75 QKEEREKEEQEAELRKRLAK-----EKYQEwlQRKARQQTKKREESHKQKAAeSASKSLAKPERK---VSQEEAKEVLQE 146
|
90 100 110
....*....|....*....|....*....|...
gi 1386635396 883 LLMTKQKLIDAEDEKRRLEEESAQLKEMCRREL 915
Cdd:pfam13904 147 WERKKLEQQQRKREEEQREQLKKEEEEQERKQL 179
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
789-924 |
2.66e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMElacNTKISQKKLKKFEKEYHTMREQQAQQEdpierferenrrlQEAnmRLEQENDDLAHElvtskiALRKD 868
Cdd:PRK09510 86 QQQAEELQQ---KQAAEQERLKQLEKERLAAQEQKKQAE-------------EAA--KQAALKQKQAEE------AAAKA 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1386635396 869 LDNAEEKADALNKELLMTKQKlidAEDEKRRLEEESAQlkemcrrelDKAESEIKK 924
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKK---AAAEAKKKAEAEAA---------KKAAAEAKK 185
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
824-1051 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 824 AQQEDPIERFERENRRLQEanmRLEQENDDLAhELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE 903
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQ---EIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 904 SAQLkemcRRELDKAESEIKK------------------NSSIIGD-------YKQICSQLSERLEKQQtANKVEIEKIR 958
Cdd:COG4942 92 IAEL----RAELEAQKEELAEllralyrlgrqpplalllSPEDFLDavrrlqyLKYLAPARREQAEELR-ADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 959 QKVddcdrcrdffnkEGRVKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDL---EHHLGLALS 1035
Cdd:COG4942 167 AEL------------EAERAELEALL----AELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIA 230
|
250
....*....|....*.
gi 1386635396 1036 EVQAAKKTWFNRTLSS 1051
Cdd:COG4942 231 RLEAEAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
835-1016 |
3.31e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 835 RENRRLQEAnMRLEQENDDLAHELVTSKIAL--------RKDLDNAEEKADALNKELLMTKQKLidaEDEKRRLEEesaq 906
Cdd:PRK04863 240 RENRMTLEA-IRVTQSDRDLFKHLITESTNYvaadymrhANERRVHLEEALELRRELYTSRRQL---AAEQYRLVE---- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 907 lkemCRRELDkaesEIKKNSSIIG-DYkqicSQLSERLEKQQTANKVEiEKIRQKVDDCDRcrdffnKEGRvkgISSAKG 985
Cdd:PRK04863 312 ----MARELA----ELNEAESDLEqDY----QAASDHLNLVQTALRQQ-EKIERYQADLEE------LEER---LEEQNE 369
|
170 180 190
....*....|....*....|....*....|.
gi 1386635396 986 VSdEDTDEEKETLKNQLREMELELAQTKLQL 1016
Cdd:PRK04863 370 VV-EEADEQQEENEARAEAAEEEVDELKSQL 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
789-963 |
3.55e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERE----NRRLQEANMRLEQENDDLAHELVTSKIA 864
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 865 LR-----------KDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKknssiigdyk 933
Cdd:COG3883 99 GGsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK-LAELEALKAELE---------- 167
|
170 180 190
....*....|....*....|....*....|
gi 1386635396 934 qicSQLSErLEKQQTANKVEIEKIRQKVDD 963
Cdd:COG3883 168 ---AAKAE-LEAQQAEQEALLAQLSAEEAA 193
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
787-1043 |
3.84e-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: 44.63 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 787 RSEENAKRLMELACNTKIsqKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALR 866
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKI--QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 867 ---KDLDNAEEKADALNKELLMTKQKLIDAEDEKRrlEEESAQLKEMCR---RELDKAESEIKKNSSIIGDYKQICSQLS 940
Cdd:TIGR04523 271 ekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKnqeKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 941 ERLEKQQTANKVEIEKIRQKVDdcdrcrdffnkegRVKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAE 1020
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQN-------------EIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
250 260
....*....|....*....|...
gi 1386635396 1021 CKIQDLEHHLGLALSEVQAAKKT 1043
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKET 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
821-1028 |
4.05e-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: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 821 EQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIAL-RKDLDNAEEKADALNKELLMTKQKLIDAEDEKRR 899
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 900 LEEESAQL----KEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEkqqtANKVEIEKIRQKVDDcdrcrdffnkeg 975
Cdd:COG4913 328 LEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLP----ASAEEFAALRAEAAA------------ 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1386635396 976 rvkgissakgvSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEH 1028
Cdd:COG4913 392 -----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
789-1059 |
5.44e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSK---IAL 865
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREeelKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 866 RKDLDNAEEKADALNKELlmtkqKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEK 945
Cdd:COG4372 156 EEQLESLQEELAALEQEL-----QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 946 QQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQD 1025
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250 260 270
....*....|....*....|....*....|....
gi 1386635396 1026 LEHHLGLALSEVQAAKKTWFNRTLSSIKTATGVQ 1059
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
841-963 |
5.56e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 841 QEANMRLEQENDDLaHELVTSKIALRKDLDNAEEKADALNKEllmtkqklidAEDEKRRLEEESAQLKEMCRRELDKAES 920
Cdd:PRK00409 505 EEAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKE----------AEKLKEELEEKKEKLQEEEDKLLEEAEK 573
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1386635396 921 EIKKnssIIGDYK----QICSQLSERLEKQQTANKV-EIEKIRQKVDD 963
Cdd:PRK00409 574 EAQQ---AIKEAKkeadEIIKELRQLQKGGYASVKAhELIEARKRLNK 618
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
767-1027 |
5.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 767 LLTDFEGALKFFRVQLpKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEanmr 846
Cdd:PRK02224 181 VLSDQRGSLDQLKAQI-EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 847 LEQENDDlahelvtskiaLRKDLDNAEEKADALnkellmtKQKLIDAEDEKRRLEEESAQLKEMCrrELDKAESEIkkns 926
Cdd:PRK02224 256 LEAEIED-----------LRETIAETEREREEL-------AEEVRDLRERLEELEEERDDLLAEA--GLDDADAEA---- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 927 siigdykqicsqLSERLEKQQTankvEIEKIRQKVDDCDRCRDFFNKEgrvkgissAKGVSDE--DTDEEKETLKNQLRE 1004
Cdd:PRK02224 312 ------------VEARREELED----RDEELRDRLEECRVAAQAHNEE--------AESLREDadDLEERAEELREEAAE 367
|
250 260
....*....|....*....|...
gi 1386635396 1005 MELELAQTKLQLVEAECKIQDLE 1027
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELE 390
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
759-1029 |
6.98e-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: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 759 LKTSKDdlLLTDFeGALKFFRVQLpkryrsEENAKRLMELAcnTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENR 838
Cdd:TIGR00606 781 EESAKV--CLTDV-TIMERFQMEL------KDVERKIAQQA--AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 839 RLQEANMRLEQENDDLAHELVTSKIALRKDLDNA---EEKADALNKELLMTKQKLIDAEDE-------KRRLEEESAQLK 908
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQdspletfLEKDQQEKEELI 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 909 EMCRRELDKAESEI----KKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAK 984
Cdd:TIGR00606 930 SSKETSNKKAQDKVndikEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1386635396 985 GVSDEDTDEEKETL---KNQLREMELELAQTKLQLVEAECKIQDLEHH 1029
Cdd:TIGR00606 1010 QKIQERWLQDNLTLrkrENELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
|
| PTB_LDLRAP-mammal-like |
cd13159 |
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ... |
144-245 |
7.18e-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: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 144 KLTYLGCASVNAPRSE---VEALR-MMSILRSQCQISLDVTLsvpNVSEGTVRLLDPQTNTEIANYPIYKILFCV--RGH 217
Cdd:cd13159 6 YLKYLGSTLVEKPKGEgatAEAVKtIIAMAKASGKKLQKVTL---TVSPKGIKVTDSATNETILEVSIYRISYCTadANH 82
|
90 100
....*....|....*....|....*...
gi 1386635396 218 DgtpesDCFAFTESHYNAELFRIHVFRC 245
Cdd:cd13159 83 D-----KVFAFIATNQDNEKLECHAFLC 105
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
830-929 |
8.20e-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: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 830 IERFERENRRLQEANMRLEQENDDLAHELVTskiALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKE 909
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLA---ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|
gi 1386635396 910 McRRELDKAESEIKKNSSII 929
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 ... |
790-1042 |
8.36e-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: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQeanmrleQENDDLA------HELVTSKI 863
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ-------QELDDLLvdldhqRQLVSNLE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 864 ALRKDLDN--AEEK--------------ADALNKE--LLMTKQKLIDAEDEKRRLEEESAQLK----------------- 908
Cdd:pfam01576 601 KKQKKFDQmlAEEKaisaryaeerdraeAEAREKEtrALSLARALEEALEAKEELERTNKQLRaemedlvsskddvgknv 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 909 ---EMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEkirqkvddcdrcRDFFNKegrvkgissakg 985
Cdd:pfam01576 681 helERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE------------RDLQAR------------ 736
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386635396 986 vsDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKK 1042
Cdd:pfam01576 737 --DEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK 791
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
860-1057 |
8.47e-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: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 860 TSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDYKQICSQL 939
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 940 SERLEKQQTANKVEIEKIRQKVDDcdrcrdffnkegrvkgiSSAKGVSDEdtdEEKETLKNQLREMELELAQTKLQLVEA 1019
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEE-----------------AEEELAEAE---AEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1386635396 1020 ECKIQDLEHHLGLALSEVQ------AAKKTWFNRTLSSIKTATG 1057
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLEslerriAATERRLEDLEEQIEELSE 852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-1027 |
8.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 787 RSEENAKRLMELACNTKISQKKLKKFEK--EYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIA 864
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 865 lrKDLDNAEE--KADALNKELLMTKQKLIDAEDEKRRLEEEsaqlKEMCRRELDKA-ESEIKKNSSIIGDYKQICSQLSE 941
Cdd:PTZ00121 1537 --DEAKKAEEkkKADELKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 942 RLEKQQTAnKVEIEKIRqkvddcdrcrdffnKEGRVKGISSAKGVSDEDTDEEKETLKNQLREMELELAQTKLQLVEAEC 1021
Cdd:PTZ00121 1611 EAKKAEEA-KIKAEELK--------------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
....*.
gi 1386635396 1022 KIQDLE 1027
Cdd:PTZ00121 1676 KAEEAK 1681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
768-949 |
9.21e-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: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 768 LTDFEGALKFFRVQLPKRYRSEENAKRLMELAcntkisQKKLKKFEKEYHTMREQQAQQ-------EDPIERFERENRRL 840
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEEL------EEQLETLRSKVAQLELQIASLnneierlEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 841 QEANMRLEQENDDLAHELVTSKIA--------LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCR 912
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEeleeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
170 180 190
....*....|....*....|....*....|....*....
gi 1386635396 913 RE--LDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTA 949
Cdd:TIGR02168 500 NLegFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAA 538
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
776-1014 |
1.17e-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: 42.80 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 776 KFFRVQLPKRYRSEENAKRLMElacntkiSQKKLKKFEKEYHTMREQQA-----QQEDPIERfERENRRLQEANMRLEQE 850
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVE-------RRRKLEEAEKARQAEMDRQAaiyaeQERMAMER-ERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 851 ---NDDLAHELVTSKIALRKDLDNaEEKADALNKEL-LMTKQKLIDAE------DEKRRLEEESAQLKEMCRRELDKAES 920
Cdd:pfam17380 364 rirQEEIAMEISRMRELERLQMER-QQKNERVRQELeAARKVKILEEErqrkiqQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 921 EIKKNSSIIGDykqicsqlsERLEKQQtankvEIEKIRQKVDDCDRCRDFFNKEGRVKGISSA--KGVSDEDTDEEKETL 998
Cdd:pfam17380 443 ERAREMERVRL---------EEQERQQ-----QVERLRQQEEERKRKKLELEKEKRDRKRAEEqrRKILEKELEERKQAM 508
|
250 260
....*....|....*....|.
gi 1386635396 999 -----KNQLREMELELAQTKL 1014
Cdd:pfam17380 509 ieeerKRKLLEKEMEERQKAI 529
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
824-1020 |
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 1386635396 824 AQQEDPIERFERENRRLQEANMRLEQENDDLAHelvtskiaLRKDLDNAEEKADALNKelLMTKQKLIDAEDEKRRLEEE 903
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQ--------QRSQLEQAKEGLSALNR--LLPRLNLLADETLADRVEEI 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 904 SAQLKEmcrreLDKAESEIKKNSSIIGDYKQICSQLS------ERLEKQQTANKVEIEKIRQKVD---DCDRCRDFFNKE 974
Cdd:PRK04863 900 REQLDE-----AEEAKRFVQQHGNALAQLEPIVSVLQsdpeqfEQLKQDYQQAQQTQRDAKQQAFaltEVVQRRAHFSYE 974
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386635396 975 GRVKGISsakgvsdeDTDEEKETLKNQLREMELELAQTKLQLVEAE 1020
Cdd:PRK04863 975 DAAEMLA--------KNSDLNEKLRQRLEQAEQERTRAREQLRQAQ 1012
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
789-966 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIerfERENRRLQEANMRLEQENDDLAhELVTSKIALRKD 868
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAALEAELA-ELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 869 LD--------------------------NAEEKADALN-----KELLMTKQKLIDA-EDEKRRLEEESAQLKEMcRRELD 916
Cdd:COG4942 99 LEaqkeelaellralyrlgrqpplalllSPEDFLDAVRrlqylKYLAPARREQAEElRADLAELAALRAELEAE-RAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1386635396 917 KAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDR 966
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1047 |
1.31e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 838 RRLQEANMRLEqENDDLAHELVTSKIALRKDLDNAEE----KADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrr 913
Cdd:COG1196 179 RKLEATEENLE-RLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEA---- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 914 ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDffnKEGRVKGISSAKGVSDEDTDE 993
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEE 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1386635396 994 EKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKKTWFNR 1047
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
790-1016 |
1.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 790 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEdpIERFERENRRLQEANMRLEQENDDLA--------HELVTS 861
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE--INKSINEYNKIESARADLEDIKIKINelkdkhdkYEEIKN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 862 KIAlRKDLDNAEEKADALNKelLMTKQKLIDAEDEKRRLEEESAQLKEMCRReLDKAESEIKKNSSIIGDY-KQICSQLS 940
Cdd:PRK01156 554 RYK-SLKLEDLDSKRTSWLN--ALAVISLIDIETNRSRSNEIKKQLNDLESR-LQEIEIGFPDDKSYIDKSiREIENEAN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635396 941 --ERLEKQQTANKVEIEKIRQKVDDcdrcrdfFNKEgrvkgISSAKGVSDedtdeEKETLKNQLREMELELAQTKLQL 1016
Cdd:PRK01156 630 nlNNKYNEIQENKILIEKLRGKIDN-------YKKQ-----IAEIDSIIP-----DLKEITSRINDIEDNLKKSRKAL 690
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
811-963 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 811 KFEKEYHTMREQQAQQEDPIERFERENrrLQEANMRLEQENDDL---------AHELVTSKIA-LRKDLDNAEEKADALN 880
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLELDE--AEEALEEIEERIDQLydllekevdAKKYVEKNLPeIEDYLEHAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 881 KELLMTKQKLIDAEDEK---RRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQtankveiEKI 957
Cdd:pfam06160 312 EELERVQQSYTLNENELervRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE-IEEEQ-------EEF 383
|
....*.
gi 1386635396 958 RQKVDD 963
Cdd:pfam06160 384 KESLQS 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
871-1054 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 871 NAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQL---KEMCRRELDKAESEIkknssiigDYKQICSQLsERLEKQQ 947
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerREALQRLAEYSWDEI--------DVASAEREI-AELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 948 ---TANKVEIEKIRQKVDDCdrcrdffnkEGRVKGISSAKgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKI- 1023
Cdd:COG4913 678 erlDASSDDLAALEEQLEEL---------EAELEELEEEL----DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAr 744
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386635396 1024 ----QDLEHHLG-LALSEVQAAKKTWFNRTLSSIKT 1054
Cdd:COG4913 745 lelrALLEERFAaALGDAVERELRENLEERIDALRA 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1027 |
2.02e-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: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 866 RKDLDNAEEK---ADALNKELLMTKQKLidaEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIgdyKQICSQLSEr 942
Cdd:TIGR02169 176 LEELEEVEENierLDLIIDEKRQQLERL---RREREKAERYQALLKEKREYEGYELLKEKEALERQK---EAIERQLAS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 943 LEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGissakgvsdedtDEEKETLKNQLREMELELAQTKLQLVEAECK 1022
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------------EEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
....*
gi 1386635396 1023 IQDLE 1027
Cdd:TIGR02169 317 LEDAE 321
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
864-1042 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 864 ALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK----------RRLEEESAQLKEMcRRELDKAESEIKKNSSiigdyk 933
Cdd:pfam12795 41 AYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleQRLLQTSAQLQEL-QNQLAQLNSQLIELQT------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 934 qicsqLSERLEKQQTANKVEIEKIRQKVDdcdrcrdffNKEGRVKGISSAKGVSDEdTDEEKETLKNQLREMEL------ 1007
Cdd:pfam12795 114 -----RPERAQQQLSEARQRLQQIRNRLN---------GPAPPGEPLSEAQRWALQ-AELAALKAQIDMLEQELlsnnnr 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386635396 1008 -ELAQTKLQLVEAecKIQDLEHHLgLALSEVQAAKK 1042
Cdd:pfam12795 179 qDLLKARRDLLTL--RIQRLEQQL-QALQELLNEKR 211
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
777-963 |
2.08e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 777 FFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQedpiERFERENRRLQEANMRLEQENddlah 856
Cdd:PRK12705 20 VLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQR----QEARREREELQREEERLVQKE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 857 elvtskialrKDLDNAEEKADALNKELLMTKQKLIDAEDEkrrLEEESAQLKEMCRRELDKAESEIKknssiigdyKQIC 936
Cdd:PRK12705 91 ----------EQLDARAEKLDNLENQLEEREKALSARELE---LEELEKQLDNELYRVAGLTPEQAR---------KLLL 148
|
170 180
....*....|....*....|....*..
gi 1386635396 937 SQLSERLEKQQTankVEIEKIRQKVDD 963
Cdd:PRK12705 149 KLLDAELEEEKA---QRVKKIEEEADL 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
784-966 |
2.13e-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: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 784 KRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnddlAHELVTSKI 863
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA----LALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 864 ALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEM-------------------------CRRELDKA 918
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltleeaealenkieddeeeARRRLKRL 977
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1386635396 919 ESEIKK----NSSIIGDYKqicsQLSERLE--KQQTANKVE-IEKIRQKVDDCDR 966
Cdd:TIGR02168 978 ENKIKElgpvNLAAIEEYE----ELKERYDflTAQKEDLTEaKETLEEAIEEIDR 1028
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
811-948 |
2.46e-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: 42.25 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 811 KFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQE----NDDLAheLVTSKIALRKDLDNAEEKADALNKELlmt 886
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLN--LVQTALRQQEKIERYQEDLEELTERL--- 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386635396 887 kqklidaeDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQicsqlseRLEKQQT 948
Cdd:COG3096 364 --------EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ-------ALDVQQT 410
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
803-961 |
3.37e-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: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 803 KISQKKLKKFEKEYHTMREQQAQQEDPIERferENRRLQEANMRLEQENDDlahelvtskiaLRKDLDNAEEKADALNKE 882
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEE-----------LEAELEEKDERIERLERE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 883 LLMTKQKL---IDAEDEKRRLEEESAQLkemcRRELDKAESEIKKnssiigdykqicsqLSERLEKQQTANKVEI--EKI 957
Cdd:COG2433 450 LSEARSEErreIRKDREISRLDREIERL----ERELEEERERIEE--------------LKRKLERLKELWKLEHsgELV 511
|
....
gi 1386635396 958 RQKV 961
Cdd:COG2433 512 PVKV 515
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
813-921 |
3.63e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 813 EKEYHTMREQQAQQedpI---ERFERENRRLQE--------ANMRLEQENDDLAHELVTSKI-------ALRKDLDNAEE 874
Cdd:COG1842 36 EEDLVEARQALAQV---IanqKRLERQLEELEAeaekweekARLALEKGREDLAREALERKAeleaqaeALEAQLAQLEE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1386635396 875 KADALNKELLMTKQKLIDAEDEKRRL--EEESAQLKEMCRRELDKAESE 921
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSGIDSD 161
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
770-1033 |
3.65e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 770 DFEGALKFFRVQLPKRYRS-EENAKRLMELACNTKISQK----------KLKKFEKEYHTMREQQAQQEDPIERFERE-- 836
Cdd:pfam12128 416 DLQALESELREQLEAGKLEfNEEEYRLKSRLGELKLRLNqatatpelllQLENFDERIERAREEQEAANAEVERLQSElr 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 837 ---------NRRLQEANMRLEQ---ENDDLAHEL-------------------------VTSKIALRKDLD---NAEEKA 876
Cdd:pfam12128 496 qarkrrdqaSEALRQASRRLEErqsALDELELQLfpqagtllhflrkeapdweqsigkvISPELLHRTDLDpevWDGSVG 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 877 DALNKELLMTKQKLIDAEdekrrleeESAQLKEMCRRELDKAESEIKKNSSIIgdykqicsqlsERLEKQQTANKVEIEK 956
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVP--------EWAASEEELRERLDKAEEALQSAREKQ-----------AAAEEQLVQANGELEK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 957 IRQKVDDCDRCrdFFNKEGRVKGISsakgvsdedtdEEKETLK---NQLREMELELAQTKLQLVEAECKIQDLEHHLGLA 1033
Cdd:pfam12128 637 ASREETFARTA--LKNARLDLRRLF-----------DEKQSEKdkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLE 703
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
755-922 |
3.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 755 ALGLLKTSKDDLLLTDFEGAlkffrVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQedpIERFE 834
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRI-----EELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ---AEEYQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 835 RENRRLQEANMRLEQENDDLAHELVTSkialrkDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcRRE 914
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEAL------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGE 470
|
....*...
gi 1386635396 915 LDKAESEI 922
Cdd:COG4717 471 LAELLQEL 478
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
784-1033 |
4.18e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 784 KRYRSE---ENAKRLM-ELACNTKISQ----KKLKKFEKEYHTMREQQAQQedpIERFERENRRLQEANMRLEQENDDLA 855
Cdd:pfam03148 15 QRNDAErlrQESRRLRnETDAKTKWDQydsnRRLGERIQDITFWKSELEKE---LEELDEEIELLLEEKRRLEKALEALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 856 H-ELVTSK-IALRK-----DL--DNAEEkadALNKEL--------LMtKQKLIDAEDEKRRLEEesaqLKEMCRREL-DK 917
Cdd:pfam03148 92 EpLHIAQEcLTLREkrqgiDLvhDEVEK---ELLKEVeliegiqeLL-QRTLEQAWEQLRLLRA----ARHKLEKDLsDK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 918 AES--------EIKKNSSIIGDY-------KQICS------------QLSERlEKQQTAN-KVEIEKIRQKVDD-----C 964
Cdd:pfam03148 164 KEAleidekclSLNNTSPNISYKpgptripPNSSTpeewekftqdniERAEK-ERAASAQlRELIDSILEQTANdlraqA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386635396 965 DRCRDFFNKegRVkgissakgvsdEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLA 1033
Cdd:pfam03148 243 DAVNFALRK--RI-----------EETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLA 298
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-999 |
4.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 787 RSEENAKRLMELACNTKI---SQKKLKKFEKEYHTMREQQAQQEDPIERFErENRRLQEANMRLEQEN-DDLAHELVTSK 862
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAE-EKKKADEAKKAEEKKKaDEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 863 IA--LRKDLDNAEEKADALNKELLMTKQKlidaeDEKRRLEEESAqlkemcRRELDKAESEIKKNSSIIGDYKQICSQLS 940
Cdd:PTZ00121 1316 KAdeAKKKAEEAKKKADAAKKKAEEAKKA-----AEAAKAEAEAA------ADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386635396 941 ERLEKQQTAN--KVEIEKIRQKVDDCDRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLK 999
Cdd:PTZ00121 1385 KKAEEKKKADeaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
779-1008 |
5.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 779 RVQLPKRYRSEENAKRLMEL--ACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDlAH 856
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-AE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 857 ELVTSKIALRKDLDNAEEKADALNKEllmtkqklidaEDEKRRLEeesaQLKEMCRRELDKAESEIKKNSSIIGDYKQIC 936
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAE----ELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386635396 937 SQLSERLEKQQTANKVEIEKirQKVDDCDRCRDFFNKEGRvkgiSSAKGVSDEDTDEEKETlknqlREMELE 1008
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEK--KKIAHLKKEEEKKAEEIR----KEKEAVIEEELDEEDEK-----RRMEVD 1797
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
810-962 |
5.53e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 810 KKFEKEYHTMREQQAQQEDPIERFERENrrLQEANMRLEQENDDL---------AHELVTSKIA-LRKDLDNAEEKADAL 879
Cdd:PRK04778 252 LDIEKEIQDLKEQIDENLALLEELDLDE--AEEKNEEIQERIDQLydilerevkARKYVEKNSDtLPDFLEHAKEQNKEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 880 NKELLMTKQKLIDAEDEK---RRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQtankveiEK 956
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE-IEKEQ-------EK 401
|
....*.
gi 1386635396 957 IRQKVD 962
Cdd:PRK04778 402 LSEMLQ 407
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
779-1056 |
7.11e-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: 40.34 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 779 RVQLPKRYRSEEnakrlMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFEREnRRLQEANMRLEQEnddlAHEL 858
Cdd:TIGR00618 196 AELLTLRSQLLT-----LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQL----LKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 859 VTSkialrkdldnaEEKADALNKELLMTkQKLIDAEDEKRRLEEESAQLKEmCRRELDKAESEIK----KNSSIIGDYKQ 934
Cdd:TIGR00618 266 RAR-----------IEELRAQEAVLEET-QERINRARKAAPLAAHIKAVTQ-IEQQAQRIHTELQskmrSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 935 ICSQLSERLEKQQTANKVEIEkirqkvddCDRCRDFFNKEGRVKGISSA---------KGVSDEDTDEEKETLKNQLREM 1005
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQ--------EIHIRDAHEVATSIREISCQqhtltqhihTLQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1386635396 1006 ELELAQTKLQLVEAEckiQDLEHHLGLALSEVQAAKKTWFNRTLSSIKTAT 1056
Cdd:TIGR00618 405 LQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
812-1027 |
8.35e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 812 FEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLahelvtskialrkdldnaEEKADALNKELLMTKQKLI 891
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL------------------REEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 892 DAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSsiigDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDff 971
Cdd:PRK02224 381 DRREEIEELEEEIEELRE----RFGDAPVDLGNAE----DFLEELREERDELREREAELEATLRTARERVEEAEALLE-- 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386635396 972 nkEGR-------VKGISSAKGVSD-----EDTDEEKETLKNQLREMELELAQTKlQLVEAECKIQDLE 1027
Cdd:PRK02224 451 --AGKcpecgqpVEGSPHVETIEEdrervEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLE 515
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
869-960 |
8.82e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 869 LDNAEEKADALNKE-LLMTKQKLI----DAEDE-KRRLEEESAQLKEMCRRE--LDKAESEIKKNSSIIGDYKQICSQLS 940
Cdd:PRK12704 44 LEEAKKEAEAIKKEaLLEAKEEIHklrnEFEKElRERRNELQKLEKRLLQKEenLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100
....*....|....*....|
gi 1386635396 941 ERLEKQQTankvEIEKIRQK 960
Cdd:PRK12704 124 QELEKKEE----ELEELIEE 139
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
789-1042 |
9.59e-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: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 789 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQ----EDPIERFERENRRLQEANMRLEQENDDLAHELvtskia 864
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQAleelTEQLEQAKRNKANLEKAKQALESENAELQAEL------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 865 lrkdldnaeekadalnKELLMTKQkliDAEDEKRRLEeesAQLKEMCRReldKAESEIKKNssiigdykqicsQLSERLE 944
Cdd:pfam01576 394 ----------------RTLQQAKQ---DSEHKRKKLE---GQLQELQAR---LSESERQRA------------ELAEKLS 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 945 KQQTankvEIEKIRQKVDDCDRcrdffnkegrvKGISSAKGVSD-----EDTDE-------EKETLKNQLREMELELAQT 1012
Cdd:pfam01576 437 KLQS----ELESVSSLLNEAEG-----------KNIKLSKDVSSlesqlQDTQEllqeetrQKLNLSTRLRQLEDERNSL 501
|
250 260 270
....*....|....*....|....*....|
gi 1386635396 1013 KLQLVEAECKIQDLEHHLGLALSEVQAAKK 1042
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
818-960 |
9.60e-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: 39.93 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 818 TMREQQAQQEDPIERFERENRRLQEANMRLEQENDdlahelvtskialRKDLDNAEEKADALNKELLMTKQKLIDA-EDE 896
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQ-------------RRLQQEQLERAEKMREELELEQQRRFEEiRLR 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386635396 897 KRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQK 960
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL-QRKKQQEEAERAEAEKQRQK 455
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
894-1020 |
9.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 894 EDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNK 973
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1386635396 974 EGRVKGISSAKGVSDEDTDEEKE------TLKNQLREMELELAQTKLQLVEAE 1020
Cdd:COG4717 131 YQELEALEAELAELPERLEELEErleelrELEEELEELEAELAELQEELEELL 183
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
738-1050 |
9.63e-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: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 738 HIIDLLLCEGISVIFNVALGLLKTSKDDLLLTDFEGALKFFRVQLPKRYRSEENAKRLMELACNTKISQ-----KKLKKF 812
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKLKAQ 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 813 EKEyhtMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALRKDLDNAEEKADALN----------KE 882
Cdd:pfam02463 800 EEE---LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITkeellqelllKE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 883 LLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVD 962
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635396 963 DCDRCRDFFNKEGRVKGISSAKGVSDEDTDEEKETLKNQLREmELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKK 1042
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE-RLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNK 1035
|
....*...
gi 1386635396 1043 TWFNRTLS 1050
Cdd:pfam02463 1036 VFFYLELG 1043
|
|
| |
