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Conserved domains on  [gi|116686122|ref|NP_036442|]
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chromosome-associated kinesin KIF4A [Homo sapiens]

Protein Classification

KISc_KIF4 and iSH2_PI3K_IA_R domain-containing protein( domain architecture ID 12916435)

KISc_KIF4 and iSH2_PI3K_IA_R domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
8-337 0e+00

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: 626.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    8 IPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   88 GQTGSGKTYSMGGAYTAEqENEPTVGVIPRVIQLLFKEID-KKSDFEFTLKVSYLEIYNEEILDLLCPSR-EKAQINIRE 165
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAE-EDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKK---------SDKNSSFRSKL 236
Cdd:cd01372   160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKngpiapmsaDDKNSTFTSKF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  237 HLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD-DKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 315
Cdd:cd01372   240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDeSKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
                         330       340
                  ....*....|....*....|..
gi 116686122  316 ADSNLEETLNTLRYADRARKIK 337
Cdd:cd01372   320 ADSNFEETLNTLKYANRARNIK 341
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-1033 5.42e-13

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  517 LRQAQMSKELVELNKALALKEALARKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAklsE 596
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARL---E 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  597 RRRK----RLQELEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV 672
Cdd:COG1196   309 ERRReleeRLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  673 IQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIE 752
Cdd:COG1196   386 EELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  753 VMVSTEEAKRHLNDLLEDRKILAQDVAQLK-----EKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEM 827
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  828 EFRSAQ------------IADLQQKLL------------DAESEDRPKQRWENIATILEAKCALKYLigELVSSKIQVSK 883
Cdd:COG1196   545 AAALQNivveddevaaaaIEYLKAAKAgratflpldkirARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTL 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  884 LESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKvlyLLSQLQQSQMAEKQLEESVSEKEQQLLSTL 963
Cdd:COG1196   623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAELEELAERLAEEELELEEAL 699
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  964 KCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQvASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEK 1033
Cdd:COG1196   700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAER-EELLEELLEEEELLEEEALEELPEPPDLEELERE 768
PRK11281 super family cl46976
mechanosensitive channel MscK;
383-646 9.87e-05

mechanosensitive channel MscK;


The actual alignment was detected with superfamily member PRK11281:

Pssm-ID: 481316 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 9.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  383 ENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERII-LTEQANEKMNAKLE--ELRQhaackLDlQKLVETLED-QE 458
Cdd:PRK11281   66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEaLKDDNDEETRETLStlSLRQ-----LE-SRLAQTLDQlQN 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  459 LKENVEIICNlqQLITQlsdETVACMA-AAIDTAVEQEAQVetspeTSRSSDAFTTQHALRQAQMSKELVELnKALALKE 537
Cdd:PRK11281  140 AQNDLAEYNS--QLVSL---QTQPERAqAALYANSQRLQQI-----RNLLKGGKVGGKALRPSQRVLLQAEQ-ALLNAQN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  538 ALARKMTQNDSQLQPI---QYQY-QDNIKELELEVINLQKEKEELVLEL--QTAKKDANQAKLSERRRKRL--QELegqi 609
Cdd:PRK11281  209 DLQRKSLEGNTQLQDLlqkQRDYlTARIQRLEHQLQLLQEAINSKRLTLseKTVQEAQSQDEAARIQANPLvaQEL---- 284
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 116686122  610 aDLKKKLNEqskllKLKESTERTVSKLNQEIRmMKNQ 646
Cdd:PRK11281  285 -EINLQLSQ-----RLLKATEKLNTLTQQNLR-VKNW 314
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
8-337 0e+00

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: 626.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    8 IPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   88 GQTGSGKTYSMGGAYTAEqENEPTVGVIPRVIQLLFKEID-KKSDFEFTLKVSYLEIYNEEILDLLCPSR-EKAQINIRE 165
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAE-EDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKK---------SDKNSSFRSKL 236
Cdd:cd01372   160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKngpiapmsaDDKNSTFTSKF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  237 HLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD-DKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 315
Cdd:cd01372   240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDeSKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
                         330       340
                  ....*....|....*....|..
gi 116686122  316 ADSNLEETLNTLRYADRARKIK 337
Cdd:cd01372   320 ADSNFEETLNTLKYANRARNIK 341
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-343 1.18e-163

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: 489.78  E-value: 1.18e-163
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122      9 PVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV-------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122     82 ATVLAYGQTGSGKTYSMGGayTAEQEneptvGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSREKaq 160
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG--TPDSP-----GIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKK-- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR-SKLHLV 239
Cdd:smart00129  152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKaSKLNLV 231
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    240 DLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSN 319
Cdd:smart00129  232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSN 311
                           330       340
                    ....*....|....*....|....
gi 116686122    320 LEETLNTLRYADRARKIKNKPIVN 343
Cdd:smart00129  312 LEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
15-336 5.39e-155

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 467.05  E-value: 5.39e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    15 RCRPLVPKEISEGCQMCLSFVPGEPQVV-------VGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVesshltnKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    88 GQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ-INIRE 165
Cdd:pfam00225   81 GQTGSGKTYTMEG-------SDEQPGIIPRALEDLFDRIQKtKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSD--KNSSFRSKLHLVDLAG 243
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggEESVKTGKLNLVDLAG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   244 SERQKKT-KAEGDRLKEGININRGLLCLGNVISALGDDKKGgFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEE 322
Cdd:pfam00225  234 SERASKTgAAGGQRLKEAANINKSLSALGNVISALADKKSK-HIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEE 312
                          330
                   ....*....|....
gi 116686122   323 TLNTLRYADRARKI 336
Cdd:pfam00225  313 TLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
43-352 9.64e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 301.66  E-value: 9.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   43 VGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGaytaeQENEPtvGVIPRVIQLL 122
Cdd:COG5059    52 KSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG-----TEEEP--GIIPLSLKEL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  123 FKEIDKKSDF-EFTLKVSYLEIYNEEILDLLCPSREKaqINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVA 201
Cdd:COG5059   125 FSKLEDLSMTkDFAVSISYLEIYNEKIYDLLSPNEES--LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  202 STAMNSQSSRSHAIFTISLEQRKKsDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDK 281
Cdd:COG5059   203 STEINDESSRSHSIFQIELASKNK-VSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  282 KGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVN----IDPQTAELN 352
Cdd:COG5059   282 KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNsssdSSREIEEIK 356
PLN03188 PLN03188
kinesin-12 family protein; Provisional
10-355 1.61e-70

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 259.48  E-value: 1.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEgcqMCLSFVPGEPQVVVGtdKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQ 89
Cdd:PLN03188  100 VKVIVRMKPLNKGEEGE---MIVQKMSNDSLTING--QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   90 TGSGKTYSM-GGAYTAEQEN--EPTVGVIPRVIQLLFKEIDKKS------DFEFTLKVSYLEIYNEEILDLLCPSREKAQ 160
Cdd:PLN03188  175 TGSGKTYTMwGPANGLLEEHlsGDQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLDPSQKNLQ 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  161 IniREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKS--DKNSSFR-SKLH 237
Cdd:PLN03188  255 I--REDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSvaDGLSSFKtSRIN 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  238 LVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGG---FVPYRDSKLTRLLQDSLGGNSHTLMIACVS 314
Cdd:PLN03188  333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 116686122  315 PADSNLEETLNTLRYADRARKIKNKPIVNIDPQTaELNHLK 355
Cdd:PLN03188  413 PSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQD-DVNFLR 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-1033 5.42e-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: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  517 LRQAQMSKELVELNKALALKEALARKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAklsE 596
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARL---E 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  597 RRRK----RLQELEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV 672
Cdd:COG1196   309 ERRReleeRLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  673 IQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIE 752
Cdd:COG1196   386 EELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  753 VMVSTEEAKRHLNDLLEDRKILAQDVAQLK-----EKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEM 827
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  828 EFRSAQ------------IADLQQKLL------------DAESEDRPKQRWENIATILEAKCALKYLigELVSSKIQVSK 883
Cdd:COG1196   545 AAALQNivveddevaaaaIEYLKAAKAgratflpldkirARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTL 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  884 LESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKvlyLLSQLQQSQMAEKQLEESVSEKEQQLLSTL 963
Cdd:COG1196   623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAELEELAERLAEEELELEEAL 699
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  964 KCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQvASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEK 1033
Cdd:COG1196   700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAER-EELLEELLEEEELLEEEALEELPEPPDLEELERE 768
PTZ00121 PTZ00121
MAEBL; Provisional
491-1004 1.17e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  491 AVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELevin 570
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA---- 1320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  571 lQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQL 650
Cdd:PTZ00121 1321 -KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  651 MRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEA--------AAANKRLKDALQKQR 722
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeakkKAEEAKKADEAKKKA 1479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  723 EVADKRKETQSRGMEGTA----ARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRR 798
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKkadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  799 TFSLTEVRGQVSESED--------SITKQIESLETEmEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYL 870
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDknmalrkaEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  871 IGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQ-QHQEKVLYLLSQLQQSQMAEKQLE 949
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKA 1718
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  950 ESVSEKEQQllstLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQK 1004
Cdd:PTZ00121 1719 EELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
385-734 1.44e-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: 62.78  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQhaacklDLQKLVETLED--QELKEN 462
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE------DLSSLEQEIENvkSELKEL 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   463 VEIICNLQQLITQLSDETvacmaaaidTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKaLALKEALARK 542
Cdd:TIGR02169  764 EARIEELEEDLHKLEEAL---------NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEK 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   543 MTQNdsqLQPIQYQYQDNIKELELEVINLQKEKEELVLELqtakkdanqaklsERRRKRLQELEGQIADLKKKLNE-QSK 621
Cdd:TIGR02169  834 EIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-------------EELEAALRDLESRLGDLKKERDElEAQ 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   622 LLKLKESTERTVSKLNQEIRMMKNQRVQLmrQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLR 701
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
                          330       340       350
                   ....*....|....*....|....*....|...
gi 116686122   702 RKTEEAAAANKRLKDALQKQREVADKRKETQSR 734
Cdd:TIGR02169  976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
383-1012 2.50e-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: 55.36  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   383 ENLQSLMEKNQSLVEENEKLsrglseaagqtaqmlERIILTEQANEKMNAKLEELRQHAAcKLDLQKLVETLEDQeLKEN 462
Cdd:pfam02463  173 EALKKLIEETENLAELIIDL---------------EELKLQELKLKEQAKKALEYYQLKE-KLELEEEYLLYLDY-LKLN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   463 VEIICNLQQLITQLSDETvACMAAAIDTAVEQEAQVETSPETSRSSDAFTTqhaLRQAQMSKELVELNKALALKEALARK 542
Cdd:pfam02463  236 EERIDLLQELLRDEQEEI-ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---EELKLLAKEEEELKSELLKLERRKVD 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   543 MTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELV-----LELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLN 617
Cdd:pfam02463  312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEikreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   618 EQSKLLKLKESTERTVSKLN---QEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV----IQLKERDRKRQYELLKLE 690
Cdd:pfam02463  392 LKEEELELKSEEEKEAQLLLelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEkeelEKQELKLLKDELELKKSE 471
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   691 RNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD--KRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLL 768
Cdd:pfam02463  472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   769 EDRKILAQDVAQLKEKKESGENPPPKLRRRTFS----LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDA 844
Cdd:pfam02463  552 EVSATADEVEERQKLVRALTELPLGARKLRLLIpklkLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKD 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   845 ESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCAD--MQKMLFEERNHFAEIETELQAELVR 922
Cdd:pfam02463  632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKaeSELAKEEILRRQLEIKKKEQREKEE 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   923 MEQQHQEKVLYLLS--QLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVA 1000
Cdd:pfam02463  712 LKKLKLEAEELLADrvQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
                          650
                   ....*....|..
gi 116686122  1001 SRQKHLPKDTLL 1012
Cdd:pfam02463  792 KEEKLKAQEEEL 803
PRK11281 PRK11281
mechanosensitive channel MscK;
383-646 9.87e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 9.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  383 ENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERII-LTEQANEKMNAKLE--ELRQhaackLDlQKLVETLED-QE 458
Cdd:PRK11281   66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEaLKDDNDEETRETLStlSLRQ-----LE-SRLAQTLDQlQN 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  459 LKENVEIICNlqQLITQlsdETVACMA-AAIDTAVEQEAQVetspeTSRSSDAFTTQHALRQAQMSKELVELnKALALKE 537
Cdd:PRK11281  140 AQNDLAEYNS--QLVSL---QTQPERAqAALYANSQRLQQI-----RNLLKGGKVGGKALRPSQRVLLQAEQ-ALLNAQN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  538 ALARKMTQNDSQLQPI---QYQY-QDNIKELELEVINLQKEKEELVLEL--QTAKKDANQAKLSERRRKRL--QELegqi 609
Cdd:PRK11281  209 DLQRKSLEGNTQLQDLlqkQRDYlTARIQRLEHQLQLLQEAINSKRLTLseKTVQEAQSQDEAARIQANPLvaQEL---- 284
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 116686122  610 aDLKKKLNEqskllKLKESTERTVSKLNQEIRmMKNQ 646
Cdd:PRK11281  285 -EINLQLSQ-----RLLKATEKLNTLTQQNLR-VKNW 314
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
386-621 1.37e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 42.32  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   386 QSLMEKNQSLVEENEKLSRGLSEAAGQTAQM-----------------LERIILTEQANEKMNAKLEELRQHAACKLD-L 447
Cdd:pfam04849   90 QSLLKQNSVLTERNEALEEQLGSAREEILQLrhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDaL 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   448 QKLVETLEDQELKenveiicnLQQLITQLSDETvacmaaaiDTAVEQEAQVetspetsrssdafttqhalrQAQMSKELV 527
Cdd:pfam04849  170 QEKLRGLEEENLK--------LRSEASHLKTET--------DTYEEKEQQL--------------------MSDCVEQLS 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   528 ELNKALA-LKEALARKMTQNDSQLQPIQyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQ--AKLSErRRKRLQE 604
Cdd:pfam04849  214 EANQQMAeLSEELARKMEENLRQQEEIT-SLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQltSELQE-LQDRYAE 291
                          250
                   ....*....|....*..
gi 116686122   605 LEGQIADLKKKLNEQSK 621
Cdd:pfam04849  292 CLGMLHEAQEELKELRK 308
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
524-702 2.63e-03

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 41.52  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    524 KELVELNKALALKEALARKMTQNDSQLQ-PIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKrL 602
Cdd:smart00533   79 RDLLRLYDSLEGLKEIRQLLESLDGPLLgLLLKVILEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREK-L 157
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    603 QELEGQIADLKKKLNEQSKLLKLKestERTVSKLNQEIRMMKNQRVQL-----MRQMKEDAEKFRQWK-QKKDKEVIQLK 676
Cdd:smart00533  158 EELEEELEELLKKEREELGIDSLK---LGYNKVHGYYIEVTKSEAKKVpkdfiRRSSLKNTERFTTPElKELENELLEAK 234
                           170       180
                    ....*....|....*....|....*..
gi 116686122    677 ERDRKRQYELLK-LERNFQKQSNVLRR 702
Cdd:smart00533  235 EEIERLEKEILReLLEKVLEYLEELRA 261
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
384-617 6.36e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  384 NLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERI-ILTEQanekmnakLEELRqhaacKLDLQKLvetlEDQELKE- 461
Cdd:COG0497   152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELdLLRFQ--------LEELE-----AAALQPG----EEEELEEe 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  462 -----NVE-IICNLQQLITQLSDETVACM------------AAAIDTAVE------QEAQVETSpETSRSsdaftTQHAL 517
Cdd:COG0497   215 rrrlsNAEkLREALQEALEALSGGEGGALdllgqalralerLAEYDPSLAelaerlESALIELE-EAASE-----LRRYL 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  518 RQAQMS-KELVELNKALALKEALARKmtqndsqlqpiqyqYQDNIKEL---------ELEVI-NLQKEKEELVLELQTAK 586
Cdd:COG0497   289 DSLEFDpERLEEVEERLALLRRLARK--------------YGVTVEELlayaeelraELAELeNSDERLEELEAELAEAE 354
                         250       260       270
                  ....*....|....*....|....*....|...
gi 116686122  587 KDANQA--KLSERRRKRLQELEGQIADLKKKLN 617
Cdd:COG0497   355 AELLEAaeKLSAARKKAAKKLEKAVTAELADLG 387
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
8-337 0e+00

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: 626.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    8 IPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   88 GQTGSGKTYSMGGAYTAEqENEPTVGVIPRVIQLLFKEID-KKSDFEFTLKVSYLEIYNEEILDLLCPSR-EKAQINIRE 165
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAE-EDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKK---------SDKNSSFRSKL 236
Cdd:cd01372   160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKngpiapmsaDDKNSTFTSKF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  237 HLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD-DKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 315
Cdd:cd01372   240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDeSKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
                         330       340
                  ....*....|....*....|..
gi 116686122  316 ADSNLEETLNTLRYADRARKIK 337
Cdd:cd01372   320 ADSNFEETLNTLKYANRARNIK 341
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-343 1.18e-163

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: 489.78  E-value: 1.18e-163
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122      9 PVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV-------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122     82 ATVLAYGQTGSGKTYSMGGayTAEQEneptvGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSREKaq 160
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG--TPDSP-----GIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKK-- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR-SKLHLV 239
Cdd:smart00129  152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKaSKLNLV 231
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    240 DLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSN 319
Cdd:smart00129  232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSN 311
                           330       340
                    ....*....|....*....|....
gi 116686122    320 LEETLNTLRYADRARKIKNKPIVN 343
Cdd:smart00129  312 LEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
15-336 5.39e-155

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 467.05  E-value: 5.39e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    15 RCRPLVPKEISEGCQMCLSFVPGEPQVV-------VGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVesshltnKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    88 GQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ-INIRE 165
Cdd:pfam00225   81 GQTGSGKTYTMEG-------SDEQPGIIPRALEDLFDRIQKtKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSD--KNSSFRSKLHLVDLAG 243
Cdd:pfam00225  154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggEESVKTGKLNLVDLAG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   244 SERQKKT-KAEGDRLKEGININRGLLCLGNVISALGDDKKGgFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEE 322
Cdd:pfam00225  234 SERASKTgAAGGQRLKEAANINKSLSALGNVISALADKKSK-HIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEE 312
                          330
                   ....*....|....
gi 116686122   323 TLNTLRYADRARKI 336
Cdd:pfam00225  313 TLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
9-334 6.08e-150

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: 453.64  E-value: 6.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    9 PVRVALRCRPLVPKEiSEGCQMCLSFVPG------EPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNA 82
Cdd:cd00106     1 NVRVAVRVRPLNGRE-ARSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   83 TVLAYGQTGSGKTYSMGGAYTAEQeneptvGVIPRVIQLLFKEIDK--KSDFEFTLKVSYLEIYNEEILDLLCPSrEKAQ 160
Cdd:cd00106    80 TIFAYGQTGSGKTYTMLGPDPEQR------GIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPV-PKKP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKS-DKNSSFRSKLHLV 239
Cdd:cd00106   153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREkSGESVTSSKLNLV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  240 DLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDdKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSN 319
Cdd:cd00106   233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSEN 311
                         330
                  ....*....|....*
gi 116686122  320 LEETLNTLRYADRAR 334
Cdd:cd00106   312 FEETLSTLRFASRAK 326
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
10-343 4.81e-118

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: 370.91  E-value: 4.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV------------GTDKSFTYDFVF------DPS-TEQEEVFNTAVA 70
Cdd:cd01365     3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNpkqadknnkatrEVPKSFSFDYSYwshdseDPNyASQEQVYEDLGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   71 PLIKGVFKGYNATVLAYGQTGSGKTYSMGGAytaeqENEPtvGVIPRVIQLLFKEIDKKSDFE--FTLKVSYLEIYNEEI 148
Cdd:cd01365    83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT-----QEQP--GIIPRLCEDLFSRIADTTNQNmsYSVEVSYMEIYNEKV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  149 LDLLCPSREKAQIN--IREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRK-- 224
Cdd:cd01365   156 RDLLNPKPKKNKGNlkVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRhd 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  225 -KSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGG------FVPYRDSKLTRLL 297
Cdd:cd01365   236 aETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskkkssFIPYRDSVLTWLL 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 116686122  298 QDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVN 343
Cdd:cd01365   316 KENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
10-338 7.51e-116

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: 363.84  E-value: 7.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGcQMCLSFVPGEPQVVVGTD-----KSFTYDFVFDPSTEQEEVFNTaVAPLIKGVFKGYNATV 84
Cdd:cd01366     4 IRVFCRVRPLLPSEENED-TSHITFPDEDGQTIELTSigakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   85 LAYGQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEI--DKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ-I 161
Cdd:cd01366    82 FAYGQTGSGKTYTMEG-------PPESPGIIPRALQELFNTIkeLKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKkL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  162 NIREDPKEG-IKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSfRSKLHLVD 240
Cdd:cd01366   155 EIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEIS-VGKLNLVD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  241 LAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGddKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNL 320
Cdd:cd01366   234 LAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR--QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNL 311
                         330
                  ....*....|....*...
gi 116686122  321 EETLNTLRYADRARKIKN 338
Cdd:cd01366   312 NETLNSLRFASKVNSCEL 329
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
10-336 3.97e-115

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: 362.16  E-value: 3.97e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTD--------KSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:cd01371     3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkataneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   82 ATVLAYGQTGSGKTYSMGGayTAEQENEPtvGVIPRVIQLLFKEIDKKSDF-EFTLKVSYLEIYNEEILDLLCPSREKaQ 160
Cdd:cd01371    83 GTIFAYGQTGTGKTYTMEG--KREDPELR--GIIPNSFAHIFGHIARSQNNqQFLVRVSYLEIYNEEIRDLLGKDQTK-R 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKK-SDKNSSFR-SKLHL 238
Cdd:cd01371   158 LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgEDGENHIRvGKLNL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  239 VDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGgFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADS 318
Cdd:cd01371   238 VDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKST-HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADY 316
                         330
                  ....*....|....*...
gi 116686122  319 NLEETLNTLRYADRARKI 336
Cdd:cd01371   317 NYDETLSTLRYANRAKNI 334
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
10-336 7.22e-115

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: 360.88  E-value: 7.22e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGCQmCLSFVPGEPQVVVGTDK-SFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYG 88
Cdd:cd01374     2 ITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYLVEPPStSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   89 QTGSGKTYSMGGAytaeqENEPtvGVIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPsrEKAQINIREDPK 168
Cdd:cd01374    81 QTSSGKTFTMSGD-----EDEP--GIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSP--TSQNLKIRDDVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  169 EGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDK--NSSFRSKLHLVDLAGSER 246
Cdd:cd01374   152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELeeGTVRVSTLNLIDLAGSER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  247 QKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNT 326
Cdd:cd01374   232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
                         330
                  ....*....|
gi 116686122  327 LRYADRARKI 336
Cdd:cd01374   312 LKFASRAKKI 321
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
10-336 1.76e-114

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: 360.89  E-value: 1.76e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGC--------QMCLSFVPGEPQVVV--------------GTDKSFTYDFVFDPSTEQEEVFNT 67
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFrrivkvmdNHMLVFDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   68 AVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAytaeqENEPtvGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNE 146
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT-----PQEP--GLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  147 EILDLLCPSreKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQ--RK 224
Cdd:cd01370   155 TIRDLLNPS--SGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqdKT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  225 KSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD-DKKGGFVPYRDSKLTRLLQDSLGG 303
Cdd:cd01370   233 ASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADpGKKNKHIPYRDSKLTRLLKDSLGG 312
                         330       340       350
                  ....*....|....*....|....*....|...
gi 116686122  304 NSHTLMIACVSPADSNLEETLNTLRYADRARKI 336
Cdd:cd01370   313 NCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
10-343 2.95e-110

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: 349.70  E-value: 2.95e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV--------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   82 ATVLAYGQTGSGKTYSMGGAYTAEQ----ENEPTVGVIPRVIQLLFKEIDKkSDFEFTLKVSYLEIYNEEILDLLCPSRE 157
Cdd:cd01364    84 CTIFAYGQTGTGKTYTMEGDRSPNEeytwELDPLAGIIPRTLHQLFEKLED-NGTEYSVKVSYLEIYNEELFDLLSPSSD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  158 KA-QINIREDP--KEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR- 233
Cdd:cd01364   163 VSeRLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVk 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  234 -SKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDdkKGGFVPYRDSKLTRLLQDSLGGNSHTLMIAC 312
Cdd:cd01364   243 iGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE--RAPHVPYRESKLTRLLQDSLGGRTKTSIIAT 320
                         330       340       350
                  ....*....|....*....|....*....|.
gi 116686122  313 VSPADSNLEETLNTLRYADRARKIKNKPIVN 343
Cdd:cd01364   321 ISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
10-336 5.89e-109

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: 345.08  E-value: 5.89e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEGCQMCLSFvPGEPQVVVGTD---KSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLA 86
Cdd:cd01369     4 IKVVCRFRPLNELEVLQGSKSIVKF-DPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   87 YGQTGSGKTYSMGGAytaeQENEPTVGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSreKAQINIRE 165
Cdd:cd01369    83 YGQTSSGKTYTMEGK----LGDPESMGIIPRIVQDIFETIYSmDENLEFHVKVSYFEIYMEKIRDLLDVS--KTNLSVHE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSfRSKLHLVDLAGSE 245
Cdd:cd01369   157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKK-SGKLYLVDLAGSE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  246 RQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKgGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLN 325
Cdd:cd01369   236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK-THIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLS 314
                         330
                  ....*....|.
gi 116686122  326 TLRYADRARKI 336
Cdd:cd01369   315 TLRFGQRAKTI 325
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
9-345 8.04e-106

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: 337.56  E-value: 8.04e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    9 PVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVG-TDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:cd01373     2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   88 GQTGSGKTYSM-GGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSD-----FEFTLKVSYLEIYNEEILDLLCPSreKAQI 161
Cdd:cd01373    82 GQTGSGKTYTMwGPSESDNESPHGLRGVIPRIFEYLFSLIQREKEkagegKSFLCKCSFLEIYNEQIYDLLDPA--SRNL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  162 NIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQR-KKSDKNSSFRSKLHLVD 240
Cdd:cd01373   160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWeKKACFVNIRTSRLNLVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  241 LAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGF--VPYRDSKLTRLLQDSLGGNSHTLMIACVSPADS 318
Cdd:cd01373   240 LAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQrhVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSK 319
                         330       340
                  ....*....|....*....|....*..
gi 116686122  319 NLEETLNTLRYADRARKIKNKPIVNID 345
Cdd:cd01373   320 CFGETLSTLRFAQRAKLIKNKAVVNED 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
43-352 9.64e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 301.66  E-value: 9.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   43 VGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGaytaeQENEPtvGVIPRVIQLL 122
Cdd:COG5059    52 KSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG-----TEEEP--GIIPLSLKEL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  123 FKEIDKKSDF-EFTLKVSYLEIYNEEILDLLCPSREKaqINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVA 201
Cdd:COG5059   125 FSKLEDLSMTkDFAVSISYLEIYNEKIYDLLSPNEES--LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  202 STAMNSQSSRSHAIFTISLEQRKKsDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDK 281
Cdd:COG5059   203 STEINDESSRSHSIFQIELASKNK-VSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  282 KGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVN----IDPQTAELN 352
Cdd:COG5059   282 KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNsssdSSREIEEIK 356
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
9-334 2.19e-82

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: 272.45  E-value: 2.19e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    9 PVRVALRCRPLVPKEISEGCQMCLSFVpGEPQVVV------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNA 82
Cdd:cd01376     1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   83 TVLAYGQTGSGKTYSMGGaytaeQENEPtvGVIPRVIQLLFkEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSreKAQIN 162
Cdd:cd01376    80 TVFAYGSTGAGKTFTMLG-----SPEQP--GLMPLTVMDLL-QMTRKEAWALSFTMSYLEIYQEKILDLLEPA--SKELV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  163 IREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFRSKLHLVDLA 242
Cdd:cd01376   150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  243 GSERQKKTKAEGDRLKEGININRGLLCLGNVISALgdDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEE 322
Cdd:cd01376   230 GSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL--NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQD 307
                         330
                  ....*....|..
gi 116686122  323 TLNTLRYADRAR 334
Cdd:cd01376   308 TLSTLNFAARSR 319
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
45-334 3.30e-78

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: 261.36  E-value: 3.30e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   45 TDKSFTYDFVFDpSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAytaeQENEPTVGVIPRVIQLLFK 124
Cdd:cd01375    46 EDWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGG----TENYKHRGIIPRALQQVFR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  125 EIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ----INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTV 200
Cdd:cd01375   121 MIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPsvtpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRII 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  201 ASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR-SKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD 279
Cdd:cd01375   201 ASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYItSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD 280
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  280 dKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRAR 334
Cdd:cd01375   281 -KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
9-332 9.04e-77

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: 256.84  E-value: 9.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    9 PVRVALRCRPLVPKEISEGCQMCLSfVPGEPQVVV------------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGV 76
Cdd:cd01367     1 KIKVCVRKRPLNKKEVAKKEIDVVS-VPSKLTLIVhepklkvdltkyIENHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   77 FKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTlkVSYLEIYNEEILDLLcpsR 156
Cdd:cd01367    80 FEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVT--VSFFEIYGGKVFDLL---N 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  157 EKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKksdKNSSFrSKL 236
Cdd:cd01367   155 RKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLH-GKL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  237 HLVDLAGSERQKKTKAEG-DRLKEGININRGLLCLGNVISALGDDKKggFVPYRDSKLTRLLQDSL-GGNSHTLMIACVS 314
Cdd:cd01367   231 SFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA--HIPFRGSKLTQVLKDSFiGENSKTCMIATIS 308
                         330
                  ....*....|....*...
gi 116686122  315 PADSNLEETLNTLRYADR 332
Cdd:cd01367   309 PGASSCEHTLNTLRYADR 326
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
9-334 3.09e-75

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: 253.09  E-value: 3.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    9 PVRVALRCRPLVPKEISEGCQMCL------SFVPGEPQVVVGTDKS---------FTYDFVFDPSTEQEEVFNTAVAPLI 73
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIevinstTVVLHPPKGSAANKSErnggqketkFSFSKVFGPNTTQKEFFQGTALPLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   74 KGVFKGYNATVLAYGQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEIDKKSDFeftlkVSYLEIYNEEILDLLC 153
Cdd:cd01368    82 QDLLHGKNGLLFTYGVTNSGKTYTMQG-------SPGDGGILPRSLDVIFNSIGGYSVF-----VSYIEIYNEYIYDLLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  154 PS-----REKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQ------ 222
Cdd:cd01368   150 PSpssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQapgdsd 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  223 -RKKSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGF---VPYRDSKLTRLLQ 298
Cdd:cd01368   230 gDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTnkmVPFRDSKLTHLFQ 309
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 116686122  299 DSLGGNSHTLMIACVSPADSNLEETLNTLRYADRAR 334
Cdd:cd01368   310 NYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
10-355 1.61e-70

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 259.48  E-value: 1.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   10 VRVALRCRPLVPKEISEgcqMCLSFVPGEPQVVVGtdKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQ 89
Cdd:PLN03188  100 VKVIVRMKPLNKGEEGE---MIVQKMSNDSLTING--QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   90 TGSGKTYSM-GGAYTAEQEN--EPTVGVIPRVIQLLFKEIDKKS------DFEFTLKVSYLEIYNEEILDLLCPSREKAQ 160
Cdd:PLN03188  175 TGSGKTYTMwGPANGLLEEHlsGDQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLDPSQKNLQ 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  161 IniREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKS--DKNSSFR-SKLH 237
Cdd:PLN03188  255 I--REDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSvaDGLSSFKtSRIN 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  238 LVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGG---FVPYRDSKLTRLLQDSLGGNSHTLMIACVS 314
Cdd:PLN03188  333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 116686122  315 PADSNLEETLNTLRYADRARKIKNKPIVNIDPQTaELNHLK 355
Cdd:PLN03188  413 PSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQD-DVNFLR 452
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
46-315 1.80e-22

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: 95.49  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   46 DKSFTYDFVFDPSTEQEEVFNTAvAPLIKGVFKGYN-ATVLAYGQTGSGKTYSMggaytaeqeneptVGVIPRVIQLLFK 124
Cdd:cd01363    17 SKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM-------------KGVIPYLASVAFN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  125 EIDKKS-DFEFTLKVSYLEIYNeEILDLLcPSREKAqiniredpkegikivgltektvlvaldtvscleqGNnsrtvAST 203
Cdd:cd01363    83 GINKGEtEGWVYLTEITVTLED-QILQAN-PILEAF----------------------------------GN-----AKT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  204 AMNSQSSRSHAIFTIsleqrkksdknssfrsklhLVDLAGSERqkktkaegdrlkeginINRGLLCLGNVISAlgddkkg 283
Cdd:cd01363   122 TRNENSSRFGKFIEI-------------------LLDIAGFEI----------------INESLNTLMNVLRA------- 159
                         250       260       270
                  ....*....|....*....|....*....|..
gi 116686122  284 gfvpyrdskltrllqdslggnSHTLMIACVSP 315
Cdd:cd01363   160 ---------------------TRPHFVRCISP 170
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
3-152 4.39e-17

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 79.19  E-value: 4.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122     3 EEVKGiPVRVALRCRPLVPKEisegCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTaVAPLIKGVFKGYNA 82
Cdd:pfam16796   16 QELKG-NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNV 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122    83 TVLAYGQTGSGKtysmggaytaeqenepTVGVIPRVIQLLFKEI-DKKSDFEFTLKVSYLEIYNEEILDLL 152
Cdd:pfam16796   90 CIFAYGQTGSGS----------------NDGMIPRAREQIFRFIsSLKKGWKYTIELQFVEIYNESSQDLL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-1033 5.42e-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: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  517 LRQAQMSKELVELNKALALKEALARKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAklsE 596
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARL---E 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  597 RRRK----RLQELEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV 672
Cdd:COG1196   309 ERRReleeRLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  673 IQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIE 752
Cdd:COG1196   386 EELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  753 VMVSTEEAKRHLNDLLEDRKILAQDVAQLK-----EKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEM 827
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  828 EFRSAQ------------IADLQQKLL------------DAESEDRPKQRWENIATILEAKCALKYLigELVSSKIQVSK 883
Cdd:COG1196   545 AAALQNivveddevaaaaIEYLKAAKAgratflpldkirARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTL 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  884 LESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKvlyLLSQLQQSQMAEKQLEESVSEKEQQLLSTL 963
Cdd:COG1196   623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAELEELAERLAEEELELEEAL 699
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  964 KCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQvASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEK 1033
Cdd:COG1196   700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAER-EELLEELLEEEELLEEEALEELPEPPDLEELERE 768
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
385-971 3.31e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQhaacklDLQKLVETLEDQELKENVE 464
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA------EEYELLAELARLEQDIARL 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  465 iicnlQQLITQLSDEtvacmaaaIDTAVEQEAQVETspetsrssdafttQHALRQAQMSKELVELNKALALKEALARKMT 544
Cdd:COG1196   308 -----EERRRELEER--------LEELEEELAELEE-------------ELEELEEELEELEEELEEAEEELEEAEAELA 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  545 QNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLK 624
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  625 LKESTErtvsklnqeirmmknqrvqlmrqmkedaekfRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT 704
Cdd:COG1196   442 EALEEA-------------------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  705 EEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVkNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEK 784
Cdd:COG1196   491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL-IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  785 KESGEN--PPPKLRRRTFSLTEVRGQVSESEdsitkqIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILE 862
Cdd:COG1196   570 KAGRATflPLDKIRARAALAAALARGAIGAA------VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  863 AKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQ 942
Cdd:COG1196   644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
                         570       580
                  ....*....|....*....|....*....
gi 116686122  943 MAEKQLEESVSEKEQQLLSTLKCQDEELE 971
Cdd:COG1196   724 EALEEQLEAEREELLEELLEEEELLEEEA 752
PTZ00121 PTZ00121
MAEBL; Provisional
491-1004 1.17e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  491 AVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELevin 570
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA---- 1320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  571 lQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQL 650
Cdd:PTZ00121 1321 -KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  651 MRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEA--------AAANKRLKDALQKQR 722
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeakkKAEEAKKADEAKKKA 1479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  723 EVADKRKETQSRGMEGTA----ARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRR 798
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKkadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  799 TFSLTEVRGQVSESED--------SITKQIESLETEmEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYL 870
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDknmalrkaEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  871 IGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQ-QHQEKVLYLLSQLQQSQMAEKQLE 949
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKA 1718
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  950 ESVSEKEQQllstLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQK 1004
Cdd:PTZ00121 1719 EELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
385-734 1.44e-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: 62.78  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQhaacklDLQKLVETLED--QELKEN 462
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE------DLSSLEQEIENvkSELKEL 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   463 VEIICNLQQLITQLSDETvacmaaaidTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKaLALKEALARK 542
Cdd:TIGR02169  764 EARIEELEEDLHKLEEAL---------NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEK 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   543 MTQNdsqLQPIQYQYQDNIKELELEVINLQKEKEELVLELqtakkdanqaklsERRRKRLQELEGQIADLKKKLNE-QSK 621
Cdd:TIGR02169  834 EIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-------------EELEAALRDLESRLGDLKKERDElEAQ 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   622 LLKLKESTERTVSKLNQEIRMMKNQRVQLmrQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLR 701
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
                          330       340       350
                   ....*....|....*....|....*....|...
gi 116686122   702 RKTEEAAAANKRLKDALQKQREVADKRKETQSR 734
Cdd:TIGR02169  976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
558-847 4.27e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  558 QDNIKELE--LEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSK 635
Cdd:COG1196   192 EDILGELErqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  636 LNQEIRMMK---NQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANK 712
Cdd:COG1196   272 LRLELEELElelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  713 RLKDALQKQREVADKRKETQSRGMEGTAARVKNW------LGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKE 786
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAeelleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122  787 SGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESE 847
Cdd:COG1196   432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
PTZ00121 PTZ00121
MAEBL; Provisional
493-992 5.38e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 5.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  493 EQEAQVEtspETSRSSDAFTTQHALRQAQMSKELVELNKalaLKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQ 572
Cdd:PTZ00121 1221 EDAKKAE---AVKKAEEAKKDAEEAKKAEEERNNEEIRK---FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  573 KEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMR 652
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  653 QMKEDAEKFRQWKQKKDK--EVIQLKERDRKRQYELLKLERNfQKQSNVLRRKTEEAAAAN--------KRLKDALQKQR 722
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKKADeakkkaeeAKKADEAKKKA 1453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  723 EVADKRKETQSRGMEGTAARVKNWLGNEI----EVMVSTEEAKRHLNDL--LEDRKILAQDVAQLKEKKESGENPPPKLR 796
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAkkadEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  797 RRTFSLTEVRgQVSESEDsiTKQIESLETEMEFRSAqiadlQQKLLDAESEDRPKQRWENIATILEAKC-ALKYLIGELV 875
Cdd:PTZ00121 1534 KKADEAKKAE-EKKKADE--LKKAEELKKAEEKKKA-----EEAKKAEEDKNMALRKAEEAKKAEEARIeEVMKLYEEEK 1605
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  876 SSKIQVSKLESSLKQSktscADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAE---KQLEES- 951
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK----AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAk 1681
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 116686122  952 -VSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQ 992
Cdd:PTZ00121 1682 kAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
598-994 1.26e-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: 59.69  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   598 RRKRLQELEGQIADLKKKLNEQSKLLKlkestertvsKLNQEIRMMKNQRVQLMRQMKEDAEKFRQwkQKKDKEVIQLKE 677
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALA----------ELRKELEELEEELEQLRKELEELSRQISA--LRKDLARLEAEV 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   678 RDRKRQYELLKLER-NFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETqsrgmegtaarvknwlgneievMVS 756
Cdd:TIGR02168  743 EQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----------------------LKA 800
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   757 TEEAKRHLNDLLEDrkiLAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIAD 836
Cdd:TIGR02168  801 LREALDELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   837 LQqklldaesedrpKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETEL 916
Cdd:TIGR02168  878 LL------------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   917 QAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVS-------------EKEQQLLSTLKCQDEELEKMRevcEQNQQL 983
Cdd:TIGR02168  946 SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyEELKERYDFLTAQKEDLTEAK---ETLEEA 1022
                          410
                   ....*....|..
gi 116686122   984 LRE-NEIIKQKL 994
Cdd:TIGR02168 1023 IEEiDREARERF 1034
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
518-839 1.56e-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: 59.30  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   518 RQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELvlelqTAKKDANQAKLSER 597
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL-----EERLEEAEEELAEA 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   598 RRKRlQELEGQIADLKKKLNEQSKLLKlkeSTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDK---EVIQ 674
Cdd:TIGR02168  781 EAEI-EELEAQIEQLKEELKALREALD---ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElseDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   675 LKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRgmegtaarvknwlgneievm 754
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE-------------------- 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   755 vsTEEAKRHLNDLLEDRKILAQDVAQLKEK-----KESGENPPPKLRRRTFSLTEVRGQVSESEDSITK----------Q 819
Cdd:TIGR02168  917 --LEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieE 994
                          330       340
                   ....*....|....*....|
gi 116686122   820 IESLETEMEFRSAQIADLQQ 839
Cdd:TIGR02168  995 YEELKERYDFLTAQKEDLTE 1014
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
377-993 2.17e-08

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: 58.90  E-value: 2.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   377 ITVEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMlERIILTEQANEKMNAKLEELRQHAACKLdLQKLVETLED 456
Cdd:TIGR00606  431 IRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS-DRILELDQELRKAERELSKAEKNSLTET-LKKEVKSLQN 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   457 QELkENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQ--------------HALRQ--A 520
Cdd:TIGR00606  509 EKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledwlHSKSKeiN 587
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   521 QMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNI------KELELEVINLQKE-----KEELVLELQTAKKDA 589
Cdd:TIGR00606  588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEiekssKQRAMLAGATAVYSQ 667
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   590 NQAKLSERRR------KRLQELEGQIADLKKKLNEQSKLLKLK-ESTERTVSKLNQEIRMMKNQrvqlmrqmkedAEKFR 662
Cdd:TIGR00606  668 FITQLTDENQsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKlKSTESELKKKEKRRDEMLGL-----------APGRQ 736
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   663 QWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDA-----LQKQREVADKRKETQSRGME 737
Cdd:TIGR00606  737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimerFQMELKDVERKIAQQAAKLQ 816
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   738 GtaarvknwlgneIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESedsiT 817
Cdd:TIGR00606  817 G------------SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN----L 880
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   818 KQIESLETEMEFRSAQIADLQQKLLDAESEDRPkqrwenIATILEAKCALKyliGELVSSKiqvsklESSLKQSKTSCAD 897
Cdd:TIGR00606  881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP------LETFLEKDQQEK---EELISSK------ETSNKKAQDKVND 945
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   898 MQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLS------------TLKC 965
Cdd:TIGR00606  946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkiqerwlqdnlTLRK 1025
                          650       660
                   ....*....|....*....|....*...
gi 116686122   966 QDEELEKMREVCEQNQQLLRENEIIKQK 993
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMK 1053
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
527-853 2.41e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.54  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   527 VELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELE--LEVINLQKEKEELVLELQTAKKDANQAKLsERRRKRLQE 604
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaERYQALLKEKREYEGYELLKEKEALERQK-EAIERQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   605 LEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIR-MMKNQRVQLMRQMKE---------DAEKFRQWKQKK-DKEVI 673
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRL---EEIEQLLEELNKKIKdLGEEEQLRVKEKIGEleaeiasleRSIAEKERELEDaEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   674 QLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEgtaarvknwlgneieV 753
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------------Y 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   754 MVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQ 833
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
                          330       340
                   ....*....|....*....|
gi 116686122   834 IADLQQKLLDAESEDRPKQR 853
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQR 490
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
657-996 5.16e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 5.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   657 DAEKFRQWKQKKDK-EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDaLQKQREVADKRKETQSRG 735
Cdd:TIGR02169  660 RAPRGGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   736 MEGTAARVKnwlgneiEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKES-----GENPPPKLRRRTFSLTEVRGQVS 810
Cdd:TIGR02169  739 LEELEEDLS-------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   811 ESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESedrpkQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQ 890
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   891 SKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQhQEKVLYLLSQLQQSQMAEKQLEESVSEK--EQQLLSTLKCQDE 968
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEE 965
                          330       340       350
                   ....*....|....*....|....*....|...
gi 116686122   969 ELEKMREVC-----EQNQQLLRENEIIKQKLTL 996
Cdd:TIGR02169  966 EIRALEPVNmlaiqEYEEVLKRLDELKEKRAKL 998
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
383-844 7.51e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 7.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  383 ENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELKEN 462
Cdd:COG1196   341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  463 VEIIcNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARK 542
Cdd:COG1196   421 EELE-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  543 MTQNDSQLQPIQYQYQ-DNIKELELEVINLQKEKEELVLELQTAKkdanQAKLSERRRKRLQELEGQIADLKKKLNEQSK 621
Cdd:COG1196   500 EADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYEAALEAAL----AAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  622 LLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFR----------QWKQKKDKEVIQLKERDRKRQYELLKLER 691
Cdd:COG1196   576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEG 655
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  692 NFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDR 771
Cdd:COG1196   656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  772 KILAQDVAQLKEKKESGENPPPKLrrrtFSLTEVRGQVseseDSITKQIESL--------------ETEMEFRSAQIADL 837
Cdd:COG1196   736 ELLEELLEEEELLEEEALEELPEP----PDLEELEREL----ERLEREIEALgpvnllaieeyeelEERYDFLSEQREDL 807
                         490
                  ....*....|
gi 116686122  838 QQ---KLLDA 844
Cdd:COG1196   808 EEareTLEEA 817
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
516-810 7.58e-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: 56.99  E-value: 7.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   516 ALRQAQMS---KELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQT-----AKK 587
Cdd:TIGR02168  221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneiSRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   588 DANQAKLSERRR---KRLQELEGQIADLKKKLNEQSKLLKlkestertvsKLNQEIRMMKNQRVQLMRQMKEDAEKFRQW 664
Cdd:TIGR02168  301 EQQKQILRERLAnleRQLEELEAQLEELESKLDELAEELA----------ELEEKLEELKEELESLEAELEELEAELEEL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   665 KQKKDKeviQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVK 744
Cdd:TIGR02168  371 ESRLEE---LEEQLETLRS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116686122   745 NWLgneievmvstEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVS 810
Cdd:TIGR02168  447 EEL----------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
460-988 9.59e-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: 56.52  E-value: 9.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   460 KENVEIICNLQQL--ITQLSDETVACMAAAIDTAVEQEAQVETspETSRSSDAFTTQHALRQAQmSKELVELNKALALKE 537
Cdd:TIGR00618  163 KEKKELLMNLFPLdqYTQLALMEFAKKKSLHGKAELLTLRSQL--LTLCTPCMPDTYHERKQVL-EKELKHLREALQQTQ 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   538 ALARKMTQND------SQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKR---LQELEGQ 608
Cdd:TIGR00618  240 QSHAYLTQKReaqeeqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAqriHTELQSK 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   609 IADLKKKLNEQSKLLKLKESTERTVSKLN----QEIRMMKNQRVQLMR-----QMKEDAEKFRQWKQKK--DKEVIQL-- 675
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIreiscQQHTLTQHIHTLQQQKttLTQKLQSlc 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   676 ----KERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDA-------LQKQREVADKRKETQSRGMEGTAARVK 744
Cdd:TIGR00618  400 keldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitctaqCEKLEKIHLQESAQSLKEREQQLQTKE 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   745 NWLGNEIEVmvSTEEAKRhLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRR------RTFSLTEVRGQVSESEDSITK 818
Cdd:TIGR00618  480 QIHLQETRK--KAVVLAR-LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqrgeqTYAQLETSEEDVYHQLTSERK 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   819 QIESLETEMEfrsaQIADLQQKLldAESEDRPKQRWENIATILEAkcaLKYLIGELVSSKIQVSKLESSLKQSKTSCADM 898
Cdd:TIGR00618  557 QRASLKEQMQ----EIQQSFSIL--TQCDNRSKEDIPNLQNITVR---LQDLTEKLSEAEDMLACEQHALLRKLQPEQDL 627
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   899 QKMLFEERNhfaeIETELQAELVRMEQqhqekvlYLLSQLQQSQ----MAEKQLEESVSEKEQQLLSTLKCQDEELEKMR 974
Cdd:TIGR00618  628 QDVRLHLQQ----CSQELALKLTALHA-------LQLTLTQERVrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
                          570
                   ....*....|....
gi 116686122   975 EVCEQNQQLLRENE 988
Cdd:TIGR00618  697 EMLAQCQTLLRELE 710
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
413-1004 1.29e-07

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: 56.22  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   413 TAQMLERI--ILTEqanekMNAKLEELRQHAACKLDLQKLVETLEDQELkenveiicnlqQLITQLSDETVACMAAAIDT 490
Cdd:TIGR02168  184 TRENLDRLedILNE-----LERQLKSLERQAEKAERYKELKAELRELEL-----------ALLVLRLEELREELEELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   491 AVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVIN 570
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   571 LQKEKEELVLELQTAKKDANQAK-LSERRRKRLQELEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQ 649
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKeELESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIER 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   650 LMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKR-QYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKR 728
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   729 KETQSRG---------MEGTAARVKNWLGNE-------------IEVMVSTEEAKR-----HLNDLL-EDRKILAQDVAQ 780
Cdd:TIGR02168  485 AQLQARLdslerlqenLEGFSEGVKALLKNQsglsgilgvlselISVDEGYEAAIEaalggRLQAVVvENLNAAKKAIAF 564
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   781 LKEKKESGENPPPKLRRRTFSLTEVRGQVSESED---------------------------------------------- 814
Cdd:TIGR02168  565 LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsyllggvlvvddldnalelakklrpg 644
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   815 ---------------SITKQIESLETEMEFRSAQIADLQQKLLDAESEdrpkqrweniatILEAKCALKYLigelvssKI 879
Cdd:TIGR02168  645 yrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEK------------IAELEKALAEL-------RK 705
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   880 QVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEkvlylLSQLQQSQMAEKQLEESVSEKEQQL 959
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEA 780
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 116686122   960 LSTLKCQDEELEKMREVCEQNQQLLREneiIKQKLTLLQVASRQK 1004
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAANL 822
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
383-1012 2.50e-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: 55.36  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   383 ENLQSLMEKNQSLVEENEKLsrglseaagqtaqmlERIILTEQANEKMNAKLEELRQHAAcKLDLQKLVETLEDQeLKEN 462
Cdd:pfam02463  173 EALKKLIEETENLAELIIDL---------------EELKLQELKLKEQAKKALEYYQLKE-KLELEEEYLLYLDY-LKLN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   463 VEIICNLQQLITQLSDETvACMAAAIDTAVEQEAQVETSPETSRSSDAFTTqhaLRQAQMSKELVELNKALALKEALARK 542
Cdd:pfam02463  236 EERIDLLQELLRDEQEEI-ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---EELKLLAKEEEELKSELLKLERRKVD 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   543 MTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELV-----LELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLN 617
Cdd:pfam02463  312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEikreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   618 EQSKLLKLKESTERTVSKLN---QEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV----IQLKERDRKRQYELLKLE 690
Cdd:pfam02463  392 LKEEELELKSEEEKEAQLLLelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEkeelEKQELKLLKDELELKKSE 471
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   691 RNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD--KRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLL 768
Cdd:pfam02463  472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   769 EDRKILAQDVAQLKEKKESGENPPPKLRRRTFS----LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDA 844
Cdd:pfam02463  552 EVSATADEVEERQKLVRALTELPLGARKLRLLIpklkLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKD 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   845 ESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCAD--MQKMLFEERNHFAEIETELQAELVR 922
Cdd:pfam02463  632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKaeSELAKEEILRRQLEIKKKEQREKEE 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   923 MEQQHQEKVLYLLS--QLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVA 1000
Cdd:pfam02463  712 LKKLKLEAEELLADrvQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
                          650
                   ....*....|..
gi 116686122  1001 SRQKHLPKDTLL 1012
Cdd:pfam02463  792 KEEKLKAQEEEL 803
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
636-1025 3.94e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 54.36  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   636 LNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEViQLKERDRKRQYELLKLERN--FQKQSNVLRRKTEEAAAANKR 713
Cdd:pfam17380  271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEEAEKARQaeMDRQAAIYAEQERMAMERERE 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   714 LKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEI----EVMVSTEEAKRHLNDLLED--RKILAQDVAQLKEKKES 787
Cdd:pfam17380  350 LERIRQEERKRELERIRQEEIAMEISRMRELERLQMERqqknERVRQELEAARKVKILEEErqRKIQQQKVEMEQIRAEQ 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   788 GENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETemefrsaQIADLQQKLLDAESEDRPKQRWENIATileakcal 867
Cdd:pfam17380  430 EEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-------QEEERKRKKLELEKEKRDRKRAEEQRR-------- 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   868 KYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEErnhfaeiETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQ 947
Cdd:pfam17380  495 KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-------ERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116686122   948 LEesVSEKEQQLLSTLKcqdeELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKHLPKDTLLSPdssfEYVPPKP 1025
Cdd:pfam17380  568 LE--AMEREREMMRQIV----ESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSP----EWATPSP 635
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
382-745 4.80e-07

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: 54.29  E-value: 4.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   382 SENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQM---LERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQE 458
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   459 LKENVEIICNLQQLITQLSDEtvacMAAAIDTAVEQEAQVetspetSRSSDAFTTQhALRQAQMSKELVELNKALALKEA 538
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEE----LKALREALDELRAEL------TLLNEEAANL-RERLESLERRIAATERRLEDLEE 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   539 LARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAklserrRKRLQELEGQIADLKKKLNE 618
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL------SEELRELESKRSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   619 QSKLLklkESTERTVSKLNQEIRmmkNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERdrkrqyeLLKLERNFQKQSN 698
Cdd:TIGR02168  920 LREKL---AQLELRLEGLEVRID---NLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-------LKRLENKIKELGP 986
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 116686122   699 VLRRKTEEAAAANKRlKDALQKQREVADKRKETQSRGMEGTAARVKN 745
Cdd:TIGR02168  987 VNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
538-726 8.36e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.84  E-value: 8.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  538 ALARKMTQNDSQLQPIQYQyqdnIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERR--------RKRLQELEGQI 609
Cdd:COG4942    17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaalEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  610 ADLKKKLNEQSKLLK-------LKESTERTVSKLNQE-----IRMMK------NQRVQLMRQMKEDAEKFRQWKQKKDKE 671
Cdd:COG4942    93 AELRAELEAQKEELAellralyRLGRQPPLALLLSPEdfldaVRRLQylkylaPARREQAEELRADLAELAALRAELEAE 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  672 VIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD 726
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
650-997 8.82e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  650 LMRQMKEDAEK-FRQWKQKKDKEVIQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDAlqkQREVADKR 728
Cdd:COG4717    47 LLERLEKEADElFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEEL---REELEKLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  729 KETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEK-KESGENPPPKLRRRTFSLTEVRG 807
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  808 QVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQrWENIATILEAKCALKYLIGELVSSKIQVSKL--- 884
Cdd:COG4717   203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLILTIAGVlfl 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  885 ---------ESSLKQSKTSCADMQKMLF---------EERNHFAE---IETELQAELVRMEQQHQEKVLYLLSQLQQsqm 943
Cdd:COG4717   282 vlgllallfLLLAREKASLGKEAEELQAlpaleeleeEELEELLAalgLPPDLSPEELLELLDRIEELQELLREAEE--- 358
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116686122  944 AEKQLEESVSEKE-QQLLSTLKCQDEE-LEKMREVCEQNQQLLRENEIIKQKLTLL 997
Cdd:COG4717   359 LEEELQLEELEQEiAALLAEAGVEDEEeLRAALEQAEEYQELKEELEELEEQLEEL 414
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
802-1004 9.49e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.10  E-value: 9.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  802 LTEVRGQVSESEDSITK-----QIESLETEMEFRSAQIADLQQKLLDAESEdrpkqrweniatILEAKCALKYLIGELVS 876
Cdd:COG3206   184 LPELRKELEEAEAALEEfrqknGLVDLSEEAKLLLQQLSELESQLAEARAE------------LAEAEARLAALRAQLGS 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  877 SKIQVSKLESS--LKQSKTSCADMQKMLFEERNHFAE-------IETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQ 947
Cdd:COG3206   252 GPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122  948 LEESVSEKEQQLLSTLKCQDEELEKMREVcEQNQQLLREneiIKQKLTLLQVASRQK 1004
Cdd:COG3206   332 LQAQLAQLEARLAELPELEAELRRLEREV-EVARELYES---LLQRLEEARLAEALT 384
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
380-1005 1.19e-06

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: 53.13  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   380 EPSENLQSLMEKNQSLV------EENEKLSRGLSEAAGQTAQMLEriiltEQANEKMNAKLEELRQHAACKLDLQKLVET 453
Cdd:TIGR00606  256 EIEHNLSKIMKLDNEIKalksrkKQMEKDNSELELKMEKVFQGTD-----EQLNDLYHNHQRTVREKERELVDCQRELEK 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   454 L--EDQELKENVEIICNlQQLITQLSDETVACMAAAIDTAVEQEA------QVETSPETSRSSDAFTTQHALRQAQMSKE 525
Cdd:TIGR00606  331 LnkERRLLNQEKTELLV-EQGRLQLQADRHQEHIRARDSLIQSLAtrleldGFERGPFSERQIKNFHTLVIERQEDEAKT 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   526 LVELNKALALKEALARKmtqndsQLQPIQYQYQDNIKELELEVINLQKEKEEL---VLELQTA--------KKD------ 588
Cdd:TIGR00606  410 AAQLCADLQSKERLKQE------QADEIRDEKKGLGRTIELKKEILEKKQEELkfvIKELQQLegssdrilELDqelrka 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   589 ------ANQAKLSERRRKRLQELEGQIADLKKKL----------NEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMR 652
Cdd:TIGR00606  484 erelskAEKNSLTETLKKEVKSLQNEKADLDRKLrkldqemeqlNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELT 563
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   653 QMKED---AEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD--- 726
Cdd:TIGR00606  564 SLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDler 643
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   727 -KRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEA-----------KRHLNDLLEDrkiLAQDVAQLKEKKESGENPPPK 794
Cdd:TIGR00606  644 lKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqtEAELQEFISD---LQSKLRLAPDKLKSTESELKK 720
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   795 L-RRRTFSLTEVRGQVSESeDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALK---YL 870
Cdd:TIGR00606  721 KeKRRDEMLGLAPGRQSII-DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMerfQM 799
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   871 IGELVSSKI--QVSKLESSLKQSKTSCADMQKmlfEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQL 948
Cdd:TIGR00606  800 ELKDVERKIaqQAAKLQGSDLDRTVQQVNQEK---QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122   949 EESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKH 1005
Cdd:TIGR00606  877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
503-800 1.23e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   503 ETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKEL---ELEVINLQKEKEELV 579
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeelEEDLHKLEEALNDLE 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   580 LELQTAKKDANQAKLSERRrKRLQELEGQIADLKKKLNeqsKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAE 659
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKLE-EEVSRIEARLREIEQKLN---RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   660 KFRQWKQKKDKevIQLKERDRKRQYELLKLER-NFQKQSNVLRRKTEEAAA----ANKRLKDALQKQREVADKRKETQSR 734
Cdd:TIGR02169  862 KKEELEEELEE--LEAALRDLESRLGDLKKERdELEAQLRELERKIEELEAqiekKRKRLSELKAKLEALEEELSEIEDP 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   735 GME-----------GTAARVKNWLGNEIEVMVST--------EEAKRHLNDLLEDRKILAQDVAQLKEKKESGEnpppKL 795
Cdd:TIGR02169  940 KGEdeeipeeelslEDVQAELQRVEEEIRALEPVnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYE----KK 1015

                   ....*
gi 116686122   796 RRRTF 800
Cdd:TIGR02169 1016 KREVF 1020
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
561-838 1.43e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  561 IKELELEVINLQK--EKEELVLELQTAKKDANQAKLSERR--RKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKL 636
Cdd:PRK03918  171 IKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREINeiSSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  637 NQEIRMMKNQRVQLMRQMKEDAEKFR------------QWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT 704
Cdd:PRK03918  251 EGSKRKLEEKIRELEERIEELKKEIEeleekvkelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  705 EEAAAANKRLKdalqkqrEVADKRKETQSRGMEgtaarvknwlgneievmvsteeakrhlndlLEDRKILAQDVAQLKE- 783
Cdd:PRK03918  331 KELEEKEERLE-------ELKKKLKELEKRLEE------------------------------LEERHELYEEAKAKKEe 373
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122  784 ----KKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQ 838
Cdd:PRK03918  374 lerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
591-835 1.47e-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: 52.07  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  591 QAKLSERRRKRLQELEGQIADLKKKLN----EQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEdaekfrqwkq 666
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAalkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---------- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  667 kKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKEtQSRGMEGTAARVKnw 746
Cdd:COG4942    88 -LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELA-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  747 lgneiEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENpppKLRRRTFSLTEVRGQVSESEDSITKQIESLETE 826
Cdd:COG4942   164 -----ALRAELEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAE 235

                  ....*....
gi 116686122  827 MEFRSAQIA 835
Cdd:COG4942   236 AAAAAERTP 244
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
518-994 4.56e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 51.33  E-value: 4.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   518 RQAQMSKELVELNKALAlkeALARKMTQNDSQLQPIQYQYQDNiKELELEVINLQKEKEELVLELQT---AKKDANQAKL 594
Cdd:pfam01576   20 RQQKAESELKELEKKHQ---QLCEEKNALQEQLQAETELCAEA-EEMRARLAARKQELEEILHELESrleEEEERSQQLQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   595 SERrrKRLQElegQIADLKKKLNEQ----SKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMK--------------- 655
Cdd:pfam01576   96 NEK--KKMQQ---HIQDLEEQLDEEeaarQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKlleeriseftsnlae 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   656 --EDAEKFRQWKQKKDKEVIQLKERDRK----RQyELLKLERNFQKQSNVLR------------------RKTEEAAAAN 711
Cdd:pfam01576  171 eeEKAKSLSKLKNKHEAMISDLEERLKKeekgRQ-ELEKAKRKLEGESTDLQeqiaelqaqiaelraqlaKKEEELQAAL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   712 KRLKD-------ALQKQREVADKRKETQS-----RGMEGTAARVKNWLGNEIEVMvsteeaKRHLNDLL-------EDRK 772
Cdd:pfam01576  250 ARLEEetaqknnALKKIRELEAQISELQEdleseRAARNKAEKQRRDLGEELEAL------KTELEDTLdttaaqqELRS 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   773 ILAQDVAQLK----EKKESGENPPPKLRRRTFS----LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDA 844
Cdd:pfam01576  324 KREQEVTELKkaleEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   845 ESEDR--PKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAEL-- 920
Cdd:pfam01576  404 EHKRKklEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETrq 483
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122   921 -----VRMEQQHQEKVlYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKL 994
Cdd:pfam01576  484 klnlsTRLRQLEDERN-SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
384-913 4.74e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  384 NLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHaacKLDLQKLVETLE-------- 455
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKEEIEelekeles 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  456 -DQELKENVEIICNLQQLITQLSDETvacmaaaidtaVEQEAQVETSPETSRSSDAFTTqhalrqaqMSKELVELNKALA 534
Cdd:PRK03918  250 lEGSKRKLEEKIRELEERIEELKKEI-----------EELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELR 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  535 LKEALARKMTQndsQLQPIQYQYQDnIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADL-K 613
Cdd:PRK03918  311 EIEKRLSRLEE---EINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtP 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  614 KKLNEQSKLL-KLKESTERTVSKLNQEIRMMKNQRVQLMRQM----------------------KEDAEKFRQWKQKKDK 670
Cdd:PRK03918  387 EKLEKELEELeKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELKRIEK 466
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  671 EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT--EEAAAANKRLK----DALQKQREVADKRKEtQSRGMEGTAARVK 744
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKkynlEELEKKAEEYEKLKE-KLIKLKGEIKSLK 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  745 NWLGNEIEVMVSTEEAKRHLNDLLEDRKILaqdvaqLKEKKESGENPPPKLRRRTFSL-------TEVRGQVSESEDsIT 817
Cdd:PRK03918  546 KELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFESVEELEERLKELepfyneyLELKDAEKELER-EE 618
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  818 KQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCAD 897
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
                         570
                  ....*....|....*.
gi 116686122  898 MQKMLFEERNHFAEIE 913
Cdd:PRK03918  699 LKEELEEREKAKKELE 714
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
558-876 9.00e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  558 QDNIKELELevinLQKEKEELVLELQTAKKDANQAK-----LSERRR------------KRLQELEGQIADLKKKLNE-- 618
Cdd:COG4913   606 FDNRAKLAA----LEAELAELEEELAEAEERLEALEaeldaLQERREalqrlaeyswdeIDVASAEREIAELEAELERld 681
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  619 --QSKLLKLkestERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKER-DRKRQYELLKLERnfqk 695
Cdd:COG4913   682 asSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEE---- 753
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  696 qsnvlRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKN-WLGNEIEVMVSTEEA---KRHLNDLLEDR 771
Cdd:COG4913   754 -----RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNReWPAETADLDADLESLpeyLALLDRLEEDG 828
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  772 kiLAQDVAQLKE--KKESGENpppklrrrtfsLTEVRGQVSESEDSITKQIE----SLEtEMEF-------------RSA 832
Cdd:COG4913   829 --LPEYEERFKEllNENSIEF-----------VADLLSKLRRAIREIKERIDplndSLK-RIPFgpgrylrlearprPDP 894
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 116686122  833 QIADLQQKLLDAESedrpkQRWENIATILEAKC-ALKYLIGELVS 876
Cdd:COG4913   895 EVREFRQELRAVTS-----GASLFDEELSEARFaALKRLIERLRS 934
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
385-988 1.13e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.79  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   385 LQSLMEKNQSLVEENEKLSRGLSEAAGQtaqmleriiLTEQANEkMNAKLEELRQHAACKLD-LQKLVETLEDQELKENv 463
Cdd:pfam01576  192 LEERLKKEEKGRQELEKAKRKLEGESTD---------LQEQIAE-LQAQIAELRAQLAKKEEeLQAALARLEEETAQKN- 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   464 EIICNLQQLITQLSD--ETVACMAAAIDTAVEQEAQVETSPETSRSS-----DAFTTQHALRqAQMSKELVELnkalalK 536
Cdd:pfam01576  261 NALKKIRELEAQISElqEDLESERAARNKAEKQRRDLGEELEALKTEledtlDTTAAQQELR-SKREQEVTEL------K 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   537 EALARKMTQNDSQLQPIQYQYQDNIKEL--ELEV-----INLQKEKEEL---VLELQTAKKDANQAKL-SERRRKRLqel 605
Cdd:pfam01576  334 KALEEETRSHEAQLQEMRQKHTQALEELteQLEQakrnkANLEKAKQALeseNAELQAELRTLQQAKQdSEHKRKKL--- 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   606 EGQIADLKKKLNEqskllklkesTERTVSKLNQEIRMMKNQrVQLMRQMKEDAEKfrqWKQKKDKEVIQLKERDRKRQYE 685
Cdd:pfam01576  411 EGQLQELQARLSE----------SERQRAELAEKLSKLQSE-LESVSSLLNEAEG---KNIKLSKDVSSLESQLQDTQEL 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   686 LLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEgtaarVKNWLGNEIEVMVSTEEAKRHLN 765
Cdd:pfam01576  477 LQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD-----MKKKLEEDAGTLEALEEGKKRLQ 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   766 DLLEDRKILAQDVAQLKEKKESGENP-PPKLRRRTFSLTEVRGQVSESEDSiTKQIESLETEMEFRSAQIADLQQKlldA 844
Cdd:pfam01576  552 RELEALTQQLEEKAAAYDKLEKTKNRlQQELDDLLVDLDHQRQLVSNLEKK-QKKFDQMLAEEKAISARYAEERDR---A 627
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   845 ESEDRPKQ-RWENIATILE-----------AKCALKYLIGELVSSKIQVSKLESSLKQSKTScadMQKMLFEERNHFAEI 912
Cdd:pfam01576  628 EAEAREKEtRALSLARALEealeakeelerTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA---LEQQVEEMKTQLEEL 704
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   913 ETELQA---------------------ELVRMEQQHQEKVLYLLSQLQQSQM--------------AEKQLEESVSEKEQ 957
Cdd:pfam01576  705 EDELQAtedaklrlevnmqalkaqferDLQARDEQGEEKRRQLVKQVRELEAelederkqraqavaAKKKLELDLKELEA 784
                          650       660       670
                   ....*....|....*....|....*....|.
gi 116686122   958 QLLSTLKCQDEELEKMREVCEQNQQLLRENE 988
Cdd:pfam01576  785 QIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
693-1003 1.61e-05

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: 49.28  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   693 FQKQSNVLRRKTEEAAAANKRLKDA----------LQKQREVADKRKETQSRGmegtaarvknwlgNEIEVMVSTeeakR 762
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDIlnelerqlksLERQAEKAERYKELKAEL-------------RELELALLV----L 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   763 HLNDLLEDRKILAQDVAQLKEKKESGENpppKLRRRTFSLTEVRGQVSESEDSI----------TKQIESLETEMEFRSA 832
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTA---ELQELEEKLEELRLEVSELEEEIeelqkelyalANEISRLEQQKQILRE 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   833 QIADLQQKLLDAESE-DRPKQRWENIATILEA-KCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFA 910
Cdd:TIGR02168  310 RLANLERQLEELEAQlEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   911 EIETElqaelvrmEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQL----LSTLKCQDEELEKMRE-VCEQNQQLLR 985
Cdd:TIGR02168  390 QLELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEeLQEELERLEE 461
                          330
                   ....*....|....*...
gi 116686122   986 ENEIIKQKLTLLQVASRQ 1003
Cdd:TIGR02168  462 ALEELREELEEAEQALDA 479
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
386-1004 2.01e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   386 QSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLErIILTEQANEKMNAKLEELRQHAacklDLQKLVETLEDQElKENVEI 465
Cdd:TIGR00618  307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS-IEEQRRLLQTLHSQEIHIRDAH----EVATSIREISCQQ-HTLTQH 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   466 ICNLQQLITQLSDETvacMAAAIDTAVEQEAQVETSPETSRssdafttQHALRQ--AQMSKELVELNKALALKEALARKM 543
Cdd:TIGR00618  381 IHTLQQQKTTLTQKL---QSLCKELDILQREQATIDTRTSA-------FRDLQGqlAHAKKQQELQQRYAELCAAAITCT 450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   544 TQNDSQLQPIQYQYQDNIKELElevinlQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKL---NEQS 620
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKERE------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdiDNPG 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   621 KLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQ---LKERDRKRQYELLKLERNFQKQS 697
Cdd:TIGR00618  525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLS 604
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   698 NVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAArvknwlgneievmvsteeAKRHLNDLLEDRKILAQD 777
Cdd:TIGR00618  605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL------------------HALQLTLTQERVREHALS 666
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   778 VAQLKEKK-ESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFR-------SAQIADLQQKLLDAESEDR 849
Cdd:TIGR00618  667 IRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFneienasSSLGSDLAAREDALNQSLK 746
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   850 PKQRweniatilEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKM--LFEERNH-FAEIETELQAEL------ 920
Cdd:TIGR00618  747 ELMH--------QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrLREEDTHlLKTLEAEIGQEIpsdedi 818
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   921 ----VRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDE--ELEKMREVCEQNQQLLRENEIIK--Q 992
Cdd:TIGR00618  819 lnlqCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiQLSDKLNGINQIKIQFDGDALIKflH 898
                          650
                   ....*....|..
gi 116686122   993 KLTLLQVASRQK 1004
Cdd:TIGR00618  899 EITLYANVRLAN 910
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
393-985 3.43e-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: 48.30  E-value: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   393 QSLVEENEKLSRGLSEAAGQTAQMLERIILteQANEKMNAKLEEL------------RQHAACKLDLQKLVETLEDQELK 460
Cdd:pfam12128  353 QSELENLEERLKALTGKHQDVTAKYNRRRS--KIKEQNNRDIAGIkdklakireardRQLAVAEDDLQALESELREQLEA 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   461 ENVEIICNLQQLITQLSDETVacmaaaidtaveQEAQVETSPETsrssdafTTQHALRQAQMSKELVELNKALALKEALA 540
Cdd:pfam12128  431 GKLEFNEEEYRLKSRLGELKL------------RLNQATATPEL-------LLQLENFDERIERAREEQEAANAEVERLQ 491
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   541 RKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLELqtakkDANQAKLSERRRKRLQELEGQIA---------- 610
Cdd:pfam12128  492 SELRQARKRRD----QASEALRQASRRLEERQSALDELELQL-----FPQAGTLLHFLRKEAPDWEQSIGkvispellhr 562
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   611 -DLKKKLNEQSKllklkeSTERTVSKLNQEI-RMMKNQRVQLMRQMKEDAEKF-------RQWKQKKDKEVIQLKERDRK 681
Cdd:pfam12128  563 tDLDPEVWDGSV------GGELNLYGVKLDLkRIDVPEWAASEEELRERLDKAeealqsaREKQAAAEEQLVQANGELEK 636
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   682 RQYELLKLERNFQKQSNVLRRKTEEaaaaNKRLKDALQKQREVADKRKETQSRGMEGTaarvKNWLGNEIEVMVST--EE 759
Cdd:pfam12128  637 ASREETFARTALKNARLDLRRLFDE----KQSEKDKKNKALAERKDSANERLNSLEAQ----LKQLDKKHQAWLEEqkEQ 708
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   760 AKRHLNDLLEDRKILAQD----VAQLKEKKESGENpppKLRRRTFSLTEVRGQVSESEDSITKQIESLETEmefrsaqIA 835
Cdd:pfam12128  709 KREARTEKQAYWQVVEGAldaqLALLKAAIAARRS---GAKAELKALETWYKRDLASLGVDPDVIAKLKRE-------IR 778
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   836 DLQQKLLDAEsEDRPK----QRWENiATILEAKCALkyligelvssKIQVSKLESSLKQSKtscADMQKMLFEERNHFAE 911
Cdd:pfam12128  779 TLERKIERIA-VRRQEvlryFDWYQ-ETWLQRRPRL----------ATQLSNIERAISELQ---QQLARLIADTKLRRAK 843
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116686122   912 IETELQAElvrMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLR 985
Cdd:pfam12128  844 LEMERKAS---EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
521-994 3.86e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  521 QMSKELVELNKALALKEALARKMTQNDSQLQPIQyqyqDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRK 600
Cdd:PRK03918  218 ELREELEKLEKEVKELEELKEEIEELEKELESLE----GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  601 RLQELEGQIADLKKKLNEQSKLL----KLKESTERTVSKL---NQEIRMMKNQRVQLMRQ---MKEDAEKFRQWKQKKDK 670
Cdd:PRK03918  294 EYIKLSEFYEEYLDELREIEKRLsrleEEINGIEERIKELeekEERLEELKKKLKELEKRleeLEERHELYEEAKAKKEE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  671 --------------EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQK----QREVADKRKEtq 732
Cdd:PRK03918  374 lerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRK-- 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  733 sRGMEGTAARVKNWLGNEIEVMVSTEEAKRHL----NDLLEDRKILAQ-----------------DVAQLKEKKESGEnp 791
Cdd:PRK03918  452 -ELLEEYTAELKRIEKELKEIEEKERKLRKELreleKVLKKESELIKLkelaeqlkeleeklkkyNLEELEKKAEEYE-- 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  792 ppKLRRRtfsLTEVRGQVSESEDSItKQIESLETEMEFRSAQIADLQQKLLDAESEDRP---KQRWENIATILEAKCALK 868
Cdd:PRK03918  529 --KLKEK---LIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYN 602
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  869 YLIgELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRM-EQQHQEKVLYLLSQLQQSQMAEKQ 947
Cdd:PRK03918  603 EYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAE 681
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 116686122  948 LEESVSEKEQ--QLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKL 994
Cdd:PRK03918  682 LEELEKRREEikKTLEKLKEELEEREKAKKELEKLEKALERVEELREKV 730
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
649-853 4.23e-05

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: 47.45  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  649 QLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKR 728
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  729 KETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGEnpppKLRRRTFSLTEVRGQ 808
Cdd:COG4942   100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 116686122  809 VSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQR 853
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
537-672 4.32e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 47.77  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  537 EALARKMTQNDSQLQPIqyqyqdniKELELEVINLQKEKEELVLELQTAKKDanqaklserrrkRLQELEGQIADLKKKL 616
Cdd:COG0542   397 EAAARVRMEIDSKPEEL--------DELERRLEQLEIEKEALKKEQDEASFE------------RLAELRDELAELEEEL 456
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  617 NEqsklLKLKESTERT----VSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV 672
Cdd:COG0542   457 EA----LKARWEAEKElieeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
383-699 4.35e-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: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  383 ENLQSLMEKNQSLVEENEKLSrglSEAAGQTAQMLERIiltEQANEKMNAKLEELRQHAACKLDLQKLV-ETLEDQELKE 461
Cdd:COG5185   246 EDLAQTSDKLEKLVEQNTDLR---LEKLGENAESSKRL---NENANNLIKQFENTKEKIAEYTKSIDIKkATESLEEQLA 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  462 NVEIICNLQQLITQlSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNkalALKEALAR 541
Cdd:COG5185   320 AAEAEQELEESKRE-TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE---STKESLDE 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  542 KMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLS-ERRRKRLQELEGQIADLKKKLNEQS 620
Cdd:COG5185   396 IPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRS 475
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122  621 KLLKLKEStERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRqwkQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNV 699
Cdd:COG5185   476 VRSKKEDL-NEELTQIESRVSTLKATLEKLRAKLERQLEGVR---SKLDQVAESLKDFMRARGYAHILALENLIPASEL 550
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
484-718 4.42e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  484 MAAAIDTAVEQ-------EAQVETspetsrssdafttqhALRQAQMSKELVELNKALalkEALARKMTQNDSQLQPIQ-Y 555
Cdd:COG4913   223 TFEAADALVEHfddleraHEALED---------------AREQIELLEPIRELAERY---AAARERLAELEYLRAALRlW 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  556 QYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAK-----LSERRR----KRLQELEGQIADLKKKLNEQS-KLLKL 625
Cdd:COG4913   285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReeldeLEAQIRgnggDRLEQLEREIERLERELEERErRRARL 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  626 KESTERTVSKLNQEIRMMKNQRVQLmRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKlERNF--QKQSNVlrrk 703
Cdd:COG4913   365 EALLAALGLPLPASAEEFAALRAEA-AALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASleRRKSNI---- 438
                         250
                  ....*....|....*
gi 116686122  704 TEEAAAANKRLKDAL 718
Cdd:COG4913   439 PARLLALRDALAEAL 453
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
509-995 4.65e-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: 48.04  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   509 DAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKD 588
Cdd:TIGR00618  155 AQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   589 ANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIrmmkNQRVQLMRqMKEDAEKFRQWKQKK 668
Cdd:TIGR00618  235 LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI----NRARKAAP-LAAHIKAVTQIEQQA 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   669 DKEVIQLKERDRKRQYELLKLErnfqkqsnvlrrkteeaaaankrlkDALQKQREVADKRKETQSrgmegtaarvknWLG 748
Cdd:TIGR00618  310 QRIHTELQSKMRSRAKLLMKRA-------------------------AHVKQQSSIEEQRRLLQT------------LHS 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   749 NEIEVMVSTEEAKRHLnDLLEDRKILAQDVAQLKEKKESGEnpppklrrrtfsltevrgQVSESEDSITKQIESLETEME 828
Cdd:TIGR00618  353 QEIHIRDAHEVATSIR-EISCQQHTLTQHIHTLQQQKTTLT------------------QKLQSLCKELDILQREQATID 413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   829 FRSAQIADLQQKLLDAESEDRPKQRWENI--ATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCaDMQKMLFEER 906
Cdd:TIGR00618  414 TRTSAFRDLQGQLAHAKKQQELQQRYAELcaAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH-LQETRKKAVV 492
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   907 NHFAEIETELQAELVRMEQQ-HQEKVLYLLSQLQQSQMaeKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLR 985
Cdd:TIGR00618  493 LARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTRRM--QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
                          490
                   ....*....|
gi 116686122   986 ENEIIKQKLT 995
Cdd:TIGR00618  571 SFSILTQCDN 580
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
382-986 5.39e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 5.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   382 SENLQSLMEKNQSLVE-ENEKLSRGLSEAAGQTAQMLERIiltEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELK 460
Cdd:pfam15921  294 ANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   461 ENVEIICNLQQLITQLSdetvacmaaaidtavEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALA 540
Cdd:pfam15921  371 ESGNLDDQLQKLLADLH---------------KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   541 RKMT-----QNDSQLQPIQYQyQDNIKELELEVINLQKEKEEL--VLELQTAKKdanqaklserrrKRLQELEGQIADLK 613
Cdd:pfam15921  436 KAMKsecqgQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLrkVVEELTAKK------------MTLESSERTVSDLT 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   614 KKLNEQSKLLklkESTERTVSKLNQEIRMmknqRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRkrQYELLKlernf 693
Cdd:pfam15921  503 ASLQEKERAI---EATNAEITKLRSRVDL----KLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK--VIEILR----- 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   694 QKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGM--EGTAARVKnwlgnEIEVMVSTEEakrhlndlLEDR 771
Cdd:pfam15921  569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIR-----ELEARVSDLE--------LEKV 635
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   772 KILAQDVAQLKEKKESGEnpppklrRRTFSLTEVRGQVSESeDSITKQIESLETEMEFRSAQIADLQQKLldaesedrpk 851
Cdd:pfam15921  636 KLVNAGSERLRAVKDIKQ-------ERDQLLNEVKTSRNEL-NSLSEDYEVLKRNFRNKSEEMETTTNKL---------- 697
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   852 qrweniatileaKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQaelvrmeqqhqekv 931
Cdd:pfam15921  698 ------------KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQ-------------- 751
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116686122   932 lyLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRE 986
Cdd:pfam15921  752 --FLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
548-728 5.66e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  548 SQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQ-----AKLSERRRKRLQELEGQIADLKKKLNEQSKL 622
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaeiAEAEAEIEERREELGERARALYRSGGSVSYL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  623 LKLKEST--ERTVSKLNQEIRMMKNQRvQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVL 700
Cdd:COG3883   106 DVLLGSEsfSDFLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
                         170       180
                  ....*....|....*....|....*...
gi 116686122  701 RRKTEEAAAANKRlKDALQKQREVADKR 728
Cdd:COG3883   185 AQLSAEEAAAEAQ-LAELEAELAAAEAA 211
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
537-940 5.87e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  537 EALARKMTQNDSQLQPIQyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRK---RLQELEGQIADLK 613
Cdd:COG4717    74 KELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaELAELPERLEELE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  614 KKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQR----VQLMRQMKEDAEKFRQWKQKKDKEVIQLKER--DRKRQYELL 687
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEEleELEEELEQL 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  688 KLERNFQKQSNVLRRKTEEAAAANKRLkDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRhLNDL 767
Cdd:COG4717   233 ENELEAAALEERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE-LQAL 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  768 LEDRKILAQDVAQLKEKKESGENPPPKLRRRTFS-LTEVRGQVSESEDSITK-QIESLETEME--FRSAQ---IADLQQK 840
Cdd:COG4717   311 PALEELEEEELEELLAALGLPPDLSPEELLELLDrIEELQELLREAEELEEElQLEELEQEIAalLAEAGvedEEELRAA 390
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  841 LLDAESEDRPKQRWENIATILEAKcALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERnhfAEIETELQA-- 918
Cdd:COG4717   391 LEQAEEYQELKEELEELEEQLEEL-LGELEELLEALDEEELEEELEELEEELEELEEELEELREEL---AELEAELEQle 466
                         410       420
                  ....*....|....*....|....*
gi 116686122  919 ---ELVRMEQQHQEkvlyLLSQLQQ 940
Cdd:COG4717   467 edgELAELLQELEE----LKAELRE 487
PRK11281 PRK11281
mechanosensitive channel MscK;
383-646 9.87e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 9.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  383 ENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERII-LTEQANEKMNAKLE--ELRQhaackLDlQKLVETLED-QE 458
Cdd:PRK11281   66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEaLKDDNDEETRETLStlSLRQ-----LE-SRLAQTLDQlQN 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  459 LKENVEIICNlqQLITQlsdETVACMA-AAIDTAVEQEAQVetspeTSRSSDAFTTQHALRQAQMSKELVELnKALALKE 537
Cdd:PRK11281  140 AQNDLAEYNS--QLVSL---QTQPERAqAALYANSQRLQQI-----RNLLKGGKVGGKALRPSQRVLLQAEQ-ALLNAQN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  538 ALARKMTQNDSQLQPI---QYQY-QDNIKELELEVINLQKEKEELVLEL--QTAKKDANQAKLSERRRKRL--QELegqi 609
Cdd:PRK11281  209 DLQRKSLEGNTQLQDLlqkQRDYlTARIQRLEHQLQLLQEAINSKRLTLseKTVQEAQSQDEAARIQANPLvaQEL---- 284
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 116686122  610 aDLKKKLNEqskllKLKESTERTVSKLNQEIRmMKNQ 646
Cdd:PRK11281  285 -EINLQLSQ-----RLLKATEKLNTLTQQNLR-VKNW 314
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
514-793 1.03e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.66  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   514 QHALRQAQMSKeLVELNKALALKEAlaRKMTQNDSQLQPIQYQYQDNI---KELELEVINLQKEK--------EELVLEL 582
Cdd:pfam17380  298 QERLRQEKEEK-AREVERRRKLEEA--EKARQAEMDRQAAIYAEQERMameRERELERIRQEERKrelerirqEEIAMEI 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   583 QTAKKDANQAKLSERRRKRL-QELEgqiADLKKKLNEQSKLLKLKEStERTVSKLNQEIRMMKNQRVQLMRQMKE-DAEK 660
Cdd:pfam17380  375 SRMRELERLQMERQQKNERVrQELE---AARKVKILEEERQRKIQQQ-KVEMEQIRAEQEEARQREVRRLEEERArEMER 450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   661 FRQWKQKKDKEVIQLK--ERDRKRQYELLKLERNFQKQSNVLRRKT-EEAAAANKRLKDALQKQREVADKRKETQSRGM- 736
Cdd:pfam17380  451 VRLEEQERQQQVERLRqqEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKAIy 530
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116686122   737 ---EGTAARVKNWLGNEIE--------VMVSTEEAKRhLNDLLEDRKILAQDVAQLKEKKESGENPPP 793
Cdd:pfam17380  531 eeeRRREAEEERRKQQEMEerrriqeqMRKATEERSR-LEAMEREREMMRQIVESEKARAEYEATTPI 597
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
447-847 1.25e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  447 LQKLVETLEDQELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKEL 526
Cdd:COG4717    39 LLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  527 VELNKALALKEALARkMTQNDSQLQPIQYQYqDNIKELELEVINLQKEKEELVLELQTAKKDANQAK--LSERRRKRLQE 604
Cdd:COG4717   119 EKLEKLLQLLPLYQE-LEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLeqLSLATEEELQD 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  605 LEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEK------------------------ 660
Cdd:COG4717   197 LAEELEELQQRLAELEEEL---EEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllslil 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  661 -------------------FRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQ 721
Cdd:COG4717   274 tiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  722 REVADKRKETQsrgMEGTAARVKNWLGneiEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEkkesgenpppklRRRTFS 801
Cdd:COG4717   354 REAEELEEELQ---LEELEQEIAALLA---EAGVEDEEELRAALEQAEEYQELKEELEELEE------------QLEELL 415
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 116686122  802 LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESE 847
Cdd:COG4717   416 GELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
379-789 1.28e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  379 VEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLED-- 456
Cdd:PRK03918  282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErh 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  457 QELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSsdafttqhalRQAQMSKELVELNKAL-AL 535
Cdd:PRK03918  362 ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA----------RIGELKKEIKELKKAIeEL 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  536 KEA------LARKMTQNDSqlQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKdanqAKLSERRRKRLQELEGQI 609
Cdd:PRK03918  432 KKAkgkcpvCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK----VLKKESELIKLKELAEQL 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  610 ADLKKKLNEQSkLLKLKESTERtVSKLNQEIRMMKNQrvqlMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKL 689
Cdd:PRK03918  506 KELEEKLKKYN-LEELEKKAEE-YEKLKEKLIKLKGE----IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  690 ERNFQKQSNVLRRKTEEAAAANKR---LKDALQKQREVADKRKETQSR---------GMEGTAARVKNWLgNEIEVMVST 757
Cdd:PRK03918  580 EELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEEldkafeelaETEKRLEELRKEL-EELEKKYSE 658
                         410       420       430
                  ....*....|....*....|....*....|..
gi 116686122  758 EEAKRHLNDLLEDRKILAQDVAQLKEKKESGE 789
Cdd:PRK03918  659 EEYEELREEYLELSRELAGLRAELEELEKRRE 690
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
535-743 1.36e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  535 LKEALARKMTQNDSQLQPIQYQ---YQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERR---RKRLQELEGQ 608
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQlpeLRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLaeaRAELAEAEAR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  609 IADLKKKLNEQSKLLKlKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRK----RQY 684
Cdd:COG3206   242 LAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRilasLEA 320
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  685 ELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVA----------DKRKETQ-SRGMEGTAARV 743
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvarelyesllQRLEEARlAEALTVGNVRV 390
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
86-280 1.47e-04

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 45.89  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   86 AYGQTGSGKTYSMggaytAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTLKvsYLEIYNEEILDLLCPSREKAQINIRE 165
Cdd:COG5059   387 AYMQSLKKETETL-----KSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQ--FLRIEIDRLLLLREEELSKKKTKIHK 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNsRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSfrskLHLVDLAGSE 245
Cdd:COG5059   460 LNKLRHDLSSLLSSIPEETSDRVESEKASKL-RSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELS----LNQVDLAGSE 534
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 116686122  246 RqKKTKAEGDRLKEGININRGLLCLGNVISALGDD 280
Cdd:COG5059   535 R-KVSQSVGELLRETQSLNKSLSSLGDVIHALGSK 568
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
522-997 1.70e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   522 MSKELVELNKALA--------LKEALARKMTQNDSQLQPIQYQYQDNIKEL----ELEVINLQKEKeelvlelQTAKKDA 589
Cdd:pfam15921  222 ISKILRELDTEISylkgrifpVEDQLEALKSESQNKIELLLQQHQDRIEQLisehEVEITGLTEKA-------SSARSQA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   590 NQAK-----LSERRR-------KRLQELEGQIADLKKKLNEQSKLLKLK-ESTERTVSKLNQEIRMMKNQRvqlmrqmke 656
Cdd:pfam15921  295 NSIQsqleiIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTER--------- 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   657 daEKFRQWKQKKDKEVIQLKERDRKRQYELlklerNFQKQSNvlrRKTEEAAAANKRLKDALQkqREVADKRKETQSrgM 736
Cdd:pfam15921  366 --DQFSQESGNLDDQLQKLLADLHKREKEL-----SLEKEQN---KRLWDRDTGNSITIDHLR--RELDDRNMEVQR--L 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   737 EGTAARVKNWLGNEIEVMVSTEEAKrhlNDLLEDRKILAqdvAQLKEKKEsgenpppKLRRRTFSLTEVRGQVSESEDSI 816
Cdd:pfam15921  432 EALLKAMKSECQGQMERQMAAIQGK---NESLEKVSSLT---AQLESTKE-------MLRKVVEELTAKKMTLESSERTV 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   817 TKQIESL---ETEMEFRSAQIADLQQKLldaeseDRPKQRWENIATILEAkcaLKYLIGELVSSKIQVSKLESSLKQSKT 893
Cdd:pfam15921  499 SDLTASLqekERAIEATNAEITKLRSRV------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQ 569
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   894 SCADMQKMLfeerNHFAEIETELQAELVRMEQQHQEKVLYL--LSQLQQSQMAE-KQLEESVSEKEQQLLSTLKCQDEEL 970
Cdd:pfam15921  570 QIENMTQLV----GQHGRTAGAMQVEKAQLEKEINDRRLELqeFKILKDKKDAKiRELEARVSDLELEKVKLVNAGSERL 645
                          490       500
                   ....*....|....*....|....*..
gi 116686122   971 EKMREVCEQNQQLLRENEIIKQKLTLL 997
Cdd:pfam15921  646 RAVKDIKQERDQLLNEVKTSRNELNSL 672
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
537-975 1.89e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.87  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   537 EALARKMTQNDSQLQPIQYQYQDNIKELELE---VINLQKEKEELVLELQTAKKDaNQAKLSERRRKR-----LQELEGQ 608
Cdd:pfam05483   88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKLEEEIQE-NKDLIKENNATRhlcnlLKETCAR 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   609 IADLKKKLNEQskllklKESTERTVSKLNQEIRMM-----------KNQRVQLMRQMKEDAEKFRQWKQKKDKEViqlke 677
Cdd:pfam05483  167 SAEKTKKYEYE------REETRQVYMDLNNNIEKMilafeelrvqaENARLEMHFKLKEDHEKIQHLEEEYKKEI----- 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   678 rdrkrqyellkleRNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKET---QSRGMEGTAARvKNWLGNEIE-V 753
Cdd:pfam05483  236 -------------NDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklQDENLKELIEK-KDHLTKELEdI 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   754 MVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLR-RRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSA 832
Cdd:pfam05483  302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   833 QIADLQQKLLDAESEDRPKQ----RWENIATILEAKCALKY------------------LIGELVSSKIQVSKLESSLKQ 890
Cdd:pfam05483  382 ITMELQKKSSELEEMTKFKNnkevELEELKKILAEDEKLLDekkqfekiaeelkgkeqeLIFLLQAREKEIHDLEIQLTA 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   891 SKTS-------CADMQKMLFEERNHFAEIETE---LQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLE------ESVSE 954
Cdd:pfam05483  462 IKTSeehylkeVEDLKTELEKEKLKNIELTAHcdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEErmlkqiENLEE 541
                          490       500
                   ....*....|....*....|.
gi 116686122   955 KEQQLLSTLKCQDEELEKMRE 975
Cdd:pfam05483  542 KEMNLRDELESVREEFIQKGD 562
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
518-861 2.12e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   518 RQAQMSKELVELNKALALKEALARKMTQNDSQLQpIQYQYQDNIKELELEV-------INLQKEKEELVLELQTAKKDAN 590
Cdd:pfam02463  154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-LIIDLEELKLQELKLKeqakkalEYYQLKEKLELEEEYLLYLDYL 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   591 QaklseRRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLN----QEIRMMKNQRVQLMRQMKEDAEKFRQWKQ 666
Cdd:pfam02463  233 K-----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENkeeeKEKKLQEEELKLLAKEEEELKSELLKLER 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   667 KKDKEVIQLKERDRKRQYELLKLER------NFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRG--MEG 738
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKekeeieELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEseRLS 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   739 TAARVKNWLGNEIEVMVST-----EEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESE 813
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEaqlllELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 116686122   814 DSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATIL 861
Cdd:pfam02463  468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAL 515
PTZ00121 PTZ00121
MAEBL; Provisional
503-828 2.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  503 ETSRSSDAFTTQHALRQAQMSKELVELNKA-----LALKEA-LARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKE 576
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAeedknMALRKAeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  577 ELVLELQTAKKDANQAKL--------SERRRKRLQELEGQIADLKKKLNEQSKL---LKLKESTERTVSKLNQEIRMMKN 645
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKaeeAKKAEEDEKKAAEALKKEAEEAK 1702
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  646 QRVQLMRQMKEDAEKFRQWKQKKDKEVIQL-----KERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQK 720
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAeeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  721 qrEVADKRKETQSRGMEGTAARVKNWLGNEIEvmvSTEEAKRHLNDlleDRKILAQDVAQLKEKKESGENPPPKLRRRTF 800
Cdd:PTZ00121 1783 --EELDEEDEKRRMEVDKKIKDIFDNFANIIE---GGKEGNLVIND---SKEMEDSAIKEVADSKNMQLEEADAFEKHKF 1854
                         330       340
                  ....*....|....*....|....*...
gi 116686122  801 SLTEVRGQVSESEDSITKQIESLETEME 828
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEE 1882
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
521-976 3.51e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   521 QMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERR-R 599
Cdd:TIGR04523  100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLlE 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   600 KRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQmkedaekfrqwKQKKDKEVIQLKERD 679
Cdd:TIGR04523  180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDN-----------IEKKQQEINEKTTEI 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   680 RKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEe 759
Cdd:TIGR04523  249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ- 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   760 akrhlNDLLEDRKI---LAQDVAQLKEKKESGENPPPKLRRRtfsLTEVRGQV----------SESEDSITKQIESLETE 826
Cdd:TIGR04523  328 -----NQISQNNKIisqLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIeklkkenqsyKQEIKNLESQINDLESK 399
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   827 MEFRSAQIADLQQKLLDAESEDRPK-QRWENI-ATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFE 904
Cdd:TIGR04523  400 IQNQEKLNQQKDEQIKKLQQEKELLeKEIERLkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116686122   905 ERNHFAEIETELQA------ELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQlLSTLKcqdEELEKMREV 976
Cdd:TIGR04523  480 IKQNLEQKQKELKSkekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK-ISDLE---DELNKDDFE 553
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
524-720 3.81e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  524 KELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEeLVLELQTAKKDANQAKLSERRRKRLQ 603
Cdd:COG1340    85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKALEKNEKLK 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  604 ELEGQIADLKKKLNEQSKllKLKESTERtVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKD---KEVIQLKERDR 680
Cdd:COG1340   164 ELRAELKELRKEAEEIHK--KIKELAEE-AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADelhEEIIELQKELR 240
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 116686122  681 KRQYELLKLernfqKQSNVLRRKTEEAAAANKRLKDALQK 720
Cdd:COG1340   241 ELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEK 275
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
758-975 4.05e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  758 EEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLT----EVRGQVSESEDSI---TKQIESLETEMEFR 830
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELaelEKEIAELRAELEAQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  831 SAQIADLQQKLLDAESEDRPKQ--RWENIATILEAKCALKYLIGELvsskiqvSKLESSLKQSKTSCADMQKMLFEERNH 908
Cdd:COG4942   103 KEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPAR-------REQAEELRADLAELAALRAELEAERAE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122  909 FAEIETELQAELVRMEQQHQEKVLyLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMRE 975
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQK-LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
775-986 4.49e-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: 43.98  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  775 AQDVAQLKEKKEsgenpppKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLldAESEDRPKQRW 854
Cdd:COG4942    19 ADAAAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEAELAELE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  855 ENIATILEAKCALKYLIGELVSSkIQVSKLESSLKQ--SKTSCADMQKML------FEERNHFAEIETELQAELVRMEQQ 926
Cdd:COG4942    90 KEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALllSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAE 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  927 HQEKVLYLLSQLQQSQMAEKQLEESVSEKeQQLLSTLKCQDEELEKMREVCEQNQQLLRE 986
Cdd:COG4942   169 LEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEA 227
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
561-986 6.67e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  561 IKELELEVINLQKEKEELVlelqtAKKDANQAKLS--ERRRKRLQELEGQIADLKKKlneqskllklKESTERTVSKLNQ 638
Cdd:PRK02224  215 LAELDEEIERYEEQREQAR-----ETRDEADEVLEehEERREELETLEAEIEDLRET----------IAETEREREELAE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  639 EIRMMKNQRVQLMRQMK-------------EDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTE 705
Cdd:PRK02224  280 EVRDLRERLEELEEERDdllaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  706 EAAAANKRLKDALQKQREVADKRKETQS---RGMEGTAARVKNwlgneieVMVSTEEAKRHLNDLLEDRKILAQDVAQLK 782
Cdd:PRK02224  360 ELREEAAELESELEEAREAVEDRREEIEeleEEIEELRERFGD-------APVDLGNAEDFLEELREERDELREREAELE 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  783 EKKESGENPPPKLRRrtfsLTEVR-----GQ-VSESEDSIT-----KQIESLETEMEFRSAQIADLQQKLLDAESedrpk 851
Cdd:PRK02224  433 ATLRTARERVEEAEA----LLEAGkcpecGQpVEGSPHVETieedrERVEELEAELEDLEEEVEEVEERLERAED----- 503
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  852 qrweniatileakcaLKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQ--E 929
Cdd:PRK02224  504 ---------------LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEeaE 568
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122  930 KVLYLLSQLQQSQMAEKQLEESVsEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRE 986
Cdd:PRK02224  569 EAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDE 624
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
345-841 1.03e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   345 DPQTAELNHLKQQvqqlqvlllqahggtlpgsitvepSENLQSLMEKNQSLVEENEKLSRglsEAAGQTAQMLERIILTE 424
Cdd:TIGR00618  372 CQQHTLTQHIHTL------------------------QQQKTTLTQKLQSLCKELDILQR---EQATIDTRTSAFRDLQG 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   425 Q-----ANEKMNAK-LEELRQHAACKLDLQKLVETLED---QELKENVEIICNLQQlITQLSDETVACMAAAIDTAVEQE 495
Cdd:TIGR00618  425 QlahakKQQELQQRyAELCAAAITCTAQCEKLEKIHLQesaQSLKEREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEP 503
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   496 AQVETS---------------PETSRSSDAFTTQHALRQA--QMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQ 558
Cdd:TIGR00618  504 CPLCGScihpnparqdidnpgPLTRRMQRGEQTYAQLETSeeDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   559 DNIKELELEVINLQKEKEELvLELQTAKKDANQAKLSERRRKrlQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQ 638
Cdd:TIGR00618  584 EDIPNLQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPE--QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERV 660
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   639 EIRMMKNQRVQLM----RQMKEDAEKFRQWKQKKDKEVI-QLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAA----A 709
Cdd:TIGR00618  661 REHALSIRVLPKEllasRQLALQKMQSEKEQLTYWKEMLaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAaredA 740
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   710 ANKRLKDALQKQREVADKRKETQSRGMEgtAARVKNWLGNEIEVMVSTEEAKRHLndLLEDRKILAQDVAQLKEKKESG- 788
Cdd:TIGR00618  741 LNQSLKELMHQARTVLKARTEAHFNNNE--EVTAALQTGAELSHLAAEIQFFNRL--REEDTHLLKTLEAEIGQEIPSDe 816
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122   789 --------------ENPPPKLRRRTFSLTEVRGQVSESEDSiTKQIESLETEmefrSAQIADLQQKL 841
Cdd:TIGR00618  817 dilnlqcetlvqeeEQFLSRLEEKSATLGEITHQLLKYEEC-SKQLAQLTQE----QAKIIQLSDKL 878
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
386-621 1.37e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 42.32  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   386 QSLMEKNQSLVEENEKLSRGLSEAAGQTAQM-----------------LERIILTEQANEKMNAKLEELRQHAACKLD-L 447
Cdd:pfam04849   90 QSLLKQNSVLTERNEALEEQLGSAREEILQLrhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDaL 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   448 QKLVETLEDQELKenveiicnLQQLITQLSDETvacmaaaiDTAVEQEAQVetspetsrssdafttqhalrQAQMSKELV 527
Cdd:pfam04849  170 QEKLRGLEEENLK--------LRSEASHLKTET--------DTYEEKEQQL--------------------MSDCVEQLS 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   528 ELNKALA-LKEALARKMTQNDSQLQPIQyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQ--AKLSErRRKRLQE 604
Cdd:pfam04849  214 EANQQMAeLSEELARKMEENLRQQEEIT-SLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQltSELQE-LQDRYAE 291
                          250
                   ....*....|....*..
gi 116686122   605 LEGQIADLKKKLNEQSK 621
Cdd:pfam04849  292 CLGMLHEAQEELKELRK 308
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
508-641 2.17e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  508 SDAFTTqhALR-----------QAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKE 576
Cdd:PRK00409  488 SNAFEI--AKRlglpeniieeaKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED 565
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122  577 ELVLEL-QTAKKDANQAKL-SERRRKRLQEL---------EGQIADLKKKLNEQSKLL---KLKESTERTVSKLNQEIR 641
Cdd:PRK00409  566 KLLEEAeKEAQQAIKEAKKeADEIIKELRQLqkggyasvkAHELIEARKRLNKANEKKekkKKKQKEKQEELKVGDEVK 644
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
433-983 2.42e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  433 KLEELRQHAACKLDlqKLVETLEDQElkENVEIICNLQQLITQLSDETVACM---AAAIDTAVEQEAQVETSPETSRS-- 507
Cdd:PRK02224  224 RYEEQREQARETRD--EADEVLEEHE--ERREELETLEAEIEDLRETIAETErerEELAEEVRDLRERLEELEEERDDll 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  508 -----SDAFTTQHALRQAQMSKELVELNKALAlKEALARKMTQNDSQlqpiqyQYQDNIKELELEVINLQKEKEELVLEL 582
Cdd:PRK02224  300 aeaglDDADAEAVEARREELEDRDEELRDRLE-ECRVAAQAHNEEAE------SLREDADDLEERAEELREEAAELESEL 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  583 QTAKKDAnqaklsERRRKRLQELEGQIADLKKKLNeqskllklkestertvsklnqeirmmkNQRVQLmrqmkEDAEKFR 662
Cdd:PRK02224  373 EEAREAV------EDRREEIEELEEEIEELRERFG---------------------------DAPVDL-----GNAEDFL 414
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  663 QwkqkkdkevIQLKERDRKRQyELLKLERNFQKQSNVLrRKTEEAAAANK-----------RLKDALQKQREvadkRKET 731
Cdd:PRK02224  415 E---------ELREERDELRE-REAELEATLRTARERV-EEAEALLEAGKcpecgqpvegsPHVETIEEDRE----RVEE 479
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  732 QSRGMEGTAARVKNwLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTfslTEVRGQVSE 811
Cdd:PRK02224  480 LEAELEDLEEEVEE-VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA---AELEAEAEE 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  812 SEDSITKQIESLETEMEfrsaQIADLQQKLldAESEDRpKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQS 891
Cdd:PRK02224  556 KREAAAEAEEEAEEARE----EVAELNSKL--AELKER-IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRER 628
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  892 ktscadmqkmLFEERNHFAEIETELQAElvRMEQQHQEKvlyllsqlQQSQMAEKQLEESVSEKEQQ---LLSTLKCQDE 968
Cdd:PRK02224  629 ----------LAEKRERKRELEAEFDEA--RIEEAREDK--------ERAEEYLEQVEEKLDELREErddLQAEIGAVEN 688
                         570
                  ....*....|....*
gi 116686122  969 ELEKMREVCEQNQQL 983
Cdd:PRK02224  689 ELEELEELRERREAL 703
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
524-702 2.63e-03

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 41.52  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    524 KELVELNKALALKEALARKMTQNDSQLQ-PIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKrL 602
Cdd:smart00533   79 RDLLRLYDSLEGLKEIRQLLESLDGPLLgLLLKVILEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREK-L 157
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122    603 QELEGQIADLKKKLNEQSKLLKLKestERTVSKLNQEIRMMKNQRVQL-----MRQMKEDAEKFRQWK-QKKDKEVIQLK 676
Cdd:smart00533  158 EELEEELEELLKKEREELGIDSLK---LGYNKVHGYYIEVTKSEAKKVpkdfiRRSSLKNTERFTTPElKELENELLEAK 234
                           170       180
                    ....*....|....*....|....*..
gi 116686122    677 ERDRKRQYELLK-LERNFQKQSNVLRR 702
Cdd:smart00533  235 EEIERLEKEILReLLEKVLEYLEELRA 261
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
424-635 2.77e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  424 EQANEKMNAKLEELRQHAACKLDLQKLVETLEDQeLKENVEIICNLQQLITQLSDEtvacmaaaIDTAVEQEAQVETSPE 503
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAE--------LAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  504 TSRSSDAFTTQHALRQAQMSKELVELN--------KALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEK 575
Cdd:COG4942   101 AQKEELAELLRALYRLGRQPPLALLLSpedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122  576 EELVLELQTAKKD-ANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSK 635
Cdd:COG4942   181 AELEEERAALEALkAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
666-841 2.89e-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: 40.68  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  666 QKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKN 745
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  746 WLGNEIEvmvSTEEAKRHLND----LLEDRKILAQDVAQLKEKkesgenpppklrrrtfsLTEVRGQVSESEDSITKQIE 821
Cdd:COG1579    93 ALQKEIE---SLKRRISDLEDeileLMERIEELEEELAELEAE-----------------LAELEAELEEKKAELDEELA 152
                         170       180
                  ....*....|....*....|
gi 116686122  822 SLETEMEFRSAQIADLQQKL 841
Cdd:COG1579   153 ELEAELEELEAEREELAAKI 172
PLN02939 PLN02939
transferase, transferring glycosyl groups
368-581 4.94e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.43  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  368 AHGGTLPGSITVEPSENLQSLMEKNQSLVEENEKLSRGLSEaagqTAQMLERIILTEQANEKMNAKLEELR-QHAACKLD 446
Cdd:PLN02939  211 LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE----VAETEERVFKLEKERSLLDASLRELEsKFIVAQED 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  447 LQKLVeTLEDQELKENVEiicNLQQLITQLSDEtVACMAAAIDTAVEQEAQVETSPETsrssdafttqhaLRQAQMSK-- 524
Cdd:PLN02939  287 VSKLS-PLQYDCWWEKVE---NLQDLLDRATNQ-VEKAALVLDQNQDLRDKVDKLEAS------------LKEANVSKfs 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  525 -ELVEL--NKALALKEALARKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLE 581
Cdd:PLN02939  350 sYKVELlqQKLKLLEERLQASDHEIHSYIQ----LYQESIKEFQDTLSKLKEESKKRSLE 405
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
577-824 5.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 5.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  577 ELVLELQTAKKDANQAKlseRRRKRLQELEGQIADLKKKLNeqsKLLKLKESTERTVSklnQEIRMMKNQRVQLMRQMKE 656
Cdd:COG4913   215 EYMLEEPDTFEAADALV---EHFDDLERAHEALEDAREQIE---LLEPIRELAERYAA---ARERLAELEYLRAALRLWF 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  657 DAEKFRQWKQkkdkEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRgm 736
Cdd:COG4913   286 AQRRLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER-- 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  737 egTAARVKNWLgNEIEVMVSTEEAkrhlnDLLEDRKILAQDVAQLKEKKESGENpppKLRRRTFSLTEVRGQvsesEDSI 816
Cdd:COG4913   360 --RRARLEALL-AALGLPLPASAE-----EFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRE----LREL 424

                  ....*...
gi 116686122  817 TKQIESLE 824
Cdd:COG4913   425 EAEIASLE 432
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
384-617 6.36e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  384 NLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERI-ILTEQanekmnakLEELRqhaacKLDLQKLvetlEDQELKE- 461
Cdd:COG0497   152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELdLLRFQ--------LEELE-----AAALQPG----EEEELEEe 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  462 -----NVE-IICNLQQLITQLSDETVACM------------AAAIDTAVE------QEAQVETSpETSRSsdaftTQHAL 517
Cdd:COG0497   215 rrrlsNAEkLREALQEALEALSGGEGGALdllgqalralerLAEYDPSLAelaerlESALIELE-EAASE-----LRRYL 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  518 RQAQMS-KELVELNKALALKEALARKmtqndsqlqpiqyqYQDNIKEL---------ELEVI-NLQKEKEELVLELQTAK 586
Cdd:COG0497   289 DSLEFDpERLEEVEERLALLRRLARK--------------YGVTVEELlayaeelraELAELeNSDERLEELEAELAEAE 354
                         250       260       270
                  ....*....|....*....|....*....|...
gi 116686122  587 KDANQA--KLSERRRKRLQELEGQIADLKKKLN 617
Cdd:COG0497   355 AELLEAaeKLSAARKKAAKKLEKAVTAELADLG 387
PRK00566 PRK00566
DNA-directed RNA polymerase subunit beta'; Provisional
536-606 8.56e-03

DNA-directed RNA polymerase subunit beta'; Provisional


Pssm-ID: 234794 [Multi-domain]  Cd Length: 1156  Bit Score: 40.44  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  536 KEALARKMTQNDSQLQPIQYQYQDN---------IKELeLEVINLQKEKEELVLELQTAKKDANQAKLSerrrKRLQELE 606
Cdd:PRK00566  141 DTPLEKKQLLTEEEYREALEEYGDEfvakmgaeaIKEL-LKNIDLEAEAEELREELKETGSEQKRKKAL----KRLKVVE 215
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
561-682 8.90e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  561 IKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRR--KRLQ----ELEGQIADLKK---KLNEQSKLLKLKESTE- 630
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEqvERLEaeveELEAELEEKDErieRLERELSEARSEERREi 461
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116686122  631 ---RTVSKLNQEIRMMKNQRvqlmRQMKEDAEKFRQwKQKKDKEVIQLKERDRKR 682
Cdd:COG2433   462 rkdREISRLDREIERLEREL----EEERERIEELKR-KLERLKELWKLEHSGELV 511
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
649-992 8.94e-03

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: 40.48  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   649 QLMRQMKEDAEKFRQWKQKKDKEVIQlKERDRKRQYELLKLERN----FQKQSNVLRRKTEEAAAANKRLKDALQKQREV 724
Cdd:pfam05483   78 RLYSKLYKEAEKIKKWKVSIEAELKQ-KENKLQENRKIIEAQRKaiqeLQFENEKVSLKLEEEIQENKDLIKENNATRHL 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   725 ADKRKETQSRGMEGTAarvknwlgneiEVMVSTEEAKRHLNDLLEDrkiLAQDVAQLKEKKESGENPPPKLRrrtFSLTE 804
Cdd:pfam05483  157 CNLLKETCARSAEKTK-----------KYEYEREETRQVYMDLNNN---IEKMILAFEELRVQAENARLEMH---FKLKE 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   805 VRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLD-----AESEDRPKQ-------RWENIATILEAKcalKYLIG 872
Cdd:pfam05483  220 DHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltfllEESRDKANQleektklQDENLKELIEKK---DHLTK 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   873 ELVSSKIQVSKLESSLKQ--------SKTSC--ADMQKMLFEERNH----FAEIETELQA------ELVRMEQQHQEKvl 932
Cdd:pfam05483  297 ELEDIKMSLQRSMSTQKAleedlqiaTKTICqlTEEKEAQMEELNKakaaHSFVVTEFEAttcsleELLRTEQQRLEK-- 374
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122   933 yllsQLQQSQMAEKQLEESVSEKEQqlLSTLKCQDE-ELEKMREVCEQNQQLLRENEIIKQ 992
Cdd:pfam05483  375 ----NEDQLKIITMELQKKSSELEE--MTKFKNNKEvELEELKKILAEDEKLLDEKKQFEK 429
COG5022 COG5022
Myosin heavy chain [General function prediction only];
598-894 9.10e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  598 RRKRLQELEGQIADLKKKLNEQSKL------------LKLKESTERTVSKLNQeIRMMKNQRVQLMRQMK-EDAEKFRQW 664
Cdd:COG5022   808 SRKEYRSYLACIIKLQKTIKREKKLreteevefslkaEVLIQKFGRSLKAKKR-FSLLKKETIYLQSAQRvELAERQLQE 886
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  665 KQKKDKEVIQLKERDRKRQYELLKLERNFQkqsNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEG---TAA 741
Cdd:COG5022   887 LKIDVKSISSLKLVNLELESEIIELKKSLS---SDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhEVE 963
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122  742 RVKNWLGNEIEVMV-STEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRG--QVSESEDSITK 818
Cdd:COG5022   964 SKLKETSEEYEDLLkKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSasKIISSESTELS 1043
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116686122  819 QIESLETEMEFRSAQIADLQQKLLDAESedrPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTS 894
Cdd:COG5022  1044 ILKPLQKLKGLLLLENNQLQARYKALKL---RRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQ 1116
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
385-724 9.63e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQ--ELKEN 462
Cdd:pfam05622   23 VSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEvlELQHR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   463 VEIICNLQQLITQLSDETVACMAAAiDTAVEQEAQVETSPE----------TSRSSDAFTTQHALRQAQMSKELVELNKA 532
Cdd:pfam05622  103 NEELTSLAEEAQALKDEMDILRESS-DKVKKLEATVETYKKkledlgdlrrQVKLLEERNAEYMQRTLQLEEELKKANAL 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   533 LALKEALARKMTQNDSQLQPIQYQY---QDNIKELELEVINLQKEKEELVLELQTAKK--------DANQAKLS------ 595
Cdd:pfam05622  182 RGQLETYKRQVQELHGKLSEESKKAdklEFEYKKLEEKLEALQKEKERLIIERDTLREtneelrcaQLQQAELSqadall 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   596 -----------------ERRRK--RLQeLEGQIADLKKKLNEQSKLLKLK---ESTERTVSKLNQEIRMmKNQRVQLMRQ 653
Cdd:pfam05622  262 spssdpgdnlaaeimpaEIREKliRLQ-HENKMLRLGQEGSYRERLTELQqllEDANRRKNELETQNRL-ANQRILELQQ 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122   654 MKEDAEKFRQW-----------KQKKDKEVIQLKERDRKRQYELLKLERNFQKQSN-----------VLRRKTEEAAAAN 711
Cdd:pfam05622  340 QVEELQKALQEqgskaedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSnlaqkidelqeALRKKDEDMKAME 419
                          410
                   ....*....|...
gi 116686122   712 KRLKDALQKQREV 724
Cdd:pfam05622  420 ERYKKYVEKAKSV 432
 
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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