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Conserved domains on  [gi|315434261|ref|NP_001186795|]
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kinesin-like protein KIF16B isoform 1 [Homo sapiens]

Protein Classification

KISc_KIF1A_KIF1B and Kinesin_assoc domain-containing protein (domain architecture ID 12915293)

protein containing domains KISc_KIF1A_KIF1B, Kinesin_assoc, and GBP_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-365 0e+00

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  Cd Length: 361  Bit Score: 561.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 315434261  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
SbcC super family cl33865
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
597-1081 6.48e-16

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


The actual alignment was detected with superfamily member COG0419:

Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 83.27  E-value: 6.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  597 EFERQQREELEKLESKRKLIEEMEEKQksdKAELERMQQEVETQRKETE----IVQLQIRKQEESLKRRSFHIENKLKDL 672
Cdd:COG0419   168 KYEKLSELLKEVIKEAKAKIEELEGQL---SELLEDIEDLLEALEEELKelkkLEEIQEEQEEEELEQEIEALEERLAEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  673 LAEKEKFEEERLREQQEIEL---------QKKRQEEETFLRVQEELQRLKELnNNEKAEKFQIFQELDQLQKEKDEQYAK 743
Cdd:COG0419   245 EEEKERLEELKARLLEIESLelealkireEELRELERLLEELEEKIERLEEL-EREIEELEEELEGLRALLEELEELLEK 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  744 LELEKKRL-------EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGE 816
Cdd:COG0419   324 LKSLEERLekleeklEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSA 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  817 ELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL----------ECLKC--EHDKES--RLLEKHDESV 882
Cdd:COG0419   404 ALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELmiaelagageKCPVCgqELPEEHekELLELYELEL 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  883 TDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNhLPTLLEEKQRAFEILDRGPLSLDNtlYQVEKEMEEKEEQLAQYQAN 962
Cdd:COG0419   484 EELEEELSREKEEAELREEIEELEKELRELEEE-LIELLELEEALKEELEEKLEKLEN--LLEELEELKEKLQLQQLKEE 560
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  963 ANQLQKLQATFEFtaniARQEEKVRKKEKEILESREKQQREaLERALARLERRHSALQR------HSTLGMEIEEQRQKL 1036
Cdd:COG0419   561 LRQLEDRLQELKE----LLEELRLLRTRKEELEELRERLKE-LKKKLKELEERLSQLEEllqsleLSEAENELEEAEEEL 635
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 315434261 1037 ASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEV 1081
Cdd:COG0419   636 ESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENE 680
Kinesin_assoc super family cl24686
Kinesin-associated;
364-476 2.10e-09

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 318424  Cd Length: 181  Bit Score: 58.34  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   364 INEDANVKLIRELRAEIARLKTLL-AQG-------------------------------NQIA----------------- 394
Cdd:pfam16183    3 INEDPNAKLIRELKEEVARLRDLLyAQGlgdiidiaadahnnptnkrastpannlstvtNAMAgaspspslsalssrags 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   395 -------LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIG 458
Cdd:pfam16183   83 vsslherIMFTPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVN 162
                          170
                   ....*....|....*...
gi 315434261   459 IDDDLLSTGIILYHLKEG 476
Cdd:pfam16183  163 LNEDPLMSECLLYYIKDG 180
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
478-543 7.95e-05

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


:

Pssm-ID: 334113 [Multi-domain]  Cd Length: 66  Bit Score: 41.78  E-value: 7.95e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315434261   478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-365 0e+00

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  Cd Length: 361  Bit Score: 561.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 315434261  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-365 2.46e-151

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: 460.89  E-value: 2.46e-151
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 315434261    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 9.17e-148

Kinesin motor domain;


Pssm-ID: 333938  Cd Length: 324  Bit Score: 451.24  E-value: 9.17e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKSRGSSDIVSVENVGSETVESSV------LTNKNKTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETTRWDEaSFRTEVSYLEIYNERVRDLLRrKSS 167
Cdd:pfam00225   68 SVLEGYNGTIFAYGQTGSGKTYTMEGSDDEDpGIIPRALEDLFDRIQKTKERNS-EFSVKVSYLEIYNEKIRDLLS-PSS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   168 KTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCeTVSK 247
Cdd:pfam00225  146 KRKPLRIREDPKRGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAVFTITLEQRNRDTGEQV-KTSK 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   248 IHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGNS 327
Cdd:pfam00225  225 LNLVDLAGSERASKTGAEGQRLKEAANINKSLSALGNVISALAD-----------GKSKHIPYRDSKLTRLLQDSLGGNS 293
                          330       340       350
                   ....*....|....*....|....*....|.
gi 315434261   328 KTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  294 KTLMIANISPSSSNYEETLSTLRFASRAKNI 324
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-508 3.26e-82

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 281.24  E-value: 3.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQ--------------- 392
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSqsslsgifaymqslk 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  393 --IALLDSPTALSMEEKLQQNEARVQEL-TKEWTNKwnETQNILKEQTLALrkegiGVVLDSELPHLIGIDDDLLSTGII 469
Cdd:COG5059   394 keTETLKSRIDLIMKSIISGTFERKKLLkEEGWKYK--STLQFLRIEIDRL-----LLLREEELSKKKTKIHKLNKLRHD 466
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 315434261  470 LYHLKEGQT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059   467 LSSLLSSIPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-392 4.17e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 271.42  E-value: 4.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454
                         410       420
                  ....*....|....*....|
gi 315434261  373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
597-1081 6.48e-16

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 83.27  E-value: 6.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  597 EFERQQREELEKLESKRKLIEEMEEKQksdKAELERMQQEVETQRKETE----IVQLQIRKQEESLKRRSFHIENKLKDL 672
Cdd:COG0419   168 KYEKLSELLKEVIKEAKAKIEELEGQL---SELLEDIEDLLEALEEELKelkkLEEIQEEQEEEELEQEIEALEERLAEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  673 LAEKEKFEEERLREQQEIEL---------QKKRQEEETFLRVQEELQRLKELnNNEKAEKFQIFQELDQLQKEKDEQYAK 743
Cdd:COG0419   245 EEEKERLEELKARLLEIESLelealkireEELRELERLLEELEEKIERLEEL-EREIEELEEELEGLRALLEELEELLEK 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  744 LELEKKRL-------EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGE 816
Cdd:COG0419   324 LKSLEERLekleeklEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSA 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  817 ELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL----------ECLKC--EHDKES--RLLEKHDESV 882
Cdd:COG0419   404 ALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELmiaelagageKCPVCgqELPEEHekELLELYELEL 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  883 TDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNhLPTLLEEKQRAFEILDRGPLSLDNtlYQVEKEMEEKEEQLAQYQAN 962
Cdd:COG0419   484 EELEEELSREKEEAELREEIEELEKELRELEEE-LIELLELEEALKEELEEKLEKLEN--LLEELEELKEKLQLQQLKEE 560
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  963 ANQLQKLQATFEFtaniARQEEKVRKKEKEILESREKQQREaLERALARLERRHSALQR------HSTLGMEIEEQRQKL 1036
Cdd:COG0419   561 LRQLEDRLQELKE----LLEELRLLRTRKEELEELRERLKE-LKKKLKELEERLSQLEEllqsleLSEAENELEEAEEEL 635
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 315434261 1037 ASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEV 1081
Cdd:COG0419   636 ESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENE 680
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
592-933 1.59e-15

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


Pssm-ID: 340095 [Multi-domain]  Cd Length: 756  Bit Score: 81.80  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIENKLKD 671
Cdd:pfam17380  271 YNGQTMTENEFLNQLLHIVQHQKSVSERQQQDKFEKMEQERIRQEKEEKARELE----RRRKLAEAEKARQAEIDRVSWG 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   672 LL---------------AEKEKFEEERLREQQEIELQKKRQEEEtflRVQEElqrlkelnnnEKAEKFQIFQELDQLQKE 736
Cdd:pfam17380  347 VFatggnlnyfqqaaiyAEQERMAMERERELERIQLEEKKREME---RIRQE----------EIAMEISKIRELERLQLE 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   737 KDEQYAKL--ELE---KKRLEEQEKEQVMLVAHLE-EQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARA 809
Cdd:pfam17380  414 RQQKNERVrqELEaarKQKILEEERQRKIKEQKREmEKIRKEQEEA---REEELRRLEEERaRELERVREEELERQHQIE 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   810 GGDEDGEELEKAQLRFFEFKRRQlvklvnLEKDLVQQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVP 889
Cdd:pfam17380  491 ILRQQEEDQKKKKLEKDKEEREK------AEAEEENKRKIIEKELEENKQAI----IEEENKRKILEKEMEDRQ--NAIY 558
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 315434261   890 QDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRaFEILDR 933
Cdd:pfam17380  559 EEEERRIAEEERRKQIEIEERKQIQEQIMIASEERSR-LDAMER 601
PTZ00121 PTZ00121
MAEBL; Provisional
599-891 1.25e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 72.87  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  599 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 670
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  671 dLLAEKEKFEEERLREQqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLELEKKR 750
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEAKK 1669
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  751 lEEQEKEQVMLVAHLEEQLREKQEmiQLLRRGE--------VQWVEEEKRDLEGIR----ESLLRVKEARAGGDEDGEEL 818
Cdd:PTZ00121 1670 -AEEDKKKAEEAKKAEEDEKKAAE--ALKKEAEeakkaeelKKKEAEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKA 1746
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434261  819 EKAQLRFFEFKrrqlvKLVNLEKDLVQQKDILKKEvqEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 891
Cdd:PTZ00121 1747 EEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKE--KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
597-894 1.08e-11

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   597 EFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEK 676
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQL 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   677 EKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   757 EQVMLVAHLE----EQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARaggdEDGEELEKAQLRFFEFKRRQ 832
Cdd:TIGR02168  401 EIERLEARLErledRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL----ERLEEALEELREELEEAEQA 476
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434261   833 LVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 894
Cdd:TIGR02168  477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 2.10e-09

Kinesin-associated;


Pssm-ID: 318424  Cd Length: 181  Bit Score: 58.34  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   364 INEDANVKLIRELRAEIARLKTLL-AQG-------------------------------NQIA----------------- 394
Cdd:pfam16183    3 INEDPNAKLIRELKEEVARLRDLLyAQGlgdiidiaadahnnptnkrastpannlstvtNAMAgaspspslsalssrags 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   395 -------LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIG 458
Cdd:pfam16183   83 vsslherIMFTPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVN 162
                          170
                   ....*....|....*...
gi 315434261   459 IDDDLLSTGIILYHLKEG 476
Cdd:pfam16183  163 LNEDPLMSECLLYYIKDG 180
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
478-543 7.95e-05

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 334113 [Multi-domain]  Cd Length: 66  Bit Score: 41.78  E-value: 7.95e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315434261   478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
607-807 3.42e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  607 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 686
Cdd:cd16269    87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  687 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAeKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLv 762
Cdd:cd16269   155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEA-ILQADQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQK- 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 315434261  763 ahLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 807
Cdd:cd16269   228 --LEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-365 0e+00

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  Cd Length: 361  Bit Score: 561.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 315434261  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-365 2.46e-151

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: 460.89  E-value: 2.46e-151
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 315434261    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 9.17e-148

Kinesin motor domain;


Pssm-ID: 333938  Cd Length: 324  Bit Score: 451.24  E-value: 9.17e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKSRGSSDIVSVENVGSETVESSV------LTNKNKTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETTRWDEaSFRTEVSYLEIYNERVRDLLRrKSS 167
Cdd:pfam00225   68 SVLEGYNGTIFAYGQTGSGKTYTMEGSDDEDpGIIPRALEDLFDRIQKTKERNS-EFSVKVSYLEIYNEKIRDLLS-PSS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   168 KTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCeTVSK 247
Cdd:pfam00225  146 KRKPLRIREDPKRGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAVFTITLEQRNRDTGEQV-KTSK 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   248 IHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGNS 327
Cdd:pfam00225  225 LNLVDLAGSERASKTGAEGQRLKEAANINKSLSALGNVISALAD-----------GKSKHIPYRDSKLTRLLQDSLGGNS 293
                          330       340       350
                   ....*....|....*....|....*....|.
gi 315434261   328 KTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  294 KTLMIANISPSSSNYEETLSTLRFASRAKNI 324
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
3-356 8.85e-141

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  Cd Length: 326  Bit Score: 432.83  E-value: 8.85e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106    66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106   145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106   223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 315434261  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106   292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
3-358 1.92e-118

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  Cd Length: 334  Bit Score: 373.33  E-value: 1.92e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371    70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371   148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371   226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 315434261  318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371   294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
3-358 5.98e-115

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  Cd Length: 341  Bit Score: 363.96  E-value: 5.98e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372    62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372   140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372   220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 315434261  309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372   291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
3-358 3.40e-104

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  Cd Length: 345  Bit Score: 334.70  E-value: 3.40e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370    76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370   154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370   231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 315434261  315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370   302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
4-367 2.71e-102

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  Cd Length: 347  Bit Score: 329.85  E-value: 2.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373    64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373   144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373   221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 315434261  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373   293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
3-358 2.71e-102

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  Cd Length: 321  Bit Score: 328.52  E-value: 2.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374    61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374   138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374   215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 315434261  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374   285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
1-358 2.79e-99

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  Cd Length: 325  Bit Score: 320.43  E-value: 2.79e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYsADTkspdyvSQEMVF 79
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFD-PNT------TQEDVY 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369    62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369   140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369   215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 315434261  317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369   284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
9-360 7.57e-99

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  Cd Length: 329  Bit Score: 319.54  E-value: 7.57e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366    71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfds 238
Cdd:cd01366   148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWL 318
Cdd:cd01366   225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 315434261  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366   288 LQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
1-367 2.57e-88

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  Cd Length: 353  Bit Score: 291.15  E-value: 2.57e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364    69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364   145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364   225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434261  305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364   291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-508 3.26e-82

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 281.24  E-value: 3.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQ--------------- 392
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSqsslsgifaymqslk 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  393 --IALLDSPTALSMEEKLQQNEARVQEL-TKEWTNKwnETQNILKEQTLALrkegiGVVLDSELPHLIGIDDDLLSTGII 469
Cdd:COG5059   394 keTETLKSRIDLIMKSIISGTFERKKLLkEEGWKYK--STLQFLRIEIDRL-----LLLREEELSKKKTKIHKLNKLRHD 466
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 315434261  470 LYHLKEGQT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059   467 LSSLLSSIPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-392 4.17e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 271.42  E-value: 4.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454
                         410       420
                  ....*....|....*....|
gi 315434261  373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
4-356 6.16e-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  Cd Length: 345  Bit Score: 247.31  E-value: 6.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368    78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368   150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368   230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 315434261  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368   303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
3-356 1.03e-71

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


Pssm-ID: 276826  Cd Length: 334  Bit Score: 243.26  E-value: 1.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375     1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375    68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375   145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375   225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 315434261  316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375   294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
4-356 3.78e-68

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  Cd Length: 319  Bit Score: 232.39  E-value: 3.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376    66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376   142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376   219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
                         330       340       350
                  ....*....|....*....|....*....|....
gi 315434261  323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376   286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
4-356 7.50e-68

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  Cd Length: 328  Bit Score: 231.80  E-value: 7.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367    63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367   141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367   217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 315434261  309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367   280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
6-288 4.71e-24

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


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 100.11  E-value: 4.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261    6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363     1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363    42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363   100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 315434261  243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363   137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
4-162 1.06e-16

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


Pssm-ID: 318905 [Multi-domain]  Cd Length: 140  Bit Score: 77.99  E-value: 1.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261     4 VKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKipeggtgdsgreRTKTFTYDFSFYSADTkspdyvsQEMVFKTLG 83
Cdd:pfam16796   22 IRVFARVRPELLSE--------AQIDYPDETIEKGS------------KNKSFSFDRVFPPESE-------QEDVFQEIS 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315434261    84 TdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796   75 Q-LVQSCLDGYNVCIFAYGQTGSG---------SNPGMIPRAREEIFKFISELKGWS---YTIELQFVEIYNESSQDLL 140
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
597-1081 6.48e-16

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 83.27  E-value: 6.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  597 EFERQQREELEKLESKRKLIEEMEEKQksdKAELERMQQEVETQRKETE----IVQLQIRKQEESLKRRSFHIENKLKDL 672
Cdd:COG0419   168 KYEKLSELLKEVIKEAKAKIEELEGQL---SELLEDIEDLLEALEEELKelkkLEEIQEEQEEEELEQEIEALEERLAEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  673 LAEKEKFEEERLREQQEIEL---------QKKRQEEETFLRVQEELQRLKELnNNEKAEKFQIFQELDQLQKEKDEQYAK 743
Cdd:COG0419   245 EEEKERLEELKARLLEIESLelealkireEELRELERLLEELEEKIERLEEL-EREIEELEEELEGLRALLEELEELLEK 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  744 LELEKKRL-------EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGE 816
Cdd:COG0419   324 LKSLEERLekleeklEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSA 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  817 ELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL----------ECLKC--EHDKES--RLLEKHDESV 882
Cdd:COG0419   404 ALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELmiaelagageKCPVCgqELPEEHekELLELYELEL 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  883 TDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNhLPTLLEEKQRAFEILDRGPLSLDNtlYQVEKEMEEKEEQLAQYQAN 962
Cdd:COG0419   484 EELEEELSREKEEAELREEIEELEKELRELEEE-LIELLELEEALKEELEEKLEKLEN--LLEELEELKEKLQLQQLKEE 560
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  963 ANQLQKLQATFEFtaniARQEEKVRKKEKEILESREKQQREaLERALARLERRHSALQR------HSTLGMEIEEQRQKL 1036
Cdd:COG0419   561 LRQLEDRLQELKE----LLEELRLLRTRKEELEELRERLKE-LKKKLKELEERLSQLEEllqsleLSEAENELEEAEEEL 635
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 315434261 1037 ASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEV 1081
Cdd:COG0419   636 ESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENE 680
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
592-933 1.59e-15

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


Pssm-ID: 340095 [Multi-domain]  Cd Length: 756  Bit Score: 81.80  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIENKLKD 671
Cdd:pfam17380  271 YNGQTMTENEFLNQLLHIVQHQKSVSERQQQDKFEKMEQERIRQEKEEKARELE----RRRKLAEAEKARQAEIDRVSWG 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   672 LL---------------AEKEKFEEERLREQQEIELQKKRQEEEtflRVQEElqrlkelnnnEKAEKFQIFQELDQLQKE 736
Cdd:pfam17380  347 VFatggnlnyfqqaaiyAEQERMAMERERELERIQLEEKKREME---RIRQE----------EIAMEISKIRELERLQLE 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   737 KDEQYAKL--ELE---KKRLEEQEKEQVMLVAHLE-EQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARA 809
Cdd:pfam17380  414 RQQKNERVrqELEaarKQKILEEERQRKIKEQKREmEKIRKEQEEA---REEELRRLEEERaRELERVREEELERQHQIE 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   810 GGDEDGEELEKAQLRFFEFKRRQlvklvnLEKDLVQQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVP 889
Cdd:pfam17380  491 ILRQQEEDQKKKKLEKDKEEREK------AEAEEENKRKIIEKELEENKQAI----IEEENKRKILEKEMEDRQ--NAIY 558
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 315434261   890 QDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRaFEILDR 933
Cdd:pfam17380  559 EEEERRIAEEERRKQIEIEERKQIQEQIMIASEERSR-LDAMER 601
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
605-908 2.90e-13

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


Pssm-ID: 340095 [Multi-domain]  Cd Length: 756  Bit Score: 74.48  E-value: 2.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   605 ELEKLESKRKliEEMEE-KQKSDKAELERMQQE---VETQR-KETEIVQLQiRKQEESLKRRSFHIENKLKDLLAEKEKF 679
Cdd:pfam17380  365 EQERMAMERE--RELERiQLEEKKREMERIRQEeiaMEISKiRELERLQLE-RQQKNERVRQELEAARKQKILEEERQRK 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   680 EEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDqlQKEKDEQYAKLELEKKRLEEQEKEQV 759
Cdd:pfam17380  442 IKEQKREMEKIRKEQEEAREEELRRLEEERARELERVREEELERQHQIEILR--QQEEDQKKKKLEKDKEEREKAEAEEE 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   760 MLVAHLEEQLREKQEMIqllrrgevqwVEEEKRdlegiRESLLRVKEARAGGDEDGEELEKAQlrffEFKRRQlvKLVNL 839
Cdd:pfam17380  520 NKRKIIEKELEENKQAI----------IEEENK-----RKILEKEMEDRQNAIYEEEERRIAE----EERRKQ--IEIEE 578
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315434261   840 EKDLVQQKDILKKE------VQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpqdfeKIKPVeYRLQYKERQ 908
Cdd:pfam17380  579 RKQIQEQIMIASEErsrldaMERERELLRQIIENEKKQKEFERQELLATTPIT-------TIKPI-YRPDISEYQ 645
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
602-912 9.64e-13

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.21  E-value: 9.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  602 QREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 681
Cdd:COG1196   665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEE 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  682 ERLREQQEIELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQV 759
Cdd:COG1196   745 ELEELEEELEELQERLEelEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  760 MLVAHLEEqLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARaggdedgEELEKAqLRFFEFKRRQLVK-LVN 838
Cdd:COG1196   825 RLEQEIEE-LEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEK-------EELEDE-LKELEEEKEELEEeLRE 895
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434261  839 LEKDLVQqkdiLKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEkikpVEYRLQYKERQLQYL 912
Cdd:COG1196   896 LESELAE----LKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETE----LEREIERLEEEIEAL 961
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
545-860 9.82e-13

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


Pssm-ID: 340095 [Multi-domain]  Cd Length: 756  Bit Score: 72.94  E-value: 9.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   545 RTNMFRfNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSRENlsavmlynPGLEFERQQREElekleskrKLIEEMEEKQK 624
Cdd:pfam17380  368 RMAMER-ERELERIQLEEKKREMERIRQEEIAMEISKIREL--------ERLQLERQQKNE--------RVRQELEAARK 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   625 SDKAELERmQQEVETQRKETEivqlQIRKQEESLKrrsfhiENKLKDLlaEKEKFEEERLREQQEIElqkkRQEEETFLR 704
Cdd:pfam17380  431 QKILEEER-QRKIKEQKREME----KIRKEQEEAR------EEELRRL--EEERARELERVREEELE----RQHQIEILR 493
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   705 VQEELQRLKELNNNEKAEKFQIFQELDQ---LQKEKDEQYAKL--ELEKKRLEEQEKEQVMLVAHLEEQLREKQEMiqll 779
Cdd:pfam17380  494 QQEEDQKKKKLEKDKEEREKAEAEEENKrkiIEKELEENKQAIieEENKRKILEKEMEDRQNAIYEEEERRIAEEE---- 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   780 RRGEVQwVEEEKRdlegIRESLLRVKEaraggdedgeelEKAQLRFFEFKRRQLVKLVNLEKdlvQQKDILKKEVQEEQE 859
Cdd:pfam17380  570 RRKQIE-IEERKQ----IQEQIMIASE------------ERSRLDAMERERELLRQIIENEK---KQKEFERQELLATTP 629

                   .
gi 315434261   860 I 860
Cdd:pfam17380  630 I 630
PTZ00121 PTZ00121
MAEBL; Provisional
599-891 1.25e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 72.87  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  599 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 670
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  671 dLLAEKEKFEEERLREQqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLELEKKR 750
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEAKK 1669
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  751 lEEQEKEQVMLVAHLEEQLREKQEmiQLLRRGE--------VQWVEEEKRDLEGIR----ESLLRVKEARAGGDEDGEEL 818
Cdd:PTZ00121 1670 -AEEDKKKAEEAKKAEEDEKKAAE--ALKKEAEeakkaeelKKKEAEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKA 1746
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434261  819 EKAQLRFFEFKrrqlvKLVNLEKDLVQQKDILKKEvqEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 891
Cdd:PTZ00121 1747 EEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKE--KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
558-1093 1.73e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 72.05  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  558 AKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQRE-ELEKLESKRKLIEEMEEKQKSDKAELERMQQE 636
Cdd:COG1196   220 AELRELELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEkEIEELKSELEELREELEELQEELLELKEEIEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  637 VETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEE-------------ETFL 703
Cdd:COG1196   300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEleeklsalleeleELFE 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  704 RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKD----------EQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQ 773
Cdd:COG1196   380 ALREELAELEAELAEIRNELEELKREIESLEERLErlserledlkEELKELEAELEELQTELEELNEELEELEEQLEELR 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  774 EMIQLLRRgEVQWVEEEKRDLEGIRESLLRVK---EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKD-------- 842
Cdd:COG1196   460 DRLKELER-ELAELQEELQRLEKELSSLEARLdrlEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKyetaleaa 538
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  843 --------LVQQKDILKKEVQEEQE---------ILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIkpveyrlqyk 905
Cdd:COG1196   539 lgnrlqavVVENEEVAKKAIEFLKEnkagratflPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPA---------- 608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  906 erqLQYLLQNHL--PTLLEEKQRAFEILDRGPL-SLDNTLY----------QVEKEMEEKEEQLAQYQAnanQLQKLQAT 972
Cdd:COG1196   609 ---VRFVLGDTLvvDDLEQARRLARKLRIKYRIvTLDGDLVepsgsitggsRNKRSSLAQKRELKELEE---ELAELEAQ 682
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  973 FEFtANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHST-LGMEIEEQRQKLASLNSGSREQSGLQA 1051
Cdd:COG1196   683 LEK-LEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEqLQSRLEELEEELEELEEELEELQERLE 761
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 315434261 1052 SLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLE 1093
Cdd:COG1196   762 ELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELE 803
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
597-894 1.08e-11

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   597 EFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEK 676
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQL 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   677 EKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   757 EQVMLVAHLE----EQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARaggdEDGEELEKAQLRFFEFKRRQ 832
Cdd:TIGR02168  401 EIERLEARLErledRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL----ERLEEALEELREELEEAEQA 476
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434261   833 LVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 894
Cdd:TIGR02168  477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
600-910 1.74e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 68.97  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQqEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 679
Cdd:COG1196   182 ERTEENLERLEDLLEELEKQLEKLERQAEKAERYQ-ELKAELRELELALLLAKLKELRKELEE--LEEELSRLEEELEEL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  680 EEERLREQQEIE-LQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 757
Cdd:COG1196   259 QEELEEAEKEIEeLKSELEElREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEE 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  758 QV----------MLVAHLEEQLREKQEMIQLLRrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQlrffE 827
Cdd:COG1196   339 LEeretlleeleQLLAELEEAKEELEEKLSALL-------EELEELFEALREELAELEAELAEIRNELEELKREI----E 407
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  828 FKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKER 907
Cdd:COG1196   408 SLEERLERLSERLEDLKEELKELEAELEELQTELEELN---EELEELEEQLEELRDRLKELERELAELQEELQRLEKELS 484

                  ...
gi 315434261  908 QLQ 910
Cdd:COG1196   485 SLE 487
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
596-865 3.89e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 67.82  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  596 LEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 674
Cdd:COG1196   742 LEEELEElEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQ 821
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  675 EKEKFEEerlreqqeiELQKKRQEEETflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 754
Cdd:COG1196   822 RRERLEQ---------EIEELEEEIEE---LEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEEL 889
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  755 EKEQVMLVAHLEEQLREKQEMIQLLRRGEvqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRffefKRRQLV 834
Cdd:COG1196   890 EEELRELESELAELKEEIEKLRERLEELE----AKLERLEVELPELEEELEEEYEDTLETELEREIERLE----EEIEAL 961
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 315434261  835 KLVNLE-----KDLVQQKDILKKEVQEEQEILECLK 865
Cdd:COG1196   962 GPVNLRaieeyEEVEERYEELKSQREDLEEAKEKLL 997
PTZ00121 PTZ00121
MAEBL; Provisional
555-814 5.00e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQ 634
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLK 1639
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  635 QEVETQRKETEivqlQIRKQEESLKRRSFHIENKlkdllAEKEKfeeeRLREQQEIELQKKRQEEETFLRVQEELQRLKE 714
Cdd:PTZ00121 1640 KKEAEEKKKAE----ELKKAEEENKIKAAEEAKK-----AEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  715 LNNNEKAEKfqifQELDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvahleEQLR---EKQEMIQLLRRGEVQWVEEEK 791
Cdd:PTZ00121 1707 LKKKEAEEK----KKAEELKKAEEENKIKAE-EAKKEAEEDKKKA-------EEAKkdeEEKKKIAHLKKEEEKKAEEIR 1774
                         250       260
                  ....*....|....*....|...
gi 315434261  792 RDLEGIRESLLRVKEARAGGDED 814
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVD 1797
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
603-1136 6.85e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 67.02  E-value: 6.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   603 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRS--FHIENKLKDLLAEKEKF 679
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEkLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   680 EEERLREQQEIELQkkrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02169  440 EEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVR 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEK---------RDLEGIRESLLRVKEARAGG 811
Cdd:TIGR02169  508 GGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAvakeaiellKRRKAGRATFLPLNKMRDER 587
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   812 DEDGEELEKAQLRF---------------------------FEFKRRQL--VKLVNLEKDLVQQ---------------- 846
Cdd:TIGR02169  588 RDLSILSEDGVIGFavdlvefdpkyepafkyvfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprggil 667
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   847 -KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESVTDVTEVpqdFEKIKPVEYRLQYKERQLQYLLQNH--LPTLLEE 923
Cdd:TIGR02169  668 fSRSEPAELQRLRERLEGLKRE---LSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEekLKERLEE 741
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   924 KQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIARQEEKVRKKEKEIL 994
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQKL 821
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   995 ESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQ 1073
Cdd:TIGR02169  822 NRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434261  1074 LKQKIYEV----------DGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRV 1136
Cdd:TIGR02169  901 LERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
597-909 7.58e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 67.02  E-value: 7.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVET-------QRKETEIVQLQIRKQEESLKRRSFHIENKL 669
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqalLKEKREYEGYELLKEKEALERQKEAIERQL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   670 KDLLAEKEKFEEERLREQQEIE----------LQKKRQEEETFLRVQEELQRLK-ELNNNEK--AEKFQIFQELDQLQKE 736
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEeieqlleelnKKIKDLGEEEQLRVKEKIGELEaEIASLERsiAEKERELEDAEERLAK 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   737 KDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLegiRESLLRVKEARAGGDEDGE 816
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA-ELEEVDKEFAET---RDELKDYREKLEKLKREIN 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   817 ELEKAQLRFFEFKRRQLVKLVNLE---KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpqdfE 893
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK------E 476
                          330
                   ....*....|....*.
gi 315434261   894 KIKPVEYRLQYKERQL 909
Cdd:TIGR02169  477 EYDRVEKELSKLQREL 492
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
595-933 7.77e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 67.02  E-value: 7.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   595 GLEFERQQREELekleskrkliEEMEEKQKSDKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLA 674
Cdd:TIGR02169  665 GILFSRSEPAEL----------QRLRERLEGLKRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQ 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   675 EKEKFEEERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRL 751
Cdd:TIGR02169  731 EEEKLKERLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRI 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   752 EE--QEKEQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE----- 819
Cdd:TIGR02169  811 EArlREIEQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkke 890
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   820 ----KAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKI 895
Cdd:TIGR02169  891 rdelEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 315434261   896 KPVEYRL--QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 933
Cdd:TIGR02169  971 EPVNMLAiqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
600-914 8.49e-11

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 8.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   600 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVET---QRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:TIGR02168  704 RKELEELEEeLEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   676 KEKFEEERLREQQEIELQKKRQEE---------ETFLRVQEELQRLKelnnNEKAEKFQIFQELDQLQKEKDEQYAKLEL 746
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDElraeltllnEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSEDIESLAA 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   747 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwvEEEKRDlEGIRESLLRVKEARAGGDEDGEELEKAQLRff 826
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRS------ELEELS-EELRELESKRSELRRELEELREKLAQLELR-- 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   827 efkrrqlvkLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHdesvtdVTEVPQDFEKIKPV------EY 900
Cdd:TIGR02168  931 ---------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKELGPVnlaaieEY 995
                          330
                   ....*....|....
gi 315434261   901 RlQYKERqLQYLLQ 914
Cdd:TIGR02168  996 E-ELKER-YDFLTA 1007
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
555-1082 1.52e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.89  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  555 KEAAKLREKRKSGLLSSFSLSMTDlsksRENLSAVMLYNPGLEFERQQREELEKLESK-RKLIEEMEEKQKSDKAELERM 633
Cdd:COG1196   302 GEISLLRERLEELENELEELEERL----EELKEKIEALKEELEERETLLEELEQLLAElEEAKEELEEKLSALLEELEEL 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  634 QQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLK 713
Cdd:COG1196   378 FEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEE-----LNEELEELE 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  714 ELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE--EQEKEQVMLVAHLEEQLREKQE-----MIQLLRRGE--- 783
Cdd:COG1196   453 EQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDrlEAEQRASQGVRAVLEALESGLPgvygpVAELIKVKEkye 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  784 ---------------VQWVEEEKRDLEGIRE-----------SLLRVKEARAGGDEDG------------EELEKAQLRF 825
Cdd:COG1196   533 taleaalgnrlqavvVENEEVAKKAIEFLKEnkagratflplDRIKPLRSLKSDAAPGflglasdlidfdPKYEPAVRFV 612
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  826 F---------------EFKRRQLVKLVNLEKDLVQQKDIL------KKEVQEEQEILECLKCEHDKESRLLEKHDESVTD 884
Cdd:COG1196   613 LgdtlvvddleqarrlARKLRIKYRIVTLDGDLVEPSGSItggsrnKRSSLAQKRELKELEEELAELEAQLEKLEEELKS 692
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  885 VTEVPQDFEKIKPvEYRLQYKERQLQYllqNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN 964
Cdd:COG1196   693 LKNELRSLEDLLE-ELRRQLEELERQL---EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELE 768
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  965 QLQ----KLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLN 1040
Cdd:COG1196   769 SLEealaKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELE 848
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 315434261 1041 SGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVD 1082
Cdd:COG1196   849 EELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELE 890
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
597-859 2.08e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.51  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI---RKQEESLKRRSFHIENKLKDLL 673
Cdd:COG1196   699 SLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELeelQERLEELEEELESLEEALAKLK 778
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  674 AEKEKFEEERLreqqeiELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 752
Cdd:COG1196   779 EEIEELEEKRQ------ALQEELEElEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE 852
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  753 EQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwVEEEKRDLEGiresllRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 832
Cdd:COG1196   853 ELEKELEELKEELEELEAEKEELEDELKE-----LEEEKEELEE------ELRELESELAELKEEIEKLRERLEELEAKL 921
                         250       260
                  ....*....|....*....|....*..
gi 315434261  833 LVKLVNLEKDLVQQKDILKKEVQEEQE 859
Cdd:COG1196   922 ERLEVELPELEEELEEEYEDTLETELE 948
PTZ00121 PTZ00121
MAEBL; Provisional
536-1153 2.34e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.55  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  536 NQGAVILLGRTNMFRFNHPKEAAKLREKRKSGL--LSSFSLSMTDLSKSRENLSAvmlynpglEFERQQREELEKLESKR 613
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADElkKAEEKKKADEAKKAEEKKKA--------DEAKKKAEEAKKADEAK 1321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  614 KLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQ 693
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  694 KKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQEKEQvmlvaHLEEQLREKQ 773
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAE-----EAKKKAEEAK 1470
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  774 EMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFEFKRrqlvKLVNLEK-DLVQ 845
Cdd:PTZ00121 1471 KADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAEEAK----KADEAKKaEEKK 1546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  846 QKDILKK--EVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlpTLLEE 923
Cdd:PTZ00121 1547 KADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--------KAEEA 1618
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  924 KQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftaniARQEEKVRKKEKEILESREKQQRE 1003
Cdd:PTZ00121 1619 KIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKK-----------AEEENKIKAAEEAKKAEEDKKKAE 1678
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261 1004 ALERALARLERRHSALQRHstlgmeiEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDG 1083
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKE-------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261 1084 VQKDhhgtlEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISEGCSTSADTMKDNEK 1153
Cdd:PTZ00121 1752 DEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
595-935 3.31e-10

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


Pssm-ID: 308206 [Multi-domain]  Cd Length: 1162  Bit Score: 64.61  E-value: 3.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   595 GLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKL 669
Cdd:pfam02463  165 GSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   670 KDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL 744
Cdd:pfam02463  245 ELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   745 ELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR 824
Cdd:pfam02463  321 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   825 FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQY 904
Cdd:pfam02463  401 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 480
                          330       340       350
                   ....*....|....*....|....*....|.
gi 315434261   905 KERQLQYLLQNHLPTLLEEKQRAFEILDRGP 935
Cdd:pfam02463  481 VKLQEQLELLLSRQKLEERSQKESKARSGLK 511
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
600-885 4.34e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 64.35  E-value: 4.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  600 RQQREELEKLE---------SKRKLIEEMEEKQKSDKAELERMQQEVetQRKETEIVQL-----QIRKQEESLKRRSFHI 665
Cdd:COG1196   216 QELKAELRELElalllaklkELRKELEELEEELSRLEEELEELQEEL--EEAEKEIEELkseleELREELEELQEELLEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  666 ENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQ-----EELQRLKELNNNEKAEKFQIFQELDQLQKE-KDE 739
Cdd:COG1196   294 KEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEAlkeelEERETLLEELEQLLAELEEAKEELEEKLSAlLEE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  740 QYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESLLRVKEARAGGDEDGEELE 819
Cdd:COG1196   374 LEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSER-LEDLKEELKELEAELEELQTELEELNEELEELE 452
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315434261  820 kAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDV 885
Cdd:COG1196   453 -EQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGV 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
600-1078 5.06e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 5.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 679
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   680 EEERLREQQEIELQKKRQEeetflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEK-DEQYAKLELEKKRLEEQEKEQ 758
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERL 459
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   759 VMLVAHLEEQLREKQEMIQLLRRGEVQwveeekrdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRqLVKLVN 838
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQ--------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELIS 530
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   839 LEK------DLVQQKDILKKEVQEEQEILECLkcEHDKESRL---------LEKHDESVTDVTEVPQDFEKIKPVEYRLQ 903
Cdd:TIGR02168  531 VDEgyeaaiEAALGGRLQAVVVENLNAAKKAI--AFLKQNELgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   904 YKERQLQYLLQNHLPTLL--EEKQRAFEILDR-----------------------GPLSLDNTLYQVEKEMEEKEEQLAQ 958
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEE 688
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   959 YQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERrhsALQRHSTLGMEIEEQRQKLAS 1038
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEE 765
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 315434261  1039 LNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1078
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
601-861 5.28e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 5.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   601 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaEK 676
Cdd:TIGR02168  674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   677 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ---YAKLELEKKRLEE 753
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   754 QEKEQVMLVAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRFFEFK- 829
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELS-EELRELESKr 910
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 315434261   830 ---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 861
Cdd:TIGR02168  911 selRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PRK03918 PRK03918
chromosome segregation protein; Provisional
600-1068 5.47e-10

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.93  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  600 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 669
Cdd:PRK03918  269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  670 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 749
Cdd:PRK03918  348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  750 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 829
Cdd:PRK03918  413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  830 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 905
Cdd:PRK03918  483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  906 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 981
Cdd:PRK03918  562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  982 QEEKVRKKEKEILESREK---QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQE 1058
Cdd:PRK03918  638 TEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKELE 714
                         490
                  ....*....|
gi 315434261 1059 ALEKDQERLE 1068
Cdd:PRK03918  715 KLEKALERVE 724
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
597-774 7.16e-10

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 318010 [Multi-domain]  Cd Length: 520  Bit Score: 63.09  E-value: 7.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAEL----ERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDL 672
Cdd:pfam15709  354 EQEEQRRLQQEQLERAEKMKEELELEQQRRAEEIrlrkQRLEEEQQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   673 LAEKEKfeeerlREQQEIELQKKRQEEETfLRVQEELQRLKELNNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLE 752
Cdd:pfam15709  434 QRKKQQ------EEAERAEAEKQRQKELE-MQLAEEQKRLMEMAEEERLEY--------QRQKQEAEEKAQLEAEERRQK 498
                          170       180
                   ....*....|....*....|..
gi 315434261   753 EQEKEQVMlvahLEEQLREKQE 774
Cdd:pfam15709  499 EEEAARLA----LEEAMKQAQE 516
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
695-1100 1.56e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 62.42  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  695 KRQEEETFLRVQEELQRLKELNNnekaEKFQIFQELDQLQKEKD--EQYAKLELEKKRLEEQekeqvMLVAHLEEQLREK 772
Cdd:COG1196   171 KERKEEAERKLERTEENLERLED----LLEELEKQLEKLERQAEkaERYQELKAELRELELA-----LLLAKLKELRKEL 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  773 QEmiqllRRGEVQWVEEEKRDLEG-IRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKdLVQQKDILK 851
Cdd:COG1196   242 EE-----LEEELSRLEEELEELQEeLEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISL-LRERLEELE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  852 KEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKpveyrlqYKERQLQYLLQNHLPTLLEEKQRAFEIL 931
Cdd:COG1196   316 NELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAK-------EELEEKLSALLEELEELFEALREELAEL 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  932 DRgplsldntlyqvekemeekeeQLAQYQanaNQLQKLQATFEFtaniarqeekvrkkekeiLESREKQQREALERALAR 1011
Cdd:COG1196   389 EA---------------------ELAEIR---NELEELKREIES------------------LEERLERLSERLEDLKEE 426
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261 1012 LErrhSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGT 1091
Cdd:COG1196   427 LK---ELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGV 503

                  ....*....
gi 315434261 1092 LEGKVASSS 1100
Cdd:COG1196   504 RAVLEALES 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
597-916 1.70e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   597 EFERQqreeLEKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQL-QIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:TIGR02168  197 ELERQ----LKSLERQAEKAERYKEL----KAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   676 KEkfeeerlreqqeiELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 754
Cdd:TIGR02168  269 LE-------------ELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   755 EKEQVML----------VAHLEEQLREKQEMIQLLRRGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 821
Cdd:TIGR02168  336 AEELAELeekleelkeeLESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   822 QLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpVEYR 901
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQA------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQ 486
                          330
                   ....*....|....*
gi 315434261   902 LQYKERQLQYLLQNH 916
Cdd:TIGR02168  487 LQARLDSLERLQENL 501
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 2.10e-09

Kinesin-associated;


Pssm-ID: 318424  Cd Length: 181  Bit Score: 58.34  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   364 INEDANVKLIRELRAEIARLKTLL-AQG-------------------------------NQIA----------------- 394
Cdd:pfam16183    3 INEDPNAKLIRELKEEVARLRDLLyAQGlgdiidiaadahnnptnkrastpannlstvtNAMAgaspspslsalssrags 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   395 -------LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIG 458
Cdd:pfam16183   83 vsslherIMFTPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVN 162
                          170
                   ....*....|....*...
gi 315434261   459 IDDDLLSTGIILYHLKEG 476
Cdd:pfam16183  163 LNEDPLMSECLLYYIKDG 180
PRK03918 PRK03918
chromosome segregation protein; Provisional
691-1165 2.48e-09

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  691 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 770
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  771 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 847
Cdd:PRK03918  242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  848 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQ-YKERQLQYllqnhlptLLEEKQR 926
Cdd:PRK03918  321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGL--------TPEKLEK 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  927 AFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESR 997
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  998 EKQQREaLERALARLER---RHSALQRHSTLGMEIEEQRQKLASLN-----SGSREQSGLQ---ASLEAEQEALEKDQER 1066
Cdd:PRK03918  472 EEKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNleeleKKAEEYEKLKeklIKLKGEIKSLKKELEK 550
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261 1067 ---LEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMdariNAYIE--------EEVQRRLQDLHR 1135
Cdd:PRK03918  551 leeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY----NEYLElkdaekelEREEKELKKLEE 626
                         490       500       510
                  ....*....|....*....|....*....|
gi 315434261 1136 VISEGCSTSADTMKDNEKLHNGTIQRKLKY 1165
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKKY 656
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
612-1012 2.83e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 61.62  E-value: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   612 KRKLIEEMEEKQKSDkAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhienkLKDLLAEKEKFEeerlreqqeiE 691
Cdd:TIGR02169  155 RRKIIDEIAGVAEFD-RKKEKALEELEEVEENIERLDLIIDEKRQQLER--------LRREREKAERYQ----------A 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   692 LQKKRQEEETFLRvqeelqrLKELNNNEKaEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLRE 771
Cdd:TIGR02169  216 LLKEKREYEGYEL-------LKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEE-----------IEQLLEE 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   772 KQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQ---KD 848
Cdd:TIGR02169  277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrRD 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   849 ILKKEVQEEQEILECLKCEHDKESrllEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAF 928
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   929 EILDRgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftaniARQEEKVRKKEKEILESREKQQREALERA 1008
Cdd:TIGR02169  431 GIEAK--------INELEEEKEDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKELSKLQRELAEA 495

                   ....
gi 315434261  1009 LARL 1012
Cdd:TIGR02169  496 EAQA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
695-1068 3.84e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 61.24  E-value: 3.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   695 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 771
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   772 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 843
Cdd:TIGR02169  749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   844 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 923
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   924 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1001
Cdd:TIGR02169  887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315434261  1002 REALERALARLERRHSAlqrhstlgmEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALEKDQERLE 1068
Cdd:TIGR02169  960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAILERIEEYE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
695-1076 5.54e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 5.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   695 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 750
Cdd:TIGR02168  171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   751 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 830
Cdd:TIGR02168  251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   831 RQLV-KLVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 906
Cdd:TIGR02168  312 ANLErQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   907 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 986
Cdd:TIGR02168  379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   987 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1065
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
                          410
                   ....*....|.
gi 315434261  1066 RLEYEIQQLKQ 1076
Cdd:TIGR02168  500 NLEGFSEGVKA 510
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
599-1080 8.97e-09

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


Pssm-ID: 308206 [Multi-domain]  Cd Length: 1162  Bit Score: 59.99  E-value: 8.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENklkdllAEKEK 678
Cdd:pfam02463  272 LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE------LEKEL 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   679 FEEERLREQQEIELQKKRQEEETFLRVQEEL--------------QRLKELNNNEKAEKFQIFQELDQL-QKEKDEQYAK 743
Cdd:pfam02463  346 KELEIKREAEEEEEEELEKLQEKLEQLEEELlakkkleserlssaAKLKEEELELKSEEEKEAQLLLELaRQLEDLLKEE 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   744 LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 823
Cdd:pfam02463  426 KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE-LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 504
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   824 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKC-----EHDKESRLLEKHDESVTDVTEVPQDFEKIKPV 898
Cdd:pfam02463  505 KARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIStavivEVSATADEVEERQKLVRALTELPLGARKLRLL 584
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   899 EYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDrgpLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTAN 978
Cdd:pfam02463  585 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE---DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   979 IARQEEKVRKKEKEILESREKQQREALERALARLERRH-----------SALQRHSTLGMEIEEQRQKLASLNSGSREQS 1047
Cdd:pfam02463  662 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQleikkkeqrekEELKKLKLEAEELLADRVQEAQDKINEELKL 741
                          490       500       510
                   ....*....|....*....|....*....|...
gi 315434261  1048 GLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1080
Cdd:pfam02463  742 LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 774
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
698-1133 3.96e-08

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 57.85  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  698 EEETFLRV----QEELQRLKELNNNEKAEKF-QIFQ--ELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLR 770
Cdd:COG0419   130 DKDTFTRSvylpQGEFDAFLKSKPKERKEILdELFGleKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALE 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  771 -EKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEAR------AGGDEDGEELEKAQLRFFEFKRRQLVKLV----NL 839
Cdd:COG0419   210 eELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKerleelKARLLEIESLELEALKIREEELRELERLLeeleEK 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  840 EKDLVQQKDILKKEVQEEQEILECLK---CEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 916
Cdd:COG0419   290 IERLEELEREIEELEEELEGLRALLEeleELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEER 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  917 LPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILES 996
Cdd:COG0419   370 LEELEKELEKALERLKQ----LEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLES 445
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261  997 REKQ------------------QREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQE 1058
Cdd:COG0419   446 KELMiaelagagekcpvcgqelPEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIELLELEE 525
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315434261 1059 ALEKDQERLEYEIQQLKQKIYEVDGvqKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDL 1133
Cdd:COG0419   526 ALKEELEEKLEKLENLLEELEELKE--KLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEELRERLKEL 598
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
597-1095 4.25e-08

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: 57.81  E-value: 4.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKdlLAEK 676
Cdd:pfam05483  251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA----LEEDLQ--IATK 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   677 EKFEEERLREQQEIELQKKR-------QEEETFLRVQEELQRLKE--LNNNEKAEKFQIFQ------ELDQLQKEKDEQY 741
Cdd:pfam05483  325 TICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTEQqrLEKNEDQLKIITMElqkkssELEEMTKFKNNKE 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   742 AKLELEKKRLEEQEK--EQVMLVAHLEEQLREK-QEMIQLLrrgevQWVEEEKRDLEgIRESLLRVKEARAGGD--EDGE 816
Cdd:pfam05483  405 VELEELKKILAEDEKllDEKKQFEKIAEELKGKeQELIFLL-----QAREKEIHDLE-IQLTAIKTSEEHYLKEveDLKT 478
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   817 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQEEQE-ILECLKCEHD--KESRLLEKHDESVTDVTE-VPQDF 892
Cdd:pfam05483  479 ELEKEKLKNIELTAHC-DKLLLENKELTQEASDMTLELKKHQEdIINCKKQEERmlKQIENLEEKEMNLRDELEsVREEF 557
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   893 ---------------EKIKPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQ 955
Cdd:pfam05483  558 iqkgdevkckldkseENARSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQ 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   956 LAQYQANANQLQ-----KLQATFEFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQ 1020
Cdd:pfam05483  631 LNAYEIKVNKLElelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALME 710
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315434261  1021 RHS-TLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGK 1095
Cdd:pfam05483  711 KHKhQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
555-880 4.67e-08

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


Pssm-ID: 308206 [Multi-domain]  Cd Length: 1162  Bit Score: 57.67  E-value: 4.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLynpgLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ 634
Cdd:pfam02463  692 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV----QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   635 QEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKE 714
Cdd:pfam02463  768 SELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQELIEQEEKI-----KEEELEELA 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   715 LNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ------- 785
Cdd:pfam02463  841 LELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekenei 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   786 --WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILEC 863
Cdd:pfam02463  921 eeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 1000
                          330
                   ....*....|....*..
gi 315434261   864 LKCEHDKESRLLEKHDE 880
Cdd:pfam02463 1001 LEEEKKKLIRAIIEETC 1017
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
599-859 4.86e-08

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 317892 [Multi-domain]  Cd Length: 374  Bit Score: 56.54  E-value: 4.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434261   599 ERQQREELEKlESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIvqlQIRKQEESLKRRSFHIENKLKDLL----- 673
Cdd:pfam15558   41 EEKRRETLER-ERQRLLQQSQEQWQAQKEQRKARLSRE