|
Name |
Accession |
Description |
Interval |
E-value |
| PTB_Rab6GAP |
cd01211 |
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ... |
141-269 |
4.94e-80 |
|
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: 256.79 E-value: 4.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 141 VVFNKLTYLGCASVNAPRSEVEALRMMSILRSQCQISLDVTLSVPNVSEGTVRLLDPQINTEIANYPIYKILFCVRGHDG 220
Cdd:cd01211 1 TIFNGVTYLGCAKVNAPRSETEALRIMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958762592 221 TPESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAFRRSAKQ 269
Cdd:cd01211 81 TSESDCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFRRVPKS 129
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
559-768 |
1.47e-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: 234.12 E-value: 1.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 559 VRSGVPEALRGEVWQLLAGCHNNDH--LVEKYRILITKESPQD----SAITRDINRTFPAHDYFKDTGGDGQDSLYKICK 632
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLKETAPDDksivHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 633 AYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLReLFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLD 711
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762592 712 ISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLL 768
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 ... |
565-768 |
1.82e-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: 220.97 E-value: 1.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 565 EALRGEVWQllagchnndhlvekyrilitkespqdSAITRDINRTFPAHDYFKDtgGDGQDSLYKICKAYSVYDEEIGYC 644
Cdd:pfam00566 1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 645 QGQSFLAAVLLL-HMPEEQAFSVLVKIMFDYGLRELFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQW 723
Cdd:pfam00566 53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958762592 724 FLTLFTAKFPLYMVFHIIDLLLCEGISV-IFNVALGLLKTSKDDLL 768
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
531-776 |
3.85e-49 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 182.69 E-value: 3.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 531 EKILETWGELL-SKWHLNLNVRPKQLSSLVRSGVPEALRGEVWQLLAG-------CHNNDHLVEKYRILITKESPQD-SA 601
Cdd:COG5210 180 LAADKLWISYLdPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGigfdldkNPGLYERLLNLHREAKIPTQEIiSQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 602 ITRDINRTFPAHDYFKDTGGDGQDSLYKICKAYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLRELF 680
Cdd:COG5210 260 IEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 681 KQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLL 760
Cdd:COG5210 340 LKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAIL 419
|
250
....*....|....*.
gi 1958762592 761 KTSKDDLLLTDFEGAL 776
Cdd:COG5210 420 KLLRDKLLKLDSDELL 435
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
303-433 |
1.74e-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: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 303 FSAVPKDK----DRQCFKLRQGIDKKIVICVQQTANKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 374
Cdd:pfam12473 2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762592 375 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 433
Cdd:pfam12473 72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
|
|
| PTB |
smart00462 |
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
139-272 |
7.95e-27 |
|
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: 106.63 E-value: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 139 DSVVFNKLTYLGCASVNAPRSEVEALR-MMSILRSQCQISLDVTLSVPNVSEGTVRLLDPQINTEIANYPIYKILFCVRG 217
Cdd:smart00462 1 GSGVSFRVKYLGSVEVPEARGLQVVQEaIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762592 218 HDGtpeSDCFAFTESHYNAELFRIHVFRCEI--QEAVSRILYSFATAFRRSAKQTPL 272
Cdd:smart00462 81 PDD---LDVFGYIARDPGSSRFACHVFRCEKaaEDIALAIGQAFQLAYELKLKARSE 134
|
|
| PTB |
cd00934 |
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ... |
145-263 |
3.50e-16 |
|
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: 75.62 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 145 KLTYLGCASVNAPR----SEVEALRMMSILRSQCQISLDVTLsvpNVSEGTVRLLDPQINTEIANYPIYKILFCVRGHDg 220
Cdd:cd00934 4 QVKYLGSVEVGSSRgvdvVEEALKALAAALKSSKRKPGPVLL---EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958762592 221 tpESDCFAFTESHYNAELFRIHVFRCEIQEAVSRILYSFATAF 263
Cdd:cd00934 80 --NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
785-1028 |
3.64e-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: 70.86 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 785 KRYRSEENAKRLMELAcntkISQKKLKKFEKEYHTMREQQAQQEDPIERFERE-----------NRRLQEANMRLEQEND 853
Cdd:TIGR02168 213 ERYKELKAELRELELA----LLVLRLEELREELEELQEELKEAEEELEELTAElqeleekleelRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 854 DL------AHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLK---EMCRRELDKAESEIK 924
Cdd:TIGR02168 289 ELyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 925 KNSSIIGDYKQICSQLSER---LEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGASSVKGVSDE------DTDEE 995
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleELEEE 448
|
250 260 270
....*....|....*....|....*....|...
gi 1958762592 996 KETLKNQLRELELELAQTKLQLVEAECKIQDLE 1028
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
782-1043 |
2.63e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 782 QLPKRYRSEENAKRLMELacntkisQKKLKKFEKEYHTMReqqaqqedpIERFERENRRLQEANMRLEQENDDLAHELVT 861
Cdd:TIGR02168 201 QLKSLERQAEKAERYKEL-------KAELRELELALLVLR---------LEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 862 SKIA---LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKemcrRELDKAESEIKKNSSIIGDYKQICS 938
Cdd:TIGR02168 265 LEEKleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE----RQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 939 QLSERLEKQQtankVEIEKIRQKVDDcdRCRDFFNKEGRVkgassvkgvsdEDTDEEKETLKNQLRELELELAQTKLQLV 1018
Cdd:TIGR02168 341 ELEEKLEELK----EELESLEAELEE--LEAELEELESRL-----------EELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260
....*....|....*....|....*
gi 1958762592 1019 EAECKIQDLEHHLGLALSEVQAAKK 1043
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-1042 |
1.89e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELvtskIALRKDLDNAEEKADALNKELLM 886
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 887 TKQKLIDAE----DEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQIcsqlsERLEKQQTANKVEIEKIRQKV 962
Cdd:COG1196 349 AEEELEEAEaelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-----EELEEAEEALLERLERLEEEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 963 DDCDRcrdffnkegrvkgassvkgvSDEDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAK 1042
Cdd:COG1196 424 EELEE--------------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
790-910 |
6.15e-09 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 54.92 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 790 EENAKRLMELacntkisQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnddlAHELVTSKIALRKD 869
Cdd:pfam20492 2 EEAEREKQEL-------EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQK----RQEAEEEKERLEES 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958762592 870 LDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKE 910
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQE 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
774-1039 |
7.59e-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: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 774 GALKFFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnd 853
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 854 dlaHELVTSKIA-LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMC---RRELDKAESEIKKNSSI 929
Cdd:TIGR02168 742 ---VEQLEERIAqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 930 IGDYKQICSQLS----------ERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEgrVKGASSVKGVSDEDTD---EEK 996
Cdd:TIGR02168 819 AANLRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALAllrSEL 896
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958762592 997 ETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLALSEVQ 1039
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
791-1043 |
1.28e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEdpIERFERENRRLQEANMRLEQENDDLAHELvtskIALRKDL 870
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEELRLEL----EELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 871 DNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTA 950
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 951 NKVEIEKIRQKVDDCDRCRDFFNKEGRVKGASSVK-------GVSDEDTDEEKETLKNQLRELELELAQTKLQLVEAECK 1023
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260
....*....|....*....|
gi 1958762592 1024 IQDLEHHLGLALSEVQAAKK 1043
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLE 463
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
761-1028 |
1.59e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 761 KTSKDDLLLTDFEGALKFFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQED--------PIE 832
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltglTPE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 833 RFERENRRLQEANMRLEQENDDLAHEL--VTSKIALRKD----LDNAEEKADALNKEL-------LMTK--QKLIDAEDE 897
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIgeLKKEIKELKKaieeLKKAKGKCPVCGRELteehrkeLLEEytAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 898 KRRLEEESAQLkemcRRELDKAESEIKKNSSIIgDYKQICSQLSERLEKqqtANKVEIEKIRQKVDDCDRCRDFFNK-EG 976
Cdd:PRK03918 468 LKEIEEKERKL----RKELRELEKVLKKESELI-KLKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKlKG 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762592 977 RVKG-ASSVKgvSDEDTDEEKETLKNQLRELELELAQTKLQLV--------EAECKIQDLE 1028
Cdd:PRK03918 540 EIKSlKKELE--KLEELKKKLAELEKKLDELEEELAELLKELEelgfesveELEERLKELE 598
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
808-964 |
2.84e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 808 KKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDdlAHELVTSKIALRKDLDNAEEKADALNKELLMT 887
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762592 888 KQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKknsSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQKVDD 964
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRL-AELEEELEEAQEELEELEEELEQ 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
800-1028 |
1.79e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 800 ACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFErenrRLQEANMRLE--QENDDLAHELVTSKialRKDLDNAEEKA 877
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIErlEERREDLEELIAER---RETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 878 DALNKEllmtKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKNS-------------SIIGDYKQICSQLSERL 944
Cdd:PRK02224 540 EELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKerieslerirtllAAIADAEDEIERLREKR 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 945 EKQQTANKVEIEKIRQKVDDCDRCRDFFNkEGRVKGASSVKGVSDE----------DTDEEKETLKNQL----RELElEL 1010
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFD-EARIEEAREDKERAEEyleqveekldELREERDDLQAEIgaveNELE-EL 693
|
250
....*....|....*...
gi 1958762592 1011 AQTKLQLVEAECKIQDLE 1028
Cdd:PRK02224 694 EELRERREALENRVEALE 711
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
804-1043 |
2.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 804 KISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMR---LEQENDDLAHELVTSKIALRKDLDNAEEKADAL 880
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEELAELLKELEELGFESVEELEER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 881 NKELLMTKQKLIDAEDEKRRLEEESAQLKEmCRRELDKAESEIKKnssIIGDYKQICSQLSErleKQQTANKVEIEKIRQ 960
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKK-LEEELDKAFEELAE---TEKRLEELRKELEE---LEKKYSEEEYEELRE 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 961 KvddcdrcrdFFNKEGRVKGAssvkgvsdedtDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEhHLGLALSEVQA 1040
Cdd:PRK03918 667 E---------YLELSRELAGL-----------RAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEE 725
|
...
gi 1958762592 1041 AKK 1043
Cdd:PRK03918 726 LRE 728
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
780-964 |
2.47e-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: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 780 RVQLpKRYRSEENAKRLMELACNTKI----SQKKLKKFEKEYHTMR-EQQAQQEDPIERFE----RENRRLQEANM---- 846
Cdd:pfam17380 382 RLQM-ERQQKNERVRQELEAARKVKIleeeRQRKIQQQKVEMEQIRaEQEEARQREVRRLEeeraREMERVRLEEQerqq 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 847 ---RLEQENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE-----SAQLKEMCRREldk 918
Cdd:pfam17380 461 qveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeerqKAIYEEERRRE--- 537
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958762592 919 AESEIKKNSSiIGDYKQICSQLSERLEKQQTANKVEIEK--IRQKVDD 964
Cdd:pfam17380 538 AEEERRKQQE-MEERRRIQEQMRKATEERSRLEAMERERemMRQIVES 584
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
786-922 |
2.53e-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: 51.49 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 786 RYRSEENAKRLMELacntkisQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEAN----MRLEQENDDLAHELVT 861
Cdd:pfam15709 337 RLRAERAEMRRLEV-------ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIrlrkQRLEEERQRQEEEERK 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762592 862 SKIALRKDLDNAEEKADALNKELLMTKQK-----LIDAEDEKRRLEEESAQLKEMCRRELDKAESE 922
Cdd:pfam15709 410 QRLQLQAAQERARQQQEEFRRKLQELQRKkqqeeAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
853-1028 |
3.27e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 853 DDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSSIIGD 932
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 933 -----YKQIC--SQLSERLEKQQTAnkveiekirqkvddcdrcrDFFNKegrvkgASSVKGVSDEDTD------EEKETL 999
Cdd:COG3883 91 raralYRSGGsvSYLDVLLGSESFS-------------------DFLDR------LSALSKIADADADlleelkADKAEL 145
|
170 180
....*....|....*....|....*....
gi 1958762592 1000 KNQLRELELELAQTKLQLVEAECKIQDLE 1028
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELE 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
790-1028 |
4.18e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 790 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLE--QENDDLAHELVTSKIALR 867
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 868 KDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCRR--ELDKAESEIKKNSSIIGDYKQICSQLS---- 941
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERLKKRLTgltp 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 942 -------ERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKE-GRVKGASSVKGVSDEDTDEEKEtlKNQLRELELELAQT 1013
Cdd:PRK03918 387 eklekelEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRI 464
|
250
....*....|....*
gi 1958762592 1014 KLQLVEAECKIQDLE 1028
Cdd:PRK03918 465 EKELKEIEEKERKLR 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
769-1028 |
6.77e-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: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 769 LTDFEGALKFFRVQLPKRYRSEENakRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRL 848
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 849 EQENDDLAhelvtskialrKDLDNAEEKADALNKELlmtkqklidaEDEKRRLEEEsaQLKEMcRRELDKAESEIKKNSS 928
Cdd:TIGR02169 757 KSELKELE-----------ARIEELEEDLHKLEEAL----------NDLEARLSHS--RIPEI-QAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 929 IIGDYKQIcsqLSERLEKQQTANKvEIEKIRQKVDDCDRCRDffnkegrvkgassvkgvsdeDTDEEKETLKNQLRELEL 1008
Cdd:TIGR02169 813 RLREIEQK---LNRLTLEKEYLEK-EIQELQEQRIDLKEQIK--------------------SIEKEIENLNGKKEELEE 868
|
250 260
....*....|....*....|
gi 1958762592 1009 ELAQTKLQLVEAECKIQDLE 1028
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLK 888
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
807-1020 |
7.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEanmRLEqenddlAHELVTSKIALRKDLDNAEEKADALnkellm 886
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RRE------ALQRLAEYSWDEIDVASAEREIAEL------ 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 887 tkqklidaEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDykqiCSQLSERLEKQQTANKVEIEKIRQKVDDCD 966
Cdd:COG4913 674 --------EAELERLDASSDDLAAL-EEQLEELEAELEELEEELDE----LKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762592 967 ---RCRDFFNKEGRVKGASsvkgvSDEDTDEEKETLKNQLRELELELAQTKLQLVEA 1020
Cdd:COG4913 741 dlaRLELRALLEERFAAAL-----GDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
803-1054 |
1.39e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 803 TKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLahelvTSKIALRKdldnaeEKADALNK 882
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-----TKKISSLK------EKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 883 ELLMTKQKLIDAEDEKRRLEEESAqlKEMCRRELDKAESEIKK----NSSIIGDYKQIcSQLSERLEKQQTANKVEIEKI 958
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEElkqtQKSLKKKQEEK-QELIDQKEKEKKDLIKEIEEK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 959 RQKVDDCDRCRDFFNKEGRvKGASSVKGVsdedtDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHhlglALSEV 1038
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENE-KLSSIIKNI-----KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT----KIDDI 678
|
250
....*....|....*.
gi 1958762592 1039 QAAKKTWFNRTLSSIK 1054
Cdd:TIGR04523 679 IELMKDWLKELSLHYK 694
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
787-1042 |
1.61e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 787 YRSEENAKRLME-LACNTKISQKKLKK----FEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDL------ 855
Cdd:pfam15921 70 YPGKEHIERVLEeYSHQVKDLQRRLNEsnelHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLrnqlqn 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 856 -AHELVTSKiALRKD-LDNAEEKADALNKELLM-------TKQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEI-KK 925
Cdd:pfam15921 150 tVHELEAAK-CLKEDmLEDSNTQIEQLRKMMLShegvlqeIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKIlRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 926 NSSIIGDYKQICSQLSERLE--KQQTANKVEI------EKIRQKVDDCDrcrdfFNKEGRVKGASSVKGVSD-------- 989
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEalKSESQNKIELllqqhqDRIEQLISEHE-----VEITGLTEKASSARSQANsiqsqlei 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762592 990 --EDTDEEKETLKNQLRELELELAQTKLQLVEA----ECKIQDLEHHLGLALSEVQAAK 1042
Cdd:pfam15921 304 iqEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEAR 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
807-1029 |
2.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQQEDPIERF---------ERENRRLQEANMRLEQENDDLAhelvtskiALRKDLDNAEEKA 877
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLA--------ALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 878 DALNKELlmtkqklIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKK-----NSSIIGDYKQIC-----SQLSERLEKQ 947
Cdd:COG4913 702 EELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERFAAALgdaveRELRENLEER 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 948 QTANKVEIEKIRQKVddcDRCRDFFNKegRVKGASSVKGVSDEDTDEEKETLkNQLRELELELAQTKLQLVEAECKIQDL 1027
Cdd:COG4913 775 IDALRARLNRAEEEL---ERAMRAFNR--EWPAETADLDADLESLPEYLALL-DRLEEDGLPEYEERFKELLNENSIEFV 848
|
..
gi 1958762592 1028 EH 1029
Cdd:COG4913 849 AD 850
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
819-1031 |
2.38e-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: 48.58 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 819 TMREQQAQQEDPIERFERENRRLQEANMRleqENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK 898
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQARNQNSMYMR---QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 899 RRLEEESAQLKEMCRR---ELDKAESEIkknssiigdykQICSQLSERLEKQQTANKVEIEKIRQKVDdcDRCRDFFNKE 975
Cdd:pfam15921 366 DQFSQESGNLDDQLQKllaDLHKREKEL-----------SLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762592 976 GRVKGASS---------VKGVSDEDTDEEK--------ETLKNQLRELELELAQTKLQLVEAECKIQDLEHHL 1031
Cdd:pfam15921 433 ALLKAMKSecqgqmerqMAAIQGKNESLEKvssltaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
788-1014 |
2.58e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 788 RSEENAKRLMELACNTKISQKK----LKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSK 863
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 864 iALRKDLDNAEEKADALNKEllmTKQKLIDAEDEKRRLEEESAQLKEMCRRELDK---AESEIKKNSSIIGDYKQICSQL 940
Cdd:PTZ00121 1706 -ELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkkiAHLKKEEEKKAEEIRKEKEAVI 1781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762592 941 SERLEKQQTANKVEIEKIRQKVDDcdrcrDFFN-KEGRVKGASSVKGVSDEDTDEEKETL--KNQLRELELELAQTK 1014
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFD-----NFANiIEGGKEGNLVINDSKEMEDSAIKEVAdsKNMQLEEADAFEKHK 1853
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
807-1060 |
3.31e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHE---LVTSKIALRKDLDNAEEKADALNKE 883
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQrkqLEAQIAELQSEIAEREEELKELEEQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 884 LLMTKQKLIDAEDEKRRLEEESA---------QLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVE 954
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAeqaldellkEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 955 IEKIRQKVDDCDRCRDFFNKEGRVKGASSVKGVSDEDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLA 1034
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
250 260
....*....|....*....|....*.
gi 1958762592 1035 LSEVQAAKKTWFNRTLSSIKTATGVQ 1060
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQ 344
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
807-964 |
4.11e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEAnmrLEQENDDLAHelvtskiaLRKDLDNA--EEKADALNKEL 884
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKK--------YEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 885 LMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDD 964
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEE----ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
783-1031 |
4.61e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 783 LPKRYRSEENAKRLMElacntkisqKKLKKFEKEYHTMREQ----QAQQEDPIERFERENRRLQEANMRLEQENddlahe 858
Cdd:pfam01576 192 LEERLKKEEKGRQELE---------KAKRKLEGESTDLQEQiaelQAQIAELRAQLAKKEEELQAALARLEEET------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 859 lvTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE---------------SAQLKEMCRRE-----LDK 918
Cdd:pfam01576 257 --AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElealkteledtldttAAQQELRSKREqevteLKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 919 A-ESEIKKNSSIIGDYKQICSQ----LSERLEkQQTANKVEIEKIRQKVDdcdrcRDFFNKEGRVKGASSVKGvsdeDTD 993
Cdd:pfam01576 335 AlEEETRSHEAQLQEMRQKHTQaleeLTEQLE-QAKRNKANLEKAKQALE-----SENAELQAELRTLQQAKQ----DSE 404
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958762592 994 EEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHL 1031
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
791-1019 |
4.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENA-KRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKiALRKD 869
Cdd:PRK03918 161 ENAyKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 870 LDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQT 949
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762592 950 ANKVEIEKIRQKVDDCDrcrdffNKEGRVkgassvkgvsdEDTDEEKETLKNQLRELE--LELAQTKLQLVE 1019
Cdd:PRK03918 318 RLEEEINGIEERIKELE------EKEERL-----------EELKKKLKELEKRLEELEerHELYEEAKAKKE 372
|
|
| PID |
pfam00640 |
Phosphotyrosine interaction domain (PTB/PID); |
148-263 |
4.86e-05 |
|
Phosphotyrosine interaction domain (PTB/PID);
Pssm-ID: 395515 Cd Length: 133 Bit Score: 44.28 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 148 YLGCASVNAPRSEVEALRMM----SILR-SQCQISLDVTLSVP---------NVSEGTVRLLDPQINTEIANYPIYKILF 213
Cdd:pfam00640 5 YLGSVEVPEERAPDKNTRMQqareAIRRvKAAKINKIRGLSGEtgpgtkvdlFISTDGLKLLNPDTQELIHDHPLVSISF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958762592 214 CVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 263
Cdd:pfam00640 85 CADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
836-1017 |
5.03e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 836 RENRRLQEAnMRLEQENDDLAHELVTSKIAL--------RKDLDNAEEKADALNKELLMTKQKLidaEDEKRRLEEesaq 907
Cdd:PRK04863 240 RENRMTLEA-IRVTQSDRDLFKHLITESTNYvaadymrhANERRVHLEEALELRRELYTSRRQL---AAEQYRLVE---- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 908 lkemCRRELDkaesEIKKNSSIIG-DYkqicSQLSERLEKQQTANKVEiEKIRQKVDDCDRcrdffnKEGRVKGASSVKg 986
Cdd:PRK04863 312 ----MARELA----ELNEAESDLEqDY----QAASDHLNLVQTALRQQ-EKIERYQADLEE------LEERLEEQNEVV- 371
|
170 180 190
....*....|....*....|....*....|.
gi 1958762592 987 vsdEDTDEEKETLKNQLRELELELAQTKLQL 1017
Cdd:PRK04863 372 ---EEADEQQEENEARAEAAEEEVDELKSQL 399
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
840-1028 |
5.30e-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: 45.69 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 840 RLQEanmrLEQENDDLAHELVTskiaLRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrrELDKA 919
Cdd:COG1579 11 DLQE----LDSELDRLEHRLKE----LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA----RIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 920 ESEIKKnssiIGDYKQIcsqlsERLEKQQTANKVEIEKIRQKVddcdrcrdfFNKEGRVKGASSVKGVSDEDTDEEKETL 999
Cdd:COG1579 79 EEQLGN----VRNNKEY-----EALQKEIESLKRRISDLEDEI---------LELMERIEELEEELAELEAELAELEAEL 140
|
170 180
....*....|....*....|....*....
gi 1958762592 1000 KNQLRELELELAQTKLQLVEAECKIQDLE 1028
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELA 169
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
807-967 |
7.34e-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: 46.07 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQenddlahelVTSKIALRKDLDNAEEKADALNKELLM 886
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE---------YLKEKAEREEEREAEREEIEEEKEREI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 887 TK--QKLIDAEDEKRRLEE------ESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKI 958
Cdd:pfam13868 187 ARlrAQQEKAQDEKAERDElraklyQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
....*....
gi 1958762592 959 RQKVDDCDR 967
Cdd:pfam13868 267 LRKQAEDEE 275
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
791-958 |
1.01e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENAKRLMELACNTKISQKKlKKFEKEYHTMREQQAQQEdpierferenRRLQEANMRLEQENDDLAHElvtskialRKDL 870
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKLE----------KRLLQKEENLDRKLELLEKR--------EEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 871 DNAEEKADALNKELLMTKQKLIDAEDEKR-RLEEESAQLKEMCRRE-LDKAESEIKKNSSIIgdYKQICSQLSERLEKQq 948
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLqELERISGLTAEEAKEIlLEKVEEEARHEAAVL--IKEIEEEAKEEADKK- 189
|
170
....*....|
gi 1958762592 949 tANKVEIEKI 958
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 ... |
836-1054 |
1.16e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 836 RENRRLQEANMRLEQENDDLAH---ELVTSKIALRKDLDNAEEKADALNK----------ELLMTKQKL-IDAEDEKRRL 901
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAEliiDLEELKLQELKLKEQAKKALEYYQLkekleleeeyLLYLDYLKLnEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 902 EEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEK----IRQKVDDCDRCRDFFNKEGR 977
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllklERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762592 978 V-KGASSVKGVSDEDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKKTWFNRTLSSIK 1054
Cdd:pfam02463 326 AeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
822-1029 |
1.35e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 822 EQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIAL-RKDLDNAEEKADALNKELLMTKQKLIDAEDEKRR 900
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 901 LEEESAQL----KEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEkqqtANKVEIEKIRQKVDDcdrcrdffnkeg 976
Cdd:COG4913 328 LEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLP----ASAEEFAALRAEAAA------------ 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958762592 977 rvkgassvkgvSDEDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEH 1029
Cdd:COG4913 392 -----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
810-1039 |
1.42e-04 |
|
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: 46.26 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 810 LKKFEKEYHTMREQQAQQED-------PIERFEREnrrLQEANM---RLEQENDDLAHEL---VTSKIALRKDLDNAEEK 876
Cdd:pfam15921 386 LHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRE---LDDRNMevqRLEALLKAMKSECqgqMERQMAAIQGKNESLEK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 877 ADALNKELLMTKQKL-----------IDAEDEKRRLEEESAQLKEMcRRELDKAESEIKKNSSII-------------GD 932
Cdd:pfam15921 463 VSSLTAQLESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEK-ERAIEATNAEITKLRSRVdlklqelqhlkneGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 933 YKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRcrdFFNKEGRVKGASSVkgvsdedtdeEKETLKNQLRELELELAQ 1012
Cdd:pfam15921 542 HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ---LVGQHGRTAGAMQV----------EKAQLEKEINDRRLELQE 608
|
250 260
....*....|....*....|....*...
gi 1958762592 1013 TKLQLVEAECKIQDLEHHLG-LALSEVQ 1039
Cdd:pfam15921 609 FKILKDKKDAKIRELEARVSdLELEKVK 636
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
788-1044 |
1.47e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 788 RSEENAKRLMELACNTKIsqKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALR 867
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKI--QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 868 ---KDLDNAEEKADALNKELLMTKQKLIDAEDEKRrlEEESAQLKEMCR---RELDKAESEIKKNSSIIGDYKQICSQLS 941
Cdd:TIGR04523 271 ekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKnqeKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 942 ERLEKQQTANKVEIEKIRQKVDDCDRcrdfFNKEgrvkgassvkgvsDEDTDEEKETLKNQLRELELELAQTKLQLVEAE 1021
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEK----LKKE-------------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
250 260
....*....|....*....|...
gi 1958762592 1022 CKIQDLEHHLGLALSEVQAAKKT 1044
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKET 434
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
791-1025 |
1.84e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENAK-RLMELACNTKISQKKLKKFEKEYHTMR-EQQAQQEDPI------ERFERENRRLQEANMRLEQENDDLAHELVTS 862
Cdd:pfam05483 481 EKEKlKNIELTAHCDKLLLENKELTQEASDMTlELKKHQEDIInckkqeERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 863 KIALRKDLDNAEEKADALNKELLMTKQKLIDAEDE----KRRLEEESAQLKEMCR-------------RELDKAESEIKK 925
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnlKKQIENKNKNIEELHQenkalkkkgsaenKQLNAYEIKVNK 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 926 NSSIIGDYKQICSQLSERLEKQQTANKV-------EIEKIRQKVDDCDRCRDFFNKEGRVKGASSVKGVSD--------- 989
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIEDKKIseeklleEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKhkhqydkii 720
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958762592 990 EDTDEEKETLKNQLRE-------LELELAQTKLQLVEAECKIQ 1025
Cdd:pfam05483 721 EERDSELGLYKNKEQEqssakaaLEIELSNIKAELLSLKKQLE 763
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
791-1028 |
1.87e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENAKrlMELACNTKISQKKLKKFEKEYHTMREQQAQQEDP--IERFERENRrLQEANMRLEqENDDLAHELVTSKIALRK 868
Cdd:pfam05483 207 ENAR--LEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLllIQITEKENK-MKDLTFLLE-ESRDKANQLEEKTKLQDE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 869 DLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEE----------ESAQLKEMCRRELDKAESeikKNSSIIGDYKQICS 938
Cdd:pfam05483 283 NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKA---AHSFVVTEFEATTC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 939 QLSE-------RLEKQQTANKVEIEKIRQKVDDCDRCRDFF-NKEGRVKGASSVKGVSDEDTDEEK--ETLKNQLRELEL 1008
Cdd:pfam05483 360 SLEEllrteqqRLEKNEDQLKIITMELQKKSSELEEMTKFKnNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQ 439
|
250 260
....*....|....*....|
gi 1958762592 1009 ELAQTkLQLVEAEckIQDLE 1028
Cdd:pfam05483 440 ELIFL-LQAREKE--IHDLE 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
783-1043 |
1.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 783 LPKRYRSEENAKRLM--------ELACNT--KIsQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRL---- 848
Cdd:PRK03918 357 LEERHELYEEAKAKKeelerlkkRLTGLTpeKL-EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkak 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 849 -----------EQENDDLAHELVTSKIALRKDLDNAEEKADALNKEL------LMTKQKLIDAEDEKRRLEEESAQLKEM 911
Cdd:PRK03918 436 gkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvLKKESELIKLKELAEQLKELEEKLKKY 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 912 CRRELDKAESEIKK-NSSIIGDYKQIcSQLSERLEKQQTANKvEIEKIRQKVDDCDRCRDFFNKEGRVKGASSVKGVSDE 990
Cdd:PRK03918 516 NLEELEKKAEEYEKlKEKLIKLKGEI-KSLKKELEKLEELKK-KLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762592 991 DTDEEKE-----TLKN---QLRELELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKK 1043
Cdd:PRK03918 594 LKELEPFyneylELKDaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1045 |
1.96e-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: 45.82 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 861 TSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLK---EMCRRELDKAESEIKKNSSIIGDYKQIC 937
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 938 SQLS---ERLEKQQTANKVEIEKIRQKVDDCDRCRDffNKEGRVKGASsvkgvsdedtdEEKETLKNQLRELELELAQTK 1014
Cdd:TIGR02168 750 AQLSkelTELEAEIEELEERLEEAEEELAEAEAEIE--ELEAQIEQLK-----------EELKALREALDELRAELTLLN 816
|
170 180 190
....*....|....*....|....*....|.
gi 1958762592 1015 LQLVEAECKIQDLEHHLGLALSEVQAAKKTW 1045
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
780-908 |
2.00e-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: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 780 RVQLPKRYRSEENAKRLMELacntKISQKKLKKFEKEYH-TMRE-QQAQQEDPIERFERENRRLQEANMRLEQENDDLAH 857
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQL----QAAQERARQQQEEFRrKLQElQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958762592 858 ELVTSKIALRKDLDNAEEKAdalnkellmtkqkLIDAEdEKRRLEEESAQL 908
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEEKA-------------RLEAE-ERRQKEEEAARL 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
825-1052 |
2.38e-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: 44.75 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 825 AQQEDPIERFERENRRLQEanmRLEQENDDLAhELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEE 904
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQ---EIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 905 SAQLkemcRRELDKAESEIKK------NSSIIGDYKQICSQ--------LSERLEKQQTANKVEIEKIRQKVDDCDRcrd 970
Cdd:COG4942 92 IAEL----RAELEAQKEELAEllralyRLGRQPPLALLLSPedfldavrRLQYLKYLAPARREQAEELRADLAELAA--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 971 ffnKEGRVKGASSVKGVSDEDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDL---EHHLGLALSEVQAAKKTWFN 1047
Cdd:COG4942 165 ---LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAE 241
|
....*
gi 1958762592 1048 RTLSS 1052
Cdd:COG4942 242 RTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
821-964 |
2.44e-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: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 821 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVtskiALRKDLDNAE-EKADALNKELLmtkqkliDAEDEKR 899
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNGgDRLEQLEREIE-------RLERELE 355
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762592 900 RLEEESAQLKEMCRR---ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDD 964
Cdd:COG4913 356 ERERRRARLEALLAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
807-916 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 807 QKKLKKFEKEYHTMREQQAQqedpiERFER--ENRRLQEANMRLEQENDDLA-HELVTSKIALRKdldNAEEKADALNKE 883
Cdd:pfam13904 75 QKEEREKEEQEAELRKRLAK-----EKYQEwlQRKARQQTKKREESHKQKAAeSASKSLAKPERK---VSQEEAKEVLQE 146
|
90 100 110
....*....|....*....|....*....|...
gi 1958762592 884 LLMTKQKLIDAEDEKRRLEEESAQLKEMCRREL 916
Cdd:pfam13904 147 WERKKLEQQQRKREEEQREQLKKEEEEQERKQL 179
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
790-925 |
2.50e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 790 EENAKRLMElacNTKISQKKLKKFEKEYHTMREQQAQQEdpierferenrrlQEAnmRLEQENDDLAHElvtskiALRKD 869
Cdd:PRK09510 86 QQQAEELQQ---KQAAEQERLKQLEKERLAAQEQKKQAE-------------EAA--KQAALKQKQAEE------AAAKA 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762592 870 LDNAEEKADALNKELLMTKQKlidAEDEKRRLEEESAQlkemcrrelDKAESEIKK 925
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKK---AAAEAKKKAEAEAA---------KKAAAEAKK 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
768-1028 |
2.64e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 768 LLTDFEGALKFFRVQLpKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEanmr 847
Cdd:PRK02224 181 VLSDQRGSLDQLKAQI-EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 848 LEQENDDLahelvtskialRKDLDNAEEKADALnkellmtKQKLIDAEDEKRRLEEESAQLKEMCrrELDKAESEIkkns 927
Cdd:PRK02224 256 LEAEIEDL-----------RETIAETEREREEL-------AEEVRDLRERLEELEEERDDLLAEA--GLDDADAEA---- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 928 siigdykqicsqLSERLEKQQTankvEIEKIRQKVDDCDRCRDFFNKEgrvkgASSVKGVSDeDTDEEKETLKNQLRELE 1007
Cdd:PRK02224 312 ------------VEARREELED----RDEELRDRLEECRVAAQAHNEE-----AESLREDAD-DLEERAEELREEAAELE 369
|
250 260
....*....|....*....|.
gi 1958762592 1008 LELAQTKLQLVEAECKIQDLE 1028
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELE 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
790-964 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 790 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERE----NRRLQEANMRLEQENDDLAHELVTSKIA 865
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 866 LR-----------KDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMcRRELDKAESEIKknssiigdyk 934
Cdd:COG3883 99 GGsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK-LAELEALKAELE---------- 167
|
170 180 190
....*....|....*....|....*....|
gi 1958762592 935 qicSQLSErLEKQQTANKVEIEKIRQKVDD 964
Cdd:COG3883 168 ---AAKAE-LEAQQAEQEALLAQLSAEEAA 193
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
788-1005 |
3.82e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 788 RSEENAKRLMELACNTKISQKKLKKFEK--EYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIA 865
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 866 lrKDLDNAEE--KADALNKELLMTKQKLIDAEDEKRRLEEEsaqlKEMCRRELDKA-ESEIKKNSSIIGDYKQICSQLSE 942
Cdd:PTZ00121 1537 --DEAKKAEEkkKADELKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762592 943 RLEKQQTAnKVEIEKIRQKVDDCDRCRDFFNKEG-RVKGASSVKGvSDEDTDEEKETLKNQLRE 1005
Cdd:PTZ00121 1611 EAKKAEEA-KIKAEELKKAEEEKKKVEQLKKKEAeEKKKAEELKK-AEEENKIKAAEEAKKAEE 1672
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
813-1028 |
4.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 813 FEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLahelvtskialrkdldnaEEKADALNKELLMTKQKLI 892
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL------------------REEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 893 DAEDEKRRLEEESAQLKEmcrrELDKAESEIKKNSsiigDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDff 972
Cdd:PRK02224 381 DRREEIEELEEEIEELRE----RFGDAPVDLGNAE----DFLEELREERDELREREAELEATLRTARERVEEAEALLE-- 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762592 973 nkEGR-------VKGASSVKGVSD-----EDTDEEKETLKNQLRELELELAQTKlQLVEAECKIQDLE 1028
Cdd:PRK02224 451 --AGKcpecgqpVEGSPHVETIEEdrervEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLE 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
693-1015 |
4.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 693 QLERLMQEyIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFnVALGLLktskddllltdF 772
Cdd:COG4717 221 ELEELEEE-LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF-LVLGLL-----------A 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 773 EGALKFFRVQLPKRYRSEEnakrLMELACNTKISQKKLKKFEKEYHTMREQQAQQedpIERFERENRRLQEANMRLEQEN 852
Cdd:COG4717 288 LLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEE---LLELLDRIEELQELLREAEELE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 853 DDLAHElvtskiALRKDLDNAEEKADALNKELLmtkQKLIDAEDEKRRLEEESAQLKEMCRRELDKAESEIKKnssiiGD 932
Cdd:COG4717 361 EELQLE------ELEQEIAALLAEAGVEDEEEL---RAALEQAEEYQELKEELEELEEQLEELLGELEELLEA-----LD 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 933 YKQICSQLsERLEKQQTANKVEIEKIRQKVDDCdrcrdffnkEGRVKGASSVKGVSDedTDEEKETLKNQLRELELELAQ 1012
Cdd:COG4717 427 EEELEEEL-EELEEELEELEEELEELREELAEL---------EAELEQLEEDGELAE--LLQELEELKAELRELAEEWAA 494
|
...
gi 1958762592 1013 TKL 1015
Cdd:COG4717 495 LKL 497
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
760-1030 |
5.07e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 760 LKTSKDdlLLTDFeGALKFFRVQLpkryrsEENAKRLMELAcnTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENR 839
Cdd:TIGR00606 781 EESAKV--CLTDV-TIMERFQMEL------KDVERKIAQQA--AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 840 RLQEANMRLEQENDDLAHELVTSKIALRKDLDNA---EEKADALNKELLMTKQKLIDAEDE-------KRRLEEESAQLK 909
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQdspletfLEKDQQEKEELI 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 910 EMCRRELDKAESEI----KKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGASSVK 985
Cdd:TIGR00606 930 SSKETSNKKAQDKVndikEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958762592 986 GVSDEDTDEEKETL---KNQLRELELELAQTKLQLVEAECKIQDLEHH 1030
Cdd:TIGR00606 1010 QKIQERWLQDNLTLrkrENELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
842-964 |
5.91e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 842 QEANMRLEQENDDLaHELVTSKIALRKDLDNAEEKADALNKEllmtkqklidAEDEKRRLEEESAQLKEMCRRELDKAES 921
Cdd:PRK00409 505 EEAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKE----------AEKLKEELEEKKEKLQEEEDKLLEEAEK 573
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958762592 922 EIKKnssIIGDYK----QICSQLSERLEKQQTANKV-EIEKIRQKVDD 964
Cdd:PRK00409 574 EAQQ---AIKEAKkeadEIIKELRQLQKGGYASVKAhELIEARKRLNK 618
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1048 |
6.62e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 839 RRLQEANMRLEqENDDLAHELVTSKIALRKDLDNAEE----KADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEmcrr 914
Cdd:COG1196 179 RKLEATEENLE-RLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEA---- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 915 ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDRCRDffnKEGRVKGASSVKGVSDEDTDE 994
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEE 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958762592 995 EKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKKTWFNR 1048
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
872-1055 |
7.72e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 872 NAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQL---KEMCRRELDKAESEIkknssiigDYKQICSQLsERLEKQQ 948
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerREALQRLAEYSWDEI--------DVASAEREI-AELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 949 ---TANKVEIEKIRQKVDDCdrcrdffnkEGRVKGASSVKgvsdEDTDEEKETLKNQLRELELELAQTKLQLVEAECKI- 1024
Cdd:COG4913 678 erlDASSDDLAALEEQLEEL---------EAELEELEEEL----DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAr 744
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958762592 1025 ----QDLEHHLG-LALSEVQAAKKTWFNRTLSSIKT 1055
Cdd:COG4913 745 lelrALLEERFAaALGDAVERELRENLEERIDALRA 780
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
831-930 |
8.21e-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: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 831 IERFERENRRLQEANMRLEQENDDLAHELVTskiALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKE 910
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLA---ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|
gi 1958762592 911 McRRELDKAESEIKKNSSII 930
Cdd:COG0542 490 L-EKELAELEEELAELAPLL 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1028 |
8.32e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 867 RKDLDNAEEK---ADALNKELLMTKQKLidaEDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIgdyKQICSQLSEr 943
Cdd:TIGR02169 176 LEELEEVEENierLDLIIDEKRQQLERL---RREREKAERYQALLKEKREYEGYELLKEKEALERQK---EAIERQLAS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 944 LEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGassvkgvsdedtDEEKETLKNQLRELELELAQTKLQLVEAECK 1023
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------------EEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
....*
gi 1958762592 1024 IQDLE 1028
Cdd:TIGR02169 317 LEDAE 321
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
777-1031 |
9.74e-04 |
|
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: 43.19 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 777 KFFRVQLPKRYRSEENAKRLMElacntkiSQKKLKKFEKEYHTMREQQA-----QQEDPIERfERENRRLQEANMRLEQE 851
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVE-------RRRKLEEAEKARQAEMDRQAaiyaeQERMAMER-ERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 852 ---NDDLAHELVTSKIALRKDLDNaEEKADALNKEL-LMTKQKLIDAE------DEKRRLEEESAQLKEMCRRELDKAES 921
Cdd:pfam17380 364 rirQEEIAMEISRMRELERLQMER-QQKNERVRQELeAARKVKILEEErqrkiqQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 922 EIKKNSSIIGDykqicsqlsERLEKQQtankvEIEKIRQKVDDCDRCRDFFNKEGRvkgassvkgvsdedtdEEKETLKN 1001
Cdd:pfam17380 443 ERAREMERVRL---------EEQERQQ-----QVERLRQQEEERKRKKLELEKEKR----------------DRKRAEEQ 492
|
250 260 270
....*....|....*....|....*....|
gi 1958762592 1002 QLRELELELAQTKLQLVEAECKIQDLEHHL 1031
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKRKLLEKEM 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
769-950 |
9.95e-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: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 769 LTDFEGALKFFRVQLPKRYRSEENAKRLMELAcntkisQKKLKKFEKEYHTMREQQAQQ-------EDPIERFERENRRL 841
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEEL------EEQLETLRSKVAQLELQIASLnneierlEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 842 QEANMRLEQENDDLAHELVTSKIA--------LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEMCR 913
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEeleeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958762592 914 RE--LDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTA 950
Cdd:TIGR02168 500 NLegFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAA 538
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
791-1043 |
1.11e-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: 43.24 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQeanmrleQENDDLA------HELVTSKI 864
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ-------QELDDLLvdldhqRQLVSNLE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 865 ALRKDLDN--AEEK--------------ADALNKE--LLMTKQKLIDAEDEKRRLEEESAQLK----------------- 909
Cdd:pfam01576 601 KKQKKFDQmlAEEKaisaryaeerdraeAEAREKEtrALSLARALEEALEAKEELERTNKQLRaemedlvsskddvgknv 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 910 ---EMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEkirqkvddcdrcRDFFNKegrvkgassvkg 986
Cdd:pfam01576 681 helERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE------------RDLQAR------------ 736
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762592 987 vsDEDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLALSEVQAAKK 1043
Cdd:pfam01576 737 --DEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK 791
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
812-1028 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 812 KFEKEYHTMREQQAQQEDPIERFERENrrLQEANMRLEQENDDL---------AHELVTSKIA-LRKDLDNAEEKADALN 881
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLELDE--AEEALEEIEERIDQLydllekevdAKKYVEKNLPeIEDYLEHAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 882 KELLMTKQKLIDAEDEK---RRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQ------TANK 952
Cdd:pfam06160 312 EELERVQQSYTLNENELervRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE-IEEEQeefkesLQSL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 953 VEIEKI-RQKVDDCDrcRDFFNKEGRVKgASSVKGVSDE------DTDEEKETLKNQLRELELELAQTKLQLVEAECKIQ 1025
Cdd:pfam06160 391 RKDELEaREKLDEFK--LELREIKRLVE-KSNLPGLPESyldyffDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVD 467
|
...
gi 1958762592 1026 DLE 1028
Cdd:pfam06160 468 TLY 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
790-967 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 790 EENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIerfERENRRLQEANMRLEQENDDLAhELVTSKIALRKD 869
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAALEAELA-ELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 870 LD--------------------------NAEEKADALN-----KELLMTKQKLIDA-EDEKRRLEEESAQLKEMcRRELD 917
Cdd:COG4942 99 LEaqkeelaellralyrlgrqpplalllSPEDFLDAVRrlqylKYLAPARREQAEElRADLAELAALRAELEAE-RAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958762592 918 KAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCDR 967
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
791-964 |
1.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 791 ENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEdpIERFERENRRLQEANMRLEQENDDLA--------HELVTS 862
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE--INKSINEYNKIESARADLEDIKIKINelkdkhdkYEEIKN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 863 KIAlRKDLDNAEEKADALNKelLMTKQKLIDAEDEKRRLEEESAQLKEMCRReLDKAESEIKKNSSIIGDY-KQICSQLS 941
Cdd:PRK01156 554 RYK-SLKLEDLDSKRTSWLN--ALAVISLIDIETNRSRSNEIKKQLNDLESR-LQEIEIGFPDDKSYIDKSiREIENEAN 629
|
170 180
....*....|....*....|....*
gi 1958762592 942 --ERLEKQQTANKVEIEKIRQKVDD 964
Cdd:PRK01156 630 nlNNKYNEIQENKILIEKLRGKIDN 654
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
865-1043 |
1.75e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 865 ALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK----------RRLEEESAQLKEMcRRELDKAESEIKKNSSiigdyk 934
Cdd:pfam12795 41 AYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleQRLLQTSAQLQEL-QNQLAQLNSQLIELQT------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 935 qicsqLSERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKgassvkgvsdedTDEEKETLKNQLRELELELAQ-- 1012
Cdd:pfam12795 114 -----RPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWA------------LQAELAALKAQIDMLEQELLSnn 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958762592 1013 -----TKLQLVEAECKIQDLEHHLgLALSEVQAAKK 1043
Cdd:pfam12795 177 nrqdlLKARRDLLTLRIQRLEQQL-QALQELLNEKR 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
895-1021 |
2.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 895 EDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQKVDDCDRCRDFFNK 974
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958762592 975 EGRVKGA-SSVKGVSD-----EDTDEEKETLKNQLRELELELAQTKLQLVEAE 1021
Cdd:COG4717 131 YQELEALeAELAELPErleelEERLEELRELEEELEELEAELAELQEELEELL 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
785-967 |
2.22e-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: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 785 KRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQEnddlAHELVTSKI 864
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA----LALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 865 ALRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKEM-------------------------CRRELDKA 919
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltleeaealenkieddeeeARRRLKRL 977
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958762592 920 ESEIKK----NSSIIGDYKqicsQLSERLE--KQQTANKVE-IEKIRQKVDDCDR 967
Cdd:TIGR02168 978 ENKIKElgpvNLAAIEEYE----ELKERYDflTAQKEDLTEaKETLEEAIEEIDR 1028
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
778-964 |
2.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 778 FFRVQLPKRYRSEENAKRLMELACNTKISQKKLKKFEKEYHTMREQQAQQedpiERFERENRRLQEANMRLEQENddlah 857
Cdd:PRK12705 20 VLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQR----QEARREREELQREEERLVQKE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 858 elvtskialrKDLDNAEEKADALNKELLMTKQKLIDAEDEkrrLEEESAQLKEMCRRELDKAESEIKknssiigdyKQIC 937
Cdd:PRK12705 91 ----------EQLDARAEKLDNLENQLEEREKALSARELE---LEELEKQLDNELYRVAGLTPEQAR---------KLLL 148
|
170 180
....*....|....*....|....*..
gi 1958762592 938 SQLSERLEKQQTankVEIEKIRQKVDD 964
Cdd:PRK12705 149 KLLDAELEEEKA---QRVKKIEEEADL 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
812-949 |
2.59e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 812 KFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQE----NDDLAheLVTSKIALRKDLDNAEEKADALNKELlmt 887
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLN--LVQTALRQQEKIERYQEDLEELTERL--- 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762592 888 kqklidaeDEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQicsqlseRLEKQQT 949
Cdd:COG3096 364 --------EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ-------ALDVQQT 410
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
877-1041 |
2.59e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 877 ADALNKELLMTKQKliDAEDEKRRLEEESAQLkemcRRELDKAESEI---KKNSSII---GDYKQICSQLSErLEKQQTA 950
Cdd:COG3206 158 AEAYLEQNLELRRE--EARKALEFLEEQLPEL----RKELEEAEAALeefRQKNGLVdlsEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 951 NKVEIEKIRQKVDdcdrcrdffnkEGRVKGASSVKGVSDEDTDEEKETLKNQLRELELELAQTKL-------QLVEAECK 1023
Cdd:COG3206 231 ARAELAEAEARLA-----------ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQ 299
|
170
....*....|....*...
gi 1958762592 1024 IQDLEHHLGLALSEVQAA 1041
Cdd:COG3206 300 IAALRAQLQQEAQRILAS 317
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
780-1000 |
3.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 780 RVQLPKRYRSEENAKRLMEL--ACNTKISQKKLKKFEKEYHTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDlAH 857
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-AE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 858 ELVTSKIALRKDLDNAEEKADALNKEllmtkqklidaEDEKRRLEeesaQLKEMCRRELDKAESEIKKNSSIIGDYKQIC 937
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAE----ELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762592 938 SQLSERLEKQQTANKVEIEKirQKVDDCDRCRDFFNKEGRVKGASSVK-GVSDEDTDEEKETLK 1000
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEK--KKIAHLKKEEEKKAEEIRKEKEAVIEeELDEEDEKRRMEVDK 1798
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
804-962 |
3.52e-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: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 804 KISQKKLKKFEKEYHTMREQQAQQEDPIERferENRRLQEANMRLEQENDDlahelvtskiaLRKDLDNAEEKADALNKE 883
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEE-----------LEAELEEKDERIERLERE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 884 LLMTKQKL---IDAEDEKRRLEEESAQLkemcRRELDKAESEIKKnssiigdykqicsqLSERLEKQQTANKVEI--EKI 958
Cdd:COG2433 450 LSEARSEErreIRKDREISRLDREIERL----ERELEEERERIEE--------------LKRKLERLKELWKLEHsgELV 511
|
....
gi 1958762592 959 RQKV 962
Cdd:COG2433 512 PVKV 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
832-1056 |
3.59e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 832 ERFERENRRLQEANMRLEQENDDLAHELVTSKIALRK-----DLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESA 906
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 907 QLKEMCRRELDKAESEIkkNSSIIGDYKQICSQLSERLEKQQ---TANKVEIEKIRQKVDDCDRcrdffNKEGRVKGASS 983
Cdd:COG3206 244 ALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSaryTPNHPDVIALRAQIAALRA-----QLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762592 984 vkgvsdeDTDEEKETLKNQLRELELELAQTK---LQLVEAECKIQDLEHhlglalsEVQAAKKTwFNRTLSSIKTA 1056
Cdd:COG3206 317 -------SLEAELEALQAREASLQAQLAQLEarlAELPELEAELRRLER-------EVEVAREL-YESLLQRLEEA 377
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
814-922 |
3.91e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 814 EKEYHTMREQQAQQedpI---ERFERENRRLQE--------ANMRLEQENDDLAHELVTSKI-------ALRKDLDNAEE 875
Cdd:COG1842 36 EEDLVEARQALAQV---IanqKRLERQLEELEAeaekweekARLALEKGREDLAREALERKAeleaqaeALEAQLAQLEE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958762592 876 KADALNKELLMTKQKLIDAEDEKRRL--EEESAQLKEMCRRELDKAESE 922
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSGIDSD 161
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
866-1028 |
4.03e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 866 LRKDLDNAEEKADALNKELLMTKQKLIDAEDEKRRLEEESAQLKemcrrelDKAESEIKKNSSIIGDYKQICSQLSERLE 945
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 946 kQQTANKVEIEKIRQKVDDCDRCRDFFNKEGRVKGASSVKGVSD-EDTDEEKETLKNQLRELELE-------LAQTKLQL 1017
Cdd:TIGR04523 118 -QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyNDLKKQKEELENELNLLEKEklniqknIDKIKNKL 196
|
170
....*....|.
gi 1958762592 1018 VEAECKIQDLE 1028
Cdd:TIGR04523 197 LKLELLLSNLK 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
788-1000 |
4.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 788 RSEENAKRLMELACNTKI---SQKKLKKFEKEYHTMREQQAQQEDPIERFErENRRLQEANMRLEQEN-DDLAHELVTSK 863
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAE-EKKKADEAKKAEEKKKaDEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 864 IA--LRKDLDNAEEKADALNKELLMTKQKlidaeDEKRRLEEESAqlkemcRRELDKAESEIKKNSSIIGDYKQICSQLS 941
Cdd:PTZ00121 1316 KAdeAKKKAEEAKKKADAAKKKAEEAKKA-----AEAAKAEAEAA------ADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762592 942 ERLEKQQTAN--KVEIEKIRQKVDDCDRCRDFFNKEGRVKGASSVKGVSDEDTDEEKETLK 1000
Cdd:PTZ00121 1385 KKAEEKKKADeaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
771-1034 |
5.04e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 771 DFEGALKFFRVQLPKRYRS-EENAKRLMELACNTKISQK----------KLKKFEKEYHTMREQQAQQEDPIERFERE-- 837
Cdd:pfam12128 416 DLQALESELREQLEAGKLEfNEEEYRLKSRLGELKLRLNqatatpelllQLENFDERIERAREEQEAANAEVERLQSElr 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 838 ---------NRRLQEANMRLEQ---ENDDLAHEL-------------------------VTSKIALRKDLD---NAEEKA 877
Cdd:pfam12128 496 qarkrrdqaSEALRQASRRLEErqsALDELELQLfpqagtllhflrkeapdweqsigkvISPELLHRTDLDpevWDGSVG 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 878 DALNKELLMTKQKLIDAEdekrrleeESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEK 957
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVP--------EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 958 IRQKVDDCDRCRDffnkegrvkgassvkgvsdedtdeEKETLK---NQLRELELELAQTKLQLVEAECKIQDLEHHLGLA 1034
Cdd:pfam12128 648 LKNARLDLRRLFD------------------------EKQSEKdkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLE 703
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
881-1031 |
5.45e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 881 NKELLMTKQKLIDAEDEKRRLEEESaqlkEMCRRELDKAESEIKKNSSIIGDYKQI----CSQLSERLEKQQTANKVEIE 956
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEH----KRARIELEKKASALKRQLDRESDRNQElqkrIRLLEKREAEAEEALREQAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 957 KIRQKVDDCDRCRDFFN-KEGRVKGASSVKGVSDEDTDEEKETLKNQLRELE------------LELAQTKLQ------- 1016
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNeKESQLADAREVISCLKNELSELRRQIQRAELELQstnseleelqerLDLLKAKASeaeqlrq 156
|
170 180
....*....|....*....|...
gi 1958762592 1017 --------LVEAECKIQDLEHHL 1031
Cdd:pfam05557 157 nlekqqssLAEAEQRIKELEFEI 179
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
811-963 |
6.03e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 811 KKFEKEYHTMREQQAQQEDPIERFERENrrLQEANMRLEQENDDL---------AHELVTSKIA-LRKDLDNAEEKADAL 880
Cdd:PRK04778 252 LDIEKEIQDLKEQIDENLALLEELDLDE--AEEKNEEIQERIDQLydilerevkARKYVEKNSDtLPDFLEHAKEQNKEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 881 NKELLMTKQKLIDAEDEK---RRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSErLEKQQtankveiEK 957
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE-IEKEQ-------EK 401
|
....*.
gi 1958762592 958 IRQKVD 963
Cdd:PRK04778 402 LSEMLQ 407
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
785-1034 |
8.97e-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: 39.84 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 785 KRYRSE---ENAKRLM-ELACNTKISQ----KKLKKFEKEYHTMREQQAQQedpIERFERENRRLQEANMRLEQENDDLA 856
Cdd:pfam03148 15 QRNDAErlrQESRRLRnETDAKTKWDQydsnRRLGERIQDITFWKSELEKE---LEELDEEIELLLEEKRRLEKALEALE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 857 H-ELVTSK-IALRK-----DL--DNAEEkadALNKEL--------LMtKQKLIDAEDEKRRLEEesaqLKEMCRREL-DK 918
Cdd:pfam03148 92 EpLHIAQEcLTLREkrqgiDLvhDEVEK---ELLKEVeliegiqeLL-QRTLEQAWEQLRLLRA----ARHKLEKDLsDK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 919 AES--------EIKKNSSIIGDYKQicsqlSERLEKQQTA----------NKVEIEKIRQkvdDCDRCRDFFNkEGRVKG 980
Cdd:pfam03148 164 KEAleidekclSLNNTSPNISYKPG-----PTRIPPNSSTpeewekftqdNIERAEKERA---ASAQLRELID-SILEQT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762592 981 ASSVKGVSD----------EDTDEEKETLKNQLRELELELAQTKLQLVEAECKIQDLEHHLGLA 1034
Cdd:pfam03148 235 ANDLRAQADavnfalrkriEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLA 298
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
870-961 |
9.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 870 LDNAEEKADALNKE-LLMTKQKLI----DAEDE-KRRLEEESAQLKEMCRRE--LDKAESEIKKNSSIIGDYKQICSQLS 941
Cdd:PRK12704 44 LEEAKKEAEAIKKEaLLEAKEEIHklrnEFEKElRERRNELQKLEKRLLQKEenLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100
....*....|....*....|
gi 1958762592 942 ERLEKQQTankvEIEKIRQK 961
Cdd:PRK12704 124 QELEKKEE----ELEELIEE 139
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
819-961 |
9.45e-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: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 819 TMREQQAQQEDPIERFERENRRLQEANMRLEQENDdlahelvtskialRKDLDNAEEKADALNKELLMTKQKLIDA-EDE 897
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQ-------------RRLQQEQLERAEKMREELELEQQRRFEEiRLR 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762592 898 KRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQK 961
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL-QRKKQQEEAERAEAEKQRQK 455
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
819-1044 |
9.63e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.67 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 819 TMREQQAQQEDPIERFERENRRLQEanmrLEQENDdlahelvtskiALRKDLDNAEEKADALNKELLMTKQKLIDAEDEK 898
Cdd:pfam19220 112 ELRDKTAQAEALERQLAAETEQNRA----LEEENK-----------ALREEAQAAEKALQRAEGELATARERLALLEQEN 176
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 899 RRL----EEESAQLKEMCRReLDKAESEIKKNSSIIGDYK-QICSQLSER------LEKQQTANKVEIEKIRQKVDDC-- 965
Cdd:pfam19220 177 RRLqalsEEQAAELAELTRR-LAELETQLDATRARLRALEgQLAAEQAEReraeaqLEEAVEAHRAERASLRMKLEALta 255
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762592 966 -----------------DRCRDFFNKEGRVKGASSvkgvsdedtdeEKETLKNQLRELELELAQTKLQLVEAECKIQDLE 1028
Cdd:pfam19220 256 raaateqllaearnqlrDRDEAIRAAERRLKEASI-----------ERDTLERRLAGLEADLERRTQQFQEMQRARAELE 324
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250
....*....|....*.
gi 1958762592 1029 HHLGlALSEVQAAKKT 1044
Cdd:pfam19220 325 ERAE-MLTKALAAKDA 339
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