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Conserved domains on  [gi|4758648|ref|NP_004512|]
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kinesin-1 heavy chain [Homo sapiens]

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: 636.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    6 ECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIAS----KPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTI 81
Cdd:cd01369   1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATsetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   82 FAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNR 161
Cdd:cd01369  81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKT 241
Cdd:cd01369 161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  242 GAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ 320
Cdd:cd01369 241 GAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                ....*
gi 4758648  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 1.03e-22

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: 92.26  E-value: 1.03e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  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 5.63e-16

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: 83.18  E-value: 5.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaskeevkevlq 493
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE------------- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     494 aLEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA---EMMASLLKDLAEIGIAVG 570
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLT 647
Cdd:TIGR02168  821 NLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     648 EYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNkvQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKA 727
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758648     728 KLITDLQDQNQKMMLEQERLRVEHEKLKA--TDQEKSRKLHElTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLF 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: 636.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    6 ECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIAS----KPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTI 81
Cdd:cd01369   1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATsetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   82 FAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNR 161
Cdd:cd01369  81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKT 241
Cdd:cd01369 161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  242 GAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ 320
Cdd:cd01369 241 GAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                ....*
gi 4758648  321 RAKTI 325
Cdd:cd01369 321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 8-332 1.97e-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: 1.97e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648       8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVI---------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYN 78
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648      79 GTIFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHED 158
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     159 KNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQE--NTQTEQKLSGKLYLVDLAGSE 236
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     237 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAE--GSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKS 314
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                          330
                   ....*....|....*...
gi 4758648     315 TLLFGQRAKTIKNTVCVN 332
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
14-325 7.11e-154

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 456.65  E-value: 7.11e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     14 RFRPLNESEVNRGDKYI---------AKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:pfam00225   1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LSVHEDKNR 161
Cdd:pfam00225  81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQT---EQKLSGKLYLVDLAGSEKV 238
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    239 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTL 316
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                  ....*....
gi 4758648    317 LFGQRAKTI 325
Cdd:pfam00225 318 RFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
8-333 6.59e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 292.41  E-value: 6.59e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGD---KYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:COG5059  17 NEKSVSDIKSTIRIIPGELGerlINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPY 164
Cdd:COG5059  97 GQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVK 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  165 VKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAE 244
Cdd:COG5059 174 VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNR 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  245 GAVLDEAKNINKSLSALGNVISAL--AEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRA 322
Cdd:COG5059 254 GTRLKEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRA 333

                       330
                ....*....|.
gi 4758648  323 KTIKNTVCVNV 333
Cdd:COG5059 334 KSIKNKIQVNS 344
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 4-515 2.05e-62

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 231.36  E-value: 2.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648      4 LAECNIKVMCRFRPLNESEvnRGDKYIAKFQGeDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFA 83
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE--EGEMIVQKMSN-DSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     84 YGQTSSGKTHTMEGKLH-------DPEGMGIIPRIVQDIFNYIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKT 151
Cdd:PLN03188  172 YGQTGSGKTYTMWGPANglleehlSGDQQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQK 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    152 NLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSG----KL 227
Cdd:PLN03188  252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRI 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    228 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGST-----YVPYRDSKMTRILQDSLGGNCRTTIVICC 302
Cdd:PLN03188  332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    303 SPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEqwkkkyekekekNKILRNTIQWLENELNRWRNGETVPIDEQfdk 382
Cdd:PLN03188  412 SPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD------------VNFLREVIRQLRDELQRVKANGNNPTNPN--- 476

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    383 ekanlEAFTVDKDitltndkPATAIGVIGNFTDAERRkceeeiaKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLAs 462
Cdd:PLN03188  477 -----VAYSTAWN-------ARRSLNLLKSFGLGPPP-------SLPHVDEDGDEEMEIDEEAVERLCVQVGLQPAGAA- 536

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4758648    463 trrdqDNMQAELNRLQAENDASKEEVKEvlQALEELAVNYDQKSQEVEDKTKE 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 1.03e-22

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: 92.26  E-value: 1.03e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  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 5.63e-16

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: 83.18  E-value: 5.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaskeevkevlq 493
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE------------- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     494 aLEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA---EMMASLLKDLAEIGIAVG 570
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLT 647
Cdd:TIGR02168  821 NLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     648 EYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNkvQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKA 727
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758648     728 KLITDLQDQNQKMMLEQERLRVEHEKLKA--TDQEKSRKLHElTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLF 803
Cdd:TIGR02168  979 NKIKELGPVNLAAIEEYEELKERYDFLTAqkEDLTEAKETLE-EAIEEIDREARERFKDTFDQVNENFQRV--FPKLF 1053
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-886 3.91e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.54  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTqmlDQEELLASTRRDQdnmqAELNRLQAENDASKEEVKEVLQA 494
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEE---ERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDR 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGIAVGNNDV 574
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE----LEEEIEELRERFGDAPV 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   575 KQPEGTGMIDEeftvarlyiskMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAA-----C--QLRISQHEAKIKSLT 647
Cdd:PRK02224 406 DLGNAEDFLEE-----------LREERDELREREAELEATLRTARERVEEAEALLEAgkcpeCgqPVEGSPHVETIEEDR 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   648 EYLQNVEQKKRQLEESVDALSEELVQLraqEKVHEMEKEhlnkVQTANEVKQAVEQQIQSHRET---HQKQISSLRDEVE 724
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERA---EDLVEAEDR----IERLEERREDLEELIAERRETieeKRERAEELRERAA 547

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   725 AKAKLITDLQDQNQKMMLEQERLRVE----HEKLKATDQEKSRkLHELTVMQDRREQARQDLKGLEETVaKELQTLHNLR 800
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEvaelNSKLAELKERIES-LERIRTLLAAIADAEDEIERLREKR-EALAELNDER 625

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   801 KLFVQDLATRVKK-SAEIDSDDTGGSAAQKQKisfLENNLEQLTKVHKQLVRDNADLRC----------ELPKLEKRLRA 869
Cdd:PRK02224 626 RERLAEKRERKRElEAEFDEARIEEAREDKER---AEEYLEQVEEKLDELREERDDLQAeigaveneleELEELRERREA 702

                        490
                 ....*....|....*..
gi 4758648   870 TAERVKALESALKEAKE 886
Cdd:PRK02224 703 LENRVEALEALYDEAEE 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 617-922 4.08e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 4.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  617 ESNKKMEENEKELAACQLRISQHEAKIKSLteylqnveqkKRQLE--ESVDALSEELVQLRAQEKVHEME--KEHLNKVQ 692
Cdd:COG1196 176 EAERKLEATEENLERLEDILGELERQLEPL----------ERQAEkaERYRELKEELKELEAELLLLKLRelEAELEELE 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  693 TANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERL----RVEHEKLKATDQEKSRKLHEL 768
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiARLEERRRELEERLEELEEEL 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  769 TVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVH-- 846
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEel 405

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648  847 KQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAK 922
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 379-900 2.02e-11

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: 68.21  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    379 QFDKEKANL---EAFTVDKDITLTNDKPAtaigvigNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLD 455
Cdd:pfam05483 126 QFENEKVSLkleEEIQENKDLIKENNATR-------HLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    456 QEELLASTRRDQDNMQAELN----RLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLA 531
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKedheKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    532 SIDAELQKLKEMTNHQKKRAAEMMASLLKDLA-----EIGIAVGNNDVKQ-PEGTGMIDEEFTVARLYISKMKSEVKTMV 605
Cdd:pfam05483 279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkalEEDLQIATKTICQlTEEKEAQMEELNKAKAAHSFVVTEFEATT 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    606 KRCKQLESTQtesNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNveqKKRQLEESVDALSEELVQLRAQEKVHEMEK 685
Cdd:pfam05483 359 CSLEELLRTE---QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN---KEVELEELKKILAEDEKLLDEKKQFEKIAE 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    686 EHLNKVQTANEVKQAVEQQI----------QSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEheklk 755
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIhdleiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE----- 507

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    756 ATDQEKSRKLHELTVMQDRREQAR--QDLKGLEETVAKELQTLHNLRKLFVQ---DLATRVKKSAEIDSDDTGGSAAQKQ 830
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERmlKQIENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648    831 KISFLENN-------LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVD 900
Cdd:pfam05483 588 QMKILENKcnnlkkqIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
 446-773 3.70e-04

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: 43.89  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     446 VEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQ 525
Cdd:smart00806  73 VEELDEVKKHIDDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARPAASPSPVLASSSSAISLANNPDKLNKE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     526 KSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLA---EIGIAVGNNDvkqpegtgmideeftvARLYISKMKSEVK 602
Cdd:smart00806 153 QRAELKSLQRELAVLRQTHNSFFTEIKESIKDILEKIDkfkSSSLSASGSS----------------NRAYVESSKKKLS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     603 TMVKR-CKQLESTQ---------------TESNKKMEENEKELAACqlrisqhEAKIKSLTEYLQNVE-QKKRQLEESVD 665
Cdd:smart00806 217 EDSDSlLTKVDDLQdiiealrkdvaqrgvRPSKKQLETVQKELETA-------RKELKKMEEYIDIEKpIWKKIWEAELD 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     666 ALSEELVQLRAQEKVHEMEKEHLNKV-QTANEVKQAVEQQIQSHRETHQKQISSlrdeVEAKAKLITDLQDQnqkMMLEQ 744
Cdd:smart00806 290 KVCEEQQFLTLQEDLIADLKEDLEKAeETFDLVEQCCEEQEKGPSKNRNKPVSL----PVPTPGTFNDLKDQ---VLMEV 362

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 4758648     745 ERLRVEHEK-LKATD-----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: 636.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    6 ECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIAS----KPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTI 81
Cdd:cd01369   1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATsetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   82 FAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNR 161
Cdd:cd01369  81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKT 241
Cdd:cd01369 161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  242 GAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ 320
Cdd:cd01369 241 GAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320


                ....*
gi 4758648  321 RAKTI 325
Cdd:cd01369 321 RAKTI 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 8-332 1.97e-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: 1.97e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648       8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVI---------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYN 78
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknrqGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648      79 GTIFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHED 158
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     159 KNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQE--NTQTEQKLSGKLYLVDLAGSE 236
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     237 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAE--GSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKS 314
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317

                          330
                   ....*....|....*...
gi 4758648     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 2.61e-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: 2.61e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIaKFQGEDTVVI--------ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNG 79
Cdd:cd00106   1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLdppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   80 TIFAYGQTSSGKTHTMEGKlhDPEGMGIIPRIVQDIFNYIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VSKTNLSVHE 157
Cdd:cd00106  80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  158 DKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQT--EQKLSGKLYLVDLAGS 235
Cdd:cd00106 158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  236 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGS-TYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKS 314
Cdd:cd00106 238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317


                ....*....
gi 4758648  315 TLLFGQRAK 323
Cdd:cd00106 318 TLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
14-325 7.11e-154

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 456.65  E-value: 7.11e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     14 RFRPLNESEVNRGDKYI---------AKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:pfam00225   1 RVRPLNEREKERGSSVIvsvesvdseTVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LSVHEDKNR 161
Cdd:pfam00225  81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    162 VPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQT---EQKLSGKLYLVDLAGSEKV 238
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    239 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTL 316
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317


                  ....*....
gi 4758648    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 8.58e-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: 8.58e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFqGEDTVV---IASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:cd01374   1 KITVTVRVRPLNSREIGINEQVAWEI-DNDTIYlvePPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   85 GQTSSGKTHTMEGKLHDPegmGIIPRIVQDIFNYIYsMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPY 164
Cdd:cd01374  80 GQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVY 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  165 VKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVkqENTQTEQKLSGK-----LYLVDLAGSEKVS 239
Cdd:cd01374 156 VAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI--ESSERGELEEGTvrvstLNLIDLAGSERAA 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  240 KTGAEGAVLDEAKNINKSLSALGNVISALAEG--STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLL 317
Cdd:cd01374 234 QTGAAGVRRKEGSHINKSLLTLGTVISKLSEGkvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLK 313


                ....*...
gi 4758648  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 1.82e-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: 360.11  E-value: 1.82e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    7 CNIKVMCRFRPLNESEVNRGDKYIAKFQ-GEDTVVI-ASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:cd01372   1 SSVRVAVRVRPLLPKEIIEGCRICVSFVpGEPQVTVgTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   85 GQTSSGKTHTMEG---KLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VSKTNLSVHED 158
Cdd:cd01372  81 GQTGSGKTYTMGTaytAEEDEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIRED 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  159 KNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQE--NTQTEQK--------LSGKLY 228
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTkkNGPIAPMsaddknstFTSKFH 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  229 LVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGS---TYVPYRDSKMTRILQDSLGGNCRTTIVICCSPS 305
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320

                       330       340
                ....*....|....*....|.
gi 4758648  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 1.78e-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: 357.29  E-value: 1.78e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVV------IASKPYAFDRVFQSSTSQEQVYNDcAKKIVKDVLEGYNGTI 81
Cdd:cd01366   3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIeltsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   82 FAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVSKTNLSVHE 157
Cdd:cd01366  82 FAYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  158 D--KNRVpYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGS 235
Cdd:cd01366 159 DseKGDT-TVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  236 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKST 315
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                       330
                ....*....|..
gi 4758648  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 6.36e-110

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: 342.90  E-value: 6.36e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKP----------YAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGY 77
Cdd:cd01371   2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkataneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   78 NGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVSKtNLSV 155
Cdd:cd01371  82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  156 HEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV----KQENTQTEQKLsGKLYLVD 231
Cdd:cd01371 161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GKLNLVD 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  232 LAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG-STYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNES 310
Cdd:cd01371 240 LAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGkSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYD 319

                       330
                ....*....|....*
gi 4758648  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 4.87e-106

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: 333.55  E-value: 4.87e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIA--------------SKPYAFDRVFQSST-------SQEQVYNDCA 66
Cdd:cd01365   2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNpkqadknnkatrevPKSFSFDYSYWSHDsedpnyaSQEQVYEDLG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   67 KKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSM-DENLEFHIKVSYFEIYLDKIRDL 145
Cdd:cd01365  82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  146 LDVS----KTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQ 221
Cdd:cd01365 159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  222 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGST--------YVPYRDSKMTRILQDS 289
Cdd:cd01365 239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkkssFIPYRDSVLTWLLKEN 318

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4758648  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 9.55e-102

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: 321.60  E-value: 9.55e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAK--------------------FQGEDTVVIASKP----YAFDRVFQSSTSQEQVYN 63
Cdd:cd01370   1 SLTVAVRVRPFSEKEKNEGFRRIVKvmdnhmlvfdpkdeedgffhGGSNNRDRRKRRNkelkYVFDRVFDETSTQEEVYE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   64 DCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPegmGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIR 143
Cdd:cd01370  81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  144 DLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQ---TE 220
Cdd:cd01370 158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTasiNQ 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  221 QKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG---STYVPYRDSKMTRILQDSLGGNCRTT 297
Cdd:cd01370 238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPgkkNKHIPYRDSKLTRLLKDSLGGNCRTV 317

                       330       340
                ....*....|....*....|....*...
gi 4758648  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 1.41e-99

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: 316.19  E-value: 1.41e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    6 ECNIKVMCRFRPLNESEVNRG----------DKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLE 75
Cdd:cd01364   1 GKNIQVVVRCRPFNLRERKASshsvvevdpvRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   76 GYNGTIFAYGQTSSGKTHTMEGK--------LHDPEGMGIIPRIVQDIFNYIYSMDEnlEFHIKVSYFEIYLDKIRDLLD 147
Cdd:cd01364  81 GYNCTIFAYGQTGTGKTYTMEGDrspneeytWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  148 VS---KTNLSVHEDKNRVP--YVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV-KQENTQTEQ 221
Cdd:cd01364 159 PSsdvSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIhIKETTIDGE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  222 KL--SGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIV 299
Cdd:cd01364 239 ELvkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSII 318

                       330       340       350
                ....*....|....*....|....*....|...
gi 4758648  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 1.08e-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: 295.19  E-value: 1.08e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKP---YAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:cd01373   2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   85 GQTSSGKTHTMEGKLHD----PEGM-GIIPRIVQDIFNYI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSV 155
Cdd:cd01373  82 GQTGSGKTYTMWGPSESdnesPHGLrGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  156 HEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVK---QENTQTEQKLSgKLYLVDL 232
Cdd:cd01373 162 REDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIEsweKKACFVNIRTS-RLNLVDL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  233 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYN 308
Cdd:cd01373 241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320

                       330       340
                ....*....|....*....|....*
gi 4758648  309 ESETKSTLLFGQRAKTIKNTVCVNV 333
Cdd:cd01373 321 FGETLSTLRFAQRAKLIKNKAVVNE 345
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
8-333 6.59e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 292.41  E-value: 6.59e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGD---KYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAY 84
Cdd:COG5059  17 NEKSVSDIKSTIRIIPGELGerlINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   85 GQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPY 164
Cdd:COG5059  97 GQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVK 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  165 VKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAE 244
Cdd:COG5059 174 VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNR 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  245 GAVLDEAKNINKSLSALGNVISAL--AEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRA 322
Cdd:COG5059 254 GTRLKEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRA 333

                       330
                ....*....|.
gi 4758648  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 1.71e-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: 245.10  E-value: 1.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIA-------SKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT 80
Cdd:cd01376   1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELAdprnhgeTLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   81 IFAYGQTSSGKTHTMEGklhDPEGMGIIPRIVQDIFNYIYSMDENLEFhiKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN 160
Cdd:cd01376  81 VFAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  161 RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV-KQENTQTEQKLSGKLYLVDLAGSEKVS 239
Cdd:cd01376 156 GNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVdQRERLAPFRQRTGKLNLIDLAGSEDNR 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  240 KTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFG 319
Cdd:cd01376 236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315


                ....
gi 4758648  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 3.87e-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: 245.00  E-value: 3.87e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    9 IKVMCRFRPLNESEVNRGD-----------------KYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVK 71
Cdd:cd01368   3 VKVYLRVRPLSKDELESEDegcievinsttvvlhppKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   72 DVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPegmGIIPRIVQDIFNYIYsmdenlEFHIKVSYFEIYLDKIRDLLDVS-- 149
Cdd:cd01368  83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  150 -----KTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINV--------KQEN 216
Cdd:cd01368 154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapgdsdGDVD 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  217 TQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG-----STYVPYRDSKMTRILQDSLG 291
Cdd:cd01368 234 QDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENqlqgtNKMVPFRDSKLTHLFQNYFD 313

                       330       340       350
                ....*....|....*....|....*....|..
gi 4758648  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 2.74e-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: 242.20  E-value: 2.74e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    8 NIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYA-------------FDRVFQSSTSQEQVYNDCAKKIVKDVL 74
Cdd:cd01367   1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKvdltkyienhtfrFDYVFDESSSNETVYRSTVKPLVPHIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   75 EGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRI-VQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDvSKTNL 153
Cdd:cd01367  81 EGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  154 SVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTqteQKLSGKLYLVDLA 233
Cdd:cd01367 160 RLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT---NKLHGKLSFVDLA 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  234 GSEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSL-GGNCRTTIVICCSPSSYNESE 311
Cdd:cd01367 237 GSERGADTSSADRqTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316

                       330
                ....*....|..
gi 4758648  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 3.49e-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: 239.40  E-value: 3.49e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   46 YAFDRVFQSStSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIySMDEN 125
Cdd:cd01375  50 FKFDGVLHNA-SQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPT 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  126 LEFHIKVSYFEIYLDKIRDLLDV------SKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNE 199
Cdd:cd01375 128 KAYTVHVSYLEIYNEQLYDLLSTlpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNK 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  200 HSSRSHSIFLINV--KQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-GSTYVP 276
Cdd:cd01375 208 NSSRSHCIFTIHLeaHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDkDRTHVP 287

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 4758648  277 YRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAK 323
Cdd:cd01375 288 FRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 4-515 2.05e-62

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 231.36  E-value: 2.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648      4 LAECNIKVMCRFRPLNESEvnRGDKYIAKFQGeDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFA 83
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE--EGEMIVQKMSN-DSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     84 YGQTSSGKTHTMEGKLH-------DPEGMGIIPRIVQDIFNYIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKT 151
Cdd:PLN03188  172 YGQTGSGKTYTMWGPANglleehlSGDQQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQK 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    152 NLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSG----KL 227
Cdd:PLN03188  252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRI 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    228 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGST-----YVPYRDSKMTRILQDSLGGNCRTTIVICC 302
Cdd:PLN03188  332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    303 SPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEqwkkkyekekekNKILRNTIQWLENELNRWRNGETVPIDEQfdk 382
Cdd:PLN03188  412 SPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD------------VNFLREVIRQLRDELQRVKANGNNPTNPN--- 476

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    383 ekanlEAFTVDKDitltndkPATAIGVIGNFTDAERRkceeeiaKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLAs 462
Cdd:PLN03188  477 -----VAYSTAWN-------ARRSLNLLKSFGLGPPP-------SLPHVDEDGDEEMEIDEEAVERLCVQVGLQPAGAA- 536

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4758648    463 trrdqDNMQAELNRLQAENDASKEEVKEvlQALEELAVNYDQKSQEVEDKTKE 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 5.59e-51

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: 176.77  E-value: 5.59e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   11 VMCRFRPLNESEVNRGDKYIAkfqgedtvviaskpyaFDRVFQSSTSQEQVYNDCAKkIVKDVLEGYNG-TIFAYGQTSS 89
Cdd:cd01363   1 VLVRVNPFKELPIYRDSKIIV----------------FYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFAYGESGA 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   90 GKTHTMegklhdpegMGIIPRIVQDIFNYIYSMDENLEFHikvsyfeiyldkirdlldvsktnlsvhedknrvpyvkgCT 169
Cdd:cd01363  64 GKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------LT 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  170 ERFVCSPDEVMDTIDEGKSNRhVAVTNMNEHSSRSHSIFLInvkqentqteqklsgklyLVDLAGSEkvsktgaegavld 249
Cdd:cd01363  97 EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------- 144

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4758648  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 2.11e-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: 102.68  E-value: 2.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648      7 CNIKVMCRFRPLNESEVNRgdKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCaKKIVKDVLEGYNGTIFAYGQ 86
Cdd:pfam16796  20 GNIRVFARVRPELLSEAQI--DYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQ 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     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 1.03e-22

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: 92.26  E-value: 1.03e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  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 5.63e-16

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: 83.18  E-value: 5.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaskeevkevlq 493
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE------------- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     494 aLEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA---EMMASLLKDLAEIGIAVG 570
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLT 647
Cdd:TIGR02168  821 NLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     648 EYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNkvQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKA 727
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758648     728 KLITDLQDQNQKMMLEQERLRVEHEKLKA--TDQEKSRKLHElTVMQDRREQARQDLKGLEETVAKELQTLhnLRKLF 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 1.03e-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: 78.96  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     495 LEElavnydqksqEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtnhqkkraaEMMASLLKDLAEIGIAVGNndv 574
Cdd:TIGR02169  249 LEE----------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----------EEQLRVKEKIGELEAEIAS--- 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     575 kqpegtgmideeftvARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVE 654
Cdd:TIGR02169  306 ---------------LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     655 QKKRQLEESVDALSEELVQLRaqEKVhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVeakAKLITDLQ 734
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYR--EKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI---NELEEEKE 444

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4758648     735 DQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETV 789
Cdd:TIGR02169  445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 479-905 2.58e-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: 77.80  E-value: 2.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     479 AENDASKEevkevlQALEELAvnydqksqEVEDKTKEYELLSDELNQksatlasidaELQKLKEMTNHqkkraAEMMASL 558
Cdd:TIGR02169  166 AEFDRKKE------KALEELE--------EVEENIERLDLIIDEKRQ----------QLERLRREREK-----AERYQAL 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     559 LKDLAEIgiavgnndvkqpegtgmideEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQ 638
Cdd:TIGR02169  217 LKEKREY--------------------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     639 HEAKIKSLTEYLQNveQKKRQLEEsvdaLSEELVQLRAQEKVHEMEKEHLnkvqtanevkQAVEQQIQSHRETHQKQISS 718
Cdd:TIGR02169  277 LNKKIKDLGEEEQL--RVKEKIGE----LEAEIASLERSIAEKERELEDA----------EERLAKLEAEIDKLLAEIEE 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     719 LRDEVEA----KAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQ 794
Cdd:TIGR02169  341 LEREIEEerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     795 TLHNLRklfvQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRAtaerv 874
Cdd:TIGR02169  421 ELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD----RVEKELSK----- 487

                          410       420       430
                   ....*....|....*....|....*....|.
gi 4758648     875 KALESALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:TIGR02169  488 LQRELAEAEAQARASEERVRGGRAVEEVLKA 518
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-886 3.91e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.54  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTqmlDQEELLASTRRDQdnmqAELNRLQAENDASKEEVKEVLQA 494
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEE---ERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDR 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGIAVGNNDV 574
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE----LEEEIEELRERFGDAPV 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   575 KQPEGTGMIDEeftvarlyiskMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAA-----C--QLRISQHEAKIKSLT 647
Cdd:PRK02224 406 DLGNAEDFLEE-----------LREERDELREREAELEATLRTARERVEEAEALLEAgkcpeCgqPVEGSPHVETIEEDR 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   648 EYLQNVEQKKRQLEESVDALSEELVQLraqEKVHEMEKEhlnkVQTANEVKQAVEQQIQSHRET---HQKQISSLRDEVE 724
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERA---EDLVEAEDR----IERLEERREDLEELIAERRETieeKRERAEELRERAA 547

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   725 AKAKLITDLQDQNQKMMLEQERLRVE----HEKLKATDQEKSRkLHELTVMQDRREQARQDLKGLEETVaKELQTLHNLR 800
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEvaelNSKLAELKERIES-LERIRTLLAAIADAEDEIERLREKR-EALAELNDER 625

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   801 KLFVQDLATRVKK-SAEIDSDDTGGSAAQKQKisfLENNLEQLTKVHKQLVRDNADLRC----------ELPKLEKRLRA 869
Cdd:PRK02224 626 RERLAEKRERKRElEAEFDEARIEEAREDKER---AEEYLEQVEEKLDELREERDDLQAeigaveneleELEELRERREA 702

                        490
                 ....*....|....*..
gi 4758648   870 TAERVKALESALKEAKE 886
Cdd:PRK02224 703 LENRVEALEALYDEAEE 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 617-922 4.08e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 4.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  617 ESNKKMEENEKELAACQLRISQHEAKIKSLteylqnveqkKRQLE--ESVDALSEELVQLRAQEKVHEME--KEHLNKVQ 692
Cdd:COG1196 176 EAERKLEATEENLERLEDILGELERQLEPL----------ERQAEkaERYRELKEELKELEAELLLLKLRelEAELEELE 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  693 TANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERL----RVEHEKLKATDQEKSRKLHEL 768
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiARLEERRRELEERLEELEEEL 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  769 TVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVH-- 846
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEel 405

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648  847 KQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAK 922
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 475-884 5.72e-13

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: 73.17  E-value: 5.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     475 NRLQAEN--DASKEEVKEVLQALEELAVNYDQKSQEVEdKTKEYELLSDELNQKSATLASIDA-ELQKLKEMTNHQKKRA 551
Cdd:TIGR02168  173 RRKETERklERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLeELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     552 AEMMASLLKDLAEIgiavgnndvkqpegtgmiDEEFTVARLYISKMKSEVKtmvkrckQLESTQTESNKKMEENEKELAA 631
Cdd:TIGR02168  252 EEELEELTAELQEL------------------EEKLEELRLEVSELEEEIE-------ELQKELYALANEISRLEQQKQI 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     632 CQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQ-EKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRE 710
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQLETLRS 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     711 ---THQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQErlrveheklkatDQEKSRKLHELTVMQDRREQARQDLKGLEE 787
Cdd:TIGR02168  387 kvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIE------------ELLKKLEEAELKELQAELEELEEELEELQE 454

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     788 TVAKELQTLHNLRKLFVQDLATRVKKSAEIDSddtggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL 867
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQ-----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI 529

                          410
                   ....*....|....*..
gi 4758648     868 RATAERVKALESALKEA 884
Cdd:TIGR02168  530 SVDEGYEAAIEAALGGR 546
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 609-911 7.09e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 7.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  609 KQLESTQTESNK-------KMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQekvh 681
Cdd:COG1196 200 RQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---- 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  682 emekehLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKmmlEQERLRVEHEKLKATDQEK 761
Cdd:COG1196 276 ------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE---LEEELEELEEELEELEEEL 346

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  762 SRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTgGSAAQKQKISFLENNLEQ 841
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEE 425

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  842 LTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNM 911
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 495-886 7.72e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 7.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  495 LEELAVNYDQKSQEVEdKTKEYELLSDELNQKSATLASI-DAELQKLKEMTNHQKKRAAEMMASLLKDLAEIgiavgnnd 573
Cdd:COG1196 195 LGELERQLEPLERQAE-KAERYRELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAEL-------- 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  574 vkqpegtgmiDEEFTVARLYISKMKSEVKtmvkrckQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNV 653
Cdd:COG1196 266 ----------EAELEELRLELEELELELE-------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  654 EQKKRQLEESVDALSEELVQLRAQEkvhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDL 733
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  734 QDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKK 813
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  814 SAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVR-------------DNADLRCELPKLEKRLRATAERVKALESA 880
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavligveaayEAALEAALAAALQNIVVEDDEVAAAAIEY 565


                ....*.
gi 4758648  881 LKEAKE 886
Cdd:COG1196 566 LKAAKA 571
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 415-905 8.48e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 8.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  495 LEELAvnydqksQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIgiavgnndv 574
Cdd:COG1196 339 LEELE-------EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL--------- 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  575 KQPEGTgmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVE 654
Cdd:COG1196 403 EELEEA-------------EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  655 QKKRQLEESVDALSEELVQLRAQEKV-HEMEKEHLNKVQTANEVKQAVEQQ--IQSHRETHQKQISSLRDEVEAKAKLIT 731
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLlLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAALEAALAAALQ 549

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  732 DLQDQNQKMMLEQERLRVEHEKLKAT----DQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQ---------TLHN 798
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYvlgdtllgrTLVA 629

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  799 LRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADlrcELPKLEKRLRATAERVKALE 878
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE---RLAEEELELEEALLAEEEEE 706

                       490       500
                ....*....|....*....|....*..
gi 4758648  879 SALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAE 733
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
417-922 1.23e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.02  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   417 ERRKCEEEIAKL---YKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKE--EVKEV 491
Cdd:PRK03918 215 ELPELREELEKLekeVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEE 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   492 LQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKdLAEIGIAVGN 571
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   572 NDVKQPEGTGMIDEEFTVARLYISKMKSEV----KTMVKRCKQLESTQTESNKKMEENEKELAACQL---RISQHEAK-- 642
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIeeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrELTEEHRKel 453

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   643 IKSLTEYLQNVEQKKRQLEESVDALSEELVQLraqEKVHEMEKEHLNKVQTANEVKqAVEQQIQSHRethqkqisslRDE 722
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELREL---EKVLKKESELIKLKELAEQLK-ELEEKLKKYN----------LEE 519

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   723 VEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGL----EETVAKELQTLHN 798
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEP 599

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   799 LRKLFV---------QDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKV------------HKQLVRDNADLR 857
Cdd:PRK03918 600 FYNEYLelkdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelreeYLELSRELAGLR 679

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758648   858 CELPKLEKRLRATAERVKALESALKEAKENASR--DRKRYQQEVDRIKEAVRS-KNMARRGHSAQIAK 922
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREKAKKEleKLEKALERVEELREKVKKyKALLKERALSKVGE 747
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 594-907 1.65e-12

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: 71.64  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     594 ISKMKSEVKTMVKRCKQLESTQTESNKKME----ENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSE 669
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLErlrrEREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     670 ELVQLraQEKVHEMEKEHLNKVQTANEVKQAVEQ-------QIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMML 742
Cdd:TIGR02169  252 ELEKL--TEEISELEKRLEEIEQLLEELNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     743 EQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLhnlrklfVQDLATRVKKSAEIdsddt 822
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET-------RDELKDYREKLEKL----- 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     823 ggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASR---DRKRYQQEV 899
Cdd:TIGR02169  398 ------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaaDLSKYEQEL 471


                   ....*...
gi 4758648     900 DRIKEAVR 907
Cdd:TIGR02169  472 YDLKEEYD 479
PTZ00121 PTZ00121
MAEBL; Provisional
 416-913 1.80e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 72.10  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMlDQEELLASTRRDQDNMQAELNRLQAENDASK-EEVKEVlqa 494
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-AKKKADAAKKKAEEKKKADEAKKKAEEDKKKaDELKKA--- 1413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    495 lEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtNHQKKRAAEMMASLLKDLAEIGIAVGNNDV 574
Cdd:PTZ00121 1414 -AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    575 KQPEGTGMIDEEFTVARLyiSKMKSEVKTMVKRCKQLESTQTESNKKMEENEKelaACQLRISQHEAKIKSL--TEYLQN 652
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEA--KKKADEAKKAEEAKKADEAKKAEEAKKADEAKK---AEEKKKADELKKAEELkkAEEKKK 1565

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    653 VEQKKRQLEESVDAL--SEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHR----ETHQKQISSLRDEVEAK 726
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEE 1645

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    727 AKLITDLQ--DQNQKMMLEQERLRVEHEKLKA-----TDQEKSRKLHELTVMQDRREQARQDLKGLEETV--AKELQTLH 797
Cdd:PTZ00121 1646 KKKAEELKkaEEENKIKAAEEAKKAEEDKKKAeeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkAEELKKAE 1725

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    798 NLRKLFVQDL---ATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRlRATAERV 874
Cdd:PTZ00121 1726 EENKIKAEEAkkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIF 1804

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 4758648    875 KALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMAR 913
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-912 7.13e-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: 69.70  E-value: 7.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     412 NFTDAERRKCEEEIAK-------LYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDAS 484
Cdd:TIGR02168  270 EELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     485 KEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtnhQKKRAAEMMASLLKDLAE 564
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEE 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     565 IGIAVGNNDVKQPEGT-GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEaki 643
Cdd:TIGR02168  426 LLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE--- 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     644 kSLTEYLQNVEQKKRQLEESVDALSEelvQLRAQEK----VHEMEKEHLNK--VQTANEVKQAVE--------------- 702
Cdd:TIGR02168  503 -GFSEGVKALLKNQSGLSGILGVLSE---LISVDEGyeaaIEAALGGRLQAvvVENLNAAKKAIAflkqnelgrvtflpl 578

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     703 -----QQIQSHRETHQKQI----SSLRDEVEAKAKL-------------ITDLQDQNQKMMLEQERLRV----------- 749
Cdd:TIGR02168  579 dsikgTEIQGNDREILKNIegflGVAKDLVKFDPKLrkalsyllggvlvVDDLDNALELAKKLRPGYRIvtldgdlvrpg 658

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     750 -----EHEKLKATDQEKSRKLHELtvmqdrreqaRQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSddtgg 824
Cdd:TIGR02168  659 gvitgGSAKTNSSILERRREIEEL----------EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----- 723

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     825 saaQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN---ASRDRKRYQQEVDR 901
Cdd:TIGR02168  724 ---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKA 800

                          570
                   ....*....|.
gi 4758648     902 IKEAVRSKNMA 912
Cdd:TIGR02168  801 LREALDELRAE 811
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 624-909 9.13e-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: 69.32  E-value: 9.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     624 ENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQekVHEMEKEHLNKVQTANEVKQAVeQ 703
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERI-A 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     704 QIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELtvmQDRREQARQDLK 783
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL---NEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     784 GLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQkisflennLEQLTKVHKQLVRDNADLRCELPKL 863
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--------LEALLNERASLEEALALLRSELEEL 899

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 4758648     864 EKRLRATAERVKALESALKEAKENASRDRKRYQ---QEVDRIKEAVRSK 909
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEgleVRIDNLQERLSEE 948
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 379-900 2.02e-11

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: 68.21  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    379 QFDKEKANL---EAFTVDKDITLTNDKPAtaigvigNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLD 455
Cdd:pfam05483 126 QFENEKVSLkleEEIQENKDLIKENNATR-------HLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    456 QEELLASTRRDQDNMQAELN----RLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLA 531
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKedheKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    532 SIDAELQKLKEMTNHQKKRAAEMMASLLKDLA-----EIGIAVGNNDVKQ-PEGTGMIDEEFTVARLYISKMKSEVKTMV 605
Cdd:pfam05483 279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkalEEDLQIATKTICQlTEEKEAQMEELNKAKAAHSFVVTEFEATT 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    606 KRCKQLESTQtesNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNveqKKRQLEESVDALSEELVQLRAQEKVHEMEK 685
Cdd:pfam05483 359 CSLEELLRTE---QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN---KEVELEELKKILAEDEKLLDEKKQFEKIAE 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    686 EHLNKVQTANEVKQAVEQQI----------QSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEheklk 755
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIhdleiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE----- 507

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    756 ATDQEKSRKLHELTVMQDRREQAR--QDLKGLEETVAKELQTLHNLRKLFVQ---DLATRVKKSAEIDSDDTGGSAAQKQ 830
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERmlKQIENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648    831 KISFLENN-------LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVD 900
Cdd:pfam05483 588 QMKILENKcnnlkkqIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 416-748 4.13e-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: 67.40  E-value: 4.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEEllaSTRRdqdnMQAELNRLQAENDASKEEvkevlqaL 495
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGE----IEKEIEQLEQEEEKLKER-------L 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     496 EELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQK-KRAAEMMASLLKDLAEIGIAVgnNDV 574
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL--REI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     575 KQPEGTGMIDEEFtvARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAK-------IKSLT 647
Cdd:TIGR02169  818 EQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdlkkeRDELE 895

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     648 EYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANE---VKQAVEQQIQSHRETHQKQISSLR---- 720
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALEpvnm 975

                          330       340       350
                   ....*....|....*....|....*....|.
gi 4758648     721 ---DEVEAKAKLITDLQDQNQKMMLEQERLR 748
Cdd:TIGR02169  976 laiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-664 5.15e-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: 5.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKL---------------KTQMLDQEELLASTRR-------DQDNMQ 471
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeqlrvKEKIGELEAEIASLERsiaekerELEDAE 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     472 AELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLK---EMTNHQK 548
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     549 KRAAEMMASLLKDLAEIGIAVGNndvkqpegtgmIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKE 628
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELAD-----------LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 4758648     629 LAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESV 664
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
435-913 2.08e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.68  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   435 KDEEINQQSQLVEkLKTQMLDQEE-----LLASTRRDQDNMQAELNRLQAEndasKEEVKEVLQALEELAVNYDQKSQEV 509
Cdd:PRK02224 179 ERVLSDQRGSLDQ-LKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERREEL 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   510 EDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASL-LKDLAEIGIAVGNNDVKQPEGTgmIDEEFT 588
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAgLDDADAEAVEARREELEDRDEE--LRDRLE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   589 VARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALS 668
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   669 EELVQLRAQ-EKVHEMEKEHLNKVQTANEVKQAVEQQIQSHR--ETHQkqisSLRDEVEAKAklITDLQDQNQKMMLEQE 745
Cdd:PRK02224 412 DFLEELREErDELREREAELEATLRTARERVEEAEALLEAGKcpECGQ----PVEGSPHVET--IEEDRERVEELEAELE 485

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   746 RLRVEHEKLKAtDQEKSRKLHELTVMQDRREQARQDLKGL----EETVAKELQTLHNLRKLfVQDLAT--RVKKSAEIDS 819
Cdd:PRK02224 486 DLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELiaerRETIEEKRERAEELRER-AAELEAeaEEKREAAAEA 563

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   820 DDTGGSAAQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR-------------LRATAERVKALESA 880
Cdd:PRK02224 564 EEEAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRealaelnderrerLAEKRERKRELEAE 642

                        490       500       510
                 ....*....|....*....|....*....|....
gi 4758648   881 LKEAK-ENASRDRKRYQQEVDRIKEAVRSKNMAR 913
Cdd:PRK02224 643 FDEARiEEAREDKERAEEYLEQVEEKLDELREER 676
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
423-816 1.44e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.71  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  423 EEIAKLYKQLDDKDEEInqqsqlvEKLKTQMLDQEELlastRRDQDNMQAELNRLQAENDASKEEVK-EVLQALEELAVN 501
Cdd:COG4717 132 QELEALEAELAELPERL-------EELEERLEELREL----EEELEELEAELAELQEELEELLEQLSlATEEELQDLAEE 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  502 YDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEmtnHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL---EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  582 MIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLE 661
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  662 E-----SVDALSEELVQLRAQEKVHEMEK-----EHLNKVQTANEVKQAVEQQIQSHRETHQKQIsslrdEVEAKAKLIT 731
Cdd:COG4717 358 EleeelQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEE 432

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  732 DLQDQNQKMMLEQERLRVEHEKLKATDQEKSR--KLHELTVMQDRREQARQDLKGLEETVAK---ELQTLHNLRKLFVQD 806
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAAlklALELLEEAREEYREE 512

                       410
                ....*....|
gi 4758648  807 LATRVKKSAE 816
Cdd:COG4717 513 RLPPVLERAS 522
PTZ00121 PTZ00121
MAEBL; Provisional
 418-922 2.67e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    418 RRKCEEEIAKLYKQLDD--KDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRlQAENDASKEEVKEVlqal 495
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEKKKA---- 1292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    496 EELAVNYDQKSQEVEDKTKEYELLSDELNQKsATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVK 575
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    576 QPEGTGMIDEEftvarlyiSKMKSEVKtmvKRCKQLESTQTESNKKMEENEKELAAcqlRISQHEAKIKSltEYLQNVEQ 655
Cdd:PTZ00121 1372 KKEEAKKKADA--------AKKKAEEK---KKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKA--EEKKKADE 1435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    656 KKRQLEESVDAlsEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQ-----QIQSHRETHQKQISSLRDEVEAKAKlI 730
Cdd:PTZ00121 1436 AKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkadEAKKKAEEAKKKADEAKKAAEAKKK-A 1512

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    731 TDLQDQNQKMMLEQ----------ERLRVEHEKLKATDQEKSRKLHEL----TVMQDRREQARQDLKGLEETVAKELQTL 796
Cdd:PTZ00121 1513 DEAKKAEEAKKADEakkaeeakkaDEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    797 HNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCElpKLEKRLRATAERVKA 876
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKA 1670

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 4758648    877 LESALK-EAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAK 922
Cdd:PTZ00121 1671 EEDKKKaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 460-679 3.44e-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: 3.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  460 LASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQK 539
Cdd:COG4942  15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  540 LKEMTNHQKKRAAEMMASLLK--DLAEIGIAVGNNDVKQPEGTGMIDEEFTVARL-YISKMKSEVKTMVKRCKQLESTQT 616
Cdd:COG4942  95 LRAELEAQKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReQAEELRADLAELAALRAELEAERA 174

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758648  617 ESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEK 679
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 595-904 5.22e-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: 60.47  E-value: 5.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     595 SKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQL 674
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     675 raQEKVHEMEKEhLNKVQT--ANEVKQAVEQQIQSHRETHQKQISSLRD----------EVEAKAKLITDLQDQNQKMML 742
Cdd:TIGR02169  771 --EEDLHKLEEA-LNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREieqklnrltlEKEYLEKEIQELQEQRIDLKE 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     743 EQERLRVEHEKLKATDQEKSRKLHELtvmQDRREQARQDLKGLEETVAKELQTLHNLRKLfVQDLATRVKKSAEIDSDdt 822
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEEL---EAALRDLESRLGDLKKERDELEAQLRELERK-IEELEAQIEKKRKRLSE-- 921

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     823 ggsaaQKQKISFLENNLEQLTKVHKQLVRDNADLrCELPKLEKRLRATAERVKALES----ALKEAKENASRdRKRYQQE 898
Cdd:TIGR02169  922 -----LKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALEPvnmlAIQEYEEVLKR-LDELKEK 994


                   ....*.
gi 4758648     899 VDRIKE 904
Cdd:TIGR02169  995 RAKLEE 1000
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
414-883 8.05e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 8.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   414 TDAERRkceEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTrrdqdnmqAELNRLQAENDASKEEVKEVLQ 493
Cdd:PRK03918 142 ESDESR---EKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRT--------ENIEELIKEKEKELEEVLREIN 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   494 ALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASlLKDLAEIgiavgnnd 573
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-IEELEEK-------- 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   574 VKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKElaacqlrisqhEAKIKSLTEYLQNV 653
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKEL 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   654 EQKKRQLEESVDALsEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVE--QQIQSHRETHQKQISSLRDEVEAKAKLIT 731
Cdd:PRK03918 351 EKRLEELEERHELY-EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIE 429

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   732 DLQDQNQKMMLEQERLRVEHEK--LKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKElQTLHNLRKLFVQDLAT 809
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKEL 508

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758648   810 RvKKSAEIDSDDTggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRcELPKLEKRLRATAERVKALESALKE 883
Cdd:PRK03918 509 E-EKLKKYNLEEL------EKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAE 574
PTZ00121 PTZ00121
MAEBL; Provisional
 417-861 8.43e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 8.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    417 ERRKCEE-----EIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEellASTRRDQDNMQAELNRLQAENDASKEEVKEV 491
Cdd:PTZ00121 1442 EAKKADEakkkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    492 LQALEElavnydQKSQEVEDKTKEYELLSDELNQKSATLASIDaELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVgn 571
Cdd:PTZ00121 1519 EEAKKA------DEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-- 1589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    572 nDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMV----------KRCKQLESTQTESNKKMEENEKELAACQLRISQHEA 641
Cdd:PTZ00121 1590 -EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkkaeeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    642 KI---KSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISS 718
Cdd:PTZ00121 1669 KAeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    719 LRDEVEAKAKLITDLQDQNQKM-MLEQERLRVEHEKLKATDQEKSRKLHELT--------VMQDRREQAR---QDLKGLE 786
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAeEIRKEKEAVIEEELDEEDEKRRMEVDKKIkdifdnfaNIIEGGKEGNlviNDSKEME 1828

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648    787 ETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQL--TKVHKQLvrDNADLRCELP 861
Cdd:PTZ00121 1829 DSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIEKI--DKDDIEREIP 1903
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 415-542 1.55e-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: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTR--RDQDNMQAELNRLQAENDASKEEVKEVL 492
Cdd:COG1579  37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELM 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4758648  493 QALEELAVNYDQKSQEVEDKTKEYELLSDELNQKsatLASIDAELQKLKE 542
Cdd:COG1579 117 ERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEA 163
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 431-879 3.78e-08

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: 57.44  E-value: 3.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     431 QLDDKDEEINQQSQLVEKLKTQMldqeellastRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVE 510
Cdd:pfam15921   86 QVKDLQRRLNESNELHEKQKFYL----------RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     511 DKtkeyELLSDELNQKSATlasidaELQKLKEMTNHQKKRAAEMMaSLLKDLAEigiAVGNndvKQPEGTGMIDEEFTVA 590
Cdd:pfam15921  156 AA----KCLKEDMLEDSNT------QIEQLRKMMLSHEGVLQEIR-SILVDFEE---ASGK---KIYEHDSMSTMHFRSL 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     591 RLYISKMKSEVKTMVKRCK--------QLESTQTESNKKME---------------ENEKELAACQLRISQHEAKIKSLT 647
Cdd:pfam15921  219 GSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIElllqqhqdrieqlisEHEVEITGLTEKASSARSQANSIQ 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     648 EYLQNVEQKKR-----------QLEESVDALSEELVQLRA--QEKVHEMEKEhlnKVQTANEVKQAveqqiQSHRETHQK 714
Cdd:pfam15921  299 SQLEIIQEQARnqnsmymrqlsDLESTVSQLRSELREAKRmyEDKIEELEKQ---LVLANSELTEA-----RTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     715 QISSLRDEVEakaKLITDLQDQNQKMMLEQErlrvEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQ 794
Cdd:pfam15921  371 ESGNLDDQLQ---KLLADLHKREKELSLEKE----QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ 443

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     795 TLHNLRKLFVQDLATRVKKSAEIDSDdtggsaaqkqkisfLENNLEQLTKVHKQLV----------RDNADLRCELPKLE 864
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSSLTAQ--------------LESTKEMLRKVVEELTakkmtlesseRTVSDLTASLQEKE 509

                          490
                   ....*....|....*
gi 4758648     865 KRLRATAERVKALES 879
Cdd:pfam15921  510 RAIEATNAEITKLRS 524
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 640-905 4.30e-08

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: 57.37  E-value: 4.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     640 EAKIKSLTEYLQNVEQKKRQLEESVDALS------EELVQLRAQEKVHEME------KEHLNKVQTANEVKQAVEQQIQS 707
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELAllvlrlEELREELEELQEELKEAEEELEE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     708 HRE---THQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKG 784
Cdd:TIGR02168  258 LTAelqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     785 LEETVAKELQTLHNLRKLFVQDLATRVKKSAEidsddtggsaaQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLE 864
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEE-----------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 4758648     865 KRLRATAERVKALESALKEAKENASR-DRKRYQQEVDRIKEA 905
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEE 448
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 424-883 5.68e-08

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: 56.90  E-value: 5.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     424 EIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDaskeevkEVLQALEELAVNYD 503
Cdd:TIGR00618  297 AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI-------HIRDAHEVATSIRE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     504 QKSQEVEDKtkeyELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASllkdlaeigiavgnNDVKQPEGTGMI 583
Cdd:TIGR00618  370 ISCQQHTLT----QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF--------------RDLQGQLAHAKK 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     584 DEEFTVARLYISKMKSEVKTMVKrcKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEES 663
Cdd:TIGR00618  432 QQELQQRYAELCAAAITCTAQCE--KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     664 VDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQS---HRETHQKQISSLRDEVEAKAKLITDLQDQNQKM 740
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSerkQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     741 MLEQERLRVEHEKLKATDQEKSRKLHELTV---MQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDlatRVKKSAEI 817
Cdd:TIGR00618  590 QNITVRLQDLTEKLSEAEDMLACEQHALLRklqPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE---RVREHALS 666

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648     818 DSDDTGGSAAQKQ-KISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKE 883
Cdd:TIGR00618  667 IRVLPKELLASRQlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 612-904 1.12e-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: 55.90  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    612 ESTQTESNKKMEENEkeLAACQLRISQHEakiKSLTEylqnveqkkRQLEESVDALSEELVQLRAQEKVHEMEK----EH 687
Cdd:pfam17380 255 EYTVRYNGQTMTENE--FLNQLLHIVQHQ---KAVSE---------RQQQEKFEKMEQERLRQEKEEKAREVERrrklEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    688 LNKVQTANEVKQAV---EQQ---IQSHRETHQKQISSLRDEVE-----------AKAKLITDLQDQNQKmmlEQERLRVE 750
Cdd:pfam17380 321 AEKARQAEMDRQAAiyaEQErmaMERERELERIRQEERKRELErirqeeiameiSRMRELERLQMERQQ---KNERVRQE 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    751 HE---KLKATDQEKSRKLH----ELTVMQDRREQARQ-DLKGLEETVAKELQTL--------HNLRKLfVQDLATRVKKS 814
Cdd:pfam17380 398 LEaarKVKILEEERQRKIQqqkvEMEQIRAEQEEARQrEVRRLEEERAREMERVrleeqerqQQVERL-RQQEEERKRKK 476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    815 AEIDSDDTGGSAAQKQKISFLENNLEQltkvHKQLVRDNADLRCELPK-LEKRLRATAERVKALESALKEAKENASRDRK 893
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKeMEERQKAIYEEERRREAEEERRKQQEMEERR 552

                         330
                  ....*....|.
gi 4758648    894 RYQQEVDRIKE 904
Cdd:pfam17380 553 RIQEQMRKATE 563
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 618-819 1.13e-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: 55.16  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  618 SNKKMEENEKELAACQLRISQHEAKI-------KSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNK 690
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELaalkkeeKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  691 VQtaNEVKQAVEQQIQSHRETHQKQISSL---RDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHE 767
Cdd:COG4942  98 EL--EAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 4758648  768 LTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDS 819
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-904 1.60e-07

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: 55.46  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     495 LEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHqkKRAAEMMAS--------LLKDLAEIG 566
Cdd:TIGR02169  457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG--GRAVEEVLKasiqgvhgTVAQLGSVG 534

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     567 --------IAVGN---------------------------------NDVKQPE--------------------------- 578
Cdd:TIGR02169  535 eryataieVAAGNrlnnvvveddavakeaiellkrrkagratflplNKMRDERrdlsilsedgvigfavdlvefdpkyep 614

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     579 ------GTGMIDEEFTVARLYISKM-----------KSEVKT--------MVKRCKQLESTQTESNKKMEENEKELAACQ 633
Cdd:TIGR02169  615 afkyvfGDTLVVEDIEAARRLMGKYrmvtlegelfeKSGAMTggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQ 694

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     634 LRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQA-VEQQIQSHREth 712
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeLEARIEELEE-- 772

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     713 qkQISSLRDEVEA-KAKLITDLQDQNQKMMLEQERLRVEHEK-LKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVA 790
Cdd:TIGR02169  773 --DLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEArLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     791 KELQTLHNLrKLFVQDLATRVKKsaeidsddtggsaaqkqkisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKR---L 867
Cdd:TIGR02169  851 SIEKEIENL-NGKKEELEEELEE---------------------LEAALRDLESRLGDLKKERDELEAQLRELERKieeL 908

                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 4758648     868 RATAERVKALESALKEAKENASRDRKRYQQEVDRIKE 904
Cdd:TIGR02169  909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 628-796 1.92e-07

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: 53.00  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  628 ELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAveqQIQS 707
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG---NVRN 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  708 HREthqkqISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELtvmQDRREQARQDLKGLEE 787
Cdd:COG1579  88 NKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159


                ....*....
gi 4758648  788 TVAKELQTL 796
Cdd:COG1579 160 ELEAEREEL 168
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 420-867 2.83e-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: 54.64  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    420 KCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEV---LQALE 496
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    497 ELAVN---YDQKSQEVEDK-----------TKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLlkDL 562
Cdd:TIGR04523 201 LLLSNlkkKIQKNKSLESQiselkkqnnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--EQ 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    563 AEIGIAVGNNDVKQpegtgmideeftvarlyiskMKSEVKTMVKRCKQleSTQTESNKKMEENEKELAACQLRISQHEAK 642
Cdd:TIGR04523 279 NNKKIKELEKQLNQ--------------------LKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKI 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    643 IKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKE-HLNKVQTANEVKQAVEQQIQshretHQKQISSLRD 721
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQ-----NQEKLNQQKD 411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    722 EVeakaklITDLQDQNQKMMLEQERLRVEHEKLKAT----DQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLH 797
Cdd:TIGR04523 412 EQ------IKKLQQEKELLEKEIERLKETIIKNNSEikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    798 NLRKLFVQDlATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL 867
Cdd:TIGR04523 486 QKQKELKSK-EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 417-780 3.38e-07

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: 54.59  E-value: 3.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELlastrrdqdnmqaELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-------------KLQELKLKEQAKKALEYYQLKEKL 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     497 ELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQ 576
Cdd:pfam02463  220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     577 pegtgmidEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKsltEYLQNVEQK 656
Cdd:pfam02463  300 --------SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKL 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     657 KRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVE--AKAKLITDLQ 734
Cdd:pfam02463  369 EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEesIELKQGKLTE 448

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 4758648     735 DQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQ 780
Cdd:pfam02463  449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
418-907 3.70e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 3.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  418 RRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndasKEEVKEVLQALEE 497
Cdd:COG4717  48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEK 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  498 LavnydqksQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmMASLLKDLAEIgiavgnndvkqp 577
Cdd:COG4717 124 L--------LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-LAELQEELEEL------------ 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  578 egtgmideeftvARLYISKMKSEVKTMVKRCKQLEstqtesnKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKK 657
Cdd:COG4717 183 ------------LEQLSLATEEELQDLAEELEELQ-------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  658 RQLEESVDALSE-ELVQLRAQEKVHEMEKEHLNKVQTANevkQAVEQQIQSHRETHQKQISSLRDEVEAKAKLiTDLQDQ 736
Cdd:COG4717 244 RLKEARLLLLIAaALLALLGLGGSLLSLILTIAGVLFLV---LGLLALLFLLLAREKASLGKEAEELQALPAL-EELEEE 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  737 NQKMMLeqERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKglEETVAKELQTLhnLRKLFVQDLATRVKKSAE 816
Cdd:COG4717 320 ELEELL--AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL--LAEAGVEDEEELRAALEQ 393

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  817 IDSDDtggsaAQKQKISFLENNLEQLTKVHKQLVRDN---------ADLRCELPKLEKRLRATAERVKALESALKEAKEN 887
Cdd:COG4717 394 AEEYQ-----ELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEELEEELEELREELAELEAELEQLEED 468

                       490       500
                ....*....|....*....|..
gi 4758648  888 ASRDRKRYQQE--VDRIKEAVR 907
Cdd:COG4717 469 GELAELLQELEelKAELRELAE 490
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 418-905 3.83e-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: 54.41  E-value: 3.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     418 RRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQ-EELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA-- 494
Cdd:pfam01576  322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAkq 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     495 -LEELAVNYDQKSQEVEDKTKEYELLSDELNQKsatLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGiavgnnd 573
Cdd:pfam01576  402 dSEHKRKKLEGQLQELQARLSESERQRAELAEK---LSKLQSELESVSSLLNEAEGKNIK----LSKDVSSLE------- 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     574 vKQPEGTGMIDEEFTVARLYISKmksevktmvkRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNV 653
Cdd:pfam01576  468 -SQLQDTQELLQEETRQKLNLST----------RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     654 EQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANE-------VKQAVEQQIQSHRETHQKQISSL------- 719
Cdd:pfam01576  537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQqelddllVDLDHQRQLVSNLEKKQKKFDQMlaeekai 616

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     720 -------RDEVEAKAK-----------LITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQD 781
Cdd:pfam01576  617 saryaeeRDRAEAEAReketralslarALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEE 696

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     782 LKGLEETVAKELQTLHNLR-KLFVQDLATRVKKSAEIDSDDTGGSAAQKQ---KISFLENNLEQLTKVHKQLVRDNADLR 857
Cdd:pfam01576  697 MKTQLEELEDELQATEDAKlRLEVNMQALKAQFERDLQARDEQGEEKRRQlvkQVRELEAELEDERKQRAQAVAAKKKLE 776

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 4758648     858 CELPKLEKRLRATAervKALESALKEAKEnASRDRKRYQQEVDRIKEA 905
Cdd:pfam01576  777 LDLKELEAQIDAAN---KGREEAVKQLKK-LQAQMKDLQRELEEARAS 820
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 419-751 4.21e-07

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: 54.35  E-value: 4.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     419 RKCEEEIAKLYKQLDDKDeeinqqsQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEvlqaLEEL 498
Cdd:pfam15921  544 RNVQTECEALKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE----FKIL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     499 AVNYDQKSQEVEDKTKEYELLSDEL-NQKSATLASIDAELQKLKEMTNHQKKRAAEmmaslLKDLAEIGIAVGNNDVKQP 577
Cdd:pfam15921  613 KDKKDAKIRELEARVSDLELEKVKLvNAGSERLRAVKDIKQERDQLLNEVKTSRNE-----LNSLSEDYEVLKRNFRNKS 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     578 EGTGMIDEEFtvaRLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKK 657
Cdd:pfam15921  688 EEMETTTNKL---KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     658 RQLEESVDALSEELVQLrAQEKvhemekehlNKVQTANEVKQAVEQQIqshrethQKQISSLRDEVEAKAKLITDLQDQN 737
Cdd:pfam15921  765 HFLKEEKNKLSQELSTV-ATEK---------NKMAGELEVLRSQERRL-------KEKVANMEVALDKASLQFAECQDII 827

                          330
                   ....*....|....
gi 4758648     738 QKMMLEQERLRVEH 751
Cdd:pfam15921  828 QRQEQESVRLKLQH 841
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 602-900 4.50e-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: 53.98  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    602 KTMVKRCKQLESTQTESNKKMEENEKELAACQlrisqheAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVH 681
Cdd:pfam05557  51 QELQKRIRLLEKREAEAEEALREQAELNRLKK-------KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    682 EMEKEHLNK----VQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQ----------------KMM 741
Cdd:pfam05557 124 ELELQSTNSeleeLQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseivknskselaripELE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    742 LEQERLRVEHEKLKATDQEKS---RKLHELTVMQDRREQARQDLKGLE---ETVAKELQTLHNLRKLFVQDLATRVKKSA 815
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLllkEEVEDLKRKLEREEKYREEAATLElekEKLEQELQSWVKLAQDTGLNLRSPEDLSR 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    816 EIDSDDTgGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLrataERVKALESALKEAKENASRDRKRY 895
Cdd:pfam05557 284 RIEQLQQ-REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL----KRHKALVRRLQRRVLLLTKERDGY 358


                  ....*
gi 4758648    896 QQEVD 900
Cdd:pfam05557 359 RAILE 363
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 420-883 4.61e-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: 53.87  E-value: 4.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    420 KCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELa 499
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL- 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    500 vnydqkSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTnhqkkraaemmaSLLKDLAEIGIAVGNN-DVKQPE 578
Cdd:TIGR04523 179 ------EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE------------SQISELKKQNNQLKDNiEKKQQE 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    579 gtgmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKR 658
Cdd:TIGR04523 241 ---------------INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    659 QleESVDALSEELVQLraQEKVHEMEKEHLNKVQTANEVKQAVEqQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQ 738
Cdd:TIGR04523 306 Q--DWNKELKSELKNQ--EKKLEEIQNQISQNNKIISQLNEQIS-QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    739 KMMLEQERLRVEHEKLKAT----DQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNL------RKLFVQDLA 808
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKiqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLtnqdsvKELIIKNLD 460

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758648    809 TRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKE 883
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 416-912 5.29e-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: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLastrrdqDNMQAELNRLQAENDASKEEVKEVLqal 495
Cdd:pfam01576   68 ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-------DEEEAARQKLQLEKVTTEAKIKKLE--- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     496 EELAVNYDQKSQevedKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDlaeigiavGNNDVK 575
Cdd:pfam01576  138 EDILLLEDQNSK----LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE--------EKGRQE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     576 QPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQN--- 652
Cdd:pfam01576  206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESera 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     653 ----VEQKKRQLEESVDALSEELV----------QLRAQEkvhEMEKEHLNKvqTANEVKQAVEQQIQSHRETHQKQISS 718
Cdd:pfam01576  286 arnkAEKQRRDLGEELEALKTELEdtldttaaqqELRSKR---EQEVTELKK--ALEEETRSHEAQLQEMRQKHTQALEE 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     719 LRDEVE-----------AKAKLITDLQD-QNQKMMLEQERLRVEHEKLKATDQeksrkLHELTVMQDRREQARQDLkglE 786
Cdd:pfam01576  361 LTEQLEqakrnkanlekAKQALESENAElQAELRTLQQAKQDSEHKRKKLEGQ-----LQELQARLSESERQRAEL---A 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     787 ETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVhKQLVRDNADLRCELPKLEKR 866
Cdd:pfam01576  433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-RQLEDERNSLQEQLEEEEEA 511

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648     867 LRATAERVKALESALKEAK----------ENASRDRKRYQQEVDRIKEAVRSKNMA 912
Cdd:pfam01576  512 KRNVERQLSTLQAQLSDMKkkleedagtlEALEEGKKRLQRELEALTQQLEEKAAA 567
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 478-707 8.88e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.14  E-value: 8.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  478 QAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMAS 557
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  558 LLK---DLAEIGIAVGNNDVkqpegTGMIDEEFTVARLyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQL 634
Cdd:COG3883  95 LYRsggSVSYLDVLLGSESF-----SDFLDRLSALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758648  635 RISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQS 707
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
6-268 9.16e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 52.82  E-value: 9.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    6 ECNIKVMCRFRPLNESEVNRGD--KYIAKFQGEDTVVIASKPYAFDR-----VFQSSTSQEQVYNDCAKKIVKDVLEGYN 78
Cdd:COG5059 304 NCNTRVICTISPSSNSFEETINtlKFASRAKSIKNKIQVNSSSDSSReieeiKFDLSEDRSEIEILVFREQSQLSQSSLS 383

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   79 GtIFAYGQTSSGKTHTMEGKlhdpeGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYF-EIYLDKIRDLL-DVSKTNLSVH 156
Cdd:COG5059 384 G-IFAYMQSLKKETETLKSR-----IDLIMKSIISGTFERKKLLKEEGWKYKSTLQFlRIEIDRLLLLReEELSKKKTKI 457

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  157 EDKNRVPYVKGCTERFvcSPDEVMDTIDEGK--SNRHVAVTNMNEHSSRSHSIFlINVKQENTQTEQKLSgkLYLVDLAG 234
Cdd:COG5059 458 HKLNKLRHDLSSLLSS--IPEETSDRVESEKasKLRSSASTKLNLRSSRSHSKF-RDHLNGSNSSTKELS--LNQVDLAG 532

                       250       260       270
                ....*....|....*....|....*....|....
gi 4758648  235 SEKVSKTgAEGAVLDEAKNINKSLSALGNVISAL 268
Cdd:COG5059 533 SERKVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 423-768 1.00e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    423 EEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNY 502
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    503 DQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRaaemMASLLKDLAEIGIAVGNNDVKQPEgtgm 582
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRES---- 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    583 IDEEFTVARLYISKMKSEVKTMVKRCKQLES---TQTESNKKMEENEKELaacqlrisqhEAKIKSLTEYLQNVEQKKRQ 659
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKelkKLNEEKKELEEKVKDL----------TKKISSLKEKIEKLESEKKE 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    660 LEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRE------THQKQISSLRDEVEAKAKLITDL 733
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLIKEIEEKEKKISSL 615

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 4758648    734 QDQNQKMMLEQERLrvehEKLKATDQEKSRKLHEL 768
Cdd:TIGR04523 616 EKELEKAKKENEKL----SSIIKNIKSKKNKLKQE 646
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
409-905 1.70e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   409 VIGNFTDAERrkCEEEIAKLYKQLDDKdEEINQQSQLVEKLKTQMLDQEELLASTRRDQDnmQAELNRLQAENDASKEEV 488
Cdd:COG4913  230 LVEHFDDLER--AHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAEL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   489 KEVLQALEELAVNYDQKSQEVEdktkeyELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmmasLLKDLAEIGIA 568
Cdd:COG4913  305 ARLEAELERLEARLDALREELD------ELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR----LEALLAALGLP 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   569 VGNNDvkqpegtgmidEEFTVARlyiskmkSEVKTMVKRCKQLESTQTEsnkKMEENEKELAACQLRISQHEAKIKSLTE 648
Cdd:COG4913  375 LPASA-----------EEFAALR-------AEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLER 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   649 ----YLQNVEQKKRQLEESVdALSE-------ELVQLRAQEKVHEM---------------EKEHLNKVQTA-NEVKQAV 701
Cdd:COG4913  434 rksnIPARLLALRDALAEAL-GLDEaelpfvgELIEVRPEEERWRGaiervlggfaltllvPPEHYAAALRWvNRLHLRG 512

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   702 EQQIQSHRETHQKQIS------SLRDEVEAKAKLITD-LQDQnqkMMLEQERLRVEHEK-LKATDQ--------EKSRKL 765
Cdd:COG4913  513 RLVYERVRTGLPDPERprldpdSLAGKLDFKPHPFRAwLEAE---LGRRFDYVCVDSPEeLRRHPRaitragqvKGNGTR 589

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   766 HEltvMQDRR----------------EQARQDLKGLEETVA---KELQTLHNLRKLfVQDLATRVKKSAEIDSDDTGGSA 826
Cdd:COG4913  590 HE---KDDRRrirsryvlgfdnraklAALEAELAELEEELAeaeERLEALEAELDA-LQERREALQRLAEYSWDEIDVAS 665

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758648   827 AQKQkisflennLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:COG4913  666 AERE--------IAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 414-564 1.71e-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: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAE------------- 480
Cdd:COG4942  39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellralyrlgr 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  481 --------NDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAA 552
Cdd:COG4942 119 qpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198

                       170
                ....*....|..
gi 4758648  553 EMMASLLKDLAE 564
Cdd:COG4942 199 KLLARLEKELAE 210
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
595-885 2.18e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   595 SKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEEsvdaLSEELVQL 674
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   675 RAQEKVHEMEKEHLnkvqtanevkQAVEQQIQSHRETHQKQISSLRD------EVEAKAKLITDLQDQNQKMMLEQERLR 748
Cdd:PRK03918 244 EKELESLEGSKRKL----------EEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIE 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   749 VEHEKLKATDQEKSRKLHELTVMQDRREQarqdLKGLEETVAKELQTLHNLRKLFvqDLATRVKKSAEIDSDDTGGSAAQ 828
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELY--EEAKAKKEELERLKKRLTGLTPE 387

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648   829 KqkisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLratAERVKALEsALKEAK 885
Cdd:PRK03918 388 K-----LEKELEELEKAKEEIEEEISKITARIGELKKEI---KELKKAIE-ELKKAK 435
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 448-755 2.40e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 51.38  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   448 KLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQaleelavNYDQKSQEVEDKTKEYELLSDELNQKs 527
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-------LYRELRKSLLANRFSFGPALDELEKQ- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   528 atLASIDAELQKLKEMT---NHQKkrAAEMMASLLKDLAEIGIAVgnNDVKQpegtgMIDEEFTVARLYISKMKSEVKTM 604
Cdd:PRK04778 174 --LENLEEEFSQFVELTesgDYVE--AREILDQLEEELAALEQIM--EEIPE-----LLKELQTELPDQLQELKAGYREL 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   605 VKRC-----KQLESTQTESNKKMEENEKELAACQL-----RISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQL 674
Cdd:PRK04778 243 VEEGyhldhLDIEKEIQDLKEQIDENLALLEELDLdeaeeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHA 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   675 RAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKL 754
Cdd:PRK04778 323 KEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKL 402


                 .
gi 4758648   755 K 755
Cdd:PRK04778 403 S 403
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 416-668 2.56e-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: 50.92  E-value: 2.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQAL 495
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  496 EELAVNYDQKSQevedktkeYELLSDELNQKSATLASIDAELqkLKEMTNHQKKRAAEMMASlLKDLAEigiavgnndvk 575
Cdd:COG4942 107 AELLRALYRLGR--------QPPLALLLSPEDFLDAVRRLQY--LKYLAPARREQAEELRAD-LAELAA----------- 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  576 qpegtgmIDEEFTVARLYISKMKSEVKtmvKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQ 655
Cdd:COG4942 165 -------LRAELEAERAELEALLAELE---EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234

                       250
                ....*....|...
gi 4758648  656 KKRQLEESVDALS 668
Cdd:COG4942 235 EAAAAAERTPAAG 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 612-833 3.10e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 3.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  612 ESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEME-KEHLNK 690
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  691 VQTANEVKQAVEQQIQShrethqKQISSLRDEVEAkaklITDLQDQNQKMMLEQERLRvehEKLKATDQEKSRKLHELTV 770
Cdd:COG3883  95 LYRSGGSVSYLDVLLGS------ESFSDFLDRLSA----LSKIADADADLLEELKADK---AELEAKKAELEAKLAELEA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758648  771 MQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKIS 833
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 356-886 4.27e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    356 NTIQWLENELNRWRNgetvpIDEQFDKEKANLEaftvdkditltndkpataigvignftdAERRKCEEEIAKLYKQLDDK 435
Cdd:TIGR04523 145 TEIKKKEKELEKLNN-----KYNDLKKQKEELE---------------------------NELNLLEKEKLNIQKNIDKI 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    436 DEEINQQSQLVEKLKTQMLDQEELLAST---RRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDK 512
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQIselKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    513 TKEYELLSDELNQKSATLASIDAELQKLKemtnhqKKRAAEMMASLLKDLAEigiavgnndvkqpegtgmIDEEFTVARL 592
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLN------NQKEQDWNKELKSELKN------------------QEKKLEEIQN 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    593 YISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEEsvdalseelv 672
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES---------- 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    673 QLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDL----QDQNQKMMLEQERLR 748
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntrESLETQLKVLSRSIN 478

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    749 VEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQ 828
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648    829 --------KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKE 886
Cdd:TIGR04523 559 lekeidekNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 610-904 4.39e-06

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: 50.74  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     610 QLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEelvqLRAQEKVHEMEKEHLN 689
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE----LRAQEAVLEETQERIN 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     690 K-------VQTANEVKQaVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKS 762
Cdd:TIGR00618  288 RarkaaplAAHIKAVTQ-IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     763 RKLHeltvmQDRREQARQDLKGLEEtvakELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQL 842
Cdd:TIGR00618  367 IREI-----SCQQHTLTQHIHTLQQ----QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758648     843 TKVHKQLVRDNADLRCElpKLEKR-LRATAERVKALESALKEaKENASRDRKRYQQEVDRIKE 904
Cdd:TIGR00618  438 RYAELCAAAITCTAQCE--KLEKIhLQESAQSLKEREQQLQT-KEQIHLQETRKKAVVLARLL 497
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
598-892 4.47e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   598 KSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQlRISQH---EAKIKSLTEYLQNVEQKKRQLEES---VDALSEEL 671
Cdd:COG4913  616 EAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYswdEIDVASAEREIAELEAELERLDASsddLAALEEQL 694

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   672 VQLRAQEKVHEMEKEHLNKVQTanevkqaveqQIQSHRETHQKQISSLRDEVEAKAKLITdlqdqnqkmmlEQERLRVEh 751
Cdd:COG4913  695 EELEAELEELEEELDELKGEIG----------RLEKELEQAEEELDELQDRLEAAEDLAR-----------LELRALLE- 752

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   752 EKLKATDQEKSRklheltvmQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLatrvkKSAEIDSDDTGGSAAQKQK 831
Cdd:COG4913  753 ERFAAALGDAVE--------RELRENLEERIDALRARLNRAEEELERAMRAFNREW-----PAETADLDADLESLPEYLA 819

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648   832 IsflennleqltkvHKQLVRDNadlrceLPKLEKRLR-----ATAERVKALESALKEAKENAsRDR 892
Cdd:COG4913  820 L-------------LDRLEEDG------LPEYEERFKellneNSIEFVADLLSKLRRAIREI-KER 865
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 422-921 7.28e-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: 50.12  E-value: 7.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     422 EEEIAKLYKQLDDKDEEINQQ-----SQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAEndaSKEEVKEVLQALE 496
Cdd:pfam15921  244 EDQLEALKSESQNKIELLLQQhqdriEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLS 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     497 ELAVNYDQKSQEVEDKTKEYEllsDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQ 576
Cdd:pfam15921  321 DLESTVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     577 PEGTGMIDEEfTVARLYISKMKSEVKTmvkrcKQLESTQTESNKKMEENEkelaaCQLRISQHEAKIKSLTEYLQNVEQK 656
Cdd:pfam15921  398 EQNKRLWDRD-TGNSITIDHLRRELDD-----RNMEVQRLEALLKAMKSE-----CQGQMERQMAAIQGKNESLEKVSSL 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     657 KRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKqavEQQIqshrETHQKQISSLRDEVEAKAKLITDLQDQ 736
Cdd:pfam15921  467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK---ERAI----EATNAEITKLRSRVDLKLQELQHLKNE 539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     737 NQKMmleqERLRVEHEKLKATDQEKSRKLHEL-----TVMQDRREQARQdlKGLEETVAKELQTLHNLRKLFVQDLAT-R 810
Cdd:pfam15921  540 GDHL----RNVQTECEALKLQMAEKDKVIEILrqqieNMTQLVGQHGRT--AGAMQVEKAQLEKEINDRRLELQEFKIlK 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     811 VKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKV------HKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEA 884
Cdd:pfam15921  614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdikqeRDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT 693

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 4758648     885 KENASRDRKRYQQEVDRIKEAVRSKNMArRGHSAQIA 921
Cdd:pfam15921  694 TNKLKMQLKSAQSELEQTRNTLKSMEGS-DGHAMKVA 729
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 676-913 7.37e-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: 49.38  E-value: 7.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  676 AQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLK 755
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  756 ATDQEKSRKLHE-LTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLfVQDLATRVKKSAEIDSDDTGGSAAQKQKISF 834
Cdd:COG4942  97 AELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERAE 175

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758648  835 LENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMAR 913
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
415-904 1.00e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   415 DAERRKCEEEIAKLYKQLDDKDEEINQQS-QLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQ 493
Cdd:COG4913  308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   494 ALEELAVNYDQKSQEVEDktkEYELLSDELNQKSATLASIDAELQKLKemtnHQKKRAAEMMASLLKDLAEigiAVGNN- 572
Cdd:COG4913  388 EAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLE----RRKSNIPARLLALRDALAE---ALGLDe 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   573 ----------DVKQPE--------------GTGMI--DEEFTVARLYISKMK-------SEVKTMVKRCKQLEST----- 614
Cdd:COG4913  458 aelpfvgeliEVRPEEerwrgaiervlggfALTLLvpPEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDpdsla 537

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   615 ---QTESNK-----KME----------ENEKEL--------AACQLRIS----QHEAKIKSLTEYL--QNVEQKKRQLEE 662
Cdd:COG4913  538 gklDFKPHPfrawlEAElgrrfdyvcvDSPEELrrhpraitRAGQVKGNgtrhEKDDRRRIRSRYVlgFDNRAKLAALEA 617

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   663 SVDALSEELVQLRAQEKVHEMEKEHLNKVQTAnevkqavEQQIQSHREThQKQISSLRDEVEAKAKLITDLQDQNQKMML 742
Cdd:COG4913  618 ELAELEEELAEAEERLEALEAELDALQERREA-------LQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDDLAA 689

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   743 EQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVA-----KELQTLHNLRKLFVQDLATRV--KKSA 815
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaedlARLELRALLEERFAAALGDAVerELRE 769

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   816 EIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRD-NADLRcELPKLEKRLRA-TAERVKALESALKEAKENASRDRK 893
Cdd:COG4913  770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADlDADLE-SLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFV 848

                        570
                 ....*....|....*.
gi 4758648   894 -----RYQQEVDRIKE 904
Cdd:COG4913  849 adllsKLRRAIREIKE 864
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 417-765 1.21e-05

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: 49.58  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam02463  189 IIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     497 ELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIgiavgnndvkq 576
Cdd:pfam02463  269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI----------- 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     577 pegtgmideeftvarLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEylQNVEQK 656
Cdd:pfam02463  338 ---------------EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--EELELK 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     657 KRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQ 736
Cdd:pfam02463  401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480

                          330       340
                   ....*....|....*....|....*....
gi 4758648     737 NQKMMLEQERLRVEHEKLKATDQEKSRKL 765
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQKESKARSGL 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
692-921 1.27e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   692 QTANEVKQAVEQqIQSHRETHQ------KQISSLRDEVEAKAKLITDLQDQNQkmmLEQERLRVEHEKLKATDQEKSRKL 765
Cdd:COG4913  222 DTFEAADALVEH-FDDLERAHEaledarEQIELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   766 HELTVMQDRREQARQDLKGLEETVAKELQTLHNLRklfvqdlatrvkksaeidsDDTGGsaaqkQKISFLENNLEQLTKV 845
Cdd:COG4913  298 EELRAELARLEAELERLEARLDALREELDELEAQI-------------------RGNGG-----DRLEQLEREIERLERE 353

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648   846 HKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIA 921
Cdd:COG4913  354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
mukB PRK04863
chromosome partition protein MukB;
437-726 1.30e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.19  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    437 EEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEEL---AVNYDQKSQEVEdKT 513
Cdd:PRK04863  348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQqtrAIQYQQAVQALE-RA 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    514 KEYELLSD-ELNQKSATLASIDAELQKLKEMTNH--QKKRAAEM--------MASLLKDLAEIGIAVGNNDVKQPEGTGm 582
Cdd:PRK04863  427 KQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSleQKLSVAQAahsqfeqaYQLVRKIAGEVSRSEAWDVARELLRRL- 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    583 IDEEFTVARLyiSKMKSEVKTMVKRCKQ---LESTQTESNKK---MEENEKELAACQlriSQHEAKIKSLTEYLQNVEQK 656
Cdd:PRK04863  506 REQRHLAEQL--QQLRMRLSELEQRLRQqqrAERLLAEFCKRlgkNLDDEDELEQLQ---EELEARLESLSESVSEARER 580

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758648    657 KRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQT----ANEVKQAVEQQIQSHREtHQKQISSLRDEVEAK 726
Cdd:PRK04863  581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeEFEDSQDVTEYMQQLLE-RERELTVERDELAAR 653
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 417-799 1.71e-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: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASK------EEVKE 490
Cdd:TIGR00618  470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAqletseEDVYH 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     491 VLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEigiAVG 570
Cdd:TIGR00618  550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP---EQD 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     571 NNDVKQPEGT---GMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNK---KMEENEKE--------LAACQLRI 636
Cdd:TIGR00618  627 LQDVRLHLQQcsqELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQlalQKMQSEKEqltywkemLAQCQTLL 706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     637 SQHEAKIKSLTEYLQNVEQ----KKRQLEESVDALSEELVQLRAQ--EKVHEMEKEHLNKVQ--TANEVKQAVEQQIQSH 708
Cdd:TIGR00618  707 RELETHIEEYDREFNEIENasssLGSDLAAREDALNQSLKELMHQarTVLKARTEAHFNNNEevTAALQTGAELSHLAAE 786

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     709 RETHQKQISSLRDEV-EAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEE 787
Cdd:TIGR00618  787 IQFFNRLREEDTHLLkTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866

                          410
                   ....*....|..
gi 4758648     788 TVAKELQTLHNL 799
Cdd:TIGR00618  867 EQAKIIQLSDKL 878
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 628-914 1.84e-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: 48.14  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    628 ELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEkehLNKVQTANEVKQAVEQQIQS 707
Cdd:pfam19220  42 ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAA---LREAEAAKEELRIELRDKTA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    708 HRETHQKQissLRDEVEakaklitdlqdQNQKMMLEQERLRvehEKLKATDQEKSRKLHELTvmqdrreQARQDLKGLEE 787
Cdd:pfam19220 119 QAEALERQ---LAAETE-----------QNRALEEENKALR---EEAQAAEKALQRAEGELA-------TARERLALLEQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    788 tvakELQTLHNLRKLFVQDLATRVKKSAEIDSDdtggSAAQKQKISFLENNLEQLTKVHKQLVR----DNADLRCELPKL 863
Cdd:pfam19220 175 ----ENRRLQALSEEQAAELAELTRRLAELETQ----LDATRARLRALEGQLAAEQAERERAEAqleeAVEAHRAERASL 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4758648    864 EKRLRATAERVKALESALKEAKeNASRDRKRYQQEVDR-IKEAVRSKNMARR 914
Cdd:pfam19220 247 RMKLEALTARAAATEQLLAEAR-NQLRDRDEAIRAAERrLKEASIERDTLER 297
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 609-922 1.85e-05

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: 48.35  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    609 KQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEME-KEH 687
Cdd:pfam07888  55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARiREL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    688 LNKVQTANEVKQAVEQQIQSHREThQKQISSLRDEVEAKAKlitDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHE 767
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKER-AKKAGAQRKEEEAERK---QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    768 LtvmQDRREQARQDLKGLEETVAKELQTLHNLRKLfvQDLATRVKKSAEIDSDDTGGSAAQK-QKISFLENNLEQLTKVH 846
Cdd:pfam07888 211 L---QDTITTLTQKLTTAHRKEAENEALLEELRSL--QERLNASERKVEGLGEELSSMAAQRdRTQAELHQARLQAAQLT 285

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648    847 KQLVRDNADLRcelpklEKRLRATAERVKALESALKEakenasRDR-KRYQQEVDRIKEAVRSKNMARRGHSAQIAK 922
Cdd:pfam07888 286 LQLADASLALR------EGRARWAQERETLQQSAEAD------KDRiEKLSAELQRLEERLQEERMEREKLEVELGR 350
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 626-916 1.93e-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: 48.80  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   626 EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLR------AQEKVHEMEKEHLNKVQTANEVKQ 699
Cdd:COG3096  835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANlladetLADRLEELREELDAAQEAQAFIQQ 914

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   700 ------AVEQQIQSHRETHQK---------QISSLRDEVEAKAKLITDL---------QDQNQkmMLEQ-----ERLRve 750
Cdd:COG3096  915 hgkalaQLEPLVAVLQSDPEQfeqlqadylQAKEQQRRLKQQIFALSEVvqrrphfsyEDAVG--LLGEnsdlnEKLR-- 990

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   751 hEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFvQDLATRVKKSAEidsddtggsAAQKQ 830
Cdd:COG3096  991 -ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL-EELGVQADAEAE---------ERARI 1059

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   831 KISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRyqqevdrikeaVRSKN 910
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRL-----------ARDND 1128


                 ....*.
gi 4758648   911 MARRGH 916
Cdd:COG3096 1129 VERRLH 1134
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 430-755 2.38e-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: 47.93  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    430 KQLDDKDEEINQQSQLVEKL-----KTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQ 504
Cdd:pfam06160  60 KSLPDIEELLFEAEELNDKYrfkkaKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    505 KS--------------QEVEDKTKEYELLSDELNQKSA--TLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGia 568
Cdd:pfam06160 140 NRfsygpaidelekqlAEIEEEFSQFEELTESGDYLEAreVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELK-- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    569 vgnNDVKQpegtgMIDEEFTVARLYISKMKSEVKTMVKRC-KQLESTQTEsnkKMEENEKELaacqlrisqhEAKIKSLT 647
Cdd:pfam06160 218 ---EGYRE-----MEEEGYALEHLNVDKEIQQLEEQLEENlALLENLELD---EAEEALEEI----------EERIDQLY 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    648 EYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKA 727
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKE 356

                         330       340
                  ....*....|....*....|....*...
gi 4758648    728 KLITDLQDQNQKMMLEQERLRVEHEKLK 755
Cdd:pfam06160 357 VAYSELQEELEEILEQLEEIEEEQEEFK 384
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 415-893 2.42e-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: 48.50  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     415 DAERRKCEEEIAKLykqldDKDEEINQQSQLVEKLKTQMLDqeelLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQA 494
Cdd:TIGR00606  477 DQELRKAERELSKA-----EKNSLTETLKKEVKSLQNEKAD----LDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     495 LEELAVNYDQKSQEVEDK----------TKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAE 564
Cdd:TIGR00606  548 DEQIRKIKSRHSDELTSLlgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     565 IGIAVGNNDV------------KQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNK------------ 620
Cdd:TIGR00606  628 LFDVCGSQDEesdlerlkeeieKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEfisdlqsklrla 707

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     621 --KMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVK 698
Cdd:TIGR00606  708 pdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVC 787

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     699 Q---AVEQQIQSHRETHQKQISSLRDEVEAkAKLITDLQDQNQKMMLEQERLRVEHEKLkatdqEKSRKLheltvMQDRR 775
Cdd:TIGR00606  788 LtdvTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQEKQHELDTVVSKI-----ELNRKL-----IQDQQ 856

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     776 EQARQDLKGLEETVAKELQTLHNLRKlfVQDLATR-VKKSAEIDSDDTGGSAAqKQKISFLENNLEQLTKVHKQLVR--- 851
Cdd:TIGR00606  857 EQIQHLKSKTNELKSEKLQIGTNLQR--RQQFEEQlVELSTEVQSLIREIKDA-KEQDSPLETFLEKDQQEKEELISske 933

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 4758648     852 -DNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRK 893
Cdd:TIGR00606  934 tSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE 976
46 PHA02562
endonuclease subunit; Provisional
 485-773 2.49e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 48.09  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   485 KEEVKEVLQALEELavnyDQKSQEVEDKTKEYELLSDELNQKSatlasiDAELQKLKEM--TNHQKKRAAEMMASLLKD- 561
Cdd:PHA02562 173 KDKIRELNQQIQTL----DMKIDHIQQQIKTYNKNIEEQRKKN------GENIARKQNKydELVEEAKTIKAEIEELTDe 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   562 LAEIgiavgnndVKQPEGTgmiDEEFTVARLYISKMKSEVKTmvkrCKQLEstqtesnkKMEENEKELAACQLRISQHEA 641
Cdd:PHA02562 243 LLNL--------VMDIEDP---SAALNKLNTAAAKIKSKIEQ----FQKVI--------KMYEKGGVCPTCTQQISEGPD 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   642 KIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKvhemekehlnkvqTANEVKQAVeqqiqshrETHQKQISSLRD 721
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK-------------KLLELKNKI--------STNKQSLITLVD 358

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4758648   722 EVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQD 773
Cdd:PHA02562 359 KAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTD 410
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 378-767 3.02e-05

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: 47.64  E-value: 3.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  378 EQFDKEKANLEAFTV-DKDITLTNDKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQ 456
Cdd:COG5185 183 GLTLGLLKGISELKKaEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQN 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  457 EELLASTRRDQDNMQAELnrlqaeNDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQK-SATLASIDA 535
Cdd:COG5185 263 TDLRLEKLGENAESSKRL------NENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQElEESKRETET 336

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  536 ELQKLKEMTNHQKKRAAEMMASLLKDLAEIgiaVGNNDVKQPEGTgmideeftvarlyISKMKSEVKTMVKRCKQLESTQ 615
Cdd:COG5185 337 GIQNLTAEIEQGQESLTENLEAIKEEIENI---VGEVELSKSSEE-------------LDSFKDTIESTKESLDEIPQNQ 400

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  616 TESNKKMEEN-EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDAlSEELVQLRAQEKVHEMEKEHLNKVQTA 694
Cdd:COG5185 401 RGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNK-VMREADEESQSRLEEAYDEINRSVRSK 479

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758648  695 NEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHE 767
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQ 552
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 417-900 3.91e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.86  E-value: 3.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     417 ERRKCEE----EIAKLYKQLD----DKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEV 488
Cdd:pfam01576  194 ERLKKEEkgrqELEKAKRKLEgestDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     489 KEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASiDAELQKLKEMTNHQKKRAAE----MMASLLKDLAE 564
Cdd:pfam01576  274 SELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAA-QQELRSKREQEVTELKKALEeetrSHEAQLQEMRQ 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     565 IGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVK-----------RCKQLESTQTESNKKMEENEKELAACQ 633
Cdd:pfam01576  353 KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakqdsehKRKKLEGQLQELQARLSESERQRAELA 432

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     634 LRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALS------EELVQLRAQEK------VHEMEKEH---LNKVQTANEVK 698
Cdd:pfam01576  433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLEsqlqdtQELLQEETRQKlnlstrLRQLEDERnslQEQLEEEEEAK 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     699 QAVEQQIQshreTHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRV-------EHEKLKATDQEKSRKLHELTVM 771
Cdd:pfam01576  513 RNVERQLS----TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYDKLEKTKNRLQQELDDLLVD 588

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     772 QDRReqaRQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTggsaaqkqKISFLENNLEQLTKVHKQLVR 851
Cdd:pfam01576  589 LDHQ---RQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET--------RALSLARALEEALEAKEELER 657

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 4758648     852 DNADLRCELPKLEKRLRATAERVKALESAlKEAKENASRDRKRYQQEVD 900
Cdd:pfam01576  658 TNKQLRAEMEDLVSSKDDVGKNVHELERS-KRALEQQVEEMKTQLEELE 705
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 422-939 4.66e-05

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: 47.44  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    422 EEEIAKLYKQLDDKDEEINQQSQLVEKLK--------------TQMLDQEELLAST---RRDQDNMQAELNRLQAENDA- 483
Cdd:pfam07111 196 QKEAELLRKQLSKTQEELEAQVTLVESLRkyvgeqvppevhsqTWELERQELLDTMqhlQEDRADLQATVELLQVRVQSl 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    484 ------SKEEVKEVLQALEELAVNYDQKSQEVEDKTKE------YELLSDELnQKSATLASIDAELQKLKEMTNHQKKRA 551
Cdd:pfam07111 276 thmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREkvfalmVQLKAQDL-EHRDSVKQLRGQVAELQEQVTSQSQEQ 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    552 AEMMASLLKDLAEIgiavgnndvkqpegtgmideeftvarlyiskmksEVKTMVKRCKQLESTQTESNKKMEENEKELAA 631
Cdd:pfam07111 355 AILQRALQDKAAEV----------------------------------EVERMSAKGLQMELSRAQEARRRQQQQTASAE 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    632 CQLRISQheAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQlrAQEKVHEMEKEHLNKVQTANEVKQA-----VEQQIQ 706
Cdd:pfam07111 401 EQLKFVV--NAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY--AVRKVHTIKGLMARKVALAQLRQEScppppPAPPVD 476

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    707 SHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQ---ERLRVeHEKLKATDQEKSRKLHELTVMQDRREQARQDLK 783
Cdd:pfam07111 477 ADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQgeaERQQL-SEVAQQLEQELQRAQESLASVGQQLEVARQGQQ 555

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    784 GLEETVAKELQTLHNLRKLFVQDLatrvkksaeidsddtggsaaqKQKISFLENNL-EQLTKVHKQL---VRDNADLRCE 859
Cdd:pfam07111 556 ESTEEAASLRQELTQQQEIYGQAL---------------------QEKVAEVETRLrEQLSDTKRRLneaRREQAKAVVS 614

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    860 LPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKE----AVRSKNMARRGHSAQI---------AKPIRP 926
Cdd:pfam07111 615 LRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLLSRYKQQRLlavlpsgldKKSVVS 694

                         570
                  ....*....|...
gi 4758648    927 GQHPAASPTHPSA 939
Cdd:pfam07111 695 SPRPECSASAPIP 707
COG5022 COG5022
Myosin heavy chain [General function prediction only];
585-910 4.68e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 47.38  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   585 EEFTVARLYIsKMKSEVKTMVKRcKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSL-TEYLQNVEQKKRQLEES 663
Cdd:COG5022  788 DYELKWRLFI-KLQPLLSLLGSR-KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLiQKFGRSLKAKKRFSLLK 865

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   664 VDALSEELVQLR--AQEKVHEMEKEhlnkVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMM 741
Cdd:COG5022  866 KETIYLQSAQRVelAERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNID 941

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   742 LE------------QERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVA---KELQTLHN-LRKLFVQ 805
Cdd:COG5022  942 LEegpsieyvklpeLNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelsKQYGALQEsTKQLKEL 1021

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   806 DLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRdNADLRCELPKLEKRLRATAERVKALESALKEAK 885
Cdd:COG5022 1022 PVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYK-ALKLRRENSLLDDKQLYQLESTENLLKTINVKD 1100

                        330       340
                 ....*....|....*....|....*
gi 4758648   886 ENASRDRKRYQQEVDRIKEAVRSKN 910
Cdd:COG5022 1101 LEVTNRNLVKPANVLQFIVAQMIKL 1125
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 415-581 4.96e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 4.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKE---- 490
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  491 ---------------------------------------VLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLA 531
Cdd:COG3883  95 lyrsggsvsyldvllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4758648  532 SIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 656-905 5.10e-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: 47.25  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   656 KKRQLEESVDAL---SEELVQLRAQEKVHEME----KEHLNKVQTAneVKQAveQQIQSHREthqkQISSLRDEVEAKAK 728
Cdd:COG3096  297 ARRQLAEEQYRLvemARELEELSARESDLEQDyqaaSDHLNLVQTA--LRQQ--EKIERYQE----DLEELTERLEEQEE 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   729 LITDLQDQNQKMMLEQERLRVEHEKLK---ATDQEKsrklheLTVMQDRREQARQDLKGLEETvakelQTLHNLRKLFVQ 805
Cdd:COG3096  369 VVEEAAEQLAEAEARLEAAEEEVDSLKsqlADYQQA------LDVQQTRAIQYQQAVQALEKA-----RALCGLPDLTPE 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   806 DLATRVKKSAEIDSDDTGGSAAQKQKISF-------LENNLEQLTKVHKQLVRDNADLRC-ELPKLEKRLRATAERVKAL 877
Cdd:COG3096  438 NAEDYLAAFRAKEQQATEEVLELEQKLSVadaarrqFEKAYELVCKIAGEVERSQAWQTArELLRRYRSQQALAQRLQQL 517

                        250       260
                 ....*....|....*....|....*...
gi 4758648   878 ESALKEAKENASRdrkryQQEVDRIKEA 905
Cdd:COG3096  518 RAQLAELEQRLRQ-----QQNAERLLEE 540
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 591-917 5.36e-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: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     591 RLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEEsvdaLSEE 670
Cdd:TIGR00606  195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     671 LVQLRAQEKvhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVE 750
Cdd:TIGR00606  271 IKALKSRKK--QMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     751 HEKLkatdQEKSRKLHELTVMQD---RREQARQDLKGLE-----------------ETVAKELQTLHNLRKLFVQDLATR 810
Cdd:TIGR00606  349 QGRL----QLQADRHQEHIRARDsliQSLATRLELDGFErgpfserqiknfhtlviERQEDEAKTAAQLCADLQSKERLK 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     811 VKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASR 890
Cdd:TIGR00606  425 QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVK 504

                          330       340
                   ....*....|....*....|....*..
gi 4758648     891 DRKRYQQEVDRIKEAVRSKNMARRGHS 917
Cdd:TIGR00606  505 SLQNEKADLDRKLRKLDQEMEQLNHHT 531
PRK12704 PRK12704
phosphodiesterase; Provisional
 414-497 5.46e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDA--------SK 485
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelerisglTA 152

                         90
                 ....*....|...
gi 4758648   486 EEVKE-VLQALEE 497
Cdd:PRK12704 153 EEAKEiLLEKVEE 165
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
594-902 6.95e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 6.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  594 ISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQ 673
Cdd:COG4372  33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  674 LRAQekVHEMEKEhLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEK 753
Cdd:COG4372 113 LQEE--LEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  754 LKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKIS 833
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758648  834 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRI 902
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 437-922 7.92e-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: 7.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     437 EEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEY 516
Cdd:pfam12128  269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     517 E-LLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEigiavgnNDVKQPEGtgmIDEEFTVARLYIS 595
Cdd:pfam12128  349 LpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD-------KLAKIREA---RDRQLAVAEDDLQ 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     596 KMKSEVKtmvkrcKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEE------SVDALSE 669
Cdd:pfam12128  419 ALESELR------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEqeaanaEVERLQS 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     670 ELVQLRaqeKVHEMEKEHLNKV-QTANEVKQAVEQQIQSHRETHQKQISSLRDEV----EAKAKLI-------TDLQDQN 737
Cdd:pfam12128  493 ELRQAR---KRRDQASEALRQAsRRLEERQSALDELELQLFPQAGTLLHFLRKEApdweQSIGKVIspellhrTDLDPEV 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     738 QKMMLEQE------RL---RVEHEKLKATDQEKSRKLheltvmqDRREQARQDLKGLEETVAKELQTLhnlrklfvqdla 808
Cdd:pfam12128  570 WDGSVGGElnlygvKLdlkRIDVPEWAASEEELRERL-------DKAEEALQSAREKQAAAEEQLVQA------------ 630

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     809 trvkkSAEIDSDDTGGSAAqKQKISFLENNLEQLTKVHKQL-VRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN 887
Cdd:pfam12128  631 -----NGELEKASREETFA-RTALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 4758648     888 ASRD-------RKRYQQEV--------DRIKEAVRSKNMARRGHSAQIAK 922
Cdd:pfam12128  705 QKEQkrearteKQAYWQVVegaldaqlALLKAAIAARRSGAKAELKALET 754
mukB PRK04863
chromosome partition protein MukB;
626-885 9.70e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.49  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    626 EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDAL---------------SEELVQLRAQ-EKVHEMEK---- 685
Cdd:PRK04863  836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALnrllprlnlladetlADRVEEIREQlDEAEEAKRfvqq 915

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    686 --EHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDeVEAKAKLITDLQ--------DQNQKMMLE----QERLRveh 751
Cdd:PRK04863  916 hgNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRD-AKQQAFALTEVVqrrahfsyEDAAEMLAKnsdlNEKLR--- 991

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    752 EKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFvQDLATRVKKSAEIDsddtggSAAQKQK 831
Cdd:PRK04863  992 QRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL-QDLGVPADSGAEER------ARARRDE 1064

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4758648    832 IS-FLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALESALKEAK 885
Cdd:PRK04863 1065 LHaRLSANRSRRNQLEKQLTFCEAEMD----NLTKKLRKLERDYHEMREQVVNAK 1115
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 427-922 1.46e-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: 45.73  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     427 KLYKQLDDKDEEINQQSQLVEKLKTQMLD--------QEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEEL 498
Cdd:TIGR00618  187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDtyherkqvLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     499 AvnydqKSQEVEDKTKEYELLSDELNQ--KSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVgnndvKQ 576
Cdd:TIGR00618  267 A-----RIEELRAQEAVLEETQERINRarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHV-----KQ 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     577 pegtgmideeftvaRLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQlrisqheaKIKSLTEYLQNVEQK 656
Cdd:TIGR00618  337 --------------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ--------HIHTLQQQKTTLTQK 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     657 KRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSH-RETHQKQISSLRDEVEAKAKL--ITDL 733
Cdd:TIGR00618  395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLkeREQQ 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     734 QDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVmqdRREQARQD----------LKGLEETVAKELQTLHNLRKLF 803
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI---HPNPARQDidnpgpltrrMQRGEQTYAQLETSEEDVYHQL 551

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     804 VQDLATRVKKSAEIDS--DDTGGSAAQKQKISFLENNLEQLTKvhkqlvrdnaDLRCELPKLEKrlratAERVKALESAL 881
Cdd:TIGR00618  552 TSERKQRASLKEQMQEiqQSFSILTQCDNRSKEDIPNLQNITV----------RLQDLTEKLSE-----AEDMLACEQHA 616

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 4758648     882 KEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAK 922
Cdd:TIGR00618  617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ 657
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
692-905 1.56e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  692 QTANEVKQA-VEQQIQSHRETH-------QKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEhEKLKATDQEKSR 763
Cdd:COG3206 152 AVANALAEAyLEQNLELRREEArkaleflEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-QQLSELESQLAE 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  764 KLHELTVMQDRREQARQDLKGLEETVAKELQ--TLHNLRklfvQDLATRVKKSAEIDSDDTGGS---AAQKQKISFLENN 838
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLR----AQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQ 306

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758648  839 LEQLT-KVHKQLVRDNADLRCELPKLEKRLRATAERVKAL---ESALKEAKENASRDRKRYQQEVDRIKEA 905
Cdd:COG3206 307 LQQEAqRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
46 PHA02562
endonuclease subunit; Provisional
 416-688 1.56e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.39  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   416 AERRKCEEEI------AKLYKQLDDKDEEINQQSQLV--------EKLKTQMLDQEELLASTRRDQDnmqaelnRLQAEN 481
Cdd:PHA02562 150 PARRKLVEDLldisvlSEMDKLNKDKIRELNQQIQTLdmkidhiqQQIKTYNKNIEEQRKKNGENIA-------RKQNKY 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   482 DASKEEVKEVLQALEELavnydqkSQEVEDKTKEYELLSDELNQKSATLASIDAELQKL-KEMTNHQKkraaemmasllk 560
Cdd:PHA02562 223 DELVEEAKTIKAEIEEL-------TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqKVIKMYEK------------ 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   561 dlaeigiavgnNDVkQPEGTGMIDEEFTVarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEE---NEKELAACQLRIS 637
Cdd:PHA02562 284 -----------GGV-CPTCTQQISEGPDR----ITKIKDKLKELQHSLEKLDTAIDELEEIMDEfneQSKKLLELKNKIS 347

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4758648   638 QHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKV-------HEMEKEHL 688
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKivktkseLVKEKYHR 405
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 410-914 1.74e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.81  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     410 IGNFTDAERRKCEEE---IAKLYKQLDDKDEEINQQSQLVEKLKTQML----DQEELLASTRRDQDNMQAELNRLQAEND 482
Cdd:TIGR00606  392 IKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADEIRDEKKGLGrtieLKKEILEKKQEELKFVIKELQQLEGSSD 471

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     483 ASKEEVKEVLQALEELAVNydQKSQEVEDKTKEYELLSdelNQKSATLASIDAELQKLKEMTNHQKKRaaEMMASLLKDL 562
Cdd:TIGR00606  472 RILELDQELRKAERELSKA--EKNSLTETLKKEVKSLQ---NEKADLDRKLRKLDQEMEQLNHHTTTR--TQMEMLTKDK 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     563 AEIGIAVGNNDVKQPEG----------TGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAAC 632
Cdd:TIGR00606  545 MDKDEQIRKIKSRHSDEltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     633 QLRI------SQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQL---------------RAQEKVHEMEKEHLNKV 691
Cdd:TIGR00606  625 EDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLtdenqsccpvcqrvfQTEAELQEFISDLQSKL 704

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     692 QTANEVKQAVEQQI---QSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLR---VEHEKLKAT--DQEKSR 763
Cdd:TIGR00606  705 RLAPDKLKSTESELkkkEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTimPEEESA 784

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     764 K--LHELTVMQDRREQARQDLKGLEETVAKE-----LQTLHNLRKLfVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLE 836
Cdd:TIGR00606  785 KvcLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQE-KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758648     837 NNLEQLtKVHKQLVRDNADLRcelPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARR 914
Cdd:TIGR00606  864 SKTNEL-KSEKLQIGTNLQRR---QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
354-568 1.75e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  354 LRNTIQWLENELNRwrngetvpIDEQFDKEKANLEAFTVDKDITLTNDKPATAIGVIGNF------TDAERRKCEEEIAK 427
Cdd:COG3206 173 ARKALEFLEEQLPE--------LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELesqlaeARAELAEAEARLAA 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  428 LYKQLDDKDEEINQ--QSQLVEKLKTQMLDQE----ELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEelaVN 501
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEaelaELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE---AE 321

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648  502 YDQKSQEVEDKTKEYEllsdELNQKSATLASIDAELQKLKEmtnhQKKRAAEMMASLLKDLAEIGIA 568
Cdd:COG3206 322 LEALQAREASLQAQLA----QLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEARLA 380
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
414-678 2.08e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  414 TDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQ 493
Cdd:COG4372  57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  494 ALEELAVNYDQKSQEVEDktkeyelLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNND 573
Cdd:COG4372 137 QIAELQSEIAEREEELKE-------LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  574 VKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNV 653
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289

                       250       260
                ....*....|....*....|....*
gi 4758648  654 EQKKRQLEESVDALSEELVQLRAQE 678
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALE 314
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 354-754 2.60e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 45.04  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    354 LRNTIQWLEN---ELNRWRNGETVpIDEqFDKEKANLEAFTVDKDitltnDKPATaigVIGNFTDAErrkCEEEIAKLYK 430
Cdd:PRK10929   50 LQSALNWLEErkgSLERAKQYQQV-IDN-FPKLSAELRQQLNNER-----DEPRS---VPPNMSTDA---LEQEILQVSS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    431 QLDDKDEEINQQ-------SQLVEKLKTQMLDQEELLA-STRRDQDNM-------QAELNRLQAENDASKEEVKEVlqAL 495
Cdd:PRK10929  117 QLLEKSRQAQQEqdrareiSDSLSQLPQQQTEARRQLNeIERRLQTLGtpntplaQAQLTALQAESAALKALVDEL--EL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    496 EELAVNYDQksqevedktkEYELLSDELNQKSATlaSIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEigiavgnNDVK 575
Cdd:PRK10929  195 AQLSANNRQ----------ELARLRSELAKKRSQ--QLDAYLQALRNQLNSQRQREAERALESTELLAE-------QSGD 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    576 QPEGtgmIDEEFTVARlyisKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAAcqLR-ISQHEAKIKSLTEYLQNV- 653
Cdd:PRK10929  256 LPKS---IVAQFKINR----ELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNT--LReQSQWLGVSNALGEALRAQv 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    654 ----EQKKRQLeesvdaLSEELVQLRAQEKVHEmekEHLNKVQTANEVKQAVEQQIQShretHQKQIssLRDEVEAKAKL 729
Cdd:PRK10929  327 arlpEMPKPQQ------LDTEMAQLRVQRLRYE---DLLNKQPQLRQIRQADGQPLTA----EQNRI--LDAQLRTQREL 391

                         410       420
                  ....*....|....*....|....*
gi 4758648    730 ITDLQDQNQKMMLEQERLRVEHEKL 754
Cdd:PRK10929  392 LNSLLSGGDTLILELTKLKVANSQL 416
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 590-770 2.70e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   590 ARLYISKMKSEVKTMVKrckqlestqtesnkKMEENEKELaacqlrisqhEAKIKSLTEYLQNVEQKKRQLEESVDALSE 669
Cdd:PRK00409 507 AKKLIGEDKEKLNELIA--------------SLEELEREL----------EQKAEEAEALLKEAEKLKEELEEKKEKLQE 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   670 ELvqlraQEKVHEMEKEHLNKVQTAnevKQAVEQQIQSHRETHQKQISSLrdeveaKAKLITDlqdqnqkmmlEQERLRV 749
Cdd:PRK00409 563 EE-----DKLLEEAEKEAQQAIKEA---KKEADEIIKELRQLQKGGYASV------KAHELIE----------ARKRLNK 618

                        170       180
                 ....*....|....*....|.
gi 4758648   750 EHEKLKATDQEKSRKLHELTV 770
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKV 639
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 555-799 3.03e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.53  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   555 MASLLKDLAEIGIaVGNNDVKQPEGtgmiDEEFTVARLYISKMkSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQL 634
Cdd:PRK05771  18 KDEVLEALHELGV-VHIEDLKEELS----NERLRKLRSLLTKL-SEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   635 --RISQHEAKIKSLTEYLQNVEQKKRQLEESVDAL------SEELVQLRAQEKVH----EMEKEHLNKVQTANEVKQAVE 702
Cdd:PRK05771  92 eeELEKIEKEIKELEEEISELENEIKELEQEIERLepwgnfDLDLSLLLGFKYVSvfvgTVPEDKLEELKLESDVENVEY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   703 qqiqsHRETHQKQISSLRDEVEAKAKLITDLQDqnqkmmLEQERLRVEHEKLkaTDQEKSRKLHELTVMQDRREQARQDL 782
Cdd:PRK05771 172 -----ISTDKGYVYVVVVVLKELSDEVEEELKK------LGFERLELEEEGT--PSELIREIKEELEEIEKERESLLEEL 238

                        250
                 ....*....|....*..
gi 4758648   783 KGLEETVAKELQTLHNL 799
Cdd:PRK05771 239 KELAKKYLEELLALYEY 255
PRK11637 PRK11637
AmiB activator; Provisional
 422-631 3.35e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   422 EEEIAKLYKQLDDK-------DEEINQQSQLVEKLKTQMLDQEELLAST-----RRDQDN-MQAELN--------RLQAE 480
Cdd:PRK11637  81 EEAISQASRKLRETqntlnqlNKQIDELNASIAKLEQQQAAQERLLAAQldaafRQGEHTgLQLILSgeesqrgeRILAY 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   481 ----NDASKEEVKEVLQALEELAVnydQKSQEVEDKTKEYELLSDELNQKsatlasidaelQKLKEMTNHQKKRAAEMMA 556
Cdd:PRK11637 161 fgylNQARQETIAELKQTREELAA---QKAELEEKQSQQKTLLYEQQAQQ-----------QKLEQARNERKKTLTGLES 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   557 SLLKDLAEIGiavgnnDVKQPEgtgmideefTVARLYISKMKSEVKTMVK---------RCKQLESTQTESNKKMEENEK 627
Cdd:PRK11637 227 SLQKDQQQLS------ELRANE---------SRLRDSIARAEREAKARAEreareaarvRDKQKQAKRKGSTYKPTESER 291


                 ....
gi 4758648   628 ELAA 631
Cdd:PRK11637 292 SLMS 295
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
 446-773 3.70e-04

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: 43.89  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     446 VEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQ 525
Cdd:smart00806  73 VEELDEVKKHIDDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARPAASPSPVLASSSSAISLANNPDKLNKE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     526 KSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLA---EIGIAVGNNDvkqpegtgmideeftvARLYISKMKSEVK 602
Cdd:smart00806 153 QRAELKSLQRELAVLRQTHNSFFTEIKESIKDILEKIDkfkSSSLSASGSS----------------NRAYVESSKKKLS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     603 TMVKR-CKQLESTQ---------------TESNKKMEENEKELAACqlrisqhEAKIKSLTEYLQNVE-QKKRQLEESVD 665
Cdd:smart00806 217 EDSDSlLTKVDDLQdiiealrkdvaqrgvRPSKKQLETVQKELETA-------RKELKKMEEYIDIEKpIWKKIWEAELD 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     666 ALSEELVQLRAQEKVHEMEKEHLNKV-QTANEVKQAVEQQIQSHRETHQKQISSlrdeVEAKAKLITDLQDQnqkMMLEQ 744
Cdd:smart00806 290 KVCEEQQFLTLQEDLIADLKEDLEKAeETFDLVEQCCEEQEKGPSKNRNKPVSL----PVPTPGTFNDLKDQ---VLMEV 362

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 4758648     745 ERLRVEHEK-LKATD-----QEKSRKLHELTVMQD 773
Cdd:smart00806 363 RALKPDHESrLEAIEraeklREKELEYRRVDEFEK 397
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 417-909 4.50e-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: 44.40  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     417 ERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:pfam01576  153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     497 ELAVNYDQKSQEVEDKTKEYEllsDELNQKSATlasidaeLQKLKEMTNHqkkraaemMASLLKDLaEIGIAVGNNDVKQ 576
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLE---EETAQKNNA-------LKKIRELEAQ--------ISELQEDL-ESERAARNKAEKQ 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     577 PEGTGmidEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQ-HEAKIKSLTEYLQNVEQ 655
Cdd:pfam01576  294 RRDLG---EELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkHTQALEELTEQLEQAKR 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     656 KKRQLEESVDALSEELVQLRAQEKV---HEMEKEHLNKVQTA--NEVkQAVEQQIQSHRETHQKQISSLRDEVEAKAKLI 730
Cdd:pfam01576  371 NKANLEKAKQALESENAELQAELRTlqqAKQDSEHKRKKLEGqlQEL-QARLSESERQRAELAEKLSKLQSELESVSSLL 449

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     731 TDLQDQNQKMMLEQERLRVEHEKLKATDQEKSR-KL---HELTVMQDRREQARQDLKGLEE---TVAKELQTLH----NL 799
Cdd:pfam01576  450 NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRqKLnlsTRLRQLEDERNSLQEQLEEEEEakrNVERQLSTLQaqlsDM 529

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     800 RKLFVQDLAT-----RVKKSAEIDSDDTGGSAAQKqkisflENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERV 874
Cdd:pfam01576  530 KKKLEEDAGTlealeEGKKRLQRELEALTQQLEEK------AAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 4758648     875 KALESALKEAKENASrdrkRYQQEVDRIKEAVRSK 909
Cdd:pfam01576  604 KKFDQMLAEEKAISA----RYAEERDRAEAEAREK 634
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 530-686 5.44e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 5.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  530 LASIDAELQKLKemtnHQKKRAAEMMASLLKDLAEIgiavgNNDVKQpegtgmIDEEFTVARLYISKMKSEVKTMVKRCK 609
Cdd:COG1579  12 LQELDSELDRLE----HRLKELPAELAELEDELAAL-----EARLEA------AKTELEDLEKEIKRLELEIEEVEARIK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  610 QLESTQTE--SNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQ--EKVHEMEK 685
Cdd:COG1579  77 KYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldEELAELEA 156


                .
gi 4758648  686 E 686
Cdd:COG1579 157 E 157
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 422-578 5.60e-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: 5.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  422 EEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAEL--------------------------- 474
Cdd:COG3883  36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfs 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  475 ---------NRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTN 545
Cdd:COG3883 116 dfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195

                       170       180       190
                ....*....|....*....|....*....|...
gi 4758648  546 HQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPE 578
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 436-777 6.41e-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: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    436 DEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKE 515
Cdd:pfam07888  37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    516 YELLSD----------ELNQKSATLA----SIDAELQKLKEmtnhqkkRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:pfam07888 117 KDALLAqraahearirELEEDIKTLTqrvlERETELERMKE-------RAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    582 MiDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAacQLRisqheakikSLTEYLQNVEQKkrqle 661
Cdd:pfam07888 190 L-SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE--ELR---------SLQERLNASERK----- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    662 esVDALSEELVQLRAQeKVHEMEKEHLNKVQTANEVKQAVEQ--QIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQK 739
Cdd:pfam07888 253 --VEGLGEELSSMAAQ-RDRTQAELHQARLQAAQLTLQLADAslALREGRARWAQERETLQQSAEADKDRIEKLSAELQR 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4758648    740 M--MLEQERLrvEHEKLKA-----------TDQEKSRKLHE----LTVMQDRREQ 777
Cdd:pfam07888 330 LeeRLQEERM--EREKLEVelgrekdcnrvQLSESRRELQElkasLRVAQKEKEQ 382
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 422-887 6.46e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    422 EEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVN 501
Cdd:TIGR04523  74 NNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    502 YDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKemtnhQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTG 581
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK-----NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    582 MIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKElaacqlrISQHEAKIKSLTEYLQNVEQKKRQLE 661
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE-------LEQNNKKIKELEKQLNQLKSEISDLN 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    662 EsvdalseelvqlraqekvhEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMm 741
Cdd:TIGR04523 302 N-------------------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK- 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    742 leQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEEtVAKELQtlhnlrklfvqdlatrvkksaeidsdd 821
Cdd:TIGR04523 362 --QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-LNQQKD--------------------------- 411

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648    822 tggsaaqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN 887
Cdd:TIGR04523 412 --------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 412-579 6.70e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 6.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  412 NFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQ-----MLDQEELLASTRRdQDNMQAELNRLQAENDASKE 486
Cdd:COG4942  79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRA 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  487 EVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEM---MASLLKDLA 563
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELealIARLEAEAA 237

                       170
                ....*....|....*.
gi 4758648  564 EIGIAVGNNDVKQPEG 579
Cdd:COG4942 238 AAAERTPAAGFAALKG 253
PRK01156 PRK01156
chromosome segregation protein; Provisional
 468-910 7.84e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.35  E-value: 7.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   468 DNMQAELNRLqaenDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNhQ 547
Cdd:PRK01156 176 DMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-M 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   548 KKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNkKMEENEK 627
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEIN-KYHAIIK 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   628 ELAACQLRISQHEAKIKSLTE-----------------YLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNK 690
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDDlnnqilelegyemdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   691 VQtaNEVKQAVeQQIQSHRETHQKQISSLR---DEVEAKAKLI----------TDLQDQ----------NQKMMLEQERL 747
Cdd:PRK01156 410 EL--NEINVKL-QDISSKVSSLNQRIRALRenlDELSRNMEMLngqsvcpvcgTTLGEEksnhiinhynEKKSRLEEKIR 486

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   748 RVEHEkLKATDQEK-----------SRKLHELTVMQDRREQARQDLKGLEETVA-------KELQTLHNLRKLFVQDLAT 809
Cdd:PRK01156 487 EIEIE-VKDIDEKIvdlkkrkeyleSEEINKSINEYNKIESARADLEDIKIKINelkdkhdKYEEIKNRYKSLKLEDLDS 565

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   810 R----VKKSAEIDSDDTGGSAAQKQKISFLENNLEQ-LTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEsALKEA 884
Cdd:PRK01156 566 KrtswLNALAVISLIDIETNRSRSNEIKKQLNDLESrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ-ENKIL 644

                        490       500
                 ....*....|....*....|....*.
gi 4758648   885 KENASRDRKRYQQEVDRIKEAVRSKN 910
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEIDSIIPDLK 670
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 485-565 7.95e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 7.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   485 KEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKsatLASIDAELQKLKEmtnHQKKRAAEMMASLLKDLAE 564
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLE---EAEKEAQQAIKEAKKEADE 588


                 .
gi 4758648   565 I 565
Cdd:PRK00409 589 I 589
PRK12704 PRK12704
phosphodiesterase; Provisional
 634-781 1.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   634 LRISQHEAKIKSLTEylqNVEQKKRQLEESVDALSEELVqLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQ 713
Cdd:PRK12704  24 VRKKIAEAKIKEAEE---EAKRILEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758648   714 KQISSL---RDEVEAKAKLITDLQDQNQKMMLEQERLRVEH----EKLKATDQEKSRKLheltVMQDRREQARQD 781
Cdd:PRK12704 100 RKLELLekrEEELEKKEKELEQKQQELEKKEEELEELIEEQlqelERISGLTAEEAKEI----LLEKVEEEARHE 170
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 728-914 1.05e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    728 KLITDLQDQNQKMMLEQERLRVEHEKlKATDQEKSRKLHEltvmqdrREQARQDLKGLEETVAKELQTLHNLRKLFVQDL 807
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEE-------AEKARQAEMDRQAAIYAEQERMAMERERELERI 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    808 ATRVKKSAEidsddtggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKL-------EKRLRATAERVKALESA 880
Cdd:pfam17380 354 RQEERKREL--------ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArkvkileEERQRKIQQQKVEMEQI 425

                         170       180       190
                  ....*....|....*....|....*....|....
gi 4758648    881 LKEAKENASRDRKRYQQEVDRIKEAVRSKNMARR 914
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQ 459
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
613-886 1.18e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  613 STQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQ-EKVHEMEKEHLNKV 691
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKrDELNEKVKELKEER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  692 QTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKaKLITDLQD--QNQKMMLEQERLRVE-----HEKLKATDQ--EKS 762
Cdd:COG1340  81 DELNEKLNELREELDELRKELAELNKAGGSIDKLR-KEIERLEWrqQTEVLSPEEEKELVEkikelEKELEKAKKalEKN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  763 RKLHEL----TVMQDRREQARQDLKGLeetvAKELQTLHN-LRKLFVQdlATRVKKSAEidsddtggsaAQKQKISFLEN 837
Cdd:COG1340 160 EKLKELraelKELRKEAEEIHKKIKEL----AEEAQELHEeMIELYKE--ADELRKEAD----------ELHKEIVEAQE 223

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 4758648  838 NLEQLTKVHKQLVRDNADLRCELPKLEKRLRAtAERVKALESALKEAKE 886
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRA-LKREKEKEELEEKAEE 271
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 433-689 1.19e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.61  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   433 DDKDE--EINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRL----QAENDASKEEVKEVLQALEELAVNYDQKS 506
Cdd:PRK05771  16 SYKDEvlEALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLrsylPKLNPLREEKKKVSVKSLEELIKDVEEEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   507 QEVEDKTKEyelLSDELNQKSATLASIDAELQKLKEMTNhqkkraAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEE 586
Cdd:PRK05771  96 EKIEKEIKE---LEEEISELENEIKELEQEIERLEPWGN------FDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   587 FTVARLYISKMKSEVKTMVKrckqlestqtesNKKMEENEKELAACQLR-------------ISQHEAKIKSLTEYLQNV 653
Cdd:PRK05771 167 ENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLGFErleleeegtpselIREIKEELEEIEKERESL 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 4758648   654 eqkKRQLEESVDALSEELVqlrAQEKVHEMEKEHLN 689
Cdd:PRK05771 235 ---LEELKELAKKYLEELL---ALYEYLEIELERAE 264
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 654-903 1.26e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.87  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    654 EQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHL---NKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLI 730
Cdd:PRK10246  215 PEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLtrlDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRP 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    731 TDLQDQNQKMMLEQERLRVE--HEKLKATDQEKSRKLHELTVMQDRREQARQDLKG-LEETVAKEL--QTLHNLRKLFVQ 805
Cdd:PRK10246  295 HWERIQEQSAALAHTRQQIEevNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwLAEHDRFRQwnNELAGWRAQFSQ 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    806 ---DLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQ---LVRDNADLRCELPKLEKRLRATAERVKALES 879
Cdd:PRK10246  375 qtsDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQ 454

                         250       260
                  ....*....|....*....|....*..
gi 4758648    880 ALKEAKENASRDRKRY---QQEVDRIK 903
Cdd:PRK10246  455 EQTQRNAALNEMRQRYkekTQQLADVK 481
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
682-813 1.77e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  682 EMEKEHLNKVQTANEVKQAVEQQiqsHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEK 761
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE 460

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4758648  762 SRKLHELTVMQDRREQARQDLKGLEETV---AKELQTLHNLRKLFVQDLATRVKK 813
Cdd:COG2433 461 IRKDREISRLDREIERLERELEEERERIeelKRKLERLKELWKLEHSGELVPVKV 515
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 435-902 1.89e-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: 42.08  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     435 KDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVlqalEELAVNYDQKSQEVEDKTK 514
Cdd:pfam01576    3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEA----EEMRARLAARKQELEEILH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     515 EYELLSDELNQKSATLASIDAELQK-LKEMTNH-QKKRAAEMMASLLKDLAEIGIAvgnndvkqpegtgMIDEEFTVARL 592
Cdd:pfam01576   79 ELESRLEEEEERSQQLQNEKKKMQQhIQDLEEQlDEEEAARQKLQLEKVTTEAKIK-------------KLEEDILLLED 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     593 YISKMKSEVKTMVKRCKQLESTQTESnkkmEENEKELAACQLRisqHEAKIKSLTEYL-------QNVEQKKRQLEESVD 665
Cdd:pfam01576  146 QNSKLSKERKLLEERISEFTSNLAEE----EEKAKSLSKLKNK---HEAMISDLEERLkkeekgrQELEKAKRKLEGEST 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     666 ALSEELVQLRAQ--EKVHEMEK--EHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMM 741
Cdd:pfam01576  219 DLQEQIAELQAQiaELRAQLAKkeEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     742 LEQERLRVEHEKL---KATDQE-KSRKLHELTVMQDRREqarqdlkglEETVAKELQtlhnlrklfVQDLatRVKKSAEI 817
Cdd:pfam01576  299 EELEALKTELEDTldtTAAQQElRSKREQEVTELKKALE---------EETRSHEAQ---------LQEM--RQKHTQAL 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     818 DSDDTGGSAAQKQKISflennleqLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQ 897
Cdd:pfam01576  359 EELTEQLEQAKRNKAN--------LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430


                   ....*
gi 4758648     898 EVDRI 902
Cdd:pfam01576  431 LAEKL 435
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
647-850 1.94e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  647 TEYL-QNVEQKKRQLEESVDALSEELVQLR-----AQEKVHEMEKEHlNKVQTANEVKQAVEQ---------QIQSHRET 711
Cdd:COG3206 159 EAYLeQNLELRREEARKALEFLEEQLPELRkeleeAEAALEEFRQKN-GLVDLSEEAKLLLQQlselesqlaEARAELAE 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  712 HQKQISSLRDEVEAK-------------AKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEksrklheltvMQDRREQA 778
Cdd:COG3206 238 AEARLAALRAQLGSGpdalpellqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ----------IAALRAQL 307

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758648  779 RQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIdsddtggsAAQKQKISFLENNLEQLTKVHKQLV 850
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEVARELYESLL 371
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
477-720 2.15e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  477 LQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYEL------LSDELNQKSATLASIDAELQKLKEMTNhQKKR 550
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknglvdLSEEAKLLLQQLSELESQLAEARAELA-EAEA 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  551 AAEMMASLLKDLAEIGIAVGNNDVkqpegtgmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELA 630
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPV-------------------IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  631 ACQLRISQH--------EAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRaqekvhEMEKEhlnkVQTANEVKQAVE 702
Cdd:COG3206 302 ALRAQLQQEaqrilaslEAELEALQAREASLQAQLAQLEARLAELPELEAELR------RLERE----VEVARELYESLL 371

                       250
                ....*....|....*...
gi 4758648  703 QQIQSHRETHQKQISSLR 720
Cdd:COG3206 372 QRLEEARLAEALTVGNVR 389
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 713-960 2.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  713 QKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRvehEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKE 792
Cdd:COG3883  22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  793 LQTLHNLRKLF----VQDLATRVKKSAEIdsddtggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL- 867
Cdd:COG3883  99 GGSVSYLDVLLgsesFSDFLDRLSALSKI-------ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKa 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  868 ---------RATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPS 938
Cdd:COG3883 172 eleaqqaeqEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251

                       250       260
                ....*....|....*....|..
gi 4758648  939 AIRGGGAFVQNSQPVAVRGGGG 960
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAG 273
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 477-792 2.51e-03

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: 41.42  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    477 LQAENDASKEEVKEVLQALEelAVNydqksQEVEDKTKEYELLSDELNQKSATLASidaELQKLKEMTNHQKKRAAEMMA 556
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQE--AAN-----RQREKEKERYKRDREQWERQRRELES---RVAELKEELRQSREKHEELEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    557 SllkdlaEIGIAVGNNDVKQPEGTGMIDEEFTVARlyISKMKSEVKTMVKRCKQLES-------TQTESNKKMEENEKEL 629
Cdd:pfam07888 102 K------YKELSASSEELSEEKDALLAQRAAHEAR--IRELEEDIKTLTQRVLERETelermkeRAKKAGAQRKEEEAER 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    630 AACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLR-----AQEKVHEME---------KEHLNKVQTA- 694
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttAHRKEAENEalleelrslQERLNASERKv 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    695 ----NEVKQAVEQQIQSHRETHQKQISSlrdeveakAKLITDLQDQNQKMMLEQERLRVEHEKLKAT---DQEKSRKLH- 766
Cdd:pfam07888 254 eglgEELSSMAAQRDRTQAELHQARLQA--------AQLTLQLADASLALREGRARWAQERETLQQSaeaDKDRIEKLSa 325

                         330       340
                  ....*....|....*....|....*.
gi 4758648    767 ELTVMQDRREQARQDLKGLEETVAKE 792
Cdd:pfam07888 326 ELQRLEERLQEERMEREKLEVELGRE 351
PRK12704 PRK12704
phosphodiesterase; Provisional
 596-729 2.83e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   596 KMKSEVKTMVKRCK-QLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELvql 674
Cdd:PRK12704  57 EALLEAKEEIHKLRnEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL--- 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4758648   675 raqEKVHEMEKEHLNKVQ--TANEVKQaveQQIQSHRETHQKQISSLRDEVEAKAKL 729
Cdd:PRK12704 134 ---EELIEEQLQELERISglTAEEAKE---ILLEKVEEEARHEAAVLIKEIEEEAKE 184
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 606-757 3.44e-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: 40.29  E-value: 3.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  606 KRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEK 685
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQK 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758648  686 EhLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAK----AKLITDLQDQNQKMMLEQERLRVEHEKLKAT 757
Cdd:COG1579  97 E-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELeaelEEKKAELDEELAELEAELEELEAEREELAAK 171
46 PHA02562
endonuclease subunit; Provisional
 424-521 3.87e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   424 EIAKLYKQLDDKDE-------EINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALE 496
Cdd:PHA02562 310 ELQHSLEKLDTAIDeleeimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389

                         90       100
                 ....*....|....*....|....*
gi 4758648   497 ELAVNYDQKSQEVEDKTKEYELLSD 521
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIVTDLLKD 414
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 441-780 4.04e-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: 40.88  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    441 QQSQLVEKLKTQMLDQE--ELLASTRRDQDNMQAELNRlQAENDASKEEVKEvlqaLEELAVNYDQKSQEV--EDKTKEY 516
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEkeEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAE----QERMAMERERELERIrqEERKREL 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    517 ELLSDElnqksatlaSIDAELQKLKEMTNHQKKRAAEmmasllkdlaeigiavgNNDVKQpegtgmideEFTVARLYI-- 594
Cdd:pfam17380 363 ERIRQE---------EIAMEISRMRELERLQMERQQK-----------------NERVRQ---------ELEAARKVKil 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    595 -----SKMKSEVKTMVK-RCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEylQNVEQKKRQL----EESV 664
Cdd:pfam17380 408 eeerqRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ--QEEERKRKKLelekEKRD 485

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    665 DALSEELvqlraQEKVHEMEKEHLNKVQTANEVKQAVeqqIQSHRETHQKQISslrdevEAKAKLITDLQDQNQKMMleQ 744
Cdd:pfam17380 486 RKRAEEQ-----RRKILEKELEERKQAMIEEERKRKL---LEKEMEERQKAIY------EEERRREAEEERRKQQEM--E 549

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 4758648    745 ERLRVEHEKLKATdQEKSRklheLTVMQDRREQARQ 780
Cdd:pfam17380 550 ERRRIQEQMRKAT-EERSR----LEAMEREREMMRQ 580
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 437-768 4.61e-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: 41.09  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   437 EEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEEL---AVNYDQKSQEVEDKT 513
Cdd:COG3096  347 EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtrAIQYQQAVQALEKAR 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   514 KEYELlsDELNQKSA--TLASIDAELQKLKE--MTNHQKKRAAEMMASLLKDLAEIGIAVgnndvkqpegTGMIDEE--F 587
Cdd:COG3096  427 ALCGL--PDLTPENAedYLAAFRAKEQQATEevLELEQKLSVADAARRQFEKAYELVCKI----------AGEVERSqaW 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   588 TVARLYISKMKSEvKTMVKRCKQLESTQTESNKKMEEN---EKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESV 664
Cdd:COG3096  495 QTARELLRRYRSQ-QALAQRLQQLRAQLAELEQRLRQQqnaERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   665 DALSEELVQLRAQEkvhemekehlnkvqtanevkQAVEQQIQSHRE------THQKQISSLRDEVEAKAKLITDLQDQNQ 738
Cdd:COG3096  574 AEAVEQRSELRQQL--------------------EQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQ 633

                        330       340       350
                 ....*....|....*....|....*....|.
gi 4758648   739 kMMLEQER-LRVEHEKLKATDQEKSRKLHEL 768
Cdd:COG3096  634 -QLLEREReATVERDELAARKQALESQIERL 663
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
717-908 5.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  717 SSLRDEVEAKAKLITDLQDQNQKMMLEQ--------ERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEEt 788
Cdd:COG4717  45 AMLLERLEKEADELFKPQGRKPELNLKElkeleeelKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK- 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  789 vAKELQTLHNLRKLFVQDLATRVKKSAEIDsddtggsaAQKQKISFLENNLEQLTKVHKQLVRD-NADLRCELPKLEKRL 867
Cdd:COG4717 124 -LLQLLPLYQELEALEAELAELPERLEELE--------ERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEEL 194

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4758648  868 RATAERVKALESALKEAKEnasrDRKRYQQEVDRIKEAVRS 908
Cdd:COG4717 195 QDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQ 231
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 616-913 6.13e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     616 TESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSE-----ELVQLRAQEKVHEMEkEHLNK 690
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaeaEEMRARLAARKQELE-EILHE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     691 VQTANEVKQAVEQQIQSHRETHQKQISSLRDEVE----AKAKLitdlqdQNQKMMLEQERLRVEHEKLKATDQeKSRKLH 766
Cdd:pfam01576   80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeeaARQKL------QLEKVTTEAKIKKLEEDILLLEDQ-NSKLSK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     767 ELTVMQDRREQARQDLkGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEidsddtggsaaQKQKISFLENNLE-QLTKV 845
Cdd:pfam01576  153 ERKLLEERISEFTSNL-AEEEEKAKSLSKLKNKHEAMISDLEERLKKEEK-----------GRQELEKAKRKLEgESTDL 220

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758648     846 HKQLVRDNA---DLRCELPKLEKRLRATAERVKAlESAlkeAKENASRDRKRYQQEVDRIKEAVRSKNMAR 913
Cdd:pfam01576  221 QEQIAELQAqiaELRAQLAKKEEELQAALARLEE-ETA---QKNNALKKIRELEAQISELQEDLESERAAR 287
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-551 6.14e-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: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648     415 DAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQ--AENDASKEEVKEVL 492
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeiPEEELSLEDVQAEL 960

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 4758648     493 QALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRA 551
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
Filament pfam00038
Intermediate filament protein;
468-709 6.86e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.52  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    468 DNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQksATLASIDAE--LQKLKEMTN 545
Cdd:pfam00038  57 EDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDE--ATLARVDLEakIESLKEELA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    546 HQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEeftVARLY---ISKMKSEVKTMVKRckQLESTQTESNKkm 622
Cdd:pfam00038 135 FLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAE---IRAQYeeiAAKNREEAEEWYQS--KLEELQQAAAR-- 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    623 eeNEKELAACQLRISQHEAKIKSLTEYLQNVEQKK----RQLEESVDALSEELVQlrAQEKVHEMEKE----------HL 688
Cdd:pfam00038 208 --NGDALRSAKEEITELRRTIQSLEIELQSLKKQKasleRQLAETEERYELQLAD--YQELISELEAElqetrqemarQL 283

                         250       260
                  ....*....|....*....|.
gi 4758648    689 NKVQTANEVKQAVEQQIQSHR 709
Cdd:pfam00038 284 REYQELLNVKLALDIEIATYR 304
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 488-677 7.00e-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: 39.14  E-value: 7.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  488 VKEVLQALEELAvNYDQKSQEVEDK----TKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLA 563
Cdd:COG1579   2 MPEDLRALLDLQ-ELDSELDRLEHRlkelPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648  564 EIGIAVGNNDVKQpegtgmideeftvarlyiskMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKI 643
Cdd:COG1579  81 QLGNVRNNKEYEA--------------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140

                       170       180       190
                ....*....|....*....|....*....|....
gi 4758648  644 kslteylqnvEQKKRQLEESVDALSEELVQLRAQ 677
Cdd:COG1579 141 ----------EEKKAELDEELAELEAELEELEAE 164
mukB PRK04863
chromosome partition protein MukB;
440-540 7.02e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    440 NQQSQLVEKLKTQMLDQEELLASTR---RDQDNMQAELNR----LQAENDASKEEVKEVLQALEELAVNYDQKSQE--VE 510
Cdd:PRK04863  981 AKNSDLNEKLRQRLEQAEQERTRAReqlRQAQAQLAQYNQvlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEEraRA 1060

                          90       100       110
                  ....*....|....*....|....*....|...
gi 4758648    511 DKTKEYELLSDELNQKSA---TLASIDAELQKL 540
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQlekQLTFCEAEMDNL 1093
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 416-719 8.10e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    416 AERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEvlqaL 495
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE----L 508

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    496 EELAVNYDQKSQEVEDKTKEyelLSDELNQKSATLASIDAELQKLKEmtnhqkkraaemmaSLLKDLAEIGIAVGNNDVK 575
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEK---LESEKKEKESKISDLEDELNKDDF--------------ELKKENLEKEIDEKNKEIE 571

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648    576 QPEGTgmideeftvarlyISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQ 655
Cdd:TIGR04523 572 ELKQT-------------QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758648    656 KKRQLEESVDALSEELVQLRaqEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSL 719
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIR--NKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRM 700
PLN02939 PLN02939
transferase, transferring glycosyl groups
 393-671 8.52e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.89  E-value: 8.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   393 DKDITLTNDKPATAIGVIGNFTdAERRKCEEEIAKLYKQLDDKDEEINQQSQlvEKLKTQMLDQE------ELL---AST 463
Cdd:PLN02939 141 EKNILLLNQARLQALEDLEKIL-TEKEALQGKINILEMRLSETDARIKLAAQ--EKIHVEILEEQleklrnELLirgATE 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   464 RRDQDNMQAELNRLQAENDASKEEVkevlQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEM 543
Cdd:PLN02939 218 GLCVHSLSKELDVLKEENMLLKDDI----QFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   544 TNH---QKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARlyISKMKSE-VKTMVKRCKQLESTQTESN 619
Cdd:PLN02939 294 QYDcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAN--VSKFSSYkVELLQQKLKLLEERLQASD 371

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4758648   620 KKMEEnekelaacQLRISQHEakIKSLTEYLQNV--EQKKRQLEESVDALSEEL 671
Cdd:PLN02939 372 HEIHS--------YIQLYQES--IKEFQDTLSKLkeESKKRSLEHPADDMPSEF 415
COG5022 COG5022
Myosin heavy chain [General function prediction only];
423-662 8.59e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.06  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   423 EEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAE--------LNRLQAENDASKE-EVKEVLQ 493
Cdd:COG5022  878 ELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEliarlkklLNNIDLEEGPSIEyVKLPELN 957

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   494 ALEELAVNYDQKSQEVEDKTKEYELL-------SDELNQKSATLASIDAELQKLKEMTNHQKKRAAEM--MASLLKDLAE 564
Cdd:COG5022  958 KLHEVESKLKETSEEYEDLLKKSTILvregnkaNSELKNFKKELAELSKQYGALQESTKQLKELPVEVaeLQSASKIISS 1037

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   565 IGIAVGN-NDVKQPEGTGMIDEEFTVARLY-ISKMKSEVKTMVKRCKQLESTQTESN----KKMEENEKELA----ACQL 634
Cdd:COG5022 1038 ESTELSIlKPLQKLKGLLLLENNQLQARYKaLKLRRENSLLDDKQLYQLESTENLLKtinvKDLEVTNRNLVkpanVLQF 1117

                        250       260       270
                 ....*....|....*....|....*....|....
gi 4758648   635 RISQ------HEAKIKSLTEYLQNVEQKKRQLEE 662
Cdd:COG5022 1118 IVAQmiklnlLQEISKFLSQLVNTLEPVFQKLSV 1151
PRK01156 PRK01156
chromosome segregation protein; Provisional
 417-631 9.05e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   417 ERRKCEEEIAKlYKQLDDKDEEI----NQQSQLVEK-LKTQMLDQE------ELLASTRRDQDNMQAELNRLQAENDAS- 484
Cdd:PRK01156 510 ESEEINKSINE-YNKIESARADLedikIKINELKDKhDKYEEIKNRykslklEDLDSKRTSWLNALAVISLIDIETNRSr 588

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758648   485 KEEVKEVLQALE----ELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEmMASLLK 560
Cdd:PRK01156 589 SNEIKKQLNDLEsrlqEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIP 667

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758648   561 DLAEIGIAVGNNDVKQPEGTGMIDEeftvARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAA 631
Cdd:PRK01156 668 DLKEITSRINDIEDNLKKSRKALDD----AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
 
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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