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Conserved domains on  [gi|109892476|sp|Q2PQA9|]
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RecName: Full=Kinesin-1 heavy chain; AltName: Full=Conventional kinesin heavy chain; AltName: Full=Ubiquitous kinesin heavy chain; Short=UKHC

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 6-325 0e+00

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


:

Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 635.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   6 ECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIAS----KPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTI 81
Cdd:cd01369    1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATsetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  82 FAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNR 161
Cdd:cd01369   81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKT 241
Cdd:cd01369  161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 242 GAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ 320
Cdd:cd01369  241 GAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                 ....*
gi 109892476 321 RAKTI 325
Cdd:cd01369  321 RAKTI 325
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 834-903 7.81e-23

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


:

Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 92.65  E-value: 7.81e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 834 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIK 903
Cdd:cd23649    1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-803 1.07e-15

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.41  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaskeevkevlq 493
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE------------- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   494 aLEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA---EMMASLLKDLAEIGIAVG 570
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLT 647
Cdd:TIGR02168  821 NLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   648 EYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNkvQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKE 727
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109892476   728 KLITDLQDQNQKMVLEQERLRVEHERLKA--VDQEKSRKLHElTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLF 803
Cdd:TIGR02168  979 NKIKELGPVNLAAIEEYEELKERYDFLTAqkEDLTEAKETLE-EAIEEIDREARERFKDTFDQVNENFQRV--FPKLF 1053
 
Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 6-325 0e+00

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 635.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   6 ECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIAS----KPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTI 81
Cdd:cd01369    1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATsetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  82 FAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNR 161
Cdd:cd01369   81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKT 241
Cdd:cd01369  161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 242 GAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ 320
Cdd:cd01369  241 GAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                 ....*
gi 109892476 321 RAKTI 325
Cdd:cd01369  321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 8-332 1.77e-155

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 461.27  E-value: 1.77e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476     8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMI---------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYN 78
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476    79 GTIFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHED 158
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   159 KNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQE--NTQTEQKLSGKLYLVDLAGSE 236
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   237 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAE--GSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKS 314
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                          330
                   ....*....|....*...
gi 109892476   315 TLLFGQRAKTIKNTVCVN 332
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
14-325 8.91e-154

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 456.65  E-value: 8.91e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   14 RFRPLNESEVNRGDKYV---------AKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:pfam00225   1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LSVHEDKNR 161
Cdd:pfam00225  81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQT---EQKLSGKLYLVDLAGSEKV 238
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  239 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTL 316
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                  ....*....
gi 109892476  317 LFGQRAKTI 325
Cdd:pfam00225 318 RFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
8-333 2.20e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 293.95  E-value: 2.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGD---KYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:COG5059   17 NEKSVSDIKSTIRIIPGELGerlINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPY 164
Cdd:COG5059   97 GQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVK 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 165 VKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAE 244
Cdd:COG5059  174 VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNR 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 245 GAVLDEAKNINKSLSALGNVISAL--AEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRA 322
Cdd:COG5059  254 GTRLKEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRA 333

                        330
                 ....*....|.
gi 109892476 323 KTIKNTVCVNV 333
Cdd:COG5059  334 KSIKNKIQVNS 344
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 5-515 1.04e-62

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 232.13  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476    5 AECNIKVMCRFRPLNESEvnRGDKYVAKFQGeDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:PLN03188   96 SDSGVKVIVRMKPLNKGE--EGEMIVQKMSN-DSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAY 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   85 GQTSSGKTHTMEGKLH-------DPEGMGIIPRIVQDIFNYIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKTN 152
Cdd:PLN03188  173 GQTGSGKTYTMWGPANglleehlSGDQQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQKN 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  153 LSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSG----KLY 228
Cdd:PLN03188  253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRIN 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  229 LVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGST-----YVPYRDSKMTRILQDSLGGNCRTTIVICCS 303
Cdd:PLN03188  333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  304 PSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEqwkkkyekekekNKTLRNTIQWLENELNRWRNGETVPideqfdke 383
Cdd:PLN03188  413 PSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD------------VNFLREVIRQLRDELQRVKANGNNP-------- 472

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  384 kanleafTADKDVAITNDKPAAAIGMAGSFTDAERRkceeeiaKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLAst 463
Cdd:PLN03188  473 -------TNPNVAYSTAWNARRSLNLLKSFGLGPPP-------SLPHVDEDGDEEMEIDEEAVERLCVQVGLQPAGAA-- 536

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109892476  464 rrdqDNMQAELNRLQAENDASKEEVKEvlQALEELAVNYDQKSQEVEDKTKE 515
Cdd:PLN03188  537 ----EGNNVDMGRVESIHSSDQQSIIK--QGSEDTDVDMEEAISEQEEKHEI 582
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 834-903 7.81e-23

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 92.65  E-value: 7.81e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 834 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIK 903
Cdd:cd23649    1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-803 1.07e-15

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: 82.41  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaskeevkevlq 493
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE------------- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   494 aLEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA---EMMASLLKDLAEIGIAVG 570
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLT 647
Cdd:TIGR02168  821 NLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   648 EYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNkvQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKE 727
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109892476   728 KLITDLQDQNQKMVLEQERLRVEHERLKA--VDQEKSRKLHElTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLF 803
Cdd:TIGR02168  979 NKIKELGPVNLAAIEEYEELKERYDFLTAqkEDLTEAKETLE-EAIEEIDREARERFKDTFDQVNENFQRV--FPKLF 1053
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-886 2.80e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 74.31  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTqmlDQEELLASTRRDQdnmqAELNRLQAENDASKEEVKEVLQA 494
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEE---ERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDR 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGIAVGNNDV 574
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE----LEEEIEELRERFGDAPV 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 575 KQPEGTGMIDEeftvarlyiskMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAA-----C--QLRISQHEAKIKSLT 647
Cdd:PRK02224 406 DLGNAEDFLEE-----------LREERDELREREAELEATLRTARERVEEAEALLEAgkcpeCgqPVEGSPHVETIEEDR 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 648 EYLQNVEQKKRQLEESVDSLGEELVQLraqEKVHEMEKEhlnkVQTANEVKQAVEQQIQSHRET---HQKQISSLRDEVE 724
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERA---EDLVEAEDR----IERLEERREDLEELIAERRETieeKRERAEELRERAA 547

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 725 AKEKLITDLQDQNQKMVLEQERLRVE----HERLKAVDQEKSRkLHELTVMQDRREQARQDLKGLEETVaKELQTLHNLR 800
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEvaelNSKLAELKERIES-LERIRTLLAAIADAEDEIERLREKR-EALAELNDER 625

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 801 KLFVQDLATRVKK-SAEVDSDDTGGSAAQKQKisfLENNLEQLTKVHKQLVRDNADLRC----------ELPKLEKRLRA 869
Cdd:PRK02224 626 RERLAEKRERKRElEAEFDEARIEEAREDKER---AEEYLEQVEEKLDELREERDDLQAeigaveneleELEELRERREA 702

                        490
                 ....*....|....*..
gi 109892476 870 TAERVKALESALKEAKE 886
Cdd:PRK02224 703 LENRVEALEALYDEAEE 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 609-911 1.97e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 609 KQLESTQTESNK-------KMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQekvh 681
Cdd:COG1196  200 RQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---- 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 682 emekehLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKmvlEQERLRVEHERLKAVDQEK 761
Cdd:COG1196  276 ------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE---LEEELEELEEELEELEEEL 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 762 SRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTgGSAAQKQKISFLENNLEQ 841
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEE 425

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 842 LTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNM 911
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 417-788 6.80e-08

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: 56.90  E-value: 6.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELlastrrdqdnmqaELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-------------KLQELKLKEQAKKALEYYQLKEKL 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   497 ELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQ 576
Cdd:pfam02463  220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   577 pegtgmidEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKsltEYLQNVEQK 656
Cdd:pfam02463  300 --------SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKL 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   657 KRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSlrdEVEAKEKLITDLQDQ 736
Cdd:pfam02463  369 EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE---ILEEEEESIELKQGK 445

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 109892476   737 NQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEET 788
Cdd:pfam02463  446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
 446-773 5.38e-05

Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.


Pssm-ID: 214826 [Multi-domain]  Cd Length: 426  Bit Score: 46.59  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   446 VEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQ 525
Cdd:smart00806  73 VEELDEVKKHIDDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARPAASPSPVLASSSSAISLANNPDKLNKE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   526 KSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLA---EIGIAVGNNDvkqpegtgmideeftvARLYISKMKSEVK 602
Cdd:smart00806 153 QRAELKSLQRELAVLRQTHNSFFTEIKESIKDILEKIDkfkSSSLSASGSS----------------NRAYVESSKKKLS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   603 TMVKR-CKQLESTQ---------------TESNKKMEENEKELAACqlrisqhEAKIKSLTEYLQNVE-QKKRQLEESVD 665
Cdd:smart00806 217 EDSDSlLTKVDDLQdiiealrkdvaqrgvRPSKKQLETVQKELETA-------RKELKKMEEYIDIEKpIWKKIWEAELD 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   666 SLGEELVQLRAQEKVHEMEKEHLNKV-QTANEVKQAVEQQIQSHRETHQKQISSlrdeVEAKEKLITDLQDQnqkMVLEQ 744
Cdd:smart00806 290 KVCEEQQFLTLQEDLIADLKEDLEKAeETFDLVEQCCEEQEKGPSKNRNKPVSL----PVPTPGTFNDLKDQ---VLMEV 362

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 109892476   745 ERLRVEHE-RLKAVD-----QEKSRKLHELTVMQD 773
Cdd:smart00806 363 RALKPDHEsRLEAIEraeklREKELEYRRVDEFEK 397
 
Name Accession Description Interval E-value
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 6-325 0e+00

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 635.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   6 ECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIAS----KPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTI 81
Cdd:cd01369    1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATsetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  82 FAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNR 161
Cdd:cd01369   81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKT 241
Cdd:cd01369  161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 242 GAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ 320
Cdd:cd01369  241 GAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                 ....*
gi 109892476 321 RAKTI 325
Cdd:cd01369  321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 8-332 1.77e-155

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 461.27  E-value: 1.77e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476     8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMI---------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYN 78
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476    79 GTIFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHED 158
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   159 KNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQE--NTQTEQKLSGKLYLVDLAGSE 236
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   237 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAE--GSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKS 314
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                          330
                   ....*....|....*...
gi 109892476   315 TLLFGQRAKTIKNTVCVN 332
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 8-323 2.81e-154

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 457.87  E-value: 2.81e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVaKFQGEDTVMI--------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNG 79
Cdd:cd00106    1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLdppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  80 TIFAYGQTSSGKTHTMEGKlhDPEGMGIIPRIVQDIFNYIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VSKTNLSVHE 157
Cdd:cd00106   80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 158 DKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQT--EQKLSGKLYLVDLAGS 235
Cdd:cd00106  158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 236 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGS-TYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKS 314
Cdd:cd00106  238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317


                 ....*....
gi 109892476 315 TLLFGQRAK 323
Cdd:cd00106  318 TLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
14-325 8.91e-154

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 456.65  E-value: 8.91e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   14 RFRPLNESEVNRGDKYV---------AKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:pfam00225   1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LSVHEDKNR 161
Cdd:pfam00225  81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQT---EQKLSGKLYLVDLAGSEKV 238
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  239 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTL 316
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                  ....*....
gi 109892476  317 LFGQRAKTI 325
Cdd:pfam00225 318 RFASRAKNI 326
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 8-325 8.86e-119

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 365.50  E-value: 8.86e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKyVAKFQGEDTVM---IASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:cd01374    1 KITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYlvePPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  85 GQTSSGKTHTMEGKLHDPegmGIIPRIVQDIFNYIYsMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPY 164
Cdd:cd01374   80 GQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 165 VKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVkqENTQTEQKLSGK-----LYLVDLAGSEKVS 239
Cdd:cd01374  156 VAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI--ESSERGELEEGTvrvstLNLIDLAGSERAA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 240 KTGAEGAVLDEAKNINKSLSALGNVISALAEG--STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLL 317
Cdd:cd01374  234 QTGAAGVRRKEGSHINKSLLTLGTVISKLSEGkvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLK 313


                 ....*...
gi 109892476 318 FGQRAKTI 325
Cdd:cd01374  314 FASRAKKI 321
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 7-326 1.39e-116

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 360.49  E-value: 1.39e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   7 CNIKVMCRFRPLNESEVNRGDKYVAKFQ-GEDTVMI-ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:cd01372    1 SSVRVAVRVRPLLPKEIIEGCRICVSFVpGEPQVTVgTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  85 GQTSSGKTHTMEG---KLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VSKTNLSVHED 158
Cdd:cd01372   81 GQTGSGKTYTMGTaytAEEDEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIRED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 159 KNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQE--NTQTEQK--------LSGKLY 228
Cdd:cd01372  161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTkkNGPIAPMsaddknstFTSKFH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 229 LVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGS---TYVPYRDSKMTRILQDSLGGNCRTTIVICCSPS 305
Cdd:cd01372  241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320

                        330       340
                 ....*....|....*....|.
gi 109892476 306 SYNESETKSTLLFGQRAKTIK 326
Cdd:cd01372  321 DSNFEETLNTLKYANRARNIK 341
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 8-327 2.47e-115

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 356.90  E-value: 2.47e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVM------IASKPYAFDRVFQSSTSQEQVYNDcAKKIVKDVLEGYNGTI 81
Cdd:cd01366    3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIeltsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  82 FAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVSKTNLSVHE 157
Cdd:cd01366   82 FAYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 158 D--KNRVpYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGS 235
Cdd:cd01366  159 DseKGDT-TVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 236 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKST 315
Cdd:cd01366  238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                        330
                 ....*....|..
gi 109892476 316 LLFGQRAKTIKN 327
Cdd:cd01366  318 LRFASKVNSCEL 329
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 8-325 1.84e-109

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 341.75  E-value: 1.84e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAKF---QGEDTVMI-------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGY 77
Cdd:cd01371    2 NVKVVVRCRPLNGKEKAAGALQIVDVdekRGQVSVRNpkatanePPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  78 NGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVSKtNLSV 155
Cdd:cd01371   82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 156 HEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV----KQENTQTEQKLsGKLYLVD 231
Cdd:cd01371  161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GKLNLVD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 232 LAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNES 310
Cdd:cd01371  240 LAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGkSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYD 319

                        330
                 ....*....|....*
gi 109892476 311 ETKSTLLFGQRAKTI 325
Cdd:cd01371  320 ETLSTLRYANRAKNI 334
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 8-332 2.26e-105

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 332.01  E-value: 2.26e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIA--------------SKPYAFDRVFQSST-------SQEQVYNDCA 66
Cdd:cd01365    2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNpkqadknnkatrevPKSFSFDYSYWSHDsedpnyaSQEQVYEDLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  67 KKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSM-DENLEFHIKVSYFEIYLDKIRDL 145
Cdd:cd01365   82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 146 LDVS----KTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQ 221
Cdd:cd01365  159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 222 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGST--------YVPYRDSKMTRILQDS 289
Cdd:cd01365  239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkkssFIPYRDSVLTWLLKEN 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 109892476 290 LGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVN 332
Cdd:cd01365  319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 8-325 1.97e-101

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 320.83  E-value: 1.97e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAK--------------------FQGEDTVMIASKP----YAFDRVFQSSTSQEQVYN 63
Cdd:cd01370    1 SLTVAVRVRPFSEKEKNEGFRRIVKvmdnhmlvfdpkdeedgffhGGSNNRDRRKRRNkelkYVFDRVFDETSTQEEVYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  64 DCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPegmGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIR 143
Cdd:cd01370   81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 144 DLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQ---TE 220
Cdd:cd01370  158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTasiNQ 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 221 QKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG---STYVPYRDSKMTRILQDSLGGNCRTT 297
Cdd:cd01370  238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPgkkNKHIPYRDSKLTRLLKDSLGGNCRTV 317

                        330       340
                 ....*....|....*....|....*...
gi 109892476 298 IVICCSPSSYNESETKSTLLFGQRAKTI 325
Cdd:cd01370  318 MIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 6-332 1.62e-100

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 318.89  E-value: 1.62e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   6 ECNIKVMCRFRPLNESEVNRG----------DKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLE 75
Cdd:cd01364    1 GKNIQVVVRCRPFNLRERKASshsvvevdpvRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  76 GYNGTIFAYGQTSSGKTHTMEGK--------LHDPEGMGIIPRIVQDIFNYIYSMDEnlEFHIKVSYFEIYLDKIRDLLD 147
Cdd:cd01364   81 GYNCTIFAYGQTGTGKTYTMEGDrspneeytWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 148 VS---KTNLSVHEDKNRVP--YVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV-KQENTQTEQ 221
Cdd:cd01364  159 PSsdvSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIhIKETTIDGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 222 KL--SGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIV 299
Cdd:cd01364  239 ELvkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSII 318

                        330       340       350
                 ....*....|....*....|....*....|...
gi 109892476 300 ICCSPSSYNESETKSTLLFGQRAKTIKNTVCVN 332
Cdd:cd01364  319 ATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 8-333 3.86e-91

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 293.65  E-value: 3.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIASKP---YAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:cd01373    2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  85 GQTSSGKTHTMEGKLHD----PEGM-GIIPRIVQDIFNYI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSV 155
Cdd:cd01373   82 GQTGSGKTYTMWGPSESdnesPHGLrGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 156 HEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVK---QENTQTEQKLSgKLYLVDL 232
Cdd:cd01373  162 REDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIEsweKKACFVNIRTS-RLNLVDL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 233 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYN 308
Cdd:cd01373  241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320

                        330       340
                 ....*....|....*....|....*
gi 109892476 309 ESETKSTLLFGQRAKTIKNTVCVNV 333
Cdd:cd01373  321 FGETLSTLRFAQRAKLIKNKAVVNE 345
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
8-333 2.20e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 293.95  E-value: 2.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGD---KYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:COG5059   17 NEKSVSDIKSTIRIIPGELGerlINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPY 164
Cdd:COG5059   97 GQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVK 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 165 VKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAE 244
Cdd:COG5059  174 VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNR 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 245 GAVLDEAKNINKSLSALGNVISAL--AEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRA 322
Cdd:COG5059  254 GTRLKEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRA 333

                        330
                 ....*....|.
gi 109892476 323 KTIKNTVCVNV 333
Cdd:COG5059  334 KSIKNKIQVNS 344
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 8-323 2.99e-73

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 244.33  E-value: 2.99e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIA-------SKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT 80
Cdd:cd01376    1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELAdprnhgeTLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  81 IFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFhiKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN 160
Cdd:cd01376   81 VFAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 161 RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV-KQENTQTEQKLSGKLYLVDLAGSEKVS 239
Cdd:cd01376  156 GNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVdQRERLAPFRQRTGKLNLIDLAGSEDNR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 240 KTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFG 319
Cdd:cd01376  236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                 ....
gi 109892476 320 QRAK 323
Cdd:cd01376  316 ARSR 319
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 9-323 7.18e-73

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 244.23  E-value: 7.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   9 IKVMCRFRPLNESEVNRGD-----------------KYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVK 71
Cdd:cd01368    3 VKVYLRVRPLSKDELESEDegcievinsttvvlhppKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  72 DVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPegmGIIPRIVQDIFNYIYsmdenlEFHIKVSYFEIYLDKIRDLLDVS-- 149
Cdd:cd01368   83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 150 -----KTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV--------KQEN 216
Cdd:cd01368  154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapgdsdGDVD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 217 TQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG-----STYVPYRDSKMTRILQDSLG 291
Cdd:cd01368  234 QDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENqlqgtNKMVPFRDSKLTHLFQNYFD 313

                        330       340       350
                 ....*....|....*....|....*....|..
gi 109892476 292 GNCRTTIVICCSPSSYNESETKSTLLFGQRAK 323
Cdd:cd01368  314 GEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 8-323 1.37e-72

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 242.97  E-value: 1.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   8 NIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIASKPYA-------------FDRVFQSSTSQEQVYNDCAKKIVKDVL 74
Cdd:cd01367    1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKvdltkyienhtfrFDYVFDESSSNETVYRSTVKPLVPHIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  75 EGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRI-VQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDvSKTNL 153
Cdd:cd01367   81 EGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 154 SVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTqteQKLSGKLYLVDLA 233
Cdd:cd01367  160 RLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT---NKLHGKLSFVDLA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 234 GSEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSL-GGNCRTTIVICCSPSSYNESE 311
Cdd:cd01367  237 GSERGADTSSADRqTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316

                        330
                 ....*....|..
gi 109892476 312 TKSTLLFGQRAK 323
Cdd:cd01367  317 TLNTLRYADRVK 328
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 46-323 2.35e-71

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 239.79  E-value: 2.35e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  46 YAFDRVFQSStSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIySMDEN 125
Cdd:cd01375   50 FKFDGVLHNA-SQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 126 LEFHIKVSYFEIYLDKIRDLLDV------SKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNE 199
Cdd:cd01375  128 KAYTVHVSYLEIYNEQLYDLLSTlpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 200 HSSRSHSIFLINV--KQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-GSTYVP 276
Cdd:cd01375  208 NSSRSHCIFTIHLeaHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDkDRTHVP 287

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 109892476 277 YRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAK 323
Cdd:cd01375  288 FRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 5-515 1.04e-62

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 232.13  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476    5 AECNIKVMCRFRPLNESEvnRGDKYVAKFQGeDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:PLN03188   96 SDSGVKVIVRMKPLNKGE--EGEMIVQKMSN-DSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAY 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   85 GQTSSGKTHTMEGKLH-------DPEGMGIIPRIVQDIFNYIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKTN 152
Cdd:PLN03188  173 GQTGSGKTYTMWGPANglleehlSGDQQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQKN 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  153 LSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSG----KLY 228
Cdd:PLN03188  253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRIN 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  229 LVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGST-----YVPYRDSKMTRILQDSLGGNCRTTIVICCS 303
Cdd:PLN03188  333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  304 PSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEqwkkkyekekekNKTLRNTIQWLENELNRWRNGETVPideqfdke 383
Cdd:PLN03188  413 PSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD------------VNFLREVIRQLRDELQRVKANGNNP-------- 472

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  384 kanleafTADKDVAITNDKPAAAIGMAGSFTDAERRkceeeiaKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLAst 463
Cdd:PLN03188  473 -------TNPNVAYSTAWNARRSLNLLKSFGLGPPP-------SLPHVDEDGDEEMEIDEEAVERLCVQVGLQPAGAA-- 536

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109892476  464 rrdqDNMQAELNRLQAENDASKEEVKEvlQALEELAVNYDQKSQEVEDKTKE 515
Cdd:PLN03188  537 ----EGNNVDMGRVESIHSSDQQSIIK--QGSEDTDVDMEEAISEQEEKHEI 582
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 11-304 1.38e-50

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 175.61  E-value: 1.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  11 VMCRFRPLNESEVNRGDKYVAkfqgedtvmiaskpyaFDRVFQSSTSQEQVYNDCAKkIVKDVLEGYNG-TIFAYGQTSS 89
Cdd:cd01363    1 VLVRVNPFKELPIYRDSKIIV----------------FYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFAYGESGA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  90 GKTHTMegklhdpegMGIIPRIVQDIFNYIYSMDENLEFHikvsyfeiyldkirdlldvsktnlsvhedknrvpyvkgCT 169
Cdd:cd01363   64 GKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------LT 96

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 170 ERFVCSPDEVMDTIDEGKSNRhVAVTNMNEHSSRSHSIFLInvkqentqteqklsgklyLVDLAGSEkvsktgaegavld 249
Cdd:cd01363   97 EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------- 144

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109892476 250 eakNINKSLSALGNVISAlaegstyvpyrdskmtrilqdslggnCRTTIVICCSP 304
Cdd:cd01363  145 ---IINESLNTLMNVLRA--------------------------TRPHFVRCISP 170
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 7-146 6.69e-25

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 101.14  E-value: 6.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476    7 CNIKVMCRFRPLNESEVNRgdKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCaKKIVKDVLEGYNGTIFAYGQ 86
Cdd:pfam16796  20 GNIRVFARVRPELLSEAQI--DYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQ 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   87 TSSGKTHTMegklhdpegmgiIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLL 146
Cdd:pfam16796  97 TGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 834-903 7.81e-23

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 92.65  E-value: 7.81e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 834 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIK 903
Cdd:cd23649    1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-803 1.07e-15

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: 82.41  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaskeevkevlq 493
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE------------- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   494 aLEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA---EMMASLLKDLAEIGIAVG 570
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLT 647
Cdd:TIGR02168  821 NLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   648 EYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNkvQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKE 727
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109892476   728 KLITDLQDQNQKMVLEQERLRVEHERLKA--VDQEKSRKLHElTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLF 803
Cdd:TIGR02168  979 NKIKELGPVNLAAIEEYEELKERYDFLTAqkEDLTEAKETLE-EAIEEIDREARERFKDTFDQVNENFQRV--FPKLF 1053
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-789 3.69e-14

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: 77.03  E-value: 3.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   495 LEElavnydqksqEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtnhqkkraaEMMASLLKDLAEIGIAVGNndv 574
Cdd:TIGR02169  249 LEE----------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----------EEQLRVKEKIGELEAEIAS--- 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   575 kqpegtgmideeftvARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVE 654
Cdd:TIGR02169  306 ---------------LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   655 QKKRQLEESVDSLGEELVQLRaqEKVhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQ 734
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYR--EKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 109892476   735 DQNQKMVLEQERLRvehERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETV 789
Cdd:TIGR02169  448 LEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 479-905 2.77e-13

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: 74.33  E-value: 2.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   479 AENDASKEevkevlQALEELAvnydqksqEVEDKTKEYELLSDELNQksatlasidaELQKLKEMTNHqkkraAEMMASL 558
Cdd:TIGR02169  166 AEFDRKKE------KALEELE--------EVEENIERLDLIIDEKRQ----------QLERLRREREK-----AERYQAL 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   559 LKDLAEIgiavgnndvkqpegtgmideEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQ 638
Cdd:TIGR02169  217 LKEKREY--------------------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   639 HEAKIKSLTEYLQNveqkkrQLEESVDSLGEELVQLRAQEKVHEMEKEHLnkvqtanevkQAVEQQIQSHRETHQKQISS 718
Cdd:TIGR02169  277 LNKKIKDLGEEEQL------RVKEKIGELEAEIASLERSIAEKERELEDA----------EERLAKLEAEIDKLLAEIEE 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   719 LRDEVEA----KEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQ 794
Cdd:TIGR02169  341 LEREIEEerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   795 TLHNLRklfvQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRAtaerv 874
Cdd:TIGR02169  421 ELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD----RVEKELSK----- 487

                          410       420       430
                   ....*....|....*....|....*....|.
gi 109892476   875 KALESALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:TIGR02169  488 LQRELAEAEAQARASEERVRGGRAVEEVLKA 518
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-886 2.80e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 74.31  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTqmlDQEELLASTRRDQdnmqAELNRLQAENDASKEEVKEVLQA 494
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEE---ERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDR 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGIAVGNNDV 574
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE----LEEEIEELRERFGDAPV 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 575 KQPEGTGMIDEeftvarlyiskMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAA-----C--QLRISQHEAKIKSLT 647
Cdd:PRK02224 406 DLGNAEDFLEE-----------LREERDELREREAELEATLRTARERVEEAEALLEAgkcpeCgqPVEGSPHVETIEEDR 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 648 EYLQNVEQKKRQLEESVDSLGEELVQLraqEKVHEMEKEhlnkVQTANEVKQAVEQQIQSHRET---HQKQISSLRDEVE 724
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERA---EDLVEAEDR----IERLEERREDLEELIAERRETieeKRERAEELRERAA 547

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 725 AKEKLITDLQDQNQKMVLEQERLRVE----HERLKAVDQEKSRkLHELTVMQDRREQARQDLKGLEETVaKELQTLHNLR 800
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEvaelNSKLAELKERIES-LERIRTLLAAIADAEDEIERLREKR-EALAELNDER 625

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 801 KLFVQDLATRVKK-SAEVDSDDTGGSAAQKQKisfLENNLEQLTKVHKQLVRDNADLRC----------ELPKLEKRLRA 869
Cdd:PRK02224 626 RERLAEKRERKRElEAEFDEARIEEAREDKER---AEEYLEQVEEKLDELREERDDLQAeigaveneleELEELRERREA 702

                        490
                 ....*....|....*..
gi 109892476 870 TAERVKALESALKEAKE 886
Cdd:PRK02224 703 LENRVEALEALYDEAEE 719
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 594-907 7.74e-13

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: 72.79  E-value: 7.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   594 ISKMKSEVKTMVKRCKQLESTQTESNKKME----ENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGE 669
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLErlrrEREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   670 ELVQLraQEKVHEMEKEHLNKVQTANEVKQAVEQ-------QIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVL 742
Cdd:TIGR02169  252 ELEKL--TEEISELEKRLEEIEQLLEELNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   743 EQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLhnlrklfVQDLATRVKKSAEVdsddt 822
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET-------RDELKDYREKLEKL----- 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   823 ggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASR---DRKRYQQEV 899
Cdd:TIGR02169  398 ------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaaDLSKYEQEL 471


                   ....*...
gi 109892476   900 DRIKEAVR 907
Cdd:TIGR02169  472 YDLKEEYD 479
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
417-922 1.04e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.40  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 417 ERRKCEEEIAKL---YKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKE--EVKEV 491
Cdd:PRK03918 215 ELPELREELEKLekeVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEE 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 492 LQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKdLAEIGIAVGN 571
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 572 NDVKQPEGTGMIDEEFTVARLYISKMKSEV----KTMVKRCKQLESTQTESNKKMEENEKELAACQL---RISQHEAK-- 642
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIeeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrELTEEHRKel 453

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 643 IKSLTEYLQNVEQKKRQLEESVDSLGEELVQLraqEKVHEMEKEHLNKVQTANEVKqAVEQQIQSHR----ETHQKQISS 718
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELREL---EKVLKKESELIKLKELAEQLK-ELEEKLKKYNleelEKKAEEYEK 529

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 719 LRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELtvmqdrREQARQDLKGLEETVA-------- 790
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL------EELGFESVEELEERLKelepfyne 603

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 791 --------KELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQ-KISFLENNLEQLTKVHKQLVRDNADLRCELP 861
Cdd:PRK03918 604 ylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELE 683

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109892476 862 KLEKRLRATAERVKALESALKEAKENASR--DRKRYQQEVDRIKEAVRS-KNMARRGHSAQIAK 922
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKEleKLEKALERVEELREKVKKyKALLKERALSKVGE 747
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 609-911 1.97e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 609 KQLESTQTESNK-------KMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQekvh 681
Cdd:COG1196  200 RQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---- 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 682 emekehLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKmvlEQERLRVEHERLKAVDQEK 761
Cdd:COG1196  276 ------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE---LEEELEELEEELEELEEEL 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 762 SRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTgGSAAQKQKISFLENNLEQ 841
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEE 425

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 842 LTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNM 911
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 624-909 2.69e-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: 71.24  E-value: 2.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   624 ENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQekVHEMEKEHLNKVQTANEVKQAVeQ 703
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERI-A 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   704 QIQSHRETHQKQISSLRDEVeakEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLK 783
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERL---EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   784 GLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQkisflennLEQLTKVHKQLVRDNADLRCELPKL 863
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--------LEALLNERASLEEALALLRSELEEL 899

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 109892476   864 EKRLRATAERVKALESALKEAKENASRDRKRYQ---QEVDRIKEAVRSK 909
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEgleVRIDNLQERLSEE 948
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-912 1.18e-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: 68.93  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   412 SFTDAERRKCEEEIAK-------LYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDAS 484
Cdd:TIGR02168  270 EELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   485 KEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtnhQKKRAAEMMASLLKDLAE 564
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEE 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   565 IGIAVGNNDVKQPEGT-GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEaki 643
Cdd:TIGR02168  426 LLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE--- 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   644 kSLTEYLQNVEQKKRQLEESVDSLGEelvQLRAQEK----VHEMEKEHLNK--VQTANEVKQAVE--------------- 702
Cdd:TIGR02168  503 -GFSEGVKALLKNQSGLSGILGVLSE---LISVDEGyeaaIEAALGGRLQAvvVENLNAAKKAIAflkqnelgrvtflpl 578

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   703 -----QQIQSHRETHQKQI----SSLRDEVEAKEKL-------------ITDLQDQNQKMVLEQERLRV----------- 749
Cdd:TIGR02168  579 dsikgTEIQGNDREILKNIegflGVAKDLVKFDPKLrkalsyllggvlvVDDLDNALELAKKLRPGYRIvtldgdlvrpg 658

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   750 -----EHERLKAVDQEKSRKLHELtvmqdrreqaRQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSddtgg 824
Cdd:TIGR02168  659 gvitgGSAKTNSSILERRREIEEL----------EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----- 723

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   825 saaQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN---ASRDRKRYQQEVDR 901
Cdd:TIGR02168  724 ---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKA 800

                          570
                   ....*....|.
gi 109892476   902 IKEAVRSKNMA 912
Cdd:TIGR02168  801 LREALDELRAE 811
PTZ00121 PTZ00121
MAEBL; Provisional
 416-913 1.75e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMlDQEELLASTRRDQDNMQAELNRLQAENDASK-EEVKEVlqa 494
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-AKKKADAAKKKAEEKKKADEAKKKAEEDKKKaDELKKA--- 1413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  495 lEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtNHQKKRAAEMMASLLKDLAEIGIAVGNNDV 574
Cdd:PTZ00121 1414 -AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  575 KQPEGTGMIDEEFTVARLyiSKMKSEVKTMVKRCKQLESTQTESNKKMEENEKelaACQLRISQHEAKIKSL--TEYLQN 652
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEA--KKKADEAKKAEEAKKADEAKKAEEAKKADEAKK---AEEKKKADELKKAEELkkAEEKKK 1565

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  653 VEQKKRQLEESVDSL--GEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHR----ETHQKQISSLRDEVEAK 726
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEE 1645

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  727 EKLITDLQ--DQNQKMVLEQERLRVEHERLKA-----VDQEKSRKLHELTVMQDRREQARQDLKGLEETV--AKELQTLH 797
Cdd:PTZ00121 1646 KKKAEELKkaEEENKIKAAEEAKKAEEDKKKAeeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkAEELKKAE 1725

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  798 NLRKLFVQDL---ATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRlRATAERV 874
Cdd:PTZ00121 1726 EENKIKAEEAkkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIF 1804

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 109892476  875 KALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMAR 913
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
435-913 2.39e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 67.76  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 435 KDEEINQQSQLVEkLKTQMLDQEE-----LLASTRRDQDNMQAELNRLQAEndasKEEVKEVLQALEELAVNYDQKSQEV 509
Cdd:PRK02224 179 ERVLSDQRGSLDQ-LKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERREEL 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 510 EDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASL-LKDLAEIGIAVGNNDVKQPEGTgmIDEEFT 588
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAgLDDADAEAVEARREELEDRDEE--LRDRLE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 589 VARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLG 668
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 669 EELVQLRAQ-EKVHEMEKEHLNKVQTANEVKQAVEQQIQSHR--ETHQK-QISSLRDEVEAKEKLITDLQDQNQKMVLEQ 744
Cdd:PRK02224 412 DFLEELREErDELREREAELEATLRTARERVEEAEALLEAGKcpECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEV 491

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 745 ERLRVEHERLK-AVDQEKsrklhELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLfVQDLAT--RVKKSAEVDSDD 821
Cdd:PRK02224 492 EEVEERLERAEdLVEAED-----RIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAeaEEKREAAAEAEE 565

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 822 TGGSAAQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR-------------LRATAERVKALESALK 882
Cdd:PRK02224 566 EAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRealaelnderrerLAEKRERKRELEAEFD 644

                        490       500       510
                 ....*....|....*....|....*....|..
gi 109892476 883 EAK-ENASRDRKRYQQEVDRIKEAVRSKNMAR 913
Cdd:PRK02224 645 EARiEEAREDKERAEEYLEQVEEKLDELREER 676
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-664 4.57e-11

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: 67.02  E-value: 4.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKL---------------KTQMLDQEELLASTRR-------DQDNMQ 471
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeqlrvKEKIGELEAEIASLERsiaekerELEDAE 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   472 AELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLK---EMTNHQK 548
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   549 KRAAEMMASLLKDLAEIGIAVGNndvkqpegtgmIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKE 628
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELAD-----------LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 109892476   629 LAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESV 664
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 416-761 6.70e-11

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: 66.63  E-value: 6.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEEllaSTRRdqdnMQAELNRLQAENDASKEEvkevlqaL 495
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGE----IEKEIEQLEQEEEKLKER-------L 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   496 EELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQK-KRAAEMMASLLKDLAEIGIAVgnNDV 574
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL--REI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   575 KQPEGTGMIDEEFtvARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAK-------IKSLT 647
Cdd:TIGR02169  818 EQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdlkkeRDELE 895

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   648 EYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANE---VKQAVEQQIQSHRETHQKQISSLR---- 720
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALEpvnm 975

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 109892476   721 ---DEVEAKEKLITDLQDQNQKMVLEQERLRvehERLKAVDQEK 761
Cdd:TIGR02169  976 laiQEYEEVLKRLDELKEKRAKLEEERKAIL---ERIEEYEKKK 1016
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 475-884 1.51e-10

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: 65.46  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   475 NRLQAEN--DASKEEVKEVLQALEELAVNYDQKSQEVEdKTKEYELLSDELNQKSATLASIDA-ELQKLKEMTNHQKKRA 551
Cdd:TIGR02168  173 RRKETERklERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLeELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   552 AEMMASLLKDLAEIgiavgnndvkqpegtgmiDEEFTVARLYISKMksevktmvkrckqlestqtesNKKMEENEKELAA 631
Cdd:TIGR02168  252 EEELEELTAELQEL------------------EEKLEELRLEVSEL---------------------EEEIEELQKELYA 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   632 CQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTA----NEVKQAVEQQIQS 707
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESleaeLEELEAELEELES 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   708 HRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAV--DQEKSRKLHELTVMQDRREQARQDLKGL 785
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEieELLKKLEEAELKELQAELEELEEELEEL 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   786 EETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSddtggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEK 865
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQ-----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527

                          410
                   ....*....|....*....
gi 109892476   866 RLRATAERVKALESALKEA 884
Cdd:TIGR02168  528 LISVDEGYEAAIEAALGGR 546
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 415-908 4.94e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 4.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASI-DAELQKLKEMTNHQKK--RAAEMMASLLKDLAEIGIAVGN 571
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaEELLEALRAAAELAAQleELEEAEEALLERLERLEEELEE 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 572 NDVKQPEgtgmIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQ 651
Cdd:COG1196  426 LEEALAE----LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 652 NVEQ-----KKRQLEESVDSLGEELVQLRAQEKVHEMEKEHL---NKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEV 723
Cdd:COG1196  502 DYEGflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 724 EAKEKLITDLQDQNQKM----------VLEQERLRVEHERLKAVDQEKSRKLHELTVM---QDRREQARQDLKGLEETVA 790
Cdd:COG1196  582 IRARAALAAALARGAIGaavdlvasdlREADARYYVLGDTLLGRTLVAARLEAALRRAvtlAGRLREVTLEGEGGSAGGS 661

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 791 KELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 870
Cdd:COG1196  662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 109892476 871 AERVKALESALKEAKENASrDRKRYQQEVDRIKEAVRS 908
Cdd:COG1196  742 LEEEELLEEEALEELPEPP-DLEELERELERLEREIEA 778
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
423-816 5.05e-10

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 5.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 423 EEIAKLYKQLDDKDEEInqqsqlvEKLKTQMLDQEELlastRRDQDNMQAELNRLQAENDASKEEVK-EVLQALEELAVN 501
Cdd:COG4717  132 QELEALEAELAELPERL-------EELEERLEELREL----EEELEELEAELAELQEELEELLEQLSlATEEELQDLAEE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 502 YDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtnHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL---EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 582 MIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLE 661
Cdd:COG4717  278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 662 E-----SVDSLGEELVQLRAQEKVHEMEK-----EHLNKVQTANEVKQAVEQQIQSHRETHQKQIsslrdEVEAKEKLIT 731
Cdd:COG4717  358 EleeelQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEE 432

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 732 DLQDQNQKMVLEQERLRVEHERLKAVDQEKSR--KLHELTVMQDRREQARQDLKGLEETVAK---ELQTLHNLRKLFVQD 806
Cdd:COG4717  433 ELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAAlklALELLEEAREEYREE 512

                        410
                 ....*....|
gi 109892476 807 LATRVKKSAE 816
Cdd:COG4717  513 RLPPVLERAS 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 640-905 7.69e-10

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: 63.15  E-value: 7.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   640 EAKIKSLTEYLQNVEQKKRQLEESVDSLG------EELVQLRAQEKVHEME------KEHLNKVQTANEVKQAVEQQIQS 707
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELAllvlrlEELREELEELQEELKEAEEELEE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   708 HRE---THQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKG 784
Cdd:TIGR02168  258 LTAelqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   785 LEETVAKELQTLHNLRKLFVQDLATRVKKSAEvdsddtggsaaQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLE 864
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEE-----------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 109892476   865 KRLRATAERVKALESALKEAKENASR-DRKRYQQEVDRIKEA 905
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEE 448
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 460-679 3.63e-09

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: 59.78  E-value: 3.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 460 LASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQK 539
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 540 LKEMTNHQKKRAAEMMASLLK--DLAEIGIAVGNNDVKQPEGTGMIDEEFTVARL-YISKMKSEVKTMVKRCKQLESTQT 616
Cdd:COG4942   95 LRAELEAQKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109892476 617 ESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEK 679
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 595-904 5.93e-09

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: 60.08  E-value: 5.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   595 SKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQL 674
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   675 raQEKVHEMEKEhLNKVQT--ANEVKQAVEQQIQSHRETHQKQISSLRD----------EVEAKEKLITDLQDQNQKMVL 742
Cdd:TIGR02169  771 --EEDLHKLEEA-LNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREieqklnrltlEKEYLEKEIQELQEQRIDLKE 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   743 EQERLRVEHERLKAVDQEKSRKLHELtvmQDRREQARQDLKGLEETVAKELQTLHNLRKLfVQDLATRVKKSAEVDSDdt 822
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEEL---EAALRDLESRLGDLKKERDELEAQLRELERK-IEELEAQIEKKRKRLSE-- 921

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   823 ggsaaQKQKISFLENNLEQLTKVHKQLVRDNADLrCELPKLEKRLRATAERVKALES----ALKEAKENASRdRKRYQQE 898
Cdd:TIGR02169  922 -----LKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALEPvnmlAIQEYEEVLKR-LDELKEK 994


                   ....*.
gi 109892476   899 VDRIKE 904
Cdd:TIGR02169  995 RAKLEE 1000
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 415-542 1.28e-08

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: 56.47  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTR--RDQDNMQAELNRLQAENDASKEEVKEVL 492
Cdd:COG1579   37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELM 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 109892476 493 QALEELAVNYDQKSQEVEDKTKEYELLSDELNQKsatLASIDAELQKLKE 542
Cdd:COG1579  117 ERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEA 163
PTZ00121 PTZ00121
MAEBL; Provisional
 417-861 1.56e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  417 ERRKCEE-----EIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEellASTRRDQDNMQAELNRLQAENDASKEEVKEV 491
Cdd:PTZ00121 1442 EAKKADEakkkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  492 LQALEElavnydQKSQEVEDKTKEYELLSDELNQKSATLASIDaELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVgn 571
Cdd:PTZ00121 1519 EEAKKA------DEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-- 1589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  572 nDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMV----------KRCKQLESTQTESNKKMEENEKELAACQLRISQHEA 641
Cdd:PTZ00121 1590 -EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkkaeeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  642 KI---KSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISS 718
Cdd:PTZ00121 1669 KAeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  719 LRDEVEAKEKLITDLQDQNQK---------MVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQAR---QDLKGLE 786
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKaeeirkekeAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlviNDSKEME 1828

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109892476  787 ETVAKELQTLHNLR----KLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEqlTKVHKQLvrDNADLRCELP 861
Cdd:PTZ00121 1829 DSAIKEVADSKNMQleeaDAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE--ADEIEKI--DKDDIEREIP 1903
PTZ00121 PTZ00121
MAEBL; Provisional
 418-922 1.66e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  418 RRKCEEEIAKLYKQLDD--KDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRlQAENDASKEEVKEVlqal 495
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEKKKA---- 1292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  496 EELAVNYDQKSQEVEDKTKEYELLSDELNQKsATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVK 575
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  576 QPEGTGMIDEEftvarlyiSKMKSEVKtmvKRCKQLESTQTESNKKMEENEKELAAcqlRISQHEAKIKSltEYLQNVEQ 655
Cdd:PTZ00121 1372 KKEEAKKKADA--------AKKKAEEK---KKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKA--EEKKKADE 1435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  656 KKRQLEESVDSlgEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQ-----QIQSHRETHQKQISSLRDEVEAKEKLI 730
Cdd:PTZ00121 1436 AKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkadEAKKKAEEAKKKADEAKKAAEAKKKAD 1513

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  731 TDLQDQNQKMVLE---------QERLRVEHERLKAVDQEKSRKLHEL----TVMQDRREQARQDLKGLEETVAKELQTLH 797
Cdd:PTZ00121 1514 EAKKAEEAKKADEakkaeeakkADEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  798 NLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCElpKLEKRLRATAERVKAL 877
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAE 1671

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 109892476  878 ESALK-EAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAK 922
Cdd:PTZ00121 1672 EDKKKaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
414-883 1.93e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 414 TDAERRkceEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTrrdqdnmqAELNRLQAENDASKEEVKEVLQ 493
Cdd:PRK03918 142 ESDESR---EKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRT--------ENIEELIKEKEKELEEVLREIN 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 494 ALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASlLKDLAEIgiavgnnd 573
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-IEELEEK-------- 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 574 VKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKElaacqlrisqhEAKIKSLTEYLQNV 653
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKEL 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 654 EQKKRQLEESVDSLgEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVE--QQIQSHRETHQKQISSLRDEVEAKEKLIT 731
Cdd:PRK03918 351 EKRLEELEERHELY-EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIE 429

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 732 DLQDQNQKMVLEQERLRVEHER--LKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKElQTLHNLRKLFVQDLAT 809
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKEL 508

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109892476 810 RvKKSAEVDSDDTggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRcELPKLEKRLRATAERVKALESALKE 883
Cdd:PRK03918 509 E-EKLKKYNLEEL------EKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAE 574
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-904 2.62e-08

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: 58.16  E-value: 2.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHqkKRAAEMMAS--------LLKDLAEIG 566
Cdd:TIGR02169  457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG--GRAVEEVLKasiqgvhgTVAQLGSVG 534

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   567 --------IAVGN---------------------------------NDVKQPE--------------------------- 578
Cdd:TIGR02169  535 eryataieVAAGNrlnnvvveddavakeaiellkrrkagratflplNKMRDERrdlsilsedgvigfavdlvefdpkyep 614

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   579 ------GTGMIDEEFTVARLYISKM-----------KSEVKT--------MVKRCKQLESTQTESNKKMEENEKELAACQ 633
Cdd:TIGR02169  615 afkyvfGDTLVVEDIEAARRLMGKYrmvtlegelfeKSGAMTggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQ 694

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   634 LRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQA-VEQQIQSHREth 712
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeLEARIEELEE-- 772

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   713 qkQISSLRDEVEAKEKLITDL---QDQNQKMVLEQERLRVEhERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETV 789
Cdd:TIGR02169  773 --DLHKLEEALNDLEARLSHSripEIQAELSKLEEEVSRIE-ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   790 AKELQTLHNLrKLFVQDLATRVKKsaevdsddtggsaaqkqkisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKR--- 866
Cdd:TIGR02169  850 KSIEKEIENL-NGKKEELEEELEE---------------------LEAALRDLESRLGDLKKERDELEAQLRELERKiee 907

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 109892476   867 LRATAERVKALESALKEAKENASRDRKRYQQEVDRIKE 904
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
415-769 3.83e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 415 DAERRKCEEEIA--KLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELlastRRDQDNMQAELNRLQAENDASKEEVK-EV 491
Cdd:COG4717  115 REELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSlAT 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 492 LQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGN 571
Cdd:COG4717  191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 572 NDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEE--------------------------- 624
Cdd:COG4717  271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllaalglppdlspeellelldrieelq 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 625 ---NEKELAACQLRISQHEAKIKSLTEY------------------LQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEM 683
Cdd:COG4717  351 ellREAEELEEELQLEELEQEIAALLAEagvedeeelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEEL 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 684 EKEHLNKVQTANEVKQAVEQQIQSHRETHQK--------QISSLRDEVEAKEKLITDLQDQNQ-----KMVLEQERLRVE 750
Cdd:COG4717  431 EEELEELEEELEELEEELEELREELAELEAEleqleedgELAELLQELEELKAELRELAEEWAalklaLELLEEAREEYR 510

                        410
                 ....*....|....*....
gi 109892476 751 HERLKAVDQEKSRKLHELT 769
Cdd:COG4717  511 EERLPPVLERASEYFSRLT 529
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 420-867 4.68e-08

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: 56.95  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  420 KCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEV---LQALE 496
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  497 ELAVN---YDQKSQEVEDK-----------TKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLlkDL 562
Cdd:TIGR04523 201 LLLSNlkkKIQKNKSLESQiselkkqnnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--EQ 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  563 AEIGIAVGNNDVKQpegtgmideeftvarlyiskMKSEVKTMVKRCKQleSTQTESNKKMEENEKELAACQLRISQHEAK 642
Cdd:TIGR04523 279 NNKKIKELEKQLNQ--------------------LKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKI 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  643 IKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKE-HLNKVQTANEVKQAVEQQIQSHRETHQK---QISS 718
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQkdeQIKK 416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  719 LRDEVEAKEKLITDLQDQNQKmvleqerLRVEHERLKAVDQEKSRKLHELtvmQDRREQARQDLKGLEETVAKELQTLHN 798
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIK-------NNSEIKDLTNQDSVKELIIKNL---DNTRESLETQLKVLSRSINKIKQNLEQ 486

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109892476  799 LRKLFVQDlATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL 867
Cdd:TIGR04523 487 KQKELKSK-EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 417-788 6.80e-08

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: 56.90  E-value: 6.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELlastrrdqdnmqaELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-------------KLQELKLKEQAKKALEYYQLKEKL 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   497 ELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQ 576
Cdd:pfam02463  220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   577 pegtgmidEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKsltEYLQNVEQK 656
Cdd:pfam02463  300 --------SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKL 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   657 KRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSlrdEVEAKEKLITDLQDQ 736
Cdd:pfam02463  369 EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE---ILEEEEESIELKQGK 445

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 109892476   737 NQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEET 788
Cdd:pfam02463  446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 628-793 8.22e-08

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: 54.16  E-value: 8.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 628 ELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAveqQIQS 707
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG---NVRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 708 HRE--THQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKA-VDQEKSRKLHELTVMQDRREQARQDLKG 784
Cdd:COG1579   88 NKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAeLEEKKAELDEELAELEAELEELEAEREE 167


                 ....*....
gi 109892476 785 LEETVAKEL 793
Cdd:COG1579  168 LAAKIPPEL 176
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 424-883 1.27e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 55.75  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   424 EIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYD 503
Cdd:TIGR00618  297 AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   504 ------QKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMtnHQKKRAAEMMASLLKDLAEIGIAVGNNdvkQP 577
Cdd:TIGR00618  377 ltqhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL--QGQLAHAKKQQELQQRYAELCAAAITC---TA 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   578 EGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKME---ENEKELAACQLRISQHEAKI---KSLTEYLQ 651
Cdd:TIGR00618  452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLelqEEPCPLCGSCIHPNPARQDIdnpGPLTRRMQ 531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   652 NVEQKKRQLEESVDSLGEELVQLRAQEKVHEmekehlNKVQTANEVKQAVEQQIQSHREthqkQISSLRDEVEAKEKLIt 731
Cdd:TIGR00618  532 RGEQTYAQLETSEEDVYHQLTSERKQRASLK------EQMQEIQQSFSILTQCDNRSKE----DIPNLQNITVRLQDLT- 600

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   732 DLQDQNQKMVLEQERlrvEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRklfvqdlaTRV 811
Cdd:TIGR00618  601 EKLSEAEDMLACEQH---ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS--------IRV 669

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109892476   812 KKSAEVDSddtggsaaQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKE 883
Cdd:TIGR00618  670 LPKELLAS--------RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 423-747 2.07e-07

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: 55.03  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  423 EEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNY 502
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  503 DQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRaaemMASLLKDLAEIGIAVGNNDVKQPEgtgm 582
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRES---- 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  583 IDEEFTVARLYISKMKSEVKTMVKRCKQLES---TQTESNKKMEENEKELaacqlrisqhEAKIKSLTEYLQNVEQKKRQ 659
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKelkKLNEEKKELEEKVKDL----------TKKISSLKEKIEKLESEKKE 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  660 LEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRE------THQKQISSLRDEVEAKEKLITDL 733
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLIKEIEEKEKKISSL 615

                         330
                  ....*....|....
gi 109892476  734 QDQNQKMVLEQERL 747
Cdd:TIGR04523 616 EKELEKAKKENEKL 629
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
418-907 2.35e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 418 RRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndasKEEVKEVLQALEE 497
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 498 LavnydqksQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmMASLLKDLAEIgiavgnndvkqp 577
Cdd:COG4717  124 L--------LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-LAELQEELEEL------------ 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 578 egtgmideeftvARLYISKMKSEVKTMVKRCKQLEstqtesnKKMEENEKELAACQLRISQHEAKIKSLTEylqnvEQKK 657
Cdd:COG4717  183 ------------LEQLSLATEEELQDLAEELEELQ-------QRLAELEEELEEAQEELEELEEELEQLEN-----ELEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 658 RQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKL--ITDLQD 735
Cdd:COG4717  239 AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALpaLEELEE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 736 QNQKMVLeqERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKglEETVAKELQTLhnLRKLFVQDLATRVKKSA 815
Cdd:COG4717  319 EELEELL--AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL--LAEAGVEDEEELRAALE 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 816 EVDSDDtggsaAQKQKISFLENNLEQLTKVHKQLVRDN---------ADLRCELPKLEKRLRATAERVKALESALKEAKE 886
Cdd:COG4717  393 QAEEYQ-----ELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEELEEELEELREELAELEAELEQLEE 467

                        490       500
                 ....*....|....*....|...
gi 109892476 887 NASRDRKRYQQE--VDRIKEAVR 907
Cdd:COG4717  468 DGELAELLQELEelKAELRELAE 490
PTZ00121 PTZ00121
MAEBL; Provisional
 369-903 2.42e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  369 RNGETVPIDEQFDKEKANLEAFTADKDVAITND--KPAAAIGMAGSFTDAERRKCEEEIAKLyKQLDDKDEEINQQSQLV 446
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEeaRKADELKKAEEKKKADEAKKAEEKKKA-DEAKKKAEEAKKADEAK 1321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  447 EKLKTQMLDQEEllASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQK 526
Cdd:PTZ00121 1322 KKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  527 SATLASIDAELQKLKEmtnhQKKRAAEmmaslLKDLAEigiavgnnDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVK 606
Cdd:PTZ00121 1400 AEEDKKKADELKKAAA----AKKKADE-----AKKKAE--------EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  607 RCKQLESTQTESNKKMEENEKElaACQLRISQHEAKIKSltEYLQNVEQKKRQLEESVDS----LGEELVQLRAQEKVHE 682
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAeeakKADEAKKAEEAKKADE 1538

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  683 M----EKEHLNKVQTANEVKQAVE-QQIQSHRETHQKQISSLRDEVEAKEkliTDLQDQNQKMVLEQERLRVEHERLKAV 757
Cdd:PTZ00121 1539 AkkaeEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAEEAKKA 1615

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  758 DQEKSrKLHELTVMQDRREQARQDLKGLEETVAKelqtlhnlrklfvqdlATRVKKSAEvdsDDTGGSAAQKQKISFLEN 837
Cdd:PTZ00121 1616 EEAKI-KAEELKKAEEEKKKVEQLKKKEAEEKKK----------------AEELKKAEE---ENKIKAAEEAKKAEEDKK 1675

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109892476  838 NLEQLTKVHKQlvrdnadlrcELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIK 903
Cdd:PTZ00121 1676 KAEEAKKAEED----------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 612-904 2.47e-07

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: 54.74  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  612 ESTQTESNKKMEENEkeLAACQLRISQHEakiKSLTEylqnveqkkRQLEESVDSLGEELVQLRAQEKVHEMEKEHlnKV 691
Cdd:pfam17380 255 EYTVRYNGQTMTENE--FLNQLLHIVQHQ---KAVSE---------RQQQEKFEKMEQERLRQEKEEKAREVERRR--KL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  692 QTANEVKQA-VEQQIQSHRETHQKQISSLR--DEVEAKEKLITDLQDQNQKMVLEQERLRvEHERL-------------- 754
Cdd:pfam17380 319 EEAEKARQAeMDRQAAIYAEQERMAMERERelERIRQEERKRELERIRQEEIAMEISRMR-ELERLqmerqqknervrqe 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  755 -------KAVDQEKSRKLH----ELTVMQDRREQARQ-DLKGLEETVAKELQTL--------HNLRKLfVQDLATRVKKS 814
Cdd:pfam17380 398 leaarkvKILEEERQRKIQqqkvEMEQIRAEQEEARQrEVRRLEEERAREMERVrleeqerqQQVERL-RQQEEERKRKK 476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  815 AEVDSDDTGGSAAQKQKISFLENNLEQltkvHKQLVRDNADLRCELPK-LEKRLRATAERVKALESALKEAKENASRDRK 893
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKeMEERQKAIYEEERRREAEEERRKQQEMEERR 552

                         330
                  ....*....|.
gi 109892476  894 RYQQEVDRIKE 904
Cdd:pfam17380 553 RIQEQMRKATE 563
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 476-900 3.17e-07

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: 54.34  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  476 RLQAENDASKEEVK-----EVLQALEElavnydQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNhQKKR 550
Cdd:pfam05483 203 RVQAENARLEMHFKlkedhEKIQHLEE------EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-QLEE 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  551 AAEMMASLLKDLAEigiavgnndvKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELA 630
Cdd:pfam05483 276 KTKLQDENLKELIE----------KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  631 ACQLRISQHEAKIKSLTEYLQNVEQKkrqLEESVDSLgeELVQLRAQEKVHEMEKehLNKVQTANEVKQAVEQQIQSHRE 710
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQR---LEKNEDQL--KIITMELQKKSSELEE--MTKFKNNKEVELEELKKILAEDE 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  711 T---HQKQISSLRDEV-----------EAKEKLITDLQ---------DQNQKMVLEQERLRVEHERLKAVD--------- 758
Cdd:pfam05483 419 KlldEKKQFEKIAEELkgkeqelifllQAREKEIHDLEiqltaiktsEEHYLKEVEDLKTELEKEKLKNIEltahcdkll 498

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  759 -------QEKSRKLHELTVMQD-------RREQARQDLKGLEETVAKELQTLHNLRKLFVQ---DLATRVKKSAEVDSDD 821
Cdd:pfam05483 499 lenkeltQEASDMTLELKKHQEdiinckkQEERMLKQIENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSI 578

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  822 TGGSAAQKQKISFLENN-------LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKR 894
Cdd:pfam05483 579 EYEVLKKEKQMKILENKcnnlkkqIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658


                  ....*.
gi 109892476  895 YQQEVD 900
Cdd:pfam05483 659 YQKEIE 664
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
6-268 3.53e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 53.97  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   6 ECNIKVMCRFRPLNESE---------VNRGDKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYND-CAKKIVKDVLE 75
Cdd:COG5059  304 NCNTRVICTISPSSNSFeetintlkfASRAKSIKNKIQVNSSSDSSREIEEIKFDLSEDRSEIEILVFrEQSQLSQSSLS 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  76 GyngtIFAYGQTSSGKTHTMEGKlhdpeGMGIIPRIVQDIFNYIysmdENLEFHIKVSY-----FEIYLDKIRDLL-DVS 149
Cdd:COG5059  384 G----IFAYMQSLKKETETLKSR-----IDLIMKSIISGTFERK----KLLKEEGWKYKstlqfLRIEIDRLLLLReEEL 450

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 150 KTNLSVHEDKNRVPYVKGCTERFvcSPDEVMDTIDEGK--SNRHVAVTNMNEHSSRSHSIFlINVKQENTQTEQKLSgkL 227
Cdd:COG5059  451 SKKKTKIHKLNKLRHDLSSLLSS--IPEETSDRVESEKasKLRSSASTKLNLRSSRSHSKF-RDHLNGSNSSTKELS--L 525

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 109892476 228 YLVDLAGSEKVSKTgAEGAVLDEAKNINKSLSALGNVISAL 268
Cdd:COG5059  526 NQVDLAGSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
595-905 5.13e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 595 SKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEE------------ 662
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieelekel 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 663 -----SVDSLGEELVQLRAQ-EKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQ---------KQISSLRDEVEAKE 727
Cdd:PRK03918 248 eslegSKRKLEEKIRELEERiEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyldelreieKRLSRLEEEINGIE 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 728 KLITDLQDQNQKmVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLE-ETVAKELQTLHNLRKLFVQD 806
Cdd:PRK03918 328 ERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEE 406

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 807 LATRVKKSAEVdsddtggsaaqKQKISFLENNLEQLTK------VHKQLVRDN------ADLRCELPKLEKRLRATAERV 874
Cdd:PRK03918 407 ISKITARIGEL-----------KKEIKELKKAIEELKKakgkcpVCGRELTEEhrkellEEYTAELKRIEKELKEIEEKE 475

                        330       340       350
                 ....*....|....*....|....*....|...
gi 109892476 875 KALESALKEAKENASRDRK--RYQQEVDRIKEA 905
Cdd:PRK03918 476 RKLRKELRELEKVLKKESEliKLKELAEQLKEL 508
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 416-912 6.65e-07

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: 53.64  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLastrrdqDNMQAELNRLQAENDASKEEVKEVLqal 495
Cdd:pfam01576   68 ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-------DEEEAARQKLQLEKVTTEAKIKKLE--- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   496 EELAVNYDQKSQevedKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDlaeigiavGNNDVK 575
Cdd:pfam01576  138 EDILLLEDQNSK----LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE--------EKGRQE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   576 QPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQ 655
Cdd:pfam01576  206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   656 KKRQLEESVDSLGEELVQLR-----------AQEKV---HEMEKEHLNKvqTANEVKQAVEQQIQSHRETHQKQISSLRD 721
Cdd:pfam01576  286 ARNKAEKQRRDLGEELEALKteledtldttaAQQELrskREQEVTELKK--ALEEETRSHEAQLQEMRQKHTQALEELTE 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   722 EVE-----------AKEKLITDLQD-QNQKMVLEQERLRVEHERLKAVDQeksrkLHELTVMQDRREQARQDLkglEETV 789
Cdd:pfam01576  364 QLEqakrnkanlekAKQALESENAElQAELRTLQQAKQDSEHKRKKLEGQ-----LQELQARLSESERQRAEL---AEKL 435

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   790 AKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVhKQLVRDNADLRCELPKLEKRLRA 869
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-RQLEDERNSLQEQLEEEEEAKRN 514

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 109892476   870 TAERVKALESALKEAK----------ENASRDRKRYQQEVDRIKEAVRSKNMA 912
Cdd:pfam01576  515 VERQLSTLQAQLSDMKkkleedagtlEALEEGKKRLQRELEALTQQLEEKAAA 567
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 618-834 6.89e-07

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: 52.46  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 618 SNKKMEENEKELAACQLRISQHEAKI-------KSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNK 690
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELaalkkeeKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 691 VQtaNEVKQAVEQQIQSHRETHQ-----------------KQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHER 753
Cdd:COG4942   98 EL--EAQKEELAELLRALYRLGRqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 754 LKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLfVQDLATRVKKSAEVDSDDTGGSAAQKQKIS 833
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERTPAAGFAALKGK 254


                 .
gi 109892476 834 F 834
Cdd:COG4942  255 L 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
417-905 7.46e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLAstRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:COG4913   249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAELERLEARLDALREELD 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  497 ELAVNYDQksqevedktkeyellsdelnQKSATLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGIAVGNNDvkq 576
Cdd:COG4913   327 ELEAQIRG--------------------NGGDRLEQLEREIERLERELEERERRRAR----LEALLAALGLPLPASA--- 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  577 pegtgmidEEFTVARlyiskmkSEVKTMVKRCKQLESTQTEsnkKMEENEKELAACQLRISQHEAKIKSLTE----YLQN 652
Cdd:COG4913   380 --------EEFAALR-------AEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERrksnIPAR 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  653 VEQKKRQLEESvdsLGE---------ELVQLRAQEKVHEM---------------EKEHLNKVQTA-NEVKQAVEQQIQS 707
Cdd:COG4913   442 LLALRDALAEA---LGLdeaelpfvgELIEVRPEEERWRGaiervlggfaltllvPPEHYAAALRWvNRLHLRGRLVYER 518

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  708 HRETHQKQIS------SLRDEVEAKEKLITD-LQDQ-NQKM----VLEQERLRVEHerlKAVDQE----KSRKLHEltvM 771
Cdd:COG4913   519 VRTGLPDPERprldpdSLAGKLDFKPHPFRAwLEAElGRRFdyvcVDSPEELRRHP---RAITRAgqvkGNGTRHE---K 592

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  772 QDRR----------------EQARQDLKGLEETVA---KELQTLHNLRKLfVQDLATRVKKSAEVDSDDTGGSAAQKQki 832
Cdd:COG4913   593 DDRRrirsryvlgfdnraklAALEAELAELEEELAeaeERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAERE-- 669

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109892476  833 sflennLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:COG4913   670 ------IAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
415-904 8.76e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  415 DAERRKCEEEIAKLYKQLDDKDEEINQQS-QLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQ 493
Cdd:COG4913   308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  494 ALEELAVNYDQKSQEVEDktkEYELLSDELNQKSATLASIDAELQKLKemtnHQKKRAAEMMASLLKDLAEigiAVGNN- 572
Cdd:COG4913   388 EAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLE----RRKSNIPARLLALRDALAE---ALGLDe 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  573 ----------DVKQPE--------------GTGMI--DEEFTVARLYISKMK-------SEVKTMVKRCKQLEST----- 614
Cdd:COG4913   458 aelpfvgeliEVRPEEerwrgaiervlggfALTLLvpPEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDpdsla 537

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  615 ---QTESNK-----KME----------ENEKEL--------AACQLRIS----QHEAKIKSLTEYL--QNVEQKKRQLEE 662
Cdd:COG4913   538 gklDFKPHPfrawlEAElgrrfdyvcvDSPEELrrhpraitRAGQVKGNgtrhEKDDRRRIRSRYVlgFDNRAKLAALEA 617

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  663 SVDSLGEELVQLRAQEKVHEMEKEHLNKVQTA-NEVKQAVEQQIQShrETHQKQISSLRDEVEAKEKLITDLQDQNQKMV 741
Cdd:COG4913   618 ELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDV--ASAEREIAELEAELERLDASSDDLAALEEQLE 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  742 LEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLFVQDLATRVkkSAEVDSDD 821
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGDAV--ERELRENL 771

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  822 TGGSAAQKQKISFLENNLEQLTKVHKQL-----------VRDNADLRCELPKLEkrlratAERVKALESALKEAKENASR 890
Cdd:COG4913   772 EERIDALRARLNRAEEELERAMRAFNREwpaetadldadLESLPEYLALLDRLE------EDGLPEYEERFKELLNENSI 845

                         570
                  ....*....|....*....
gi 109892476  891 DRK-----RYQQEVDRIKE 904
Cdd:COG4913   846 EFVadllsKLRRAIREIKE 864
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 602-900 9.63e-07

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: 52.82  E-value: 9.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  602 KTMVKRCKQLESTQTESNKKMEENEKELAACQlrisqheAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVH 681
Cdd:pfam05557  51 QELQKRIRLLEKREAEAEEALREQAELNRLKK-------KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  682 EMEKEHLNK----VQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQ----------------KMV 741
Cdd:pfam05557 124 ELELQSTNSeleeLQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseivknskselaripELE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  742 LEQERLRVEHERLKAVDQEKS---RKLHELTVMQDRREQARQDLKGLE---ETVAKELQTLHNLRKLFVQDLATRVKKSA 815
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLllkEEVEDLKRKLEREEKYREEAATLElekEKLEQELQSWVKLAQDTGLNLRSPEDLSR 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  816 EVDSDDTgGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLrataERVKALESALKEAKENASRDRKRY 895
Cdd:pfam05557 284 RIEQLQQ-REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL----KRHKALVRRLQRRVLLLTKERDGY 358


                  ....*
gi 109892476  896 QQEVD 900
Cdd:pfam05557 359 RAILE 363
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
598-892 1.13e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  598 KSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQlRISQH---EAKIKSLTEYLQNVEQKKRQLEES---VDSLGEEL 671
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYswdEIDVASAEREIAELEAELERLDASsddLAALEEQL 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  672 VQLRAQEKVHEMEKEHLNKVQTanevkqaveqQIQSHRETHQKQISSLRDEVEAKEKLITdlqdqnqkmvlEQERLRVEh 751
Cdd:COG4913   695 EELEAELEELEEELDELKGEIG----------RLEKELEQAEEELDELQDRLEAAEDLAR-----------LELRALLE- 752

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  752 ERLKAVDQEKSRklheltvmQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLatrvkKSAEVDSDDTGGSAAQKQK 831
Cdd:COG4913   753 ERFAAALGDAVE--------RELRENLEERIDALRARLNRAEEELERAMRAFNREW-----PAETADLDADLESLPEYLA 819

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109892476  832 IsflennleqltkvHKQLVRDNadlrceLPKLEKRLR-----ATAERVKALESALKEAKENAsRDR 892
Cdd:COG4913   820 L-------------LDRLEEDG------LPEYEERFKellneNSIEFVADLLSKLRRAIREI-KER 865
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 418-905 1.20e-06

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: 52.48  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   418 RRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQ-EELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA-- 494
Cdd:pfam01576  322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAkq 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   495 -LEELAVNYDQKSQEVEDKTKEYELLSDELNQKsatLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGiavgnnd 573
Cdd:pfam01576  402 dSEHKRKKLEGQLQELQARLSESERQRAELAEK---LSKLQSELESVSSLLNEAEGKNIK----LSKDVSSLE------- 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   574 vKQPEGTGMIDEEFTVARLYISKmksevktmvkRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNV 653
Cdd:pfam01576  468 -SQLQDTQELLQEETRQKLNLST----------RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   654 EQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANE-------VKQAVEQQIQSHRETHQKQISSL------- 719
Cdd:pfam01576  537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQqelddllVDLDHQRQLVSNLEKKQKKFDQMlaeekai 616

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   720 ---------RDEVEAKEK---------LITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQD 781
Cdd:pfam01576  617 saryaeerdRAEAEAREKetralslarALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEE 696

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   782 LKGLEETVAKELQTLHNLR-KLFVQDLATRVKKSAEVDSDDTGGSAAQKQ---KISFLENNLEQLTKVHKQLVRDNADLR 857
Cdd:pfam01576  697 MKTQLEELEDELQATEDAKlRLEVNMQALKAQFERDLQARDEQGEEKRRQlvkQVRELEAELEDERKQRAQAVAAKKKLE 776

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 109892476   858 CELPKLEKRLRATAervKALESALKEAKEnASRDRKRYQQEVDRIKEA 905
Cdd:pfam01576  777 LDLKELEAQIDAAN---KGREEAVKQLKK-LQAQMKDLQRELEEARAS 820
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 478-707 1.79e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 478 QAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMAS 557
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 558 LLK---DLAEIGIAVGNNDVkqpegTGMIDEEFTVARLyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQL 634
Cdd:COG3883   95 LYRsggSVSYLDVLLGSESF-----SDFLDRLSALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109892476 635 RISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQS 707
Cdd:COG3883  169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 403-668 1.89e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.30  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 403 PAAAIGMAGSFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEND 482
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 483 ASKEEVKEVLQALEELAVNYDQKSQevedktkeYELLSDELNQKSATLASIDAELqkLKEMTNHQKKRAAEMMASlLKDL 562
Cdd:COG4942   94 ELRAELEAQKEELAELLRALYRLGR--------QPPLALLLSPEDFLDAVRRLQY--LKYLAPARREQAEELRAD-LAEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 563 AEigiavgnndvkqpegtgmIDEEFTVARLYISKMKSEVKtmvKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAK 642
Cdd:COG4942  163 AA------------------LRAELEAERAELEALLAELE---EERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                        250       260
                 ....*....|....*....|....*.
gi 109892476 643 IKSLTEYLQNVEQKKRQLEESVDSLG 668
Cdd:COG4942  222 AEELEALIARLEAEAAAAAERTPAAG 247
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 419-751 2.11e-06

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: 52.04  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   419 RKCEEEIAKLYKQLDDKDeeinqqsQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEvlqaLEEL 498
Cdd:pfam15921  544 RNVQTECEALKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE----FKIL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   499 AVNYDQKSQEVEDKTKEYELLSDEL-NQKSATLASIDAELQKLKEMTNHQKKRAAEmmaslLKDLAEIGIAVGNNDVKQP 577
Cdd:pfam15921  613 KDKKDAKIRELEARVSDLELEKVKLvNAGSERLRAVKDIKQERDQLLNEVKTSRNE-----LNSLSEDYEVLKRNFRNKS 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   578 EGTGMIDEEFtvaRLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKK 657
Cdd:pfam15921  688 EEMETTTNKL---KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   658 RQLEESVDSLGEELVQLrAQEKvhemekehlNKVQTANEVKQAVEQQIqshrethQKQISSLRDEVEAKEKLITDLQDQN 737
Cdd:pfam15921  765 HFLKEEKNKLSQELSTV-ATEK---------NKMAGELEVLRSQERRL-------KEKVANMEVALDKASLQFAECQDII 827

                          330
                   ....*....|....
gi 109892476   738 QKMVLEQERLRVEH 751
Cdd:pfam15921  828 QRQEQESVRLKLQH 841
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 448-802 2.83e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 50.99  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 448 KLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQaleelavNYDQKSQEVEDKTKEYELLSDELNQKs 527
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-------LYRELRKSLLANRFSFGPALDELEKQ- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 528 atLASIDAELQKLKEMT---NHQKkrAAEMMASLLKDLAEIGIAVgnNDVKQpegtgMIDEEFTVARLYISKMKSEVKTM 604
Cdd:PRK04778 174 --LENLEEEFSQFVELTesgDYVE--AREILDQLEEELAALEQIM--EEIPE-----LLKELQTELPDQLQELKAGYREL 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 605 VKRC-----KQLESTQTESNKKMEENEKELAACQL-----RISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQL 674
Cdd:PRK04778 243 VEEGyhldhLDIEKEIQDLKEQIDENLALLEELDLdeaeeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHA 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 675 RAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDqNQKMVLEQerlrveherl 754
Cdd:PRK04778 323 KEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQE-ELEEILKQ---------- 391

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109892476 755 kavdqeksrklheLTVMQDRREQARQDLKGL--EETVAKEL-----QTLHNLRKL 802
Cdd:PRK04778 392 -------------LEEIEKEQEKLSEMLQGLrkDELEAREKleryrNKLHEIKRY 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 676-938 4.07e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 676 AQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLK 755
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 756 AVDQEKSRKLHE-LTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLfvqdlatrvkksAEVDSDDTGGSAAQKQKISF 834
Cdd:COG4942   97 AELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL------------APARREQAEELRADLAELAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 835 LENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRI--KEAVRSKNMA 912
Cdd:COG4942  165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLeaEAAAAAERTP 244

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 109892476 913 RRGHSAQIAKPIRP---------GQHPAASPTHPG 938
Cdd:COG4942  245 AAGFAALKGKLPWPvsgrvvrrfGERDGGGGRNKG 279
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
692-921 4.14e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  692 QTANEVKQAVEQqIQSHRETHQ------KQISSLRDEVEAKEKLITDLQDQNQkmvLEQERLRVEHERLKAVDQEKSRKL 765
Cdd:COG4913   222 DTFEAADALVEH-FDDLERAHEaledarEQIELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  766 HELTVMQDRREQARQDLKGLEETVAKELQTLHNLRklfvqdlatrvkksaevdsDDTGGsaaqkQKISFLENNLEQLTKV 845
Cdd:COG4913   298 EELRAELARLEAELERLEARLDALREELDELEAQI-------------------RGNGG-----DRLEQLEREIERLERE 353

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109892476  846 HKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIA 921
Cdd:COG4913   354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 612-833 5.81e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 612 ESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEME-KEHLNK 690
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 691 VQTANEVKQAVEQQIQShrethqKQISSLRDEVEAkeklITDLQDQNQKMVLEQERLRVEHERLKAvdqEKSRKLHELTV 770
Cdd:COG3883   95 LYRSGGSVSYLDVLLGS------ESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKA---ELEAKLAELEA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109892476 771 MQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKIS 833
Cdd:COG3883  162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
mukB PRK04863
chromosome partition protein MukB;
437-757 5.83e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  437 EEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEEL---AVNYDQKSQEVEdKT 513
Cdd:PRK04863  348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQqtrAIQYQQAVQALE-RA 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  514 KEYELLSD-ELNQKSATLASIDAELQKLKEMTNH--QKKRAAEM--------MASLLKDLAEIGIAVGNNDVKQPEGTGm 582
Cdd:PRK04863  427 KQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSleQKLSVAQAahsqfeqaYQLVRKIAGEVSRSEAWDVARELLRRL- 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  583 IDEEFTVARLyiSKMKSEVKTMVKRCKQ---LESTQTESNKK---MEENEKELAACQlriSQHEAKIKSLTEYLQNVEQK 656
Cdd:PRK04863  506 REQRHLAEQL--QQLRMRLSELEQRLRQqqrAERLLAEFCKRlgkNLDDEDELEQLQ---EELEARLESLSESVSEARER 580

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  657 KRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQT----ANEVKQAVEQQIQSHREtHQKQISSLRDEVEAKEKlitD 732
Cdd:PRK04863  581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeEFEDSQDVTEYMQQLLE-RERELTVERDELAARKQ---A 656

                         330       340
                  ....*....|....*....|....*....
gi 109892476  733 LQDQNQKMVL----EQERLRVEHERLKAV 757
Cdd:PRK04863  657 LDEEIERLSQpggsEDPRLNALAERFGGV 685
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 417-765 5.94e-06

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: 50.36  E-value: 5.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam02463  189 IIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   497 ELAVNYDQKSQEVEDKTKEYELLSDELNQKSatlasidAELQKLKEMTNHQKKRAAEMMASLLKDLAEIgiavgnndvkq 576
Cdd:pfam02463  269 QVLKENKEEEKEKKLQEEELKLLAKEEEELK-------SELLKLERRKVDDEEKLKESEKEKKKAEKEL----------- 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   577 pegtgmIDEEFTVARLyiSKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEylQNVEQK 656
Cdd:pfam02463  331 ------KKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--EELELK 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   657 KRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQ 736
Cdd:pfam02463  401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480

                          330       340
                   ....*....|....*....|....*....
gi 109892476   737 NQKMVLEQERLRVEHERLKAVDQEKSRKL 765
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQKESKARSGL 509
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
692-905 6.97e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 692 QTANEVKQA-VEQQIQSHRETH-------QKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEhERLKAVDQEKSR 763
Cdd:COG3206  152 AVANALAEAyLEQNLELRREEArkaleflEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-QQLSELESQLAE 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 764 KLHELTVMQDRREQARQDLKGLEETVAKELQ--TLHNLRklfvQDLATRVKKSAEVDSDDTGGS---AAQKQKISFLENN 838
Cdd:COG3206  231 ARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLR----AQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQ 306

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109892476 839 LEQLT-KVHKQLVRDNADLRCELPKLEKRLRATAERVKAL---ESALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:COG3206  307 LQQEAqRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
611-781 8.62e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 611 LESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEES--VDSLGEELVQLRAQEKvhEMEKEHL 688
Cdd:COG3206  210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELA--ELSARYT 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 689 NK---VQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAvDQEKSRKL 765
Cdd:COG3206  288 PNhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLER-EVEVAREL 366

                        170
                 ....*....|....*.
gi 109892476 766 HELtvMQDRREQARQD 781
Cdd:COG3206  367 YES--LLQRLEEARLA 380
mukB PRK04863
chromosome partition protein MukB;
452-786 1.06e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  452 QMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEElAVNYDQKSQEVEDKTKEYELLSDELNQKSATLA 531
Cdd:PRK04863  287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-ASDHLNLVQTALRQQEKIERYQADLEELEERLE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  532 S---IDAELQKLKEMTNHQKKRAAEMMASLLKDLAeigiavgnnDVKQPegtgmIDEEFTVARLYiskmkSEVKTMVKRC 608
Cdd:PRK04863  366 EqneVVEEADEQQEENEARAEAAEEEVDELKSQLA---------DYQQA-----LDVQQTRAIQY-----QQAVQALERA 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  609 KQLestqtesnkkMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQK-------KRQLE---ESVDSLGEELVQLRAQE 678
Cdd:PRK04863  427 KQL----------CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvaqaaHSQFEqayQLVRKIAGEVSRSEAWD 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  679 KVHEMEKEHLNKVQTANEVkQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNqkmvlEQERLRVEHE-RLKAV 757
Cdd:PRK04863  497 VARELLRRLREQRHLAEQL-QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED-----ELEQLQEELEaRLESL 570

                         330       340
                  ....*....|....*....|....*....
gi 109892476  758 DQEKSRKLHELTVMQDRREQARQDLKGLE 786
Cdd:PRK04863  571 SESVSEARERRMALRQQLEQLQARIQRLA 599
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 626-916 1.24e-05

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: 49.57  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  626 EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLR------AQEKVHEMEkEHLNKVQTAnevkq 699
Cdd:COG3096   835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANlladetLADRLEELR-EELDAAQEA----- 908

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  700 avEQQIQSHRETHQK---QISSLRDEVEAKEKLITDLQ--DQNQKMV------LEQERLRVEH------ERLKAVDQEKS 762
Cdd:COG3096   909 --QAFIQQHGKALAQlepLVAVLQSDPEQFEQLQADYLqaKEQQRRLkqqifaLSEVVQRRPHfsyedaVGLLGENSDLN 986

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  763 RKLHE-LTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLF------VQDLATRVkKSAEVdSDDTGGSAAQKQKISFL 835
Cdd:COG3096   987 EKLRArLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRdakqqtLQELEQEL-EELGV-QADAEAEERARIRRDEL 1064

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  836 ENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRyqqevdrikeaVRSKNMARRG 915
Cdd:COG3096  1065 HEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRL-----------ARDNDVERRL 1133


                  .
gi 109892476  916 H 916
Cdd:COG3096  1134 H 1134
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 430-789 1.34e-05

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: 49.08  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  430 KQLDDKDEEINQQSQLVEKLKTQmldqeellaSTRRDQDNMQAELNRLqaendasKEEVKEVLQALEELAVNYDQKSQEV 509
Cdd:pfam06160  60 KSLPDIEELLFEAEELNDKYRFK---------KAKKALDEIEELLDDI-------EEDIKQILEELDELLESEEKNREEV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  510 EDKTKEYELLSDELNQKSAT-----------LASIDAELQKLKEMT---NHQK-----KRAAEMMASLLKDLAEI--GIA 568
Cdd:pfam06160 124 EELKDKYRELRKTLLANRFSygpaidelekqLAEIEEEFSQFEELTesgDYLEarevlEKLEEETDALEELMEDIppLYE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  569 VGNNDVKQP-----EG-TGMIDEEFTVARLYISKMKSEVKTMVKRC-KQLESTQTES----NKKMEEN--------EKEL 629
Cdd:pfam06160 204 ELKTELPDQleelkEGyREMEEEGYALEHLNVDKEIQQLEEQLEENlALLENLELDEaeeaLEEIEERidqlydllEKEV 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  630 AACQlrisQHEAKIKSLTEYLQNVEQKKRQLEESVDSL-------GEELVQLRA-QEKVHEMEKEHL-------NKVQT- 693
Cdd:pfam06160 284 DAKK----YVEKNLPEIEDYLEHAEEQNKELKEELERVqqsytlnENELERVRGlEKQLEELEKRYDeiverleEKEVAy 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  694 ---ANEVKQAVEQ--QIQSHRETHQKQISSLR-DEVEAKEKLIT-DLQDQNQKMVLEQERL-----------RVEHERLK 755
Cdd:pfam06160 360 selQEELEEILEQleEIEEEQEEFKESLQSLRkDELEAREKLDEfKLELREIKRLVEKSNLpglpesyldyfFDVSDEIE 439

                         410       420       430
                  ....*....|....*....|....*....|....
gi 109892476  756 AVDQEKSRKLHELTVMQDRREQARQDLKGLEETV 789
Cdd:pfam06160 440 DLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKT 473
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 422-908 1.50e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.96  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   422 EEEIAKLYKQLDDKDEEINQQ-----SQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaSKEEVKEVLQALE 496
Cdd:pfam15921  244 EDQLEALKSESQNKIELLLQQhqdriEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLS 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   497 ELAVNYDQKSQEVEDKTKEYEllsDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQ 576
Cdd:pfam15921  321 DLESTVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   577 PEGTGMIDEEfTVARLYISKMKSEVKTmvkrcKQLESTQTESNKKMEENEkelaaCQLRISQHEA----------KIKSL 646
Cdd:pfam15921  398 EQNKRLWDRD-TGNSITIDHLRRELDD-----RNMEVQRLEALLKAMKSE-----CQGQMERQMAaiqgknesleKVSSL 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   647 TEYLQNVEQ-----------KKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQS---HRETH 712
Cdd:pfam15921  467 TAQLESTKEmlrkvveeltaKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdHLRNV 546

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   713 QKQISSLRDEVEAKEKLITDLQDQNQKMV-------------------LEQE--RLRVEHERLKAVDQEKSRKLHELTV- 770
Cdd:pfam15921  547 QTECEALKLQMAEKDKVIEILRQQIENMTqlvgqhgrtagamqvekaqLEKEinDRRLELQEFKILKDKKDAKIRELEAr 626

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   771 -------------MQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATrVKKSAEVDSDDTGGSAAQ-KQKISFLE 836
Cdd:pfam15921  627 vsdlelekvklvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV-LKRNFRNKSEEMETTTNKlKMQLKSAQ 705

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109892476   837 NNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESA---LKEAKENASRDRKRYQQEVDRIKEAVRS 908
Cdd:pfam15921  706 SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQELST 780
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 431-909 1.51e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.96  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   431 QLDDKDEEINQQSQLVEKLKTQMldqeellastRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVE 510
Cdd:pfam15921   86 QVKDLQRRLNESNELHEKQKFYL----------RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   511 DKtkeyELLSDELNQKSATlasidaELQKLKEMTNHQKKRAAEMMaSLLKDLAEigiAVGNndvKQPEGTGMIDEEFTVA 590
Cdd:pfam15921  156 AA----KCLKEDMLEDSNT------QIEQLRKMMLSHEGVLQEIR-SILVDFEE---ASGK---KIYEHDSMSTMHFRSL 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   591 RLYISKMKSEVKTMVKRCK--------QLESTQTESNKKMEenekelaacqLRISQHEAKIkslteylqnvEQKKRQLEE 662
Cdd:pfam15921  219 GSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIE----------LLLQQHQDRI----------EQLISEHEV 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   663 SVDSLGEELVQLRAQEkvhemekehlNKVQTANEVkqaVEQQIQSHRETHQKQISSLRDEVEakeKLITDLQdqnqkmvl 742
Cdd:pfam15921  279 EITGLTEKASSARSQA----------NSIQSQLEI---IQEQARNQNSMYMRQLSDLESTVS---QLRSELR-------- 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   743 eqERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKlfvqDLATRVKKSAEVDSDDT 822
Cdd:pfam15921  335 --EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK----ELSLEKEQNKRLWDRDT 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   823 GGSAAQKQKISFLEN------NLEQLTKVHK-----QLVRDNADLRCELPKLEK------RLRATAERVKALESALKEAK 885
Cdd:pfam15921  409 GNSITIDHLRRELDDrnmevqRLEALLKAMKsecqgQMERQMAAIQGKNESLEKvssltaQLESTKEMLRKVVEELTAKK 488

                          490       500       510
                   ....*....|....*....|....*....|
gi 109892476   886 ---ENASR---DRKRYQQEVDRIKEAVRSK 909
Cdd:pfam15921  489 mtlESSERtvsDLTASLQEKERAIEATNAE 518
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 404-581 1.67e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 404 AAAIGMAGSFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDA 483
Cdd:COG3883    4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 484 SKEEVKE-------------------------------------------VLQALEELAVNYDQKSQEVEDKTKEYELLS 520
Cdd:COG3883   84 RREELGEraralyrsggsvsyldvllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALK 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109892476 521 DELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:COG3883  164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 610-886 2.01e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.81  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   610 QLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVdslgEELVQLRAQEKVHEMEKEHLN 689
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR----ARIEELRAQEAVLEETQERIN 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   690 K-------VQTANEVKQaVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKS 762
Cdd:TIGR00618  288 RarkaaplAAHIKAVTQ-IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   763 RKLH---ELTVMQDRREQARQ--DLKGLEETVAKELQTLHNLR-KLFVQDLATRVKKSAEVDSDDTggSAAQKQKISFLE 836
Cdd:TIGR00618  367 IREIscqQHTLTQHIHTLQQQktTLTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCA 444

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 109892476   837 NNLEQLTKVHKQLVRdnadlrcELPKLEKRLRATAERVKALESALKEAKE 886
Cdd:TIGR00618  445 AAITCTAQCEKLEKI-------HLQESAQSLKEREQQLQTKEQIHLQETR 487
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 425-794 2.05e-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: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   425 IAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQ 504
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   505 KSQEVEDKT---KEYELLSDELNQKSATLAS-IDAELQKLKEMTNH-------------------QKKRAAEMMASLLKD 561
Cdd:pfam15921  494 SERTVSDLTaslQEKERAIEATNAEITKLRSrVDLKLQELQHLKNEgdhlrnvqtecealklqmaEKDKVIEILRQQIEN 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   562 LAEI----GIAVGNNDVKQPEGTGMIDE---EFTVARLYISKMKSEVKTMVKRCKQLE-------STQTESNKKMEENEK 627
Cdd:pfam15921  574 MTQLvgqhGRTAGAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELEARVSDLElekvklvNAGSERLRAVKDIKQ 653

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   628 ELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEEL-VQLRAQEKVHEMEKEHLNKVQTAN----EVKQAVE 702
Cdd:pfam15921  654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkMQLKSAQSELEQTRNTLKSMEGSDghamKVAMGMQ 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   703 QQIQSHR---ETHQKQISSLRDEV-----------EAKEKLITDLQD---QNQKMVLEQERLRVEHERLK--------AV 757
Cdd:pfam15921  734 KQITAKRgqiDALQSKIQFLEEAMtnankekhflkEEKNKLSQELSTvatEKNKMAGELEVLRSQERRLKekvanmevAL 813

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 109892476   758 DQeKSRKLHELTVMQDRREQARQDLKGLEETVAKELQ 794
Cdd:pfam15921  814 DK-ASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 591-917 3.14e-05

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: 48.12  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   591 RLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEEsvdsLGEE 670
Cdd:TIGR00606  195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   671 LVQLRAQEKvhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVE 750
Cdd:TIGR00606  271 IKALKSRKK--QMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   751 HERLkavdQEKSRKLHELTVMQD---RREQARQDLKGLE-----------------ETVAKELQTLHNLRKLFVQDLATR 810
Cdd:TIGR00606  349 QGRL----QLQADRHQEHIRARDsliQSLATRLELDGFErgpfserqiknfhtlviERQEDEAKTAAQLCADLQSKERLK 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   811 VKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASR 890
Cdd:TIGR00606  425 QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVK 504

                          330       340
                   ....*....|....*....|....*..
gi 109892476   891 DRKRYQQEVDRIKEAVRSKNMARRGHS 917
Cdd:TIGR00606  505 SLQNEKADLDRKLRKLDQEMEQLNHHT 531
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 650-914 3.33e-05

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: 47.37  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  650 LQNVEQKKRQLEESVDSLGEELVQLRaqEKVHEMEKEHLNKVQTAnevkQAVEQQIQSHRETHQKQISSLRDE---VEAK 726
Cdd:pfam19220  50 LLELEALLAQERAAYGKLRRELAGLT--RRLSAAEGELEELVARL----AKLEAALREAEAAKEELRIELRDKtaqAEAL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  727 EKLITDLQDQNQKMVLEQERLRvehERLKAVDQEKSRKLHELTvmqdrreQARQDLKGLEEtvakELQTLHNLRKLFVQD 806
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALR---EEAQAAEKALQRAEGELA-------TARERLALLEQ----ENRRLQALSEEQAAE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  807 LATRVKKSAEVDSDdtggSAAQKQKISFLENNLEQLTKVHKQLVR----DNADLRCELPKLEKRLRATAERVKALESALK 882
Cdd:pfam19220 190 LAELTRRLAELETQ----LDATRARLRALEGQLAAEQAERERAEAqleeAVEAHRAERASLRMKLEALTARAAATEQLLA 265

                         250       260       270
                  ....*....|....*....|....*....|...
gi 109892476  883 EAKeNASRDRKRYQQEVDR-IKEAVRSKNMARR 914
Cdd:pfam19220 266 EAR-NQLRDRDEAIRAAERrLKEASIERDTLER 297
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 656-905 3.40e-05

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: 48.02  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  656 KKRQLEESVDSLGE---ELVQLRAQEKVHEME----KEHLNKVQTAneVKQAveQQIQSHREthqkQISSLRDEVEAKEK 728
Cdd:COG3096   297 ARRQLAEEQYRLVEmarELEELSARESDLEQDyqaaSDHLNLVQTA--LRQQ--EKIERYQE----DLEELTERLEEQEE 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  729 LITDLQDQNQKMVLEQERLRVEHERLKA--VDQEKSrklheLTVMQDRREQARQDLKGLEETvakelQTLHNLRKLFVQD 806
Cdd:COG3096   369 VVEEAAEQLAEAEARLEAAEEEVDSLKSqlADYQQA-----LDVQQTRAIQYQQAVQALEKA-----RALCGLPDLTPEN 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  807 LATRVKKSAEVDSDDTGGSAAQKQKISF-------LENNLEQLTKVHKQLVRDNADLRC-ELPKLEKRLRATAERVKALE 878
Cdd:COG3096   439 AEDYLAAFRAKEQQATEEVLELEQKLSVadaarrqFEKAYELVCKIAGEVERSQAWQTArELLRRYRSQQALAQRLQQLR 518

                         250       260
                  ....*....|....*....|....*..
gi 109892476  879 SALKEAKENASRdrkryQQEVDRIKEA 905
Cdd:COG3096   519 AQLAELEQRLRQ-----QQNAERLLEE 540
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 417-799 4.06e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.66  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASK------EEVKE 490
Cdd:TIGR00618  470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAqletseEDVYH 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   491 VLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEigiAVG 570
Cdd:TIGR00618  550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP---EQD 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNK---KMEENEKE--------LAACQLRI 636
Cdd:TIGR00618  627 LQDVRLHLQQcsqELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQlalQKMQSEKEqltywkemLAQCQTLL 706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   637 SQHEAKIKSLTEYLQNVEQ----KKRQLEESVDSLGEELVQLRAQ--EKVHEMEKEHLNKVQ--TANEVKQAVEQQIQSH 708
Cdd:TIGR00618  707 RELETHIEEYDREFNEIENasssLGSDLAAREDALNQSLKELMHQarTVLKARTEAHFNNNEevTAALQTGAELSHLAAE 786

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   709 RETHQKQISSLRDEVEAKEKLI-TDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEE 787
Cdd:TIGR00618  787 IQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866

                          410
                   ....*....|..
gi 109892476   788 TVAKELQTLHNL 799
Cdd:TIGR00618  867 EQAKIIQLSDKL 878
mukB PRK04863
chromosome partition protein MukB;
626-885 4.80e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.64  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  626 EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESV---------------DSLGEELVQLRAQEKVHEMEKEHLNK 690
Cdd:PRK04863  836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladETLADRVEEIREQLDEAEEAKRFVQQ 915

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  691 VQTANEvkqAVEQQIQSHREThQKQISSLRDEVEAKEKLITDLqdQNQKMVLEQERLRVEH------ERLKAVDQEKSRK 764
Cdd:PRK04863  916 HGNALA---QLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDA--KQQAFALTEVVQRRAHfsyedaAEMLAKNSDLNEK 989

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  765 LHE-LTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLF------VQDLATRVKK-SAEVDSDDTGGSAAQKQKIS-FL 835
Cdd:PRK04863  990 LRQrLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYdakrqmLQELKQELQDlGVPADSGAEERARARRDELHaRL 1069

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 109892476  836 ENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALESALKEAK 885
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEMD----NLTKKLRKLERDYHEMREQVVNAK 1115
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 415-893 4.92e-05

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: 47.35  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   415 DAERRKCEEEIAKLykqldDKDEEINQQSQLVEKLKTQMLDqeelLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:TIGR00606  477 DQELRKAERELSKA-----EKNSLTETLKKEVKSLQNEKAD----LDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   495 LEELAVNYDQKSQEVEDK----------TKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAE 564
Cdd:TIGR00606  548 DEQIRKIKSRHSDELTSLlgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   565 IGIAVGNNDV------------KQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNK------------ 620
Cdd:TIGR00606  628 LFDVCGSQDEesdlerlkeeieKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEfisdlqsklrla 707

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   621 --KMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVK 698
Cdd:TIGR00606  708 pdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVC 787

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   699 Q---AVEQQIQSHRETHQKQISSLRDEVEAKEKLITdLQDQNQKMVLEQERLRVEHERLkavdqEKSRKLheltvMQDRR 775
Cdd:TIGR00606  788 LtdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-VQQVNQEKQEKQHELDTVVSKI-----ELNRKL-----IQDQQ 856

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   776 EQARQDLKGLEETVAKELQTLHNLRKlfVQDLATR-VKKSAEVDSDDTGGSAAqKQKISFLENNLEQLTKVHKQLVR--- 851
Cdd:TIGR00606  857 EQIQHLKSKTNELKSEKLQIGTNLQR--RQQFEEQlVELSTEVQSLIREIKDA-KEQDSPLETFLEKDQQEKEELISske 933

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 109892476   852 -DNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRK 893
Cdd:TIGR00606  934 tSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE 976
PRK12704 PRK12704
phosphodiesterase; Provisional
 414-497 5.10e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDA--------SK 485
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelerisglTA 152

                         90
                 ....*....|...
gi 109892476 486 EEVKE-VLQALEE 497
Cdd:PRK12704 153 EEAKEiLLEKVEE 165
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
 446-773 5.38e-05

Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.


Pssm-ID: 214826 [Multi-domain]  Cd Length: 426  Bit Score: 46.59  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   446 VEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQ 525
Cdd:smart00806  73 VEELDEVKKHIDDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARPAASPSPVLASSSSAISLANNPDKLNKE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   526 KSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLA---EIGIAVGNNDvkqpegtgmideeftvARLYISKMKSEVK 602
Cdd:smart00806 153 QRAELKSLQRELAVLRQTHNSFFTEIKESIKDILEKIDkfkSSSLSASGSS----------------NRAYVESSKKKLS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   603 TMVKR-CKQLESTQ---------------TESNKKMEENEKELAACqlrisqhEAKIKSLTEYLQNVE-QKKRQLEESVD 665
Cdd:smart00806 217 EDSDSlLTKVDDLQdiiealrkdvaqrgvRPSKKQLETVQKELETA-------RKELKKMEEYIDIEKpIWKKIWEAELD 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   666 SLGEELVQLRAQEKVHEMEKEHLNKV-QTANEVKQAVEQQIQSHRETHQKQISSlrdeVEAKEKLITDLQDQnqkMVLEQ 744
Cdd:smart00806 290 KVCEEQQFLTLQEDLIADLKEDLEKAeETFDLVEQCCEEQEKGPSKNRNKPVSL----PVPTPGTFNDLKDQ---VLMEV 362

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 109892476   745 ERLRVEHE-RLKAVD-----QEKSRKLHELTVMQD 773
Cdd:smart00806 363 RALKPDHEsRLEAIEraeklREKELEYRRVDEFEK 397
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
594-902 5.54e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 594 ISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQ 673
Cdd:COG4372   33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 674 LRAQekVHEMEKEhLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHER 753
Cdd:COG4372  113 LQEE--LEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 754 LKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKIS 833
Cdd:COG4372  190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109892476 834 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRI 902
Cdd:COG4372  270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 422-887 5.80e-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: 46.94  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  422 EEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVN 501
Cdd:TIGR04523  74 NNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  502 YDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKemtnhQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK-----NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  582 MIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKElaacqlrISQHEAKIKSLTEYLQNVEQKKRQLE 661
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE-------LEQNNKKIKELEKQLNQLKSEISDLN 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  662 EsvdslgeelvqlraqekvhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMv 741
Cdd:TIGR04523 302 N-------------------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK- 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  742 leQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEEtVAKELQtlhnlrklfvqdlatrvkksaevdsdd 821
Cdd:TIGR04523 362 --QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-LNQQKD--------------------------- 411

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109892476  822 tggsaaqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN 887
Cdd:TIGR04523 412 --------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 437-922 8.84e-05

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: 46.76  E-value: 8.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   437 EEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEY 516
Cdd:pfam12128  269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   517 E-LLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEigiavgnNDVKQPEGtgmIDEEFTVARLYIS 595
Cdd:pfam12128  349 LpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD-------KLAKIREA---RDRQLAVAEDDLQ 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   596 KMKSEVKtmvkrcKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEE------SVDSLGE 669
Cdd:pfam12128  419 ALESELR------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEqeaanaEVERLQS 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   670 ELVQLRaqeKVHEMEKEHLNKV-QTANEVKQAVEQQIQSHRETHQKQISSLRDEV----EAKEKLI-------TDLQ-DQ 736
Cdd:pfam12128  493 ELRQAR---KRRDQASEALRQAsRRLEERQSALDELELQLFPQAGTLLHFLRKEApdweQSIGKVIspellhrTDLDpEV 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   737 NQKMVLEQERLRVEHERLKAVDQEKSrklheltvmQDRREQARQDLKGLEETvakeLQTLHNLRKLFVQDLATRVKKSAE 816
Cdd:pfam12128  570 WDGSVGGELNLYGVKLDLKRIDVPEW---------AASEEELRERLDKAEEA----LQSAREKQAAAEEQLVQANGELEK 636

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   817 VDSDDTGGSAAQKQKisflENNLEQLTKVHKQL-VRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRD---- 891
Cdd:pfam12128  637 ASREETFARTALKNA----RLDLRRLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkrea 712

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 109892476   892 ---RKRYQQEV--------DRIKEAVRSKNMARRGHSAQIAK 922
Cdd:pfam12128  713 rteKQAYWQVVegaldaqlALLKAAIAARRSGAKAELKALET 754
46 PHA02562
endonuclease subunit; Provisional
 416-688 1.12e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.78  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 416 AERRKCEEEI------AKLYKQLDDKDEEINQQSQLV--------EKLKTQMLDQEELLASTRRDQDnmqaelnRLQAEN 481
Cdd:PHA02562 150 PARRKLVEDLldisvlSEMDKLNKDKIRELNQQIQTLdmkidhiqQQIKTYNKNIEEQRKKNGENIA-------RKQNKY 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 482 DASKEEVKEVLQALEELavnydqkSQEVEDKTKEYELLSDELNQKSATLASIDAELQKL-KEMTNHQKkraaemmasllk 560
Cdd:PHA02562 223 DELVEEAKTIKAEIEEL-------TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqKVIKMYEK------------ 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 561 dlaeigiavgnNDVkQPEGTGMIDEEFTVarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEE---NEKELAACQLRIS 637
Cdd:PHA02562 284 -----------GGV-CPTCTQQISEGPDR----ITKIKDKLKELQHSLEKLDTAIDELEEIMDEfneQSKKLLELKNKIS 347

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109892476 638 QHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKV-------HEMEKEHL 688
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKivktkseLVKEKYHR 405
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 308-886 1.20e-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: 46.17  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  308 NESETKSTLLFGQRAKTIKNTVCVNVELTAEQwkKKYEKEKEKNKTLRNTIQWLENELNrwrngetvpideQFDKEKANL 387
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKE--KELEKLNNKYNDLKKQKEELENELN------------LLEKEKLNI 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  388 EaftadKDVAITNDKpaaaigmagsftdaerrkceeeIAKLYKQLDDkdeeINQQSQLVEKLKTQMLDQEELLASTRRDQ 467
Cdd:TIGR04523 186 Q-----KNIDKIKNK----------------------LLKLELLLSN----LKKKIQKNKSLESQISELKKQNNQLKDNI 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  468 DNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQksatlasIDAELQKLKemtnhq 547
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ-------LKSEISDLN------ 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  548 KKRAAEMMASLLKDLAEigiavgnndvkqpegtgmIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEK 627
Cdd:TIGR04523 302 NQKEQDWNKELKSELKN------------------QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  628 ELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEEsvdslgeelvQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQS 707
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES----------KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  708 HRETHQKQISSLRDEVEAKEKLITDL----QDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLK 783
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLdntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  784 GLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQ--------KQKISFLENNLEQLTKVHKQLVRDNAD 855
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeidekNKEIEELKQTQKSLKKKQEEKQELIDQ 593

                         570       580       590
                  ....*....|....*....|....*....|.
gi 109892476  856 LRCELPKLEKRLRATAERVKALESALKEAKE 886
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
414-733 1.31e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQ 493
Cdd:COG4372   57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 494 ALEELAVNYDQKSQEVEDktkeyelLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNND 573
Cdd:COG4372  137 QIAELQSEIAEREEELKE-------LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 574 VKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNV 653
Cdd:COG4372  210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 654 EQKKRQLEESVDS-LGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITD 732
Cdd:COG4372  290 EAALELKLLALLLnLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369


                 .
gi 109892476 733 L 733
Cdd:COG4372  370 G 370
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 422-903 1.34e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 45.90  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  422 EEEIAKLYKQLDDKDEEINQQSQLVEKLK--------------TQMLDQEELLAST---RRDQDNMQAELNRLQAENDA- 483
Cdd:pfam07111 196 QKEAELLRKQLSKTQEELEAQVTLVESLRkyvgeqvppevhsqTWELERQELLDTMqhlQEDRADLQATVELLQVRVQSl 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  484 ------SKEEVKEVLQALEELAVNYDQKSQEVEDKTKE------YELLSDELnQKSATLASIDAELQKLKEMTNHQKKRA 551
Cdd:pfam07111 276 thmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREkvfalmVQLKAQDL-EHRDSVKQLRGQVAELQEQVTSQSQEQ 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  552 AEMMASLLKDLAEIgiavgnndvkqpegtgmideeftvarlyiskmksEVKTMVKRCKQLESTQTESNKKMEENEKELAA 631
Cdd:pfam07111 355 AILQRALQDKAAEV----------------------------------EVERMSAKGLQMELSRAQEARRRQQQQTASAE 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  632 CQLRISQheAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQlrAQEKVHEMEKEHLNKVQTANEVKQA-----VEQQIQ 706
Cdd:pfam07111 401 EQLKFVV--NAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY--AVRKVHTIKGLMARKVALAQLRQEScppppPAPPVD 476

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  707 SHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQ---ERLRVeHERLKAVDQEKSRKLHELTVMQDRREQARQDLK 783
Cdd:pfam07111 477 ADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQgeaERQQL-SEVAQQLEQELQRAQESLASVGQQLEVARQGQQ 555

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  784 GLEETVAKELQTLHNLRKLFVQDLATRVkksAEVDSDdtggsaaqkqkisfLENNLEQLTKVHKQLVRDNADLRCELPKL 863
Cdd:pfam07111 556 ESTEEAASLRQELTQQQEIYGQALQEKV---AEVETR--------------LREQLSDTKRRLNEARREQAKAVVSLRQI 618

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 109892476  864 EKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIK 903
Cdd:pfam07111 619 QHRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDK 658
PRK12704 PRK12704
phosphodiesterase; Provisional
 634-781 1.54e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 634 LRISQHEAKIKSLTEYLQN-VEQKKRQLEESvdslgEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETH 712
Cdd:PRK12704  24 VRKKIAEAKIKEAEEEAKRiLEEAKKEAEAI-----KKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109892476 713 QKQISSL---RDEVEAKEKLITDLQDQNQKMVLEQERLRVEH----ERLKAVDQEKSRKLheltVMQDRREQARQD 781
Cdd:PRK12704  99 DRKLELLekrEEELEKKEKELEQKQQELEKKEEELEELIEEQlqelERISGLTAEEAKEI----LLEKVEEEARHE 170
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 417-900 1.65e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   417 ERRKCEE----EIAKLYKQLD----DKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEV 488
Cdd:pfam01576  194 ERLKKEEkgrqELEKAKRKLEgestDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   489 KEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASiDAELQKLKEMTNHQKKRAAE----MMASLLKDLAE 564
Cdd:pfam01576  274 SELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAA-QQELRSKREQEVTELKKALEeetrSHEAQLQEMRQ 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   565 IGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVK-----------RCKQLESTQTESNKKMEENEKELAACQ 633
Cdd:pfam01576  353 KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakqdsehKRKKLEGQLQELQARLSESERQRAELA 432

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   634 LRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLG------EELVQLRAQEK------VHEMEKEH---LNKVQTANEVK 698
Cdd:pfam01576  433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdtQELLQEETRQKlnlstrLRQLEDERnslQEQLEEEEEAK 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   699 QAVEQQIQshreTHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRV-EHERLKAVDQ-EKSRK-----LHELTVM 771
Cdd:pfam01576  513 RNVERQLS----TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqLEEKAAAYDKlEKTKNrlqqeLDDLLVD 588

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   772 QDRReqaRQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTggsaaqkqKISFLENNLEQLTKVHKQLVR 851
Cdd:pfam01576  589 LDHQ---RQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET--------RALSLARALEEALEAKEELER 657

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 109892476   852 DNADLRCELPKLEKRLRATAERVKALESAlKEAKENASRDRKRYQQEVD 900
Cdd:pfam01576  658 TNKQLRAEMEDLVSSKDDVGKNVHELERS-KRALEQQVEEMKTQLEELE 705
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
682-813 1.81e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 682 EMEKEHLNKVQTANEVKQAVEQQiqsHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEK 761
Cdd:COG2433  384 ELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE 460

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109892476 762 SRKLHELTVMQDRREQARQDLKGLEETV---AKELQTLHNLRKLFVQDLATRVKK 813
Cdd:COG2433  461 IRKDREISRLDREIERLERELEEERERIeelKRKLERLKELWKLEHSGELVPVKV 515
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 422-754 2.25e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 45.43  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  422 EEEIAKLYKQLDDKDEEINQQ-------SQLVEKLKTQMLDQEELLA-STRRDQDNM-------QAELNRLQAENDASKE 486
Cdd:PRK10929  108 EQEILQVSSQLLEKSRQAQQEqdrareiSDSLSQLPQQQTEARRQLNeIERRLQTLGtpntplaQAQLTALQAESAALKA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  487 EVKEVlqALEELAVNYDQksqevedktkEYELLSDELNQKSATlaSIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEig 566
Cdd:PRK10929  188 LVDEL--ELAQLSANNRQ----------ELARLRSELAKKRSQ--QLDAYLQALRNQLNSQRQREAERALESTELLAE-- 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  567 iavgnNDVKQPEGtgmIDEEFTVARlyiskmksevktmvkrckQLESTQTESNKKMeenekELAACQLRisQHEAKIKSL 646
Cdd:PRK10929  252 -----QSGDLPKS---IVAQFKINR------------------ELSQALNQQAQRM-----DLIASQQR--QAASQTLQV 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  647 TEYLQNVEQKKRQLEESvDSLGEelvQLRAQ-EKVHEMEK-------------------EHLNKVQTANEVKQAVEQQIQ 706
Cdd:PRK10929  299 RQALNTLREQSQWLGVS-NALGE---ALRAQvARLPEMPKpqqldtemaqlrvqrlryeDLLNKQPQLRQIRQADGQPLT 374

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 109892476  707 ShretHQKQIssLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERL 754
Cdd:PRK10929  375 A----EQNRI--LDAQLRTQRELLNSLLSGGDTLILELTKLKVANSQL 416
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
646-819 2.71e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  646 LTEYLQNVEQKKRQLE--ESVDSLGEELVQLRAQEKVHEMEKEHLN--KVQTANEVKQAVEQQIQSHRETHQKQISSLRD 721
Cdd:COG4913   237 LERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEA 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  722 EVEAKEKLITDLQDQ------NQKMVLEQE--RLRVEHERLKAVDQEKSRKLHELTV--------MQDRREQARQDLKGL 785
Cdd:COG4913   317 RLDALREELDELEAQirgnggDRLEQLEREieRLERELEERERRRARLEALLAALGLplpasaeeFAALRAEAAALLEAL 396

                         170       180       190
                  ....*....|....*....|....*....|....
gi 109892476  786 EETVAKELQTLHNLRKLFVQDLATRVKKSAEVDS 819
Cdd:COG4913   397 EEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
613-886 3.42e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 613 STQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQ-EKVHEMEKEHLNKV 691
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKrDELNEKVKELKEER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 692 QTANEVKQAVEQQIQSHRETHqKQISSLRDEVEAKEKLITDLQD--QNQKMVLEQERLRVE---------HERLKAVDQE 760
Cdd:COG1340   81 DELNEKLNELREELDELRKEL-AELNKAGGSIDKLRKEIERLEWrqQTEVLSPEEEKELVEkikelekelEKAKKALEKN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 761 KS--RKLHELTVMQDRREQARQDLKGLeetvAKELQTLHN-LRKLFVQdlATRVKKSAEvdsddtggsaAQKQKISFLEN 837
Cdd:COG1340  160 EKlkELRAELKELRKEAEEIHKKIKEL----AEEAQELHEeMIELYKE--ADELRKEAD----------ELHKEIVEAQE 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 109892476 838 NLEQLTKVHKQLVRDNADLRCELPKLEKRLRAtAERVKALESALKEAKE 886
Cdd:COG1340  224 KADELHEEIIELQKELRELRKELKKLRKKQRA-LKREKEKEELEEKAEE 271
PRK11637 PRK11637
AmiB activator; Provisional
 422-631 3.75e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.91  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 422 EEEIAKLYKQLDDK-------DEEINQQSQLVEKLKTQMLDQEELLAST-----RRDQDN-MQAELN--------RLQAE 480
Cdd:PRK11637  81 EEAISQASRKLRETqntlnqlNKQIDELNASIAKLEQQQAAQERLLAAQldaafRQGEHTgLQLILSgeesqrgeRILAY 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 481 ----NDASKEEVKEVLQALEELAVnydQKSQEVEDKTKEYELLSDELNQKsatlasidaelQKLKEMTNHQKKRAAEMMA 556
Cdd:PRK11637 161 fgylNQARQETIAELKQTREELAA---QKAELEEKQSQQKTLLYEQQAQQ-----------QKLEQARNERKKTLTGLES 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 557 SLLKDLAEIGiavgnnDVKQPEgtgmideefTVARLYISKMKSEVKTMVK---------RCKQLESTQTESNKKMEENEK 627
Cdd:PRK11637 227 SLQKDQQQLS------ELRANE---------SRLRDSIARAEREAKARAEreareaarvRDKQKQAKRKGSTYKPTESER 291


                 ....
gi 109892476 628 ELAA 631
Cdd:PRK11637 292 SLMS 295
COG5022 COG5022
Myosin heavy chain [General function prediction only];
585-910 3.85e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  585 EEFTVARLYIsKMKSEVKTMVKRcKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSL-TEYLQNVEQKKRQLEES 663
Cdd:COG5022   788 DYELKWRLFI-KLQPLLSLLGSR-KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLiQKFGRSLKAKKRFSLLK 865

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  664 VDSLGEELVQLR--AQEKVHEMEKEhlnkVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMV 741
Cdd:COG5022   866 KETIYLQSAQRVelAERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNID 941

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  742 LE------------QERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVA---KELQTLHN-LRKLFVQ 805
Cdd:COG5022   942 LEegpsieyvklpeLNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelsKQYGALQEsTKQLKEL 1021

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  806 DLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRdNADLRCELPKLEKRLRATAERVKALESALKEAK 885
Cdd:COG5022  1022 PVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYK-ALKLRRENSLLDDKQLYQLESTENLLKTINVKD 1100

                         330       340
                  ....*....|....*....|....*
gi 109892476  886 ENASRDRKRYQQEVDRIKEAVRSKN 910
Cdd:COG5022  1101 LEVTNRNLVKPANVLQFIVAQMIKL 1125
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 590-765 4.69e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.05  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 590 ARLYISKMKSEVKTMVKrckqlestqtesnkKMEENEKELaacqlrisqhEAKIKSLTEYLQNVEQKKRQLEEsvdslge 669
Cdd:PRK00409 507 AKKLIGEDKEKLNELIA--------------SLEELEREL----------EQKAEEAEALLKEAEKLKEELEE------- 555

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 670 elvQLRAQEKVHEMEKEHL-NKVQTA-NEVKQAVEQQIQSHRETHQKQISSLRDEvEAKEKLiTDLQDQNQKMVLEQERL 747
Cdd:PRK00409 556 ---KKEKLQEEEDKLLEEAeKEAQQAiKEAKKEADEIIKELRQLQKGGYASVKAH-ELIEAR-KRLNKANEKKEKKKKKQ 630

                        170
                 ....*....|....*...
gi 109892476 748 RVEHERLKAVDQEKSRKL 765
Cdd:PRK00409 631 KEKQEELKVGDEVKYLSL 648
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 483-932 4.76e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 4.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   483 ASKEEVKEVLQALEELAVnYDQKSQEVEDK-----------TKEYELLSDELNQK-----------SATLASIDAELQKL 540
Cdd:TIGR00618  160 AKSKEKKELLMNLFPLDQ-YTQLALMEFAKkkslhgkaellTLRSQLLTLCTPCMpdtyherkqvlEKELKHLREALQQT 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   541 KEMTNH--QKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEgtgmidEEFTVARLYISKMKSEVKTMVKRCKQLESTQTES 618
Cdd:TIGR00618  239 QQSHAYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAV------LEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   619 NKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEkEHLNKVQTANEVK 698
Cdd:TIGR00618  313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT-QHIHTLQQQKTTL 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   699 QAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQ---DRR 775
Cdd:TIGR00618  392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslKER 471

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   776 EQARQDLKGLEETVaKELQTLHNLRKLFVQDLATRVKKS------AEVDSDDTGGsaaqkqkisfLENNLEQLTKVHKQL 849
Cdd:TIGR00618  472 EQQLQTKEQIHLQE-TRKKAVVLARLLELQEEPCPLCGScihpnpARQDIDNPGP----------LTRRMQRGEQTYAQL 540

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   850 VRDNADLRCELPKLEKR---LRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRP 926
Cdd:TIGR00618  541 ETSEEDVYHQLTSERKQrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620


                   ....*.
gi 109892476   927 GQHPAA 932
Cdd:TIGR00618  621 LQPEQD 626
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 422-578 6.33e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 422 EEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAEL--------------------------- 474
Cdd:COG3883   36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfs 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 475 ---------NRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTN 545
Cdd:COG3883  116 dfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 109892476 546 HQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPE 578
Cdd:COG3883  196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 485-565 6.82e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 485 KEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKsatLASIDAELQKLKEmtnHQKKRAAEMMASLLKDLAE 564
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLE---EAEKEAQQAIKEAKKEADE 588


                 .
gi 109892476 565 I 565
Cdd:PRK00409 589 I 589
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
354-568 6.92e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 354 LRNTIQWLENELNRwrngetvpIDEQFDKEKANLEAFTADKDVAITNDKPAAAIGMAGSF------TDAERRKCEEEIAK 427
Cdd:COG3206  173 ARKALEFLEEQLPE--------LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELesqlaeARAELAEAEARLAA 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 428 LYKQLDDKDEEINQ--QSQLVEKLKTQMLDQE----ELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEelaVN 501
Cdd:COG3206  245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEaelaELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE---AE 321

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109892476 502 YDQKSQEVEDKTKEYEllsdELNQKSATLASIDAELQKLKEmtnhQKKRAAEMMASLLKDLAEIGIA 568
Cdd:COG3206  322 LEALQAREASLQAQLA----QLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEARLA 380
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 436-777 6.99e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.35  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  436 DEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKE 515
Cdd:pfam07888  37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  516 YELLSD----------ELNQKSATLA----SIDAELQKLKEmtnhqkkRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:pfam07888 117 KDALLAqraahearirELEEDIKTLTqrvlERETELERMKE-------RAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  582 MiDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAacQLRisqheakikSLTEYLQNVEQKkrqle 661
Cdd:pfam07888 190 L-SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE--ELR---------SLQERLNASERK----- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  662 esVDSLGEELVQLRAQeKVHEMEKEHLNKVQTANEVKQAVEQ--QIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQK 739
Cdd:pfam07888 253 --VEGLGEELSSMAAQ-RDRTQAELHQARLQAAQLTLQLADAslALREGRARWAQERETLQQSAEADKDRIEKLSAELQR 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 109892476  740 M-------VLEQERLRVEHERLKAVDQ----EKSRKLHE----LTVMQDRREQ 777
Cdd:pfam07888 330 LeerlqeeRMEREKLEVELGREKDCNRvqlsESRRELQElkasLRVAQKEKEQ 382
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 417-900 1.05e-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: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam01576  153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   497 ELAVNYDQKSQEVEDKTKEYEllsDELNQKSATLASID------AELQKLKEMTNHQKKRAAEMMASLLKDL----AEIG 566
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLE---EETAQKNNALKKIReleaqiSELQEDLESERAARNKAEKQRRDLGEELealkTELE 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   567 IAVGNNDVKQ----------PEGTGMIDEEFTVARLYISKMKSevktmvKRCKQLE--STQTESNKKMEEN-EKELAACQ 633
Cdd:pfam01576  310 DTLDTTAAQQelrskreqevTELKKALEEETRSHEAQLQEMRQ------KHTQALEelTEQLEQAKRNKANlEKAKQALE 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   634 LRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLgeeLVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQ 713
Cdd:pfam01576  384 SENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL---QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   714 KQISS-----------LRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDL 782
Cdd:pfam01576  461 KDVSSlesqlqdtqelLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   783 KGLEETVAKELQTLHNLRKLFVQDLA-------TRVKKSAEVDsDDTGGSAAQKQKISflenNLEQLTKVHKQLVRDNAD 855
Cdd:pfam01576  541 EALEEGKKRLQRELEALTQQLEEKAAaydklekTKNRLQQELD-DLLVDLDHQRQLVS----NLEKKQKKFDQMLAEEKA 615

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 109892476   856 LRCELPklEKRLRATAE------RVKALESAL---KEAKENASRDRKRYQQEVD 900
Cdd:pfam01576  616 ISARYA--EERDRAEAEareketRALSLARALeeaLEAKEELERTNKQLRAEME 667
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 433-689 1.10e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.99  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 433 DDKDE--EINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRL----QAENDASKEEVKEVLQALEELAVNYDQKS 506
Cdd:PRK05771  16 SYKDEvlEALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLrsylPKLNPLREEKKKVSVKSLEELIKDVEEEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 507 QEVEDKTKEyelLSDELNQKSATLASIDAELQKLKEMTNhqkkraAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEE 586
Cdd:PRK05771  96 EKIEKEIKE---LEEEISELENEIKELEQEIERLEPWGN------FDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 587 FTVARLYISKMKSEVKTMVKrckqlestqtesNKKMEENEKELAACQLR-------------ISQHEAKIKSLTEYLQNV 653
Cdd:PRK05771 167 ENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLGFErleleeegtpselIREIKEELEEIEKERESL 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 109892476 654 eqkKRQLEESVDSLGEELVqlrAQEKVHEMEKEHLN 689
Cdd:PRK05771 235 ---LEELKELAKKYLEELL---ALYEYLEIELERAE 264
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 727-914 1.58e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  727 EKLITDLQDQNQKMVLEQERLRVEHERlKAVDQEKSRKLHEltvmqdrREQARQDLKGLEETVAKELQTLHNLRKLFVQD 806
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEE-------AEKARQAEMDRQAAIYAEQERMAMERERELER 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  807 LATRVKKSAEvdsddtggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKL-------EKRLRATAERVKALES 879
Cdd:pfam17380 353 IRQEERKREL--------ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArkvkileEERQRKIQQQKVEMEQ 424

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 109892476  880 ALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARR 914
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQ 459
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 530-686 1.73e-03

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: 41.06  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 530 LASIDAELQKLKemtnHQKKRAAEMMASLLKDLAEIgiavgNNDVKQpegtgmIDEEFTVARLYISKMKSEVKTMVKRCK 609
Cdd:COG1579   12 LQELDSELDRLE----HRLKELPAELAELEDELAAL-----EARLEA------AKTELEDLEKEIKRLELEIEEVEARIK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 610 QLESTQTE--SNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQ--EKVHEMEK 685
Cdd:COG1579   77 KYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldEELAELEA 156


                 .
gi 109892476 686 E 686
Cdd:COG1579  157 E 157
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 594-799 1.92e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.84  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 594 ISKM--------KSEVKTMVKRCKQLESTQTESNKKMEENEK--ELAACQLRISQH-------------------EAKIK 644
Cdd:PRK05771   3 PVRMkkvlivtlKSYKDEVLEALHELGVVHIEDLKEELSNERlrKLRSLLTKLSEAldklrsylpklnplreekkKVSVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 645 SLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHL-----------------NKVQTANEV-KQAVEQQIQ 706
Cdd:PRK05771  83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLepwgnfdldlslllgfkYVSVFVGTVpEDKLEELKL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 707 SHRETHQKQISSLRDEV--------EAKEKLITDLQDqnqkmvLEQERLRVEHErlKAVDQEKSRKLHELTVMQDRREQA 778
Cdd:PRK05771 163 ESDVENVEYISTDKGYVyvvvvvlkELSDEVEEELKK------LGFERLELEEE--GTPSELIREIKEELEEIEKERESL 234

                        250       260
                 ....*....|....*....|.
gi 109892476 779 RQDLKGLEETVAKELQTLHNL 799
Cdd:PRK05771 235 LEELKELAKKYLEELLALYEY 255
PRK01156 PRK01156
chromosome segregation protein; Provisional
 468-910 1.96e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 468 DNMQAELNRLqaenDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNhQ 547
Cdd:PRK01156 176 DMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-M 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 548 KKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNkKMEENEK 627
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEIN-KYHAIIK 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 628 ELAACQLRISQHEAKIKSLTE-----------------YLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNK 690
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDDlnnqilelegyemdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 691 VQtaNEVKQAVeQQIQSHRETHQKQISSLR---DEVEAKEKLI----------TDLQDQ----------NQKMVLEQERL 747
Cdd:PRK01156 410 EL--NEINVKL-QDISSKVSSLNQRIRALRenlDELSRNMEMLngqsvcpvcgTTLGEEksnhiinhynEKKSRLEEKIR 486

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 748 RVEHErLKAVDQEK-----------SRKLHELTVMQDRREQARQDLKGLEETVA-------KELQTLHNLRKLFVQDLAT 809
Cdd:PRK01156 487 EIEIE-VKDIDEKIvdlkkrkeyleSEEINKSINEYNKIESARADLEDIKIKINelkdkhdKYEEIKNRYKSLKLEDLDS 565

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 810 R----VKKSAEVDSDDTGGSAAQKQKISFLENNLEQ-LTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEsALKEA 884
Cdd:PRK01156 566 KrtswLNALAVISLIDIETNRSRSNEIKKQLNDLESrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ-ENKIL 644

                        490       500
                 ....*....|....*....|....*.
gi 109892476 885 KENASRDRKRYQQEVDRIKEAVRSKN 910
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEIDSIIPDLK 670
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 437-729 2.34e-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: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  437 EEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEEL---AVNYDQKSQEVEDKT 513
Cdd:COG3096   347 EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtrAIQYQQAVQALEKAR 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  514 KEYELlsDELNQKSA--TLASIDAELQKLKE--MTNHQKKRAAEMMASLLKDLAEIGIAVgnndvkqpegTGMIDEE--F 587
Cdd:COG3096   427 ALCGL--PDLTPENAedYLAAFRAKEQQATEevLELEQKLSVADAARRQFEKAYELVCKI----------AGEVERSqaW 494

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  588 TVARLYISKMKSEvKTMVKRCKQLESTQTESNKKMEEN---EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESV 664
Cdd:COG3096   495 QTARELLRRYRSQ-QALAQRLQQLRAQLAELEQRLRQQqnaERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  665 DSLGEELVQLRAQEKVHEMEKEHLNK------------VQTANEVKQAVE--QQIQSHRET---HQKQISSLRDEV-EAK 726
Cdd:COG3096   574 AEAVEQRSELRQQLEQLRARIKELAArapawlaaqdalERLREQSGEALAdsQEVTAAMQQlleREREATVERDELaARK 653


                  ...
gi 109892476  727 EKL 729
Cdd:COG3096   654 QAL 656
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
647-850 2.49e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 647 TEYL-QNVEQKKRQLEESVDSLGEELVQLR-----AQEKVHEMEKEHlNKVQTANEVKQAVEQ---------QIQSHRET 711
Cdd:COG3206  159 EAYLeQNLELRREEARKALEFLEEQLPELRkeleeAEAALEEFRQKN-GLVDLSEEAKLLLQQlselesqlaEARAELAE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 712 HQKQISSLRDEVEAKE-------------KLITDLQDQNQKMVLEQERLRVEHERLKAVDQEksrklheltvMQDRREQA 778
Cdd:COG3206  238 AEARLAALRAQLGSGPdalpellqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQ----------IAALRAQL 307

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109892476 779 RQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVdsddtggsAAQKQKISFLENNLEQLTKVHKQLV 850
Cdd:COG3206  308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEVARELYESLL 371
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
477-720 2.51e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 477 LQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYEL------LSDELNQKSATLASIDAELQKLKEMTNhQKKR 550
Cdd:COG3206  162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknglvdLSEEAKLLLQQLSELESQLAEARAELA-EAEA 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 551 AAEMMASLLKDLAEIGIAVGNNDVkqpegtgmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELA 630
Cdd:COG3206  241 RLAALRAQLGSGPDALPELLQSPV-------------------IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 631 ACQLRISQH--------EAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRaqekvhEMEKEhlnkVQTANEVKQAVE 702
Cdd:COG3206  302 ALRAQLQQEaqrilaslEAELEALQAREASLQAQLAQLEARLAELPELEAELR------RLERE----VEVARELYESLL 371

                        250
                 ....*....|....*...
gi 109892476 703 QQIQSHRETHQKQISSLR 720
Cdd:COG3206  372 QRLEEARLAEALTVGNVR 389
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 422-767 3.12e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 422 EEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELnrlqaeNDASKEEVKEVLQALEELAVN 501
Cdd:COG5185  228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRL------NENANNLIKQFENTKEKIAEY 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 502 YDQKSQEVEDKTKEYELLSDELNQK-SATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIgiaVGNNDVKQPEGT 580
Cdd:COG5185  302 TKSIDIKKATESLEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI---VGEVELSKSSEE 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 581 gmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEEN-EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQ 659
Cdd:COG5185  379 -------------LDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 660 LEESVDSLgEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQK 739
Cdd:COG5185  446 LISELNKV-MREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAE 524

                        330       340
                 ....*....|....*....|....*...
gi 109892476 740 MVLEQERLRVEHERLKAVDQEKSRKLHE 767
Cdd:COG5185  525 SLKDFMRARGYAHILALENLIPASELIQ 552
46 PHA02562
endonuclease subunit; Provisional
 424-521 3.12e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 424 EIAKLYKQLDDKDE-------EINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:PHA02562 310 ELQHSLEKLDTAIDeleeimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389

                         90       100
                 ....*....|....*....|....*
gi 109892476 497 ELAVNYDQKSQEVEDKTKEYELLSD 521
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIVTDLLKD 414
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 435-902 3.16e-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: 41.31  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   435 KDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVlqalEELAVNYDQKSQEVEDKTK 514
Cdd:pfam01576    3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEA----EEMRARLAARKQELEEILH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   515 EYELLSDELNQKSATLASIDAELQK-LKEMTNH-QKKRAAEMMASLLKDLAEIGIAvgnndvkqpegtgMIDEEFTVARL 592
Cdd:pfam01576   79 ELESRLEEEEERSQQLQNEKKKMQQhIQDLEEQlDEEEAARQKLQLEKVTTEAKIK-------------KLEEDILLLED 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   593 YISKMKSEVKTMVKRCKQLESTQTESnkkmEENEKELAACQLRisqHEAKIKSLTEYL-------QNVEQKKRQLEESVD 665
Cdd:pfam01576  146 QNSKLSKERKLLEERISEFTSNLAEE----EEKAKSLSKLKNK---HEAMISDLEERLkkeekgrQELEKAKRKLEGEST 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   666 SLGEELVQLRAQ--EKVHEMEK--EHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMV 741
Cdd:pfam01576  219 DLQEQIAELQAQiaELRAQLAKkeEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   742 LEQERLRVEHERL---KAVDQE-KSRKLHELTVMQDRREqarqdlkglEETVAKELQtlhnlrklfVQDLatRVKKSAEV 817
Cdd:pfam01576  299 EELEALKTELEDTldtTAAQQElRSKREQEVTELKKALE---------EETRSHEAQ---------LQEM--RQKHTQAL 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   818 DSDDTGGSAAQKQKISflennleqLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQ 897
Cdd:pfam01576  359 EELTEQLEQAKRNKAN--------LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430


                   ....*
gi 109892476   898 EVDRI 902
Cdd:pfam01576  431 LAEKL 435
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 654-903 4.58e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.94  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  654 EQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHL---NKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLI 730
Cdd:PRK10246  215 PEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLtrlDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRP 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  731 TDLQDQNQKMVLEQERLRVE--HERLKAVDQEKSRKLHELTVMQDRREQARQDLKG-LEETVAKEL--QTLHNLRKLFVQ 805
Cdd:PRK10246  295 HWERIQEQSAALAHTRQQIEevNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwLAEHDRFRQwnNELAGWRAQFSQ 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  806 ---DLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQ---LVRDNADLRCELPKLEKRLRATAERVKALES 879
Cdd:PRK10246  375 qtsDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQ 454

                         250       260
                  ....*....|....*....|....*..
gi 109892476  880 ALKEAKENASRDRKRY---QQEVDRIK 903
Cdd:PRK10246  455 EQTQRNAALNEMRQRYkekTQQLADVK 481
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 713-963 5.39e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 713 QKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRvehERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKE 792
Cdd:COG3883   22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 793 LQTLHNLRKLF----VQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLR 868
Cdd:COG3883   99 GGSVSYLDVLLgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 869 ATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPGAVRGGGSFVQ 948
Cdd:COG3883  179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258

                        250
                 ....*....|....*
gi 109892476 949 NNQPVGLRGGGGKQA 963
Cdd:COG3883  259 AGSAGAAGAAAGAAG 273
COG5022 COG5022
Myosin heavy chain [General function prediction only];
423-671 6.07e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  423 EEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAE--------LNRLQAENDASKE-EVKEVLQ 493
Cdd:COG5022   878 ELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEliarlkklLNNIDLEEGPSIEyVKLPELN 957

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  494 ALEELAVNYDQKSQEVEDKTKEYELL-------SDELNQKSATLASIDAELQKLKEMTNHQKKRAAEM--MASLLKDLAE 564
Cdd:COG5022   958 KLHEVESKLKETSEEYEDLLKKSTILvregnkaNSELKNFKKELAELSKQYGALQESTKQLKELPVEVaeLQSASKIISS 1037

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  565 IGIAVGN-NDVKQPEGTGMIDEEFTVARLY-ISKMKSEVKTMVKRCKQLESTQTESN----KKMEENEKEL--------- 629
Cdd:COG5022  1038 ESTELSIlKPLQKLKGLLLLENNQLQARYKaLKLRRENSLLDDKQLYQLESTENLLKtinvKDLEVTNRNLvkpanvlqf 1117

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 109892476  630 ---AACQLRISQHEAK-IKSLTEYLQNVEQKKRQLEESVDSLGEEL 671
Cdd:COG5022  1118 ivaQMIKLNLLQEISKfLSQLVNTLEPVFQKLSVLQLELDGLFWEA 1163
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-551 6.24e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 6.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476   415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQ--AENDASKEEVKEVL 492
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeiPEEELSLEDVQAEL 960

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 109892476   493 QALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRA 551
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
PRK01156 PRK01156
chromosome segregation protein; Provisional
 417-631 6.84e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 417 ERRKCEEEIAKlYKQLDDKDEEI----NQQSQLVEK-LKTQMLDQE------ELLASTRRDQDNMQAELNRLQAENDAS- 484
Cdd:PRK01156 510 ESEEINKSINE-YNKIESARADLedikIKINELKDKhDKYEEIKNRykslklEDLDSKRTSWLNALAVISLIDIETNRSr 588

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 485 KEEVKEVLQALE----ELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmMASLLK 560
Cdd:PRK01156 589 SNEIKKQLNDLEsrlqEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIP 667

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109892476 561 DLAEIGIAVGNNDVKQPEGTGMIDEeftvARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAA 631
Cdd:PRK01156 668 DLKEITSRINDIEDNLKKSRKALDD----AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 416-719 7.01e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEvlqaL 495
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE----L 508

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  496 EELAVNYDQKSQEVEDKTKEyelLSDELNQKSATLASIDAELQKLKEmtnhqkkraaemmaSLLKDLAEIGIAVGNNDVK 575
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEK---LESEKKEKESKISDLEDELNKDDF--------------ELKKENLEKEIDEKNKEIE 571

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  576 QPEGTgmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQ 655
Cdd:TIGR04523 572 ELKQT-------------QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109892476  656 KKRQLEESVDSLGEELVQLRaqEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSL 719
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIR--NKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRM 700
mukB PRK04863
chromosome partition protein MukB;
440-540 7.26e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  440 NQQSQLVEKLKTQMLDQEELLASTR---RDQDNMQAELNR----LQAENDASKEEVKEVLQALEELAVNYDQKSQE--VE 510
Cdd:PRK04863  981 AKNSDLNEKLRQRLEQAEQERTRAReqlRQAQAQLAQYNQvlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEEraRA 1060

                          90       100       110
                  ....*....|....*....|....*....|...
gi 109892476  511 DKTKEYELLSDELNQKSA---TLASIDAELQKL 540
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQlekQLTFCEAEMDNL 1093
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 419-798 7.29e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 419 RKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNrlqAENDASKEEVKEVLQALEEL 498
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLL---ANRFSFGPALDELEKQLENL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 499 avnydqksqevEDKTKEYELLSDELN--QKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEigIAVGNNDvkq 576
Cdd:PRK04778 178 -----------EEEFSQFVELTESGDyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQE--LKAGYRE--- 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 577 pegtgMIDEEFTVARLyisKMKSEVKTMVKRCKQLEstQTESNKKMEENEKELAACQLRISQ------HEAK-------- 642
Cdd:PRK04778 242 -----LVEEGYHLDHL---DIEKEIQDLKEQIDENL--ALLEELDLDEAEEKNEEIQERIDQlydileREVKarkyvekn 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 643 IKSLTEYLQNVEQKKRQLEESVDSLGE-------ELVQLRA-QEKVHEMEKEHLnkvqtanEVKQAVEQQIQSHrethqk 714
Cdd:PRK04778 312 SDTLPDFLEHAKEQNKELKEEIDRVKQsytlnesELESVRQlEKQLESLEKQYD-------EITERIAEQEIAY------ 378

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 715 qiSSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELtvmqdRREQARQDLKGLEE------- 787
Cdd:PRK04778 379 --SELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEI-----KRYLEKSNLPGLPEdylemff 451

                        410
                 ....*....|.
gi 109892476 788 TVAKELQTLHN 798
Cdd:PRK04778 452 EVSDEIEALAE 462
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
717-908 8.63e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 8.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 717 SSLRDEVEAKEKLITDLQDQNQKMVLEQ--------ERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEEt 788
Cdd:COG4717   45 AMLLERLEKEADELFKPQGRKPELNLKElkeleeelKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 789 vAKELQTLHNLRKLFVQDLATRVKKSAEVDsddtggsaAQKQKISFLENNLEQLTKVHKQLVRD-NADLRCELPKLEKRL 867
Cdd:COG4717  124 -LLQLLPLYQELEALEAELAELPERLEELE--------ERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEEL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 109892476 868 RATAERVKALESALKEAKEnasrDRKRYQQEVDRIKEAVRS 908
Cdd:COG4717  195 QDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQ 231
PRK12705 PRK12705
hypothetical protein; Provisional
 422-564 9.35e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 422 EEEIAKLYKQLDDKDEEINQQSQLVEKLKtqmLDQEELLASTRR------DQDNMQAELNRLQAENDASKEEVKEVLQAL 495
Cdd:PRK12705  45 EAEEKLEAALLEAKELLLRERNQQRQEAR---REREELQREEERlvqkeeQLDARAEKLDNLENQLEEREKALSARELEL 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109892476 496 EELAVNYDQKSQEVEDKTKE------YELLSDELNQKSATLasIDAELQKLKEmtnHQKKRAAEMMASLLKDLAE 564
Cdd:PRK12705 122 EELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQR--VKKIEEEADL---EAERKAQNILAQAMQRIAS 191
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 636-765 9.39e-03

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 39.20  E-value: 9.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476  636 ISQHEAKIKSLTEYLQNVEQKKRQLEESV----DSLGE-----ELVQL---RAQEKVHEMEKEHLN---KVQTANEVKQA 700
Cdd:pfam14915 139 VSNLRDENEILSQQLSKAESKANSLENELhrtrDALREktlllESVQRdlsQAQCQKKELEHMYQNeqdKVNKYIGKQES 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109892476  701 VEQ---QIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVleqERLRVEHERLKAVDQEKSRKL 765
Cdd:pfam14915 219 LEErlaQLQSENMLLRQQLEDAQNKADAKEKTVIDIQDQFQDIV---KKLQAESEKQVLLLEERNKEL 283
PRK12704 PRK12704
phosphodiesterase; Provisional
 596-728 9.90e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109892476 596 KMKSEVKTMVKRCK-QLESTQTESNKKMEENEKelaacqlRISQHEakiKSLTEYLQNVEQKKRQLEESVDSLGEELVQL 674
Cdd:PRK12704  57 EALLEAKEEIHKLRnEFEKELRERRNELQKLEK-------RLLQKE---ENLDRKLELLEKREEELEKKEKELEQKQQEL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109892476 675 RAQEK-VHEMEKEHLNKVQ-----TANEVKQaveQQIQSHRETHQKQISSL--RDEVEAKEK 728
Cdd:PRK12704 127 EKKEEeLEELIEEQLQELErisglTAEEAKE---ILLEKVEEEARHEAAVLikEIEEEAKEE 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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