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Conserved domains on  [gi|115648101|ref|NP_776123.3|]
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centromere-associated protein E

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List of domain hits

Name Accession Description Interval E-value
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
6-329 2.90e-164

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: 509.95  E-value: 2.90e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELGEatHIYWKTDKNAIYQSD-GGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFA 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINE--QVAWEIDNDTIYLVEpPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   85 YGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPEREFLLRVSYMEIYNETITDLLCNAqkMKPLIIREDTNRTVYV 164
Cdd:cd01374    79 YGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLKIRDDVEKGVYV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  165 SDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPsnCDGSVKVSHLNLVDLAGSERAAQ 244
Cdd:cd01374   157 AGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGEL--EEGTVRVSTLNLIDLAGSERAAQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  245 TGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTTLQF 322
Cdd:cd01374   235 TGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAEshVEETLNTLKF 314

                  ....*..
gi 115648101  323 ASTAKYM 329
Cdd:cd01374   315 ASRAKKI 321
DUF972 super family cl22921
Protein of unknown function (DUF972); This family consists of several hypothetical bacterial ...
1041-1119 8.77e-03

Protein of unknown function (DUF972); This family consists of several hypothetical bacterial sequences. The function of this family is unknown.


The actual alignment was detected with superfamily member pfam06156:

Pssm-ID: 283750  Cd Length: 106  Bit Score: 37.15  E-value: 8.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115648101  1041 DSLMQENSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEelriLRDELKRQQEVAAQEKdhatEKTQELSRTQERLAK 1119
Cdd:pfam06156    8 DQLDELEEQLGQLLAELGELKDQLAELLEENAELRIENEH----LRERLEEEEKEEEKEK----EKKQGLGEGYDNLAR 78
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
6-336 1.40e-138

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: 438.16  E-value: 1.40e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101      6 SVAVCVRVRPLNSREEELGEATHIYW------KTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFpdkvgkTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101     80 GTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKF-PEREFLLRVSYMEIYNETITDLLCNAQKmkPLIIREDT 158
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLNPSSK--KLEIREDE 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    159 NRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSncdGSVKVSHLNLVDLAG 238
Cdd:smart00129  159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS---GSGKASKLNLVDLAG 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    239 SERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPA--SLDET 316
Cdd:smart00129  236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSssNLEET 315
                           330       340
                    ....*....|....*....|
gi 115648101    317 LTTLQFASTAKYMKNTPYVN 336
Cdd:smart00129  316 LSTLRFASRAKEIKNKPIVN 335
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1100-1841 7.97e-06

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: 50.11  E-value: 7.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1100 KDHATEKTQELSRTQERLAK-----------TEEKLEEKNQKLQETQQQLLSTQEAMSKLQ--AKVIDMESLQNEFRNQG 1166
Cdd:pfam05483   66 KDSDFENSEGLSRLYSKLYKeaekikkwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQfeNEKVSLKLEEEIQENKD 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1167 LALERVETEKL--ELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELniaHANLKEYQE 1244
Cdd:pfam05483  146 LIKENNATRHLcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEM---HFKLKEDHE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1245 IITELRgsisENEAQGASTQDTAKSAPELQGEVPEQELLPVVKEARHSAEKVNGLEpvgaHSRTVHSMTMEGIEIENLRL 1324
Cdd:pfam05483  223 KIQHLE----EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDENLKELIEKKDHL 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1325 TKKLEESQMEiscLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETE 1404
Cdd:pfam05483  295 TKELEDIKMS---LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1405 LSSVRGQLALTTAELERKVQELCE-----KQEELTRKETSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEES 1479
Cdd:pfam05483  372 LEKNEDQLKIITMELQKKSSELEEmtkfkNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1480 QE--EMKTLREEREELRRMQEALHVESEQQKESMKEI----SSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEA 1553
Cdd:pfam05483  452 IHdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltaHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1554 QKSTLEKVEMENVNLtqrlhetleemrsvakeRDELWSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQE 1633
Cdd:pfam05483  532 MLKQIENLEEKEMNL-----------------RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1634 TINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEaqsstlesREIEKL 1713
Cdd:pfam05483  595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ--------KEIEDK 666
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1714 ELTQQlnenlkkiTLVTKENDSLKIMDEALREERdQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETM-SEK 1792
Cdd:pfam05483  667 KISEE--------KLLEEVEKAKAIADEAVKLQK-EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKeQEQ 737
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*....
gi 115648101  1793 TEEISNMKMELENVNMKLQEKVQELKTSERQRVKLKADASEAKKELKEQ 1841
Cdd:pfam05483  738 SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
586-1436 6.00e-24

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: 109.76  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   586 LLKEKEEQIKNLQeyIDAQKSEKMKidlsytsDATEDLKQAMRTLSDLDTVALDAKKEsaflrsenlELKEKINELSDSR 665
Cdd:TIGR02168  194 ILNELERQLKSLE--RQAEKAERYK-------ELKAELRELELALLVLRLEELREELE---------ELQEELKEAEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   666 KQMESDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVdgkgllSNLELEKRITDlQKELNKEAEEKQTLQEEVNL 745
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI------SRLEQQKQILR-ERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   746 LSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQLSRRGSDGEWQALESL 825
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   826 HAELEHRhagvleeRERLKQEIGALSKEAESLAFslDSVKAELSHKTQELEQktvegqerlnkmeaLREELESRDSSLQS 905
Cdd:TIGR02168  409 LERLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEE--------------LQEELERLEEALEE 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   906 VEKEKVLLTEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLR---------SDIQDTVNMNIDTQEQLLNALEslkqh 976
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKallknqsglSGILGVLSELISVDEGYEAAIE----- 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   977 qetinmlkmKAAEELSDNLHVKDRGGARDEAQqkmdgIDEQNESAHTL---LGGGKDNEVTEEQRkiDSLMQENSGLQQT 1053
Cdd:TIGR02168  541 ---------AALGGRLQAVVVENLNAAKKAIA-----FLKQNELGRVTflpLDSIKGTEIQGNDR--EILKNIEGFLGVA 604
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1054 LESVRAEKEQLKM------------DLKENIEMSIENQEELRI--LRDELKRQQEVAAQEKDHAT----EKTQELSRTQE 1115
Cdd:TIGR02168  605 KDLVKFDPKLRKAlsyllggvlvvdDLDNALELAKKLRPGYRIvtLDGDLVRPGGVITGGSAKTNssilERRREIEELEE 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1116 RLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQglaLERVETEKLELAQRLHESYEEVKSITK 1195
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---LARLEAEVEQLEERIAQLSKELTELEA 761
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1196 ERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQEIITELRGSISENEAQGASTQDTAKSAPELQG 1275
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1276 EVPEQellpvVKEARHSAEKVNGLepvgahsrtvhsmtMEGIEIENLRLTKKLEESQMEISCLTREREDLRRTQETLQVE 1355
Cdd:TIGR02168  842 DLEEQ-----IEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1356 CTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSqretELSSVRGQLALT-TAELERKVQELCEKQEELT 1434
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----EEYSLTLEEAEAlENKIEDDEEEARRRLKRLE 978

                   ..
gi 115648101  1435 RK 1436
Cdd:TIGR02168  979 NK 980
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1570-2128 6.52e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


:

Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 56.69  E-value: 6.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1570 QRLHETLEEMRSVAKERDELWS--MEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTD 1647
Cdd:COG0419   174 ELLKEVIKEAKAKIEELEGQLSelLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEE 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1648 EishtqgdlkhtnavveaqNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKIT 1727
Cdd:COG0419   254 L------------------KARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1728 LVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETMSEKTEEISNMKMELENVN 1807
Cdd:COG0419   316 ELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELK 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1808 MKLQE---KVQELKTSERQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEM-------KSVRKERDdlK 1877
Cdd:COG0419   396 EELAElsaALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGekcpvcgQELPEEHE--K 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1878 KLEEILRMERDQLKDNLREAMLKAHQNHE------ETMKCGKGLLCAGEYCTGRLREKCFRIEKLLKRYSEMANDYECLN 1951
Cdd:COG0419   474 ELLELYELELEELEEELSREKEEAELREEieelekELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQ 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1952 KVSLDLERETKTQKELSVtvrTKLSLPHTQTKEMEKLLTANQRCSLEFHRALKRLKYVLSSIARIKEEQHESINKREM-- 2029
Cdd:COG0419   554 LQQLKEELRQLEDRLQEL---KELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELee 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 2030 ------AFIQEVEKQNELQIQIQSLSQTYRIPARDLQIKLSQEmDLHIEEMLKDFSENDFLT-IKTEVQQVLNNRKEITE 2102
Cdd:COG0419   631 aeeeleSELEKLNLQAELEELLQAALEELEEKVEELEAEIRRE-LQRIENEEQLEEKLEELEqLEEELEQLREELEELLK 709
                         570       580
                  ....*....|....*....|....*.
gi 115648101 2103 FLGKWLNTLFDTENLKSTIQKENKSI 2128
Cdd:COG0419   710 KLGEIEQLIEELESRKAELEELKKEL 735
 
Name Accession Description Interval E-value
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
6-329 2.90e-164

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: 509.95  E-value: 2.90e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELGEatHIYWKTDKNAIYQSD-GGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFA 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINE--QVAWEIDNDTIYLVEpPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   85 YGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPEREFLLRVSYMEIYNETITDLLCNAqkMKPLIIREDTNRTVYV 164
Cdd:cd01374    79 YGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLKIRDDVEKGVYV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  165 SDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPsnCDGSVKVSHLNLVDLAGSERAAQ 244
Cdd:cd01374   157 AGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGEL--EEGTVRVSTLNLIDLAGSERAAQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  245 TGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTTLQF 322
Cdd:cd01374   235 TGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAEshVEETLNTLKF 314

                  ....*..
gi 115648101  323 ASTAKYM 329
Cdd:cd01374   315 ASRAKKI 321
DUF972 pfam06156
Protein of unknown function (DUF972); This family consists of several hypothetical bacterial ...
1041-1119 8.77e-03

Protein of unknown function (DUF972); This family consists of several hypothetical bacterial sequences. The function of this family is unknown.


Pssm-ID: 283750  Cd Length: 106  Bit Score: 37.15  E-value: 8.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115648101  1041 DSLMQENSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEelriLRDELKRQQEVAAQEKdhatEKTQELSRTQERLAK 1119
Cdd:pfam06156    8 DQLDELEEQLGQLLAELGELKDQLAELLEENAELRIENEH----LRERLEEEEKEEEKEK----EKKQGLGEGYDNLAR 78
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
6-336 1.40e-138

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: 438.16  E-value: 1.40e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101      6 SVAVCVRVRPLNSREEELGEATHIYW------KTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFpdkvgkTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101     80 GTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKF-PEREFLLRVSYMEIYNETITDLLCNAQKmkPLIIREDT 158
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLNPSSK--KLEIREDE 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    159 NRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSncdGSVKVSHLNLVDLAG 238
Cdd:smart00129  159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS---GSGKASKLNLVDLAG 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    239 SERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPA--SLDET 316
Cdd:smart00129  236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSssNLEET 315
                           330       340
                    ....*....|....*....|
gi 115648101    317 LTTLQFASTAKYMKNTPYVN 336
Cdd:smart00129  316 LSTLRFASRAKEIKNKPIVN 335
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1100-1841 7.97e-06

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: 50.11  E-value: 7.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1100 KDHATEKTQELSRTQERLAK-----------TEEKLEEKNQKLQETQQQLLSTQEAMSKLQ--AKVIDMESLQNEFRNQG 1166
Cdd:pfam05483   66 KDSDFENSEGLSRLYSKLYKeaekikkwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQfeNEKVSLKLEEEIQENKD 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1167 LALERVETEKL--ELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELniaHANLKEYQE 1244
Cdd:pfam05483  146 LIKENNATRHLcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEM---HFKLKEDHE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1245 IITELRgsisENEAQGASTQDTAKSAPELQGEVPEQELLPVVKEARHSAEKVNGLEpvgaHSRTVHSMTMEGIEIENLRL 1324
Cdd:pfam05483  223 KIQHLE----EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDENLKELIEKKDHL 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1325 TKKLEESQMEiscLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETE 1404
Cdd:pfam05483  295 TKELEDIKMS---LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1405 LSSVRGQLALTTAELERKVQELCE-----KQEELTRKETSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEES 1479
Cdd:pfam05483  372 LEKNEDQLKIITMELQKKSSELEEmtkfkNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1480 QE--EMKTLREEREELRRMQEALHVESEQQKESMKEI----SSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEA 1553
Cdd:pfam05483  452 IHdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltaHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1554 QKSTLEKVEMENVNLtqrlhetleemrsvakeRDELWSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQE 1633
Cdd:pfam05483  532 MLKQIENLEEKEMNL-----------------RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1634 TINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEaqsstlesREIEKL 1713
Cdd:pfam05483  595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ--------KEIEDK 666
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1714 ELTQQlnenlkkiTLVTKENDSLKIMDEALREERdQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETM-SEK 1792
Cdd:pfam05483  667 KISEE--------KLLEEVEKAKAIADEAVKLQK-EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKeQEQ 737
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*....
gi 115648101  1793 TEEISNMKMELENVNMKLQEKVQELKTSERQRVKLKADASEAKKELKEQ 1841
Cdd:pfam05483  738 SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
Kinesin pfam00225
Kinesin motor domain;
12-327 6.09e-136

Kinesin motor domain;


Pssm-ID: 278646 [Multi-domain]  Cd Length: 325  Bit Score: 430.45  E-value: 6.09e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    12 RVRPLNSREEELGEA-------THIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFA 84
Cdd:pfam00225    1 RVRPLNEREKSRGSSdivsveePVDSETVESSHLTNKNKPKTFTFDKVFDPEATQEDVYEEVAKPLVESVLEGYNVTIFA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    85 YGQTASGKTHTMMGSEDCL-GVIPRAIHDIFQRIKKFP-EREFLLRVSYMEIYNETITDLLCNAQKMKPLIIREDTNRTV 162
Cdd:pfam00225   81 YGQTGSGKTYTMEGSPDEDpGIIPRALEDLFDRIQKTPrNFSFSVKVSYLEIYNEKIRDLLSPESKRKPLRIREDPKKGV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   163 YVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEpsncDGSVKVSHLNLVDLAGSERA 242
Cdd:pfam00225  161 YVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAVFTITLEQRNRST----GGEVKTSKLNLVDLAGSERA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   243 AQTG-AEGVRLKEGCFINRNLFILGQVIKKLSDGQvGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTT 319
Cdd:pfam00225  237 SKTGaAEGQRLKEAANINKSLSALGNVISALADGK-SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSsnYEETLST 315

                   ....*...
gi 115648101   320 LQFASTAK 327
Cdd:pfam00225  316 LRFASRAK 323
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
21-425 1.70e-68

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 244.65  E-value: 1.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   21 EELGEATHIYWKTDKNAI--YQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFAYGQTASGKTHTMMG 98
Cdd:COG5059    30 IIPGELGERLINTSKKSHvsLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   99 SEDCLGVIPRAIHDIFQRIKKFP-EREFLLRVSYMEIYNETITDLL-CNAQKmkpLIIREDTNRTVYVSDLTEEVVYTAE 176
Cdd:COG5059   110 TEEEPGIIPLSLKELFSKLEDLSmTKDFAVSISYLEIYNEKIYDLLsPNEES---LNIREDSLLGVKVAGLTEKHVSSKE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  177 MALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDGSvkvshLNLVDLAGSERAAQTGAEGVRLKEGC 256
Cdd:COG5059   187 EILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSK-----LSLVDLAGSERAARTGNRGTRLKEGA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  257 FINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTTLQFASTAKYMKNTPY 334
Cdd:COG5059   262 SINKSLLTLGNVINALGDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSnsFEETINTLKFASRAKSIKNKIQ 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  335 VNEVSNDEALLKRYRREIADLRKQleevNTKTRAQEMEKDQLAQLLDEKDLLQKVQDEKINNLKRMLVTSSSIALQQELE 414
Cdd:COG5059   342 VNSSSDSSREIEEIKFDLSEDRSE----IEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFER 417
                         410
                  ....*....|.
gi 115648101  415 IKRKRRVTWCY 425
Cdd:COG5059   418 KKLLKEEGWKY 428
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-362 4.07e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.53  E-value: 4.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    4 EASVAVCVRVRPLNSREEElgeaTHIYWKTDKNAIyqSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIF 83
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGEEG----EMIVQKMSNDSL--TINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVF 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   84 AYGQTASGKTHTMMG----------SEDCLGVIPRAIHDIFQRIK----KFPERE--FLLRVSYMEIYNETITDLLCNAQ 147
Cdd:PLN03188  171 AYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINeeqiKHADRQlkYQCRCSFLEIYNEQITDLLDPSQ 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  148 KmkPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKaepSNCDG--S 225
Cdd:PLN03188  251 K--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCK---SVADGlsS 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  226 VKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSD-GQVGG--FINYRDSKLTRILQNSLGGNAKT 302
Cdd:PLN03188  326 FKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKqrHIPYRDSRLTFLLQESLGGNAKL 405
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115648101  303 RIICTITPAS--LDETLTTLQFASTAKYMKNTPYVNEVSNDEalLKRYRREIADLRKQLEEV 362
Cdd:PLN03188  406 AMVCAISPSQscKSETFSTLRFAQRAKAIKNKAVVNEVMQDD--VNFLREVIRQLRDELQRV 465
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
834-1620 3.33e-24

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 110.57  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  834 AGVLEERERLKQEIGALSKEAESLafsldsvkaeLSHKTQELEQKTVEGQERLNKMEALREELESRDSSLQSVEKEKVLL 913
Cdd:COG1196   189 ERLEDLLEELEKQLEKLERQAEKA----------ERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEEL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  914 TEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLRSDIQDTVNMNIDTQEQLLNALESLKQHQETINMLKMKAAEELSD 993
Cdd:COG1196   259 QEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEE 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  994 NLHVKDRGGARDEAQQKMDGIDEQNESAHTLLGGGKDNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKMDLKENIE 1073
Cdd:COG1196   339 LEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSE 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1074 MSIENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLlstqeamSKLQAKVI 1153
Cdd:COG1196   419 RLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKEL-------SSLEARLD 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1154 DMESLQNEFRNQGLALERVETEKLELAQRLHE--SYEEVKSITKER-----------NDLKELQESFEIEKKQLKEYARE 1220
Cdd:COG1196   492 RLEAEQRASQGVRAVLEALESGLPGVYGPVAEliKVKEKYETALEAalgnrlqavvvENEEVAKKAIEFLKENKAGRATF 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1221 IEAAGLQTKEELNIAHAN------------------------------------------LKEYQEIIT------ELRGS 1252
Cdd:COG1196   572 LPLDRIKPLRSLKSDAAPgflglasdlidfdpkyepavrfvlgdtlvvddleqarrlarkLRIKYRIVTldgdlvEPSGS 651
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1253 ISENEAQGASTQDTAKSAPELQGEVpeQELLPVVKEARHSAEKVNG-----LEPVGAHSRTVHSMTMEGIEIENL--RLT 1325
Cdd:COG1196   652 ITGGSRNKRSSLAQKRELKELEEEL--AELEAQLEKLEEELKSLKNelrslEDLLEELRRQLEELERQLEELKRElaALE 729
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1326 KKLEESQMEISCLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETEL 1405
Cdd:COG1196   730 EELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRL 809
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1406 SSVRGQLALTTAELERKVQELCEKQEELtrketSEAQGKMSELEQLRELLLAQasaLQNAESDRLRLNTQLEESQEEMKT 1485
Cdd:COG1196   810 DALERELESLEQRRERLEQEIEELEEEI-----EELEEKLDELEEELEELEKE---LEELKEELEELEAEKEELEDELKE 881
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1486 LREEREELRRMQEALHVESEQQKESMKEISSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEAQKSTLEK--VEM 1563
Cdd:COG1196   882 LEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEeiEAL 961
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115648101 1564 ENVNLtqrlhETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVTKGMEKEEE 1620
Cdd:COG1196   962 GPVNL-----RAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
586-1436 6.00e-24

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: 109.76  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   586 LLKEKEEQIKNLQeyIDAQKSEKMKidlsytsDATEDLKQAMRTLSDLDTVALDAKKEsaflrsenlELKEKINELSDSR 665
Cdd:TIGR02168  194 ILNELERQLKSLE--RQAEKAERYK-------ELKAELRELELALLVLRLEELREELE---------ELQEELKEAEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   666 KQMESDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVdgkgllSNLELEKRITDlQKELNKEAEEKQTLQEEVNL 745
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI------SRLEQQKQILR-ERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   746 LSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQLSRRGSDGEWQALESL 825
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   826 HAELEHRhagvleeRERLKQEIGALSKEAESLAFslDSVKAELSHKTQELEQktvegqerlnkmeaLREELESRDSSLQS 905
Cdd:TIGR02168  409 LERLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEE--------------LQEELERLEEALEE 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   906 VEKEKVLLTEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLR---------SDIQDTVNMNIDTQEQLLNALEslkqh 976
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKallknqsglSGILGVLSELISVDEGYEAAIE----- 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   977 qetinmlkmKAAEELSDNLHVKDRGGARDEAQqkmdgIDEQNESAHTL---LGGGKDNEVTEEQRkiDSLMQENSGLQQT 1053
Cdd:TIGR02168  541 ---------AALGGRLQAVVVENLNAAKKAIA-----FLKQNELGRVTflpLDSIKGTEIQGNDR--EILKNIEGFLGVA 604
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1054 LESVRAEKEQLKM------------DLKENIEMSIENQEELRI--LRDELKRQQEVAAQEKDHAT----EKTQELSRTQE 1115
Cdd:TIGR02168  605 KDLVKFDPKLRKAlsyllggvlvvdDLDNALELAKKLRPGYRIvtLDGDLVRPGGVITGGSAKTNssilERRREIEELEE 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1116 RLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQglaLERVETEKLELAQRLHESYEEVKSITK 1195
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---LARLEAEVEQLEERIAQLSKELTELEA 761
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1196 ERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQEIITELRGSISENEAQGASTQDTAKSAPELQG 1275
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1276 EVPEQellpvVKEARHSAEKVNGLepvgahsrtvhsmtMEGIEIENLRLTKKLEESQMEISCLTREREDLRRTQETLQVE 1355
Cdd:TIGR02168  842 DLEEQ-----IEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1356 CTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSqretELSSVRGQLALT-TAELERKVQELCEKQEELT 1434
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----EEYSLTLEEAEAlENKIEDDEEEARRRLKRLE 978

                   ..
gi 115648101  1435 RK 1436
Cdd:TIGR02168  979 NK 980
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
604-1259 1.55e-22

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 104.80  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  604 QKSEKMKIDLSYTSDATEDLKQAMRTLSDLDTVALDAKKESAFLRS-ENLELKEKINELSDSRKQMESDIQMYQRQLEAK 682
Cdd:COG1196   179 RKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRElELALLLAKLKELRKELEELEEELSRLEEELEEL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  683 KKMQTDLDKELQLAFQEISklsalvdgkgllsnlELEKRITDLQKELNKEAEEKQTLQEEVNLL----SELKSLPSEVET 758
Cdd:COG1196   259 QEELEEAEKEIEELKSELE---------------ELREELEELQEELLELKEEIEELEGEISLLrerlEELENELEELEE 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  759 LRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQlsrrgsDGEWQALESLHAELEHRHAGVLE 838
Cdd:COG1196   324 RLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEEL------EELFEALREELAELEAELAEIRN 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  839 ERERLKQEIGALSKEAESLAFSLDSVKAELSHKTQELEQKTVEGQERLNKMEALREELESRDSSLQSVEKEKVLLTEKLQ 918
Cdd:COG1196   398 ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQ 477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  919 QALKEVKALTQEKKNLKQLQESLQTERDQLR--------------------------------SDIQDTVNMNIDTQEQL 966
Cdd:COG1196   478 RLEKELSSLEARLDRLEAEQRASQGVRAVLEalesglpgvygpvaelikvkekyetaleaalgNRLQAVVVENEEVAKKA 557
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  967 LNALESLKQHQETINML-KMKAAEELSDNLH------------------------------VKDRGGARDEAQQKMDGI- 1014
Cdd:COG1196   558 IEFLKENKAGRATFLPLdRIKPLRSLKSDAApgflglasdlidfdpkyepavrfvlgdtlvVDDLEQARRLARKLRIKYr 637
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1015 ------DEQNESAHTLLGGGKDNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKmdlkENIEMSIENQEELRILRDE 1088
Cdd:COG1196   638 ivtldgDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLK----NELRSLEDLLEELRRQLEE 713
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1089 LKRQQEVAAQEKDHATEKTQELsrtQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRN---- 1164
Cdd:COG1196   714 LERQLEELKRELAALEEELEQL---QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEkrqa 790
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1165 QGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQE 1244
Cdd:COG1196   791 LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEA 870
                         730
                  ....*....|....*
gi 115648101 1245 IITELRGSISENEAQ 1259
Cdd:COG1196   871 EKEELEDELKELEEE 885
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1077-1896 4.76e-22

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: 103.21  E-value: 4.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1077 ENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDME 1156
Cdd:TIGR02168  222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1157 S----LQNEFRNQGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEEL 1232
Cdd:TIGR02168  302 QqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1233 NIAHANLKEYQEIITELRGSISENEAQGastQDTAKSAPELQGEVPEQELLPVVKEARHSAEKVNGLEpvgahsrtvhsM 1312
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE-----------E 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1313 TMEGIEIENLRLTKKLEESQMEISCLTREREDLRRTQETLQVECTQLK------EDARRTLANHLETEEELNLARCCLKE 1386
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqenlEGFSEGVKALLKNQSGLSGILGVLSE 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1387 Q-------ENKIDTLITSLSQR---ETELSSVRGQLALTTAELERK----VQELCEKQEELTRKETSEAQGKMSELEQLR 1452
Cdd:TIGR02168  528 LisvdegyEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1453 ELLLAQASALQNAESDRLRLNTQLEESQEEMKTLREEREELRRMQEALHVESEQQKESMKEISSKLQelQNKEYECLAmK 1532
Cdd:TIGR02168  608 VKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE--RRREIEELE-E 684
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1533 TINETQGsrcEMDHLNQQLEAQKSTLEKVEMENVNLTQRLHETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVT 1612
Cdd:TIGR02168  685 KIEELEE---KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1613 KGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQME 1692
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1693 QLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLriah 1772
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL---- 917
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1773 mnlkehqetiDRLMETMSEKTEEISNMKMELENVNMKLQEKVQ-ELKTSERQRVKLKADASEAKKELKEqgLTLSKIEME 1851
Cdd:TIGR02168  918 ----------EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKR--LENKIKELG 985
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*
gi 115648101  1852 NLNLAQkihenLEEMKSVRKERDDLKKLEEILRMERDQLKDNLRE 1896
Cdd:TIGR02168  986 PVNLAA-----IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
PTZ00121 PTZ00121
MAEBL; Provisional
1105-1910 1.18e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 75.95  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1105 EKTQELSR--TQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEfrnQGLALERVETEKLELAQR 1182
Cdd:PTZ00121 1027 EKIEELTEygNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKE---DNRADEATEEAFGKAEEA 1103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1183 LHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAgLQTKEELNIAHANLKEYQEIITELRGSISENEAQGAS 1262
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEA-RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1263 TQDTAKSAPELQgevpEQELLPVVKEARHsAEKVNGLEPVGAHSrtvhsmtmEGIEIENLRLTKKLEESQMEisclTRER 1342
Cdd:PTZ00121 1183 KAEEVRKAEELR----KAEDARKAEAARK-AEEERKAEEARKAE--------DAKKAEAVKKAEEAKKDAEE----AKKA 1245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1343 EDLRRTQETLQVECTQLKEDARRTLAnhLETEEELNLARCCLKEQENKIDTLITSLSQRETELSSVRGQLALTTAELERK 1422
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAA--IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1423 VQELCEKQEELTRKETSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEESQEEMKTLREEREElrrmqEALHV 1502
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKK 1398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1503 ESEQQKESMKEISSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEAQKSTLEKVEMENVNLTQRLHETLEEMRSV 1582
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1583 AKER---DELWSMEERLTVERDQLKKSLEET--VTKGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTDEISHTQGDLK 1657
Cdd:PTZ00121 1479 AEEAkkaDEAKKKAEEAKKKADEAKKAAEAKkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1658 HTNAVVEAQNQDLREKEHQLSQVKAD-LRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKENDSL 1736
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1737 KIMDEALREERDQLRKSlqqteardlENQEKLRIAHMNLKEHQetiDRLMETMSEKTEEISNMKMELENVNMKLQEKVQE 1816
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---------EEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1817 LKTSERQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEMKSVRK-ERDDLKKLEEILRMERDQLKDNLR 1895
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlKKEEEKKAEEIRKEKEAVIEEELD 1786
                         810
                  ....*....|....*
gi 115648101 1896 EAMLKAHQNHEETMK 1910
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
PRK03918 PRK03918
chromosome segregation protein; Provisional
719-1269 5.89e-13

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 73.17  E-value: 5.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  719 EKRITDLQKELNKEAEEKQT-LQEEVNLLSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEmahkdsriqglLEE 797
Cdd:PRK03918  164 YKNLGEVIKEIKRRIERLEKfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----------VKE 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  798 IGNTRDDLATSQLSRRGSDGEWQALESLHAELEHRHAGVLEERERLKQEIGALsKEAESLAFSLDSVKAELShktqELEQ 877
Cdd:PRK03918  233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYE----EYLD 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  878 KTVEGQERLNKMEALREELESRDSSLQSVEKEKVLLTEKLQQALKEVKALtQEKKNLKQLQESLQTERDQLRSDIQDtvn 957
Cdd:PRK03918  308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTG--- 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  958 mniDTQEQLLNALESLKQHQETInmlkMKAAEELSDnlhvkDRGGARDEAQQKMDGIDEQNESAHTLLGGGKdnEVTEEQ 1037
Cdd:PRK03918  384 ---LTPEKLEKELEELEKAKEEI----EEEISKITA-----RIGELKKEIKELKKAIEELKKAKGKCPVCGR--ELTEEH 449
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1038 RK--IDSLMQENSGLQQTLESVRAEKEQLKMDLKEnIEMSIENQEELRILRDELKRQQEVAAQEKDHATEKtqelsrtqe 1115
Cdd:PRK03918  450 RKelLEEYTAELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE--------- 519
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1116 rLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQGLALERVETEKLELA----QRLHESYEEVK 1191
Cdd:PRK03918  520 -LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELE 598
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115648101 1192 SITKERNDLKELQESFEIEKKQLKEYAREIEAAglqtKEELNIAHANLKEYQEIITELRGSISENEAQGASTQDTAKS 1269
Cdd:PRK03918  599 PFYNEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS 672
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
511-1245 4.91e-11

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 metabolizm and recombination.


Pssm-ID: 280601 [Multi-domain]  Cd Length: 1162  Bit Score: 67.30  E-value: 4.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   511 NDLVLDYEQLRRENEDLKLKLKEKNELEEFELLEQKEERDQEMQLMHEVSNLKNLIKHAEEYNQDLENDLSSKVKLL-KE 589
Cdd:pfam02463  185 NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIeKE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   590 KEEQIKNLQEYIDAQKSEKMKIDLSYTSDATEDLKQAMRTLSDLDTVALDAKKESAFLRSENLELKEKINELSDSRKQME 669
Cdd:pfam02463  265 EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   670 SDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVDGKGLLS-----NLELEKRITDLQKELNKEAEEKQTLQEEVN 744
Cdd:pfam02463  345 LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkEEELELKSEEEKEAQLLLELARQLEDLLKE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   745 LLSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNT-----------RDDLATSQLSRR 813
Cdd:pfam02463  425 EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVklqeklelllsRQKLEERSQKES 504
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   814 GSDGEWQALESLHAELEHRHAGVLEERERLKQEIGALSKEAESLAFSLDSVKAELSHKTQELEQKTVEGQER-LNKMEAL 892
Cdd:pfam02463  505 KARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLL 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   893 REELESRDSSLQSVEKEKVLLTEKLQQALKEVK------ALTQEKKNLKQLQESLQTERDQLRSDIQDTVNMNIDTQEQL 966
Cdd:pfam02463  585 IPKLKLPLKSIAVLEIDPILNLIQLDKATLEYDednkraKVNTGILKDTLLTGLKESKKALLSGLSFGKSLEEKGAEKSE 664
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   967 LNALESLKQHQETINMLKMKAAEELSDNLHVKdrggARDEAQQKMDGIDEQNESAHTLLGGGKDNEVTEEQRKIDSLMQE 1046
Cdd:pfam02463  665 RKASLSELTKELLEIQELQEKAESELAKEEIL----RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELK 740
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1047 NSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEELRILRDELKRQQEVAAQEKdhatEKTQELSRTQERLAKTEEKLEE 1126
Cdd:pfam02463  741 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE----EKLKAQEEELRALEEELKEEAE 816
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1127 KNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQES 1206
Cdd:pfam02463  817 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIAKEELLQELLLKEEELEEQKLKDELESKEEKE 896
                          730       740       750
                   ....*....|....*....|....*....|....*....
gi 115648101  1207 FEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQEI 1245
Cdd:pfam02463  897 KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 935
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1570-2128 6.52e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 56.69  E-value: 6.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1570 QRLHETLEEMRSVAKERDELWS--MEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTD 1647
Cdd:COG0419   174 ELLKEVIKEAKAKIEELEGQLSelLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEE 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1648 EishtqgdlkhtnavveaqNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKIT 1727
Cdd:COG0419   254 L------------------KARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1728 LVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETMSEKTEEISNMKMELENVN 1807
Cdd:COG0419   316 ELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELK 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1808 MKLQE---KVQELKTSERQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEM-------KSVRKERDdlK 1877
Cdd:COG0419   396 EELAElsaALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGekcpvcgQELPEEHE--K 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1878 KLEEILRMERDQLKDNLREAMLKAHQNHE------ETMKCGKGLLCAGEYCTGRLREKCFRIEKLLKRYSEMANDYECLN 1951
Cdd:COG0419   474 ELLELYELELEELEEELSREKEEAELREEieelekELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQ 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1952 KVSLDLERETKTQKELSVtvrTKLSLPHTQTKEMEKLLTANQRCSLEFHRALKRLKYVLSSIARIKEEQHESINKREM-- 2029
Cdd:COG0419   554 LQQLKEELRQLEDRLQEL---KELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELee 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 2030 ------AFIQEVEKQNELQIQIQSLSQTYRIPARDLQIKLSQEmDLHIEEMLKDFSENDFLT-IKTEVQQVLNNRKEITE 2102
Cdd:COG0419   631 aeeeleSELEKLNLQAELEELLQAALEELEEKVEELEAEIRRE-LQRIENEEQLEEKLEELEqLEEELEQLREELEELLK 709
                         570       580
                  ....*....|....*....|....*.
gi 115648101 2103 FLGKWLNTLFDTENLKSTIQKENKSI 2128
Cdd:COG0419   710 KLGEIEQLIEELESRKAELEELKKEL 735
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1670-1894 9.93e-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: 49.68  E-value: 9.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1670 LREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENL--------KKITLVTKENDSLKIMDE 1741
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEIASLERSIA 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1742 ALREERDQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETMSEKTEEISNMKMELENVNMKLQEKVQELKTSE 1821
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115648101  1822 RQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEMKSVRKERDDLKKLEEILRMERDQLKDNL 1894
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1568-2348 2.33e-05

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


Pssm-ID: 280601 [Multi-domain]  Cd Length: 1162  Bit Score: 48.43  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1568 LTQRLHETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEH-QETINKLRKMVSDYT 1646
Cdd:pfam02463  172 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQ 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1647 DEISHTQGD-------LKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQL 1719
Cdd:pfam02463  252 EEIESSKQEiekeeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1720 NENLKKITLVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENqeklriahmnLKEHQETIDRLMETMSEKTEEISNM 1799
Cdd:pfam02463  332 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL----------LAKKKLESERLSSAAKLKEEELELK 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1800 KMELENV--NMKLQEKVQELKTSERQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEMKSVRKERDDLK 1877
Cdd:pfam02463  402 SEEEKEAqlLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1878 KLEEILRMERDQLKDNLREAMLKAHQNHEETMKCGKGLLCAGEYCTgrlrekcfrIEKLLKRYSEMANDYECLNKVSLDL 1957
Cdd:pfam02463  482 KLQEKLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS---------AHGRLGDLGVAVENYKVAISTAVIV 552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1958 ERetktqkelSVTVRTKLSLPHTQTKEMEKLLTANQRCSLEFHRALKRLKYVLSSIARIKEEqhESINKREMAFIQEVEK 2037
Cdd:pfam02463  553 EV--------SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--IQLDKATLEYDEDNKR 622
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  2038 QNELQIQIQSLSQTYRIPARDLQIKLSQEMdlhIEEMLKDFSENDFLTIKTEVQQVLNNRKEITEFLGKWLNTLFDTENL 2117
Cdd:pfam02463  623 AKVNTGILKDTLLTGLKESKKALLSGLSFG---KSLEEKGAEKSERKASLSELTKELLEIQELQEKAESELAKEEILRRQ 699
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  2118 KSTIQKENKSIGLVNNFYHSRITAMINESTEFEERSATRSKDLDQYLKSLKETTEQLSEVYQTLTASQSVVHLHPTVQPS 2197
Cdd:pfam02463  700 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 779
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  2198 TRDSERPQAASGAEQLTSKNKIALGAVPYKEEIEDLKMQ------LVKSDLEKKATAKEFDKKILSLKATVEHQEEMIRL 2271
Cdd:pfam02463  780 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLeeeqllIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 859
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115648101  2272 LRENLRGHQQAQDTSMISEQDSQLLSKPLTCGGGSGIVQSTKALILKSEYKRMGSEISKLKQQNEQLRKQNNQLLSD 2348
Cdd:pfam02463  860 LEEEIAKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 936
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
336-702 6.98e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.02  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  336 NEVSNDEALLKRYRREIADLRKQLEEVNTKTRAQEMEKDQLAQLLDEKDLLQKVQDEKINNLKRMLVTSSSIALQQELEI 415
Cdd:COG1196   688 EELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  416 KRKRRvtwcygkmKDSNYEKEFKVPTSITTRKRKTSVTSLRENSLMKFGESAASSEFEMLNNTLESLAEvewssattllS 495
Cdd:COG1196   768 ESLEE--------ALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQ----------E 829
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  496 EENVESELNSLNAQYNDLVLDYEQLRRENEDLKLKLKEKNELEEFELLEQKEERDQEMQLMHEVSNLKNLIKHAEEYNQD 575
Cdd:COG1196   830 IEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEK 909
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  576 LENDLSSKVKLLKEKEEQIKNLQEYIDAQksekmkIDLSYTSDATEDLKQAMRTLSDLDTVALDAKKESAFLRSENLELK 655
Cdd:COG1196   910 LRERLEELEAKLERLEVELPELEEELEEE------YEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELK 983
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 115648101  656 EKINELSDSRKQMESDIQMYQRQLEAK-KKMQTDLDKELQLAFQEISK 702
Cdd:COG1196   984 SQREDLEEAKEKLLEVIEELDKEKRERfKETFDKINENFSEIFKELFG 1031
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1779-1908 1.70e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1779 QETIDRLMETMSEKTEEISNMKMELENVNMKLQEKVQELKTSERQRVKLKADASEAKKELKEQgltlskIEMENLNLAQK 1858
Cdd:PRK00409  501 ENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE------EDKLLEEAEKE 574
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115648101 1859 IHENLEEMKsvrKERDD-LKKLEEILRMERDQLKDNLREAMLKA-HQNHEET 1908
Cdd:PRK00409  575 AQQAIKEAK---KEADEiIKELRQLQKGGYASVKAHELIEARKRlNKANEKK 623
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
1750-1877 2.98e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 41.18  E-value: 2.98e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   1750 LRKSLQQTEARDLENQEK-LRIAHMN-----LKEHQETI----DRLMETMSEKTEEISNMKMELEnVNMKLQEKV----Q 1815
Cdd:smart00435  233 LQEQLKELTAKDGNVAEKiLAYNRANrevaiLCNHQRTVskthEKSMEKLQEKIKALKYQLKRLK-KMILLFEMIsdlkR 311
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115648101   1816 ELKTS-ERQRVKLKADASEAKKELKEQGLTLSKIEmenlnlaqKIHENLEEMKSVRKERDDLK 1877
Cdd:smart00435  312 KLKSKfERDNEKLDAEVKEKKKEKKKEEKKKKQIE--------RLEERIEKLEVQATDKEENK 366
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1009-1160 7.74e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 7.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   1009 QKMDGIDEQNESAHTLLGGGKdNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKMDLKENIEmsienqeelrilrDE 1088
Cdd:smart00787  140 KLLEGLKEGLDENLEGLKEDY-KLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP-------------TE 205
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   1089 LKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLLSTQEA-----------MSKLQAKVIDMES 1157
Cdd:smart00787  206 LDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKleqcrgftfkeIEKLKEQLKLLQS 285

                    ...
gi 115648101   1158 LQN 1160
Cdd:smart00787  286 LTG 288
PRK02224 PRK02224
chromosome segregation protein; Provisional
349-897 9.52e-03

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  349 RREIADLRKQLEEVNTKTRAQEMEKDQLA-QLLDEKDLLQKVQDEKINNLKRMLVTSSSI-ALQQELEIKRKRrvtwcyg 426
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAeEVRDLRERLEELEEERDDLLAEAGLDDADAeAVEARREELEDR------- 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  427 kmKDSNYEKEFKVPTSITTrkRKTSVTSLRENSLMKFGESA-ASSEFEMLNNTLESlAEVEWSSATTLLSEenVESELNS 505
Cdd:PRK02224  323 --DEELRDRLEECRVAAQA--HNEEAESLREDADDLEERAEeLREEAAELESELEE-AREAVEDRREEIEE--LEEEIEE 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  506 LNAQYNDLVLDYEQLRRENEDLklklkekneleefeLLEQKEERDQEMQLMHEVSNLKNLIKHAE---------EYNQDL 576
Cdd:PRK02224  396 LRERFGDAPVDLGNAEDFLEEL--------------REERDELREREAELEATLRTARERVEEAEalleagkcpECGQPV 461
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  577 ENdlSSKVKLLKEKEEQIKNLQEyidaqksekmkiDLSYTSDATEDLKQAMRTLSDLdtvaldakKESAFLRSENLELKE 656
Cdd:PRK02224  462 EG--SPHVETIEEDRERVEELEA------------ELEDLEEEVEEVEERLERAEDL--------VEAEDRIERLEERRE 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  657 KINELSDSRkqmESDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVDgkgllsnlELEKRITDLQKELNKEAEEK 736
Cdd:PRK02224  520 DLEELIAER---RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE--------EAREEVAELNSKLAELKERI 588
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  737 QTLQEEVNLLSELKSLPSEVETLRrelyEKSEELHIITTEREKLFSEmahKDSRIQGLLEEIGNTRDDLATSQLSRrgsd 816
Cdd:PRK02224  589 ESLERIRTLLAAIADAEDEIERLR----EKREALAELNDERRERLAE---KRERKRELEAEFDEARIEEAREDKER---- 657
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  817 gewqaLESLHAELEHRHAGVLEERERLKQEIGALSKEAESLafsldsvkaelshktQELEQKTVEGQERLNKMEALREEL 896
Cdd:PRK02224  658 -----AEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL---------------EELRERREALENRVEALEALYDEA 717

                  .
gi 115648101  897 E 897
Cdd:PRK02224  718 E 718
 
Name Accession Description Interval E-value
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
6-329 2.90e-164

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: 509.95  E-value: 2.90e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELGEatHIYWKTDKNAIYQSD-GGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFA 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINE--QVAWEIDNDTIYLVEpPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   85 YGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPEREFLLRVSYMEIYNETITDLLCNAqkMKPLIIREDTNRTVYV 164
Cdd:cd01374    79 YGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLKIRDDVEKGVYV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  165 SDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPsnCDGSVKVSHLNLVDLAGSERAAQ 244
Cdd:cd01374   157 AGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGEL--EEGTVRVSTLNLIDLAGSERAAQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  245 TGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTTLQF 322
Cdd:cd01374   235 TGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAEshVEETLNTLKF 314

                  ....*..
gi 115648101  323 ASTAKYM 329
Cdd:cd01374   315 ASRAKKI 321
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
6-327 2.65e-133

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: 422.82  E-value: 2.65e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELGEATHIYWKTDKNAIY----QSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGT 81
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDppknRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   82 IFAYGQTASGKTHTMMGSEDC-LGVIPRAIHDIFQRIKKFPE--REFLLRVSYMEIYNETITDLLCNAQKmKPLIIREDT 158
Cdd:cd00106    81 IFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKRKEtkSSFSVSASYLEIYNEKIYDLLSPVPK-KPLSLREDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  159 NRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKaepSNCDGSVKVSHLNLVDLAG 238
Cdd:cd00106   160 KRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNR---EKSGESVTSSKLNLVDLAG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  239 SERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQvGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDET 316
Cdd:cd00106   237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQ-NKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSenFEET 315
                         330
                  ....*....|.
gi 115648101  317 LTTLQFASTAK 327
Cdd:cd00106   316 LSTLRFASRAK 326
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
6-330 1.85e-99

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: 326.60  E-value: 1.85e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELGEATHIYWKTDKNAIyQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFAY 85
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQV-TVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   86 GQTASGKTHTMMGS------EDCLGVIPRAIHDIFQRI-KKFPEREFLLRVSYMEIYNETITDLLCNA-QKMKPLIIRED 157
Cdd:cd01372    81 GQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIeKKKDTFEFQLKVSFLEIYNEEIRDLLDPEtDKKPTISIRED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  158 TNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDG-----SVKVSHLN 232
Cdd:cd01372   161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSaddknSTFTSKFH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  233 LVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQ-VGGFINYRDSKLTRILQNSLGGNAKTRIICTITPA 311
Cdd:cd01372   241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
                         330       340
                  ....*....|....*....|.
gi 115648101  312 S--LDETLTTLQFASTAKYMK 330
Cdd:cd01372   321 DsnFEETLNTLKYANRARNIK 341
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
6-327 2.45e-99

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: 325.95  E-value: 2.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELGEATHIYWKTDKNAIYQSDGG-------KSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGY 78
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKataneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   79 NGTIFAYGQTASGKTHTMMG---SEDCLGVIPRAIHDIFQRIKKFPE-REFLLRVSYMEIYNETITDLLCNAQKMKpLII 154
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQTKR-LEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  155 REDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEpsncDGS--VKVSHLN 232
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGE----DGEnhIRVGKLN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  233 LVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQvGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS 312
Cdd:cd01371   237 LVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGK-STHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPAD 315
                         330
                  ....*....|....*..
gi 115648101  313 --LDETLTTLQFASTAK 327
Cdd:cd01371   316 ynYDETLSTLRYANRAK 332
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
4-327 1.06e-98

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: 323.90  E-value: 1.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    4 EASVAVCVRVRPLNSREEELG-EATHIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTI 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGsKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   83 FAYGQTASGKTHTMMGSEDC---LGVIPRAIHDIFQRIKKFPER-EFLLRVSYMEIYNETITDLLcnAQKMKPLIIREDT 158
Cdd:cd01369    81 FAYGQTSSGKTYTMEGKLGDpesMGIIPRIVQDIFETIYSMDENlEFHVKVSYFEIYMEKIRDLL--DVSKTNLSVHEDK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  159 NRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESRekaepSNCDGSVKVSHLNLVDLAG 238
Cdd:cd01369   159 NRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-----NVETEKKKSGKLYLVDLAG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  239 SERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQvGGFINYRDSKLTRILQNSLGGNAKTRIICTITPASLD--ET 316
Cdd:cd01369   234 SEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGK-KTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNesET 312
                         330
                  ....*....|.
gi 115648101  317 LTTLQFASTAK 327
Cdd:cd01369   313 LSTLRFGQRAK 323
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
5-336 1.61e-97

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: 321.99  E-value: 1.61e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    5 ASVAVCVRVRPLNSREEELGEATHIYWK-----------TDKNAIYQSDGGKSFQFDRVFDSNE-------TTKNVYEEI 66
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSgkettlknpkqADKNNKATREVPKSFSFDYSYWSHDsedpnyaSQEQVYEDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   67 AVPIISSAIQGYNGTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRI--KKFPEREFLLRVSYMEIYNETITDLLC 144
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  145 --NAQKMKPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFrMILESREKAEPSNC 222
Cdd:cd01365   161 pkPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVF-TIVLTQKRHDAETN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  223 DGSVKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGG------FINYRDSKLTRILQNSL 296
Cdd:cd01365   240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskkkssFIPYRDSVLTWLLKENL 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 115648101  297 GGNAKTRIICTITPASL--DETLTTLQFASTAKYMKNTPYVN 336
Cdd:cd01365   320 GGNSKTAMIAAISPADInyEETLSTLRYADRAKKIVNRAVVN 361
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
12-324 6.06e-94

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: 310.29  E-value: 6.06e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   12 RVRPLNSrEEELGEATHI-YWKTDKNAIYQSDGG---KSFQFDRVFDSNETTKNVYEEIAvPIISSAIQGYNGTIFAYGQ 87
Cdd:cd01366     9 RVRPLLP-SEENEDTSHItFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEEVS-PLVQSALDGYNVCIFAYGQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   88 TASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPER--EFLLRVSYMEIYNETITDLLCNAQ-KMKPLIIREDT-NRTVY 163
Cdd:cd01366    87 TGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKgwSYTIKASMLEIYNETIRDLLAPGNaPQKKLEIRHDSeKGDTT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  164 VSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDGSvkvshLNLVDLAGSERAA 243
Cdd:cd01366   167 VTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGK-----LNLVDLAGSERLN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  244 QTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQvgGFINYRDSKLTRILQNSLGGNAKTRIICTITPA--SLDETLTTLQ 321
Cdd:cd01366   242 KSGATGDRLKETQAINKSLSALGDVISALRQKQ--SHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAesNLNETLNSLR 319

                  ...
gi 115648101  322 FAS 324
Cdd:cd01366   320 FAS 322
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
7-339 7.49e-93

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: 307.90  E-value: 7.49e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    7 VAVCVRVRPLNSREEELGEATHIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFAYG 86
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   87 QTASGKTHTMMG---------SEDClGVIPRAIHDIFQRIKKFPER-----EFLLRVSYMEIYNETITDLLCNAQkmKPL 152
Cdd:cd01373    83 QTGSGKTYTMWGpsesdnespHGLR-GVIPRIFEYLFSLIQREKEKagegkSFLCKCSFLEIYNEQIYDLLDPAS--RNL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  153 IIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKaepSNCDGSVKVSHLN 232
Cdd:cd01373   160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEK---KACFVNIRTSRLN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  233 LVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGF--INYRDSKLTRILQNSLGGNAKTRIICTITP 310
Cdd:cd01373   237 LVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQrhVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 316
                         330       340       350
                  ....*....|....*....|....*....|.
gi 115648101  311 ASLD--ETLTTLQFASTAKYMKNTPYVNEVS 339
Cdd:cd01373   317 SSKCfgETLSTLRFAQRAKLIKNKAVVNEDT 347
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
6-327 8.43e-92

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: 305.04  E-value: 8.43e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEELG---------------------EATHIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYE 64
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGfrrivkvmdnhmlvfdpkdeeDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   65 EIAVPIISSAIQGYNGTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKF-PEREFLLRVSYMEIYNETITDLL 143
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLkDEKEFEVSMSYLEIYNETIRDLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  144 CNAQkmKPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCD 223
Cdd:cd01370   161 NPSS--GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  224 gsVKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSD-GQVGGFINYRDSKLTRILQNSLGGNAKT 302
Cdd:cd01370   239 --VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADpGKKNKHIPYRDSKLTRLLKDSLGGNCRT 316
                         330       340
                  ....*....|....*....|....*..
gi 115648101  303 RIICTITPASL--DETLTTLQFASTAK 327
Cdd:cd01370   317 VMIANISPSSSsyEETHNTLKYANRAK 343
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
4-337 1.38e-87

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: 293.08  E-value: 1.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    4 EASVAVCVRVRPLNSREEELGEATHIYWKTDKNAIYQSDGG-------KSFQFDRVFDSNETTKNVYEEIAVPIISSAIQ 76
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGladksstKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   77 GYNGTIFAYGQTASGKTHTMMGSE-----------DCLGVIPRAIHDIFQRIKKfPEREFLLRVSYMEIYNETITDLL-C 144
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKLED-NGTEYSVKVSYLEIYNEELFDLLsP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  145 NAQKMKPLIIREDTNRT--VYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAepSNC 222
Cdd:cd01364   160 SSDVSERLRMFDDPRNKrgVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETT--IDG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  223 DGSVKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGqvGGFINYRDSKLTRILQNSLGGNAKT 302
Cdd:cd01364   238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVER--APHVPYRESKLTRLLQDSLGGRTKT 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 115648101  303 RIICTITPAS--LDETLTTLQFASTAKYMKNTPYVNE 337
Cdd:cd01364   316 SIIATISPASvnLEETLSTLEYAHRAKNIKNKPEVNQ 352
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
7-327 2.98e-73

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


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 251.54  E-value: 2.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    7 VAVCVRVRPLNSREEELGEATHI-----------------YWKTDKNAIYQSdggKSFQFDRVFDSNETTKNVYEEIAVP 69
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIevinsttvvlhppkgsaANKSERNGGQKE---TKFSFSKVFGPNTTQKEFFQGTALP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   70 IISSAIQGYNGTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKkfperEFLLRVSYMEIYNETITDLL-----C 144
Cdd:cd01368    80 LVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLepspsS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  145 NAQKMKPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDG 224
Cdd:cd01368   155 PTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVDQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  225 ---SVKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFIN---YRDSKLTRILQNSLGG 298
Cdd:cd01368   235 dkdQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKmvpFRDSKLTHLFQNYFDG 314
                         330       340       350
                  ....*....|....*....|....*....|.
gi 115648101  299 NAKTRIICTITPASL--DETLTTLQFASTAK 327
Cdd:cd01368   315 EGKASMIVNVNPCASdyDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
6-327 3.78e-72

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: 247.88  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    6 SVAVCVRVRPLNSREEEL------GEATHIYWKTDKNA--IYQSDGGKSFQFDRVFDsNETTKNVYEEIAVPIISSAIQG 77
Cdd:cd01375     1 KVQAFVRVRPTDDFAHEMikygedGKSISIHLKKDLRRgvVNNQQEDWSFKFDGVLH-NASQELVYETVAKDVVSSALAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   78 YNGTIFAYGQTASGKTHTMMGSEDCL---GVIPRAIHDIFQRIKKFPEREFLLRVSYMEIYNETITDLLCN----AQKMK 150
Cdd:cd01375    80 YNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTlpyvGPSVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  151 PLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKaEPSncDGSVKVSH 230
Cdd:cd01375   160 PMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSR-TLS--SEKYITSK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  231 LNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDgQVGGFINYRDSKLTRILQNSLGGNAKTRIICTIT- 309
Cdd:cd01375   237 LNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYg 315
                         330
                  ....*....|....*....
gi 115648101  310 -PASLDETLTTLQFASTAK 327
Cdd:cd01375   316 eAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
7-327 5.54e-65

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: 226.62  E-value: 5.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    7 VAVCVRVRPLNSREEELGEATHIYWkTDKNAIYQSDG-----GKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGT 81
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSG-IDSCSVELADPrnhgeTLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   82 IFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPEREFLLrVSYMEIYNETITDLLcnAQKMKPLIIREDTNRT 161
Cdd:cd01376    81 VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEAWALSFT-MSYLEIYQEKILDLL--EPASKELVIREDKDGN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  162 VYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREkaepSNCDGSVKVSHLNLVDLAGSER 241
Cdd:cd01376   158 ILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE----RLAPFRQRTGKLNLIDLAGSED 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  242 AAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQvgGFINYRDSKLTRILQNSLGGNAKTRIICTITP--ASLDETLTT 319
Cdd:cd01376   234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNL--PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPerTFYQDTLST 311

                  ....*...
gi 115648101  320 LQFASTAK 327
Cdd:cd01376   312 LNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
9-327 8.28e-61

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: 214.85  E-value: 8.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    9 VCVRVRPLNSREEELGEaTHIYWKTDKNAIY------QSDGGK-----SFQFDRVFDSNETTKNVYEEIAVPIISSAIQG 77
Cdd:cd01367     4 VCVRKRPLNKKEVAKKE-IDVVSVPSKLTLIvhepklKVDLTKyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   78 YNGTIFAYGQTASGKTHTMMGS----EDCLGVIPRAIHDIFQRIKKFPEREFL-LRVSYMEIYNETITDLLcnaQKMKPL 152
Cdd:cd01367    83 GKATCFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLPYKDNLgVTVSFFEIYGGKVFDLL---NRKKRV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  153 IIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKaepsNCDGSVkvshLN 232
Cdd:cd01367   160 RLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT----NKLHGK----LS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  233 LVDLAGSERAAQTGAEGV-RLKEGCFINRNLFILGQVIKKLSDGQVggFINYRDSKLTRILQNSL-GGNAKTRIICTITP 310
Cdd:cd01367   232 FVDLAGSERGADTSSADRqTRMEGAEINKSLLALKECIRALGQNKA--HIPFRGSKLTQVLKDSFiGENSKTCMIATISP 309
                         330
                  ....*....|....*....
gi 115648101  311 A--SLDETLTTLQFASTAK 327
Cdd:cd01367   310 GasSCEHTLNTLRYADRVK 328
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
9-269 1.38e-23

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  Cd Length: 170  Bit Score: 101.27  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    9 VCVRVRPLNSREeelgeathiywktdknaIYQSDggKSFQFDRVFDSNETTKNVYEeIAVPIISSAIQGYNG-TIFAYGQ 87
Cdd:cd01363     1 VLVRVNPFKELP-----------------IYRDS--KIIVFYRGFRRSESQPHVFA-IADPAYQSMLDGYNNqSIFAYGE 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   88 TASGKTHTMMgsedclGVIPRAIHDIFQRIKKfperefllrvsymeiynetitdllcnaqkmkpliiredtNRTVYVSDL 167
Cdd:cd01363    61 SGAGKTETMK------GVIPYLASVAFNGINK---------------------------------------GETEGWVYL 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  168 TEEVVYTAEMALKWLATGEKNRHyGITKMNQRSSRSHTIFRMilesrekaepsncdgsvkvshlnLVDLAGSERaaqtga 247
Cdd:cd01363    96 TEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEI-----------------------LLDIAGFEI------ 145
                         250       260
                  ....*....|....*....|..
gi 115648101  248 egvrlkegcfINRNLFILGQVI 269
Cdd:cd01363   146 ----------INESLNTLMNVL 157
DUF972 pfam06156
Protein of unknown function (DUF972); This family consists of several hypothetical bacterial ...
1041-1119 8.77e-03

Protein of unknown function (DUF972); This family consists of several hypothetical bacterial sequences. The function of this family is unknown.


Pssm-ID: 283750  Cd Length: 106  Bit Score: 37.15  E-value: 8.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115648101  1041 DSLMQENSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEelriLRDELKRQQEVAAQEKdhatEKTQELSRTQERLAK 1119
Cdd:pfam06156    8 DQLDELEEQLGQLLAELGELKDQLAELLEENAELRIENEH----LRERLEEEEKEEEKEK----EKKQGLGEGYDNLAR 78
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
6-336 1.40e-138

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: 438.16  E-value: 1.40e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101      6 SVAVCVRVRPLNSREEELGEATHIYW------KTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYN 79
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFpdkvgkTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101     80 GTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKF-PEREFLLRVSYMEIYNETITDLLCNAQKmkPLIIREDT 158
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLNPSSK--KLEIREDE 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    159 NRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSncdGSVKVSHLNLVDLAG 238
Cdd:smart00129  159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS---GSGKASKLNLVDLAG 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    239 SERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPA--SLDET 316
Cdd:smart00129  236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSssNLEET 315
                           330       340
                    ....*....|....*....|
gi 115648101    317 LTTLQFASTAKYMKNTPYVN 336
Cdd:smart00129  316 LSTLRFASRAKEIKNKPIVN 335
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1100-1841 7.97e-06

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: 50.11  E-value: 7.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1100 KDHATEKTQELSRTQERLAK-----------TEEKLEEKNQKLQETQQQLLSTQEAMSKLQ--AKVIDMESLQNEFRNQG 1166
Cdd:pfam05483   66 KDSDFENSEGLSRLYSKLYKeaekikkwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQfeNEKVSLKLEEEIQENKD 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1167 LALERVETEKL--ELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELniaHANLKEYQE 1244
Cdd:pfam05483  146 LIKENNATRHLcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEM---HFKLKEDHE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1245 IITELRgsisENEAQGASTQDTAKSAPELQGEVPEQELLPVVKEARHSAEKVNGLEpvgaHSRTVHSMTMEGIEIENLRL 1324
Cdd:pfam05483  223 KIQHLE----EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDENLKELIEKKDHL 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1325 TKKLEESQMEiscLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETE 1404
Cdd:pfam05483  295 TKELEDIKMS---LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1405 LSSVRGQLALTTAELERKVQELCE-----KQEELTRKETSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEES 1479
Cdd:pfam05483  372 LEKNEDQLKIITMELQKKSSELEEmtkfkNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1480 QE--EMKTLREEREELRRMQEALHVESEQQKESMKEI----SSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEA 1553
Cdd:pfam05483  452 IHdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltaHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1554 QKSTLEKVEMENVNLtqrlhetleemrsvakeRDELWSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQE 1633
Cdd:pfam05483  532 MLKQIENLEEKEMNL-----------------RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1634 TINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEaqsstlesREIEKL 1713
Cdd:pfam05483  595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ--------KEIEDK 666
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1714 ELTQQlnenlkkiTLVTKENDSLKIMDEALREERdQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETM-SEK 1792
Cdd:pfam05483  667 KISEE--------KLLEEVEKAKAIADEAVKLQK-EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKeQEQ 737
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*....
gi 115648101  1793 TEEISNMKMELENVNMKLQEKVQELKTSERQRVKLKADASEAKKELKEQ 1841
Cdd:pfam05483  738 SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
Kinesin pfam00225
Kinesin motor domain;
12-327 6.09e-136

Kinesin motor domain;


Pssm-ID: 278646 [Multi-domain]  Cd Length: 325  Bit Score: 430.45  E-value: 6.09e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    12 RVRPLNSREEELGEA-------THIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFA 84
Cdd:pfam00225    1 RVRPLNEREKSRGSSdivsveePVDSETVESSHLTNKNKPKTFTFDKVFDPEATQEDVYEEVAKPLVESVLEGYNVTIFA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    85 YGQTASGKTHTMMGSEDCL-GVIPRAIHDIFQRIKKFP-EREFLLRVSYMEIYNETITDLLCNAQKMKPLIIREDTNRTV 162
Cdd:pfam00225   81 YGQTGSGKTYTMEGSPDEDpGIIPRALEDLFDRIQKTPrNFSFSVKVSYLEIYNEKIRDLLSPESKRKPLRIREDPKKGV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   163 YVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEpsncDGSVKVSHLNLVDLAGSERA 242
Cdd:pfam00225  161 YVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAVFTITLEQRNRST----GGEVKTSKLNLVDLAGSERA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   243 AQTG-AEGVRLKEGCFINRNLFILGQVIKKLSDGQvGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTT 319
Cdd:pfam00225  237 SKTGaAEGQRLKEAANINKSLSALGNVISALADGK-SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSsnYEETLST 315

                   ....*...
gi 115648101   320 LQFASTAK 327
Cdd:pfam00225  316 LRFASRAK 323
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
21-425 1.70e-68

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 244.65  E-value: 1.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   21 EELGEATHIYWKTDKNAI--YQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFAYGQTASGKTHTMMG 98
Cdd:COG5059    30 IIPGELGERLINTSKKSHvsLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   99 SEDCLGVIPRAIHDIFQRIKKFP-EREFLLRVSYMEIYNETITDLL-CNAQKmkpLIIREDTNRTVYVSDLTEEVVYTAE 176
Cdd:COG5059   110 TEEEPGIIPLSLKELFSKLEDLSmTKDFAVSISYLEIYNEKIYDLLsPNEES---LNIREDSLLGVKVAGLTEKHVSSKE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  177 MALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDGSvkvshLNLVDLAGSERAAQTGAEGVRLKEGC 256
Cdd:COG5059   187 EILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSK-----LSLVDLAGSERAARTGNRGTRLKEGA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  257 FINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPAS--LDETLTTLQFASTAKYMKNTPY 334
Cdd:COG5059   262 SINKSLLTLGNVINALGDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSnsFEETINTLKFASRAKSIKNKIQ 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  335 VNEVSNDEALLKRYRREIADLRKQleevNTKTRAQEMEKDQLAQLLDEKDLLQKVQDEKINNLKRMLVTSSSIALQQELE 414
Cdd:COG5059   342 VNSSSDSSREIEEIKFDLSEDRSE----IEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFER 417
                         410
                  ....*....|.
gi 115648101  415 IKRKRRVTWCY 425
Cdd:COG5059   418 KKLLKEEGWKY 428
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-362 4.07e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.53  E-value: 4.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101    4 EASVAVCVRVRPLNSREEElgeaTHIYWKTDKNAIyqSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIF 83
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGEEG----EMIVQKMSNDSL--TINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVF 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   84 AYGQTASGKTHTMMG----------SEDCLGVIPRAIHDIFQRIK----KFPERE--FLLRVSYMEIYNETITDLLCNAQ 147
Cdd:PLN03188  171 AYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINeeqiKHADRQlkYQCRCSFLEIYNEQITDLLDPSQ 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  148 KmkPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKaepSNCDG--S 225
Cdd:PLN03188  251 K--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCK---SVADGlsS 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  226 VKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSD-GQVGG--FINYRDSKLTRILQNSLGGNAKT 302
Cdd:PLN03188  326 FKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKqrHIPYRDSRLTFLLQESLGGNAKL 405
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115648101  303 RIICTITPAS--LDETLTTLQFASTAKYMKNTPYVNEVSNDEalLKRYRREIADLRKQLEEV 362
Cdd:PLN03188  406 AMVCAISPSQscKSETFSTLRFAQRAKAIKNKAVVNEVMQDD--VNFLREVIRQLRDELQRV 465
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
834-1620 3.33e-24

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 110.57  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  834 AGVLEERERLKQEIGALSKEAESLafsldsvkaeLSHKTQELEQKTVEGQERLNKMEALREELESRDSSLQSVEKEKVLL 913
Cdd:COG1196   189 ERLEDLLEELEKQLEKLERQAEKA----------ERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEEL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  914 TEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLRSDIQDTVNMNIDTQEQLLNALESLKQHQETINMLKMKAAEELSD 993
Cdd:COG1196   259 QEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEE 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  994 NLHVKDRGGARDEAQQKMDGIDEQNESAHTLLGGGKDNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKMDLKENIE 1073
Cdd:COG1196   339 LEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSE 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1074 MSIENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLlstqeamSKLQAKVI 1153
Cdd:COG1196   419 RLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKEL-------SSLEARLD 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1154 DMESLQNEFRNQGLALERVETEKLELAQRLHE--SYEEVKSITKER-----------NDLKELQESFEIEKKQLKEYARE 1220
Cdd:COG1196   492 RLEAEQRASQGVRAVLEALESGLPGVYGPVAEliKVKEKYETALEAalgnrlqavvvENEEVAKKAIEFLKENKAGRATF 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1221 IEAAGLQTKEELNIAHAN------------------------------------------LKEYQEIIT------ELRGS 1252
Cdd:COG1196   572 LPLDRIKPLRSLKSDAAPgflglasdlidfdpkyepavrfvlgdtlvvddleqarrlarkLRIKYRIVTldgdlvEPSGS 651
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1253 ISENEAQGASTQDTAKSAPELQGEVpeQELLPVVKEARHSAEKVNG-----LEPVGAHSRTVHSMTMEGIEIENL--RLT 1325
Cdd:COG1196   652 ITGGSRNKRSSLAQKRELKELEEEL--AELEAQLEKLEEELKSLKNelrslEDLLEELRRQLEELERQLEELKRElaALE 729
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1326 KKLEESQMEISCLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETEL 1405
Cdd:COG1196   730 EELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRL 809
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1406 SSVRGQLALTTAELERKVQELCEKQEELtrketSEAQGKMSELEQLRELLLAQasaLQNAESDRLRLNTQLEESQEEMKT 1485
Cdd:COG1196   810 DALERELESLEQRRERLEQEIEELEEEI-----EELEEKLDELEEELEELEKE---LEELKEELEELEAEKEELEDELKE 881
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1486 LREEREELRRMQEALHVESEQQKESMKEISSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEAQKSTLEK--VEM 1563
Cdd:COG1196   882 LEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEeiEAL 961
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115648101 1564 ENVNLtqrlhETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVTKGMEKEEE 1620
Cdd:COG1196   962 GPVNL-----RAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
586-1436 6.00e-24

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: 109.76  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   586 LLKEKEEQIKNLQeyIDAQKSEKMKidlsytsDATEDLKQAMRTLSDLDTVALDAKKEsaflrsenlELKEKINELSDSR 665
Cdd:TIGR02168  194 ILNELERQLKSLE--RQAEKAERYK-------ELKAELRELELALLVLRLEELREELE---------ELQEELKEAEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   666 KQMESDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVdgkgllSNLELEKRITDlQKELNKEAEEKQTLQEEVNL 745
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI------SRLEQQKQILR-ERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   746 LSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQLSRRGSDGEWQALESL 825
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   826 HAELEHRhagvleeRERLKQEIGALSKEAESLAFslDSVKAELSHKTQELEQktvegqerlnkmeaLREELESRDSSLQS 905
Cdd:TIGR02168  409 LERLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEE--------------LQEELERLEEALEE 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   906 VEKEKVLLTEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLR---------SDIQDTVNMNIDTQEQLLNALEslkqh 976
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKallknqsglSGILGVLSELISVDEGYEAAIE----- 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   977 qetinmlkmKAAEELSDNLHVKDRGGARDEAQqkmdgIDEQNESAHTL---LGGGKDNEVTEEQRkiDSLMQENSGLQQT 1053
Cdd:TIGR02168  541 ---------AALGGRLQAVVVENLNAAKKAIA-----FLKQNELGRVTflpLDSIKGTEIQGNDR--EILKNIEGFLGVA 604
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1054 LESVRAEKEQLKM------------DLKENIEMSIENQEELRI--LRDELKRQQEVAAQEKDHAT----EKTQELSRTQE 1115
Cdd:TIGR02168  605 KDLVKFDPKLRKAlsyllggvlvvdDLDNALELAKKLRPGYRIvtLDGDLVRPGGVITGGSAKTNssilERRREIEELEE 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1116 RLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQglaLERVETEKLELAQRLHESYEEVKSITK 1195
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---LARLEAEVEQLEERIAQLSKELTELEA 761
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1196 ERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQEIITELRGSISENEAQGASTQDTAKSAPELQG 1275
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1276 EVPEQellpvVKEARHSAEKVNGLepvgahsrtvhsmtMEGIEIENLRLTKKLEESQMEISCLTREREDLRRTQETLQVE 1355
Cdd:TIGR02168  842 DLEEQ-----IEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1356 CTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSqretELSSVRGQLALT-TAELERKVQELCEKQEELT 1434
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----EEYSLTLEEAEAlENKIEDDEEEARRRLKRLE 978

                   ..
gi 115648101  1435 RK 1436
Cdd:TIGR02168  979 NK 980
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1067-1901 5.67e-23

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 106.34  E-value: 5.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1067 DLKENIEMSIENQEELRILRDELKRQQEVAAQEKDHAtEKTQELSRTQERLAKTE--EKLEEKNQKLQETQQQLLSTQEA 1144
Cdd:COG1196   176 EAERKLERTEENLERLEDLLEELEKQLEKLERQAEKA-ERYQELKAELRELELALllAKLKELRKELEELEEELSRLEEE 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1145 MSKLQAKVIDMESLQNEFRNQglaLERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAA 1224
Cdd:COG1196   255 LEELQEELEEAEKEIEELKSE---LEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEK 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1225 GLQTKEELNIAHANLKEYQEIITELRGSISENEaqgaSTQDTAKSAPELQGEVPEQELlpvVKEARHSAEKVNGLEPVGA 1304
Cdd:COG1196   332 IEALKEELEERETLLEELEQLLAELEEAKEELE----EKLSALLEELEELFEALREEL---AELEAELAEIRNELEELKR 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1305 hsrtvhsmTMEGIEIENLRLTKKLEESQMEISCLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCL 1384
Cdd:COG1196   405 --------EIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEEL 476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1385 KEQENKIDTLITSLSQRETELSSVRGQLALTTAELER------KVQELCEKQEELTRkeTSEAQGKMSELEQLRELLLAQ 1458
Cdd:COG1196   477 QRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGlpgvygPVAELIKVKEKYET--ALEAALGNRLQAVVVENEEVA 554
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1459 ASALQNAESDRLRLNTQLE-ESQEEMKTLREEREELRRMQEALHVESEQQKE-------------SMKEISSKLQELQNK 1524
Cdd:COG1196   555 KKAIEFLKENKAGRATFLPlDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEpavrfvlgdtlvvDDLEQARRLARKLRI 634
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1525 EYECL---------------AMKTINETQGSRCEMDHLNQQLEAQKSTLEKVEMENVNLTQRLHETLEEMRSVAKERDEL 1589
Cdd:COG1196   635 KYRIVtldgdlvepsgsitgGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEEL 714
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1590 WSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQD 1669
Cdd:COG1196   715 ERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE 794
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1670 LREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKENDSLKIMDEALREERDQ 1749
Cdd:COG1196   795 LEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEE 874
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1750 LRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETMSEKTEEISNMKMELENVNMKLQEKVQELKTSERQRVKlka 1829
Cdd:COG1196   875 LEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREI--- 951
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115648101 1830 daseakKELKEQGLTLSKIEMENLNLAQKIHENLEEMKSvrkERDDLKKLEEILRMERDQLKDNLREAMLKA 1901
Cdd:COG1196   952 ------ERLEEEIEALGPVNLRAIEEYEEVEERYEELKS---QREDLEEAKEKLLEVIEELDKEKRERFKET 1014
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
604-1259 1.55e-22

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 104.80  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  604 QKSEKMKIDLSYTSDATEDLKQAMRTLSDLDTVALDAKKESAFLRS-ENLELKEKINELSDSRKQMESDIQMYQRQLEAK 682
Cdd:COG1196   179 RKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRElELALLLAKLKELRKELEELEEELSRLEEELEEL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  683 KKMQTDLDKELQLAFQEISklsalvdgkgllsnlELEKRITDLQKELNKEAEEKQTLQEEVNLL----SELKSLPSEVET 758
Cdd:COG1196   259 QEELEEAEKEIEELKSELE---------------ELREELEELQEELLELKEEIEELEGEISLLrerlEELENELEELEE 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  759 LRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQlsrrgsDGEWQALESLHAELEHRHAGVLE 838
Cdd:COG1196   324 RLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEEL------EELFEALREELAELEAELAEIRN 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  839 ERERLKQEIGALSKEAESLAFSLDSVKAELSHKTQELEQKTVEGQERLNKMEALREELESRDSSLQSVEKEKVLLTEKLQ 918
Cdd:COG1196   398 ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQ 477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  919 QALKEVKALTQEKKNLKQLQESLQTERDQLR--------------------------------SDIQDTVNMNIDTQEQL 966
Cdd:COG1196   478 RLEKELSSLEARLDRLEAEQRASQGVRAVLEalesglpgvygpvaelikvkekyetaleaalgNRLQAVVVENEEVAKKA 557
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  967 LNALESLKQHQETINML-KMKAAEELSDNLH------------------------------VKDRGGARDEAQQKMDGI- 1014
Cdd:COG1196   558 IEFLKENKAGRATFLPLdRIKPLRSLKSDAApgflglasdlidfdpkyepavrfvlgdtlvVDDLEQARRLARKLRIKYr 637
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1015 ------DEQNESAHTLLGGGKDNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKmdlkENIEMSIENQEELRILRDE 1088
Cdd:COG1196   638 ivtldgDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLK----NELRSLEDLLEELRRQLEE 713
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1089 LKRQQEVAAQEKDHATEKTQELsrtQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRN---- 1164
Cdd:COG1196   714 LERQLEELKRELAALEEELEQL---QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEkrqa 790
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1165 QGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQE 1244
Cdd:COG1196   791 LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEA 870
                         730
                  ....*....|....*
gi 115648101 1245 IITELRGSISENEAQ 1259
Cdd:COG1196   871 EKEELEDELKELEEE 885
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1077-1896 4.76e-22

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: 103.21  E-value: 4.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1077 ENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDME 1156
Cdd:TIGR02168  222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1157 S----LQNEFRNQGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEEL 1232
Cdd:TIGR02168  302 QqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1233 NIAHANLKEYQEIITELRGSISENEAQGastQDTAKSAPELQGEVPEQELLPVVKEARHSAEKVNGLEpvgahsrtvhsM 1312
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE-----------E 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1313 TMEGIEIENLRLTKKLEESQMEISCLTREREDLRRTQETLQVECTQLK------EDARRTLANHLETEEELNLARCCLKE 1386
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqenlEGFSEGVKALLKNQSGLSGILGVLSE 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1387 Q-------ENKIDTLITSLSQR---ETELSSVRGQLALTTAELERK----VQELCEKQEELTRKETSEAQGKMSELEQLR 1452
Cdd:TIGR02168  528 LisvdegyEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1453 ELLLAQASALQNAESDRLRLNTQLEESQEEMKTLREEREELRRMQEALHVESEQQKESMKEISSKLQelQNKEYECLAmK 1532
Cdd:TIGR02168  608 VKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE--RRREIEELE-E 684
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1533 TINETQGsrcEMDHLNQQLEAQKSTLEKVEMENVNLTQRLHETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVT 1612
Cdd:TIGR02168  685 KIEELEE---KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1613 KGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQME 1692
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1693 QLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLriah 1772
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL---- 917
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1773 mnlkehqetiDRLMETMSEKTEEISNMKMELENVNMKLQEKVQ-ELKTSERQRVKLKADASEAKKELKEqgLTLSKIEME 1851
Cdd:TIGR02168  918 ----------EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKR--LENKIKELG 985
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*
gi 115648101  1852 NLNLAQkihenLEEMKSVRKERDDLKKLEEILRMERDQLKDNLRE 1896
Cdd:TIGR02168  986 PVNLAA-----IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1032-1840 3.65e-20

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 97.09  E-value: 3.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1032 EVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEELRILRDELKRQQEVAAQEKDHATEKTQELS 1111
Cdd:COG1196   226 ELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIS 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1112 RTQERL-------AKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRN-QGLALERVETEKLELAQRL 1183
Cdd:COG1196   306 LLRERLeelenelEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEkLSALLEELEELFEALREEL 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1184 HESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAAGLQTKEELNIAHANLKEYQEIITELRGSISENEAQGAST 1263
Cdd:COG1196   386 AELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKEL 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1264 QDTAKSAPELQGEV--PEQELLPVVKEARHSAEKVNGLEPVgahsRTVHSMTMEGIE---IENLRLTKKLEESqMEIsCL 1338
Cdd:COG1196   466 ERELAELQEELQRLekELSSLEARLDRLEAEQRASQGVRAV----LEALESGLPGVYgpvAELIKVKEKYETA-LEA-AL 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1339 TREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDT---LITSLSQRETELSSVRGQLALT 1415
Cdd:COG1196   540 GNRLQAVVVENEEVAKKAIEFLKENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLasdLIDFDPKYEPAVRFVLGDTLVV 619
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1416 -TAELERKVQELCEKQEELTRKE--TSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEESQEEmktlreeree 1492
Cdd:COG1196   620 dDLEQARRLARKLRIKYRIVTLDgdLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEE---------- 689
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1493 lrrmQEALHVESEQQKESMKEISSKLQELQNKEYECLAMKTINETQGSRcemdhLNQQLEAQKSTLEKVEMENVNLTQRL 1572
Cdd:COG1196   690 ----LKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQ-----LQSRLEELEEELEELEEELEELQERL 760
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1573 HETLEEMRSVAKERDELWSMEERLTVERDQLKKsleetvtkgmekeeelrvahvHLEEHQETINKLRKmvsdytdEISHT 1652
Cdd:COG1196   761 EELEEELESLEEALAKLKEEIEELEEKRQALQE---------------------ELEELEEELEEAER-------RLDAL 812
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1653 QGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKE 1732
Cdd:COG1196   813 ERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEE 892
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101 1733 NDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLRIAHMNLKEhqETIDRLMETMSEKTEEISNMKMELENVNMKLQE 1812
Cdd:COG1196   893 LRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEE--EYEDTLETELEREIERLEEEIEALGPVNLRAIE 970
                         810       820
                  ....*....|....*....|....*...
gi 115648101 1813 KVQELKTSERQRVKLKADASEAKKELKE 1840
Cdd:COG1196   971 EYEEVEERYEELKSQREDLEEAKEKLLE 998
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
568-1265 5.75e-20

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: 96.68  E-value: 5.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   568 HAEEYnQDL-----ENDLSSKVKLLKEKEEQIKNLQEYIDAQKSEKMKIDlSYTSDATEDLKQAMRTLSDLdtvaldAKK 642
Cdd:TIGR02169  209 KAERY-QALlkekrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLT-EEISELEKRLEEIEQLLEEL------NKK 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   643 ESAFLRSENLELKEKINELSDSRKQMESDIQMYQRQLEakkkmqtDLDKELQLAFQEISKLSALVDgkgllsnlELEKRI 722
Cdd:TIGR02169  281 IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE-------DAEERLAKLEAEIDKLLAEIE--------ELEREI 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   723 TDLQKELNKEAEEKQTLQEEVNLL-SELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNT 801
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLrAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   802 RDDLAtsqlsrrgsdgewqALESLHAELEhrhagvlEERERLKQEIGALSKEAESLAFSLDSVKAELSHKTQE---LEQK 878
Cdd:TIGR02169  426 NAAIA--------------GIEAKINELE-------EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEydrVEKE 484
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   879 TVEGQERLNKMEALREELESRDSSLQSVEKekvLLTEKLQQALKEVKALTQEKKNLKQLQESLQTERDQlrsdiqdtvNM 958
Cdd:TIGR02169  485 LSKLQRELAEAEAQARASEERVRGGRAVEE---VLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLN---------NV 552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101   959 NIDTQEQLLNALESLKQHQET----INMLKMKAAEELSDNLHvkdRGGARDEAQQKMD----------------GIDEQN 1018
Cdd:TIGR02169  553 VVEDDAVAKEAIELLKRRKAGratfLPLNKMRDERRDLSILS---EDGVIGFAVDLVEfdpkyepafkyvfgdtLVVEDI 629
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1019 ESAHTLLG-------------------GGKDN-------------EVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKM 1066
Cdd:TIGR02169  630 EAARRLMGkyrmvtlegelfeksgamtGGSRAprggilfsrsepaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1067 DLKENIEMSIENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQL--LSTQEA 1144
Cdd:TIGR02169  710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLS 789
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115648101  1145 MSKLQAKVIDMESLQNEFRNQGLALERVEteklelaQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAA 1224
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIE-------QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 115648101  1225 GLQTKEELNIAHANLKEYQEIITELRGSISENEAQGASTQD 1265
Cdd:TIGR02169  863 KEELEEELEELEAALRDLESRLGDLKKERDEL