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Conserved domains on  [gi|355390331|ref|NP_001239032|]
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kinesin-like protein KIF21B isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
7-371 0e+00

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


:

Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 597.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    7 CCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   87 GQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDSTRdpd 166
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPET--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  167 trHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVN 246
Cdd:cd01372   150 --DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  247 eavtglpdgtpPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSK 326
Cdd:cd01372   228 -----------ADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 355390331  327 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 371
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1292-1600 4.47e-65

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 222.98  E-value: 4.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1292 EGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVST-SYIKVWDIRDSaK 1368
Cdd:cd00200     6 KGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDLETG-E 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1369 CIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGKLTGHIGPVMCLT 1447
Cdd:cd00200    85 CVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1448 VTQTasqHDLVVTGSKDHYVKMFELGecvtgTIGPTHNFEPpHYDGIECLAIQGD--ILFSGSRDNGIKKWDLDQQELIQ 1525
Cdd:cd00200   143 FSPD---GTFVASSSQDGTIKLWDLR-----TGKCVATLTG-HTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 1526 QIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:cd00200   214 TLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRIWD 289
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
929-1010 4.06e-43

regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.


:

Pssm-ID: 410203 [Multi-domain]  Cd Length: 82  Bit Score: 151.88  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22262     1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80

                  ..
gi 355390331 1009 TK 1010
Cdd:cd22262    81 TK 82
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
633-842 9.25e-14

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 74.80  E-value: 9.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV---LQNLSTMECYTEEKANKIKAD 709
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  710 YEKRLR---------------------EMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE 768
Cdd:COG4942   106 LAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355390331  769 EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRlAKPMSERVAGRAGLKPP 842
Cdd:COG4942   186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLPWP 258
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
472-1064 9.17e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  472 EAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSpyslgaspaapafggspassmEDASEVIRRAKQDLERL 551
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL---------------------EEAQAEEYELLAELARL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  552 KKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKE-- 629
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEee 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  630 -VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteekankika 708
Cdd:COG1196   381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL---------------- 444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  709 dyEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQMREEQQ-----RRRLVETKRNRE 783
Cdd:COG1196   445 --EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRG 521
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  784 IAQLKKEQRRQEF----QIRALESQKRQQemVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSASTTSSEA 859
Cdd:COG1196   522 LAGAVAVLIGVEAayeaALEAALAAALQN--IVVEDDEVAAAAIEYLK---AAKAGRATFLPLDKIRARAALAAALARGA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  860 ESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARkkfqkkgasqsfskaARLKWQSLERRIIDIVMQRMTIVNLEAD 939
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE---------------AALRRAVTLAGRLREVTLEGEGGSAGGS 661
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  940 MERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDgitdcQATIVQLEETKEELDSTDTS 1019
Cdd:COG1196   662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER-----LEEELEEEALEEQLEAEREE 736
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 355390331 1020 VVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1064
Cdd:COG1196   737 LLE---ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
379-539 1.81e-03

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  379 DKTSQQISALRAEIARLQMELME-----YKAGKRVIGED---GAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINN 450
Cdd:COG3883    68 DKLQAEIAEAEAEIEERREELGEraralYRSGGSVSYLDvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  451 RVTQLMSQEANL--LLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGG 528
Cdd:COG3883   148 KKAELEAKLAELeaLKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
                         170
                  ....*....|.
gi 355390331  529 SPASSMEDASE 539
Cdd:COG3883   228 AAAAAAAAAAA 238
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
7-371 0e+00

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


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 597.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    7 CCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   87 GQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDSTRdpd 166
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPET--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  167 trHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVN 246
Cdd:cd01372   150 --DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  247 eavtglpdgtpPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSK 326
Cdd:cd01372   228 -----------ADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 355390331  327 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 371
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-377 1.33e-138

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


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 430.84  E-value: 1.33e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331      9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVL-------LGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNA 81
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNA 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331     82 TVLAYGQTGAGKTYTMGTgfdmatSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDS 161
Cdd:smart00129   82 TIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNP 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    162 trdpdtrhRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMrmctq 241
Cdd:smart00129  148 --------SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQK----- 214
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    242 pdlvneavtglpdGTPPSSEyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVvHVP 321
Cdd:smart00129  215 -------------IKNSSSG-SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR-HIP 279
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331    322 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 377
Cdd:smart00129  280 YRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
14-370 2.85e-137

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 426.99  E-value: 2.85e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    14 RIRPQLSKEKIEGCHICTSVTPGEPQVLL-------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    87 GQTGAGKTYTMGTgfdmatSEEEQGIIPRAIAHLFGGIAERKRRaqeqgvagPEFKVSAQFLELYNEEILDLFDSTRDPD 166
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPSNKNK 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   167 TrhrrsNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRmctqpdlvn 246
Cdd:pfam00225  147 R-----KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRN--------- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   247 eavtglpdgTPPSSEYETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRDS 325
Cdd:pfam00225  213 ---------RSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK--HIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 355390331   326 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
43-507 6.99e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 298.58  E-value: 6.99e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   43 GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGtgfdmaTSEEEQGIIPRAIAHLFG 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMS------GTEEEPGIIPLSLKELFS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  123 GIAERKRRAqeqgvagpEFKVSAQFLELYNEEILDLFDSTRDPdtrhrrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQ 202
Cdd:COG5059   127 KLEDLSMTK--------DFAVSISYLEIYNEKIYDLLSPNEES--------LNIREDSLLGVKVAGLTEKHVSSKEEILD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  203 CLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrmctqpdlvneavtglpDGTPPSSEYeTLTAKFHFVDLAGSERLKR 282
Cdd:COG5059   191 LLRKGEKNRTTASTEINDESSRSHSIFQIEL--------------------ASKNKVSGT-SETSKLSLVDLAGSERAAR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  283 TGATGERAKEGISINCGLLALGNVISALGDQsKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLK 362
Cdd:COG5059   250 TGNRGTRLKEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  363 YANRARNIKNKVVVNQDK-TSQQISALRAEIARLQMELMEYKAGKRVIGEDgaegySDLFRENAMLQKengaLRLRVKAM 441
Cdd:COG5059   329 FASRAKSIKNKIQVNSSSdSSREIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQS----LKKETETL 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  442 QEAIDAINNRVTQLMSQEANLLLAKaGDGNEAIGALIQNYI----REIEELRTKLLESEAMNESLRRSLS 507
Cdd:COG5059   400 KSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIdrllLLREEELSKKKTKIHKLNKLRHDLS 468
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-404 3.75e-65

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 244.07  E-value: 3.75e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    3 GQGDCCVKVAVRIRPQLSKEKIEgchicTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:PLN03188   94 GVSDSGVKVIVRMKPLNKGEEGE-----MIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   83 VLAYGQTGAGKTYTM----GTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVagpEFKVSAQFLELYNEEILDL 158
Cdd:PLN03188  169 VFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQIKHADRQL---KYQCRCSFLEIYNEQITDL 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  159 FDSTRdpdtrhrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTihlcqmrm 238
Cdd:PLN03188  246 LDPSQ--------KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT-------- 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  239 CtqpdLVNEAVTGLPDGTppsSEYETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD--QSKK 316
Cdd:PLN03188  310 C----VVESRCKSVADGL---SSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisQTGK 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  317 VVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDkTSQQISALRAEIARLQ 396
Cdd:PLN03188  381 QRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLR 459

                  ....*...
gi 355390331  397 MELMEYKA 404
Cdd:PLN03188  460 DELQRVKA 467
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1292-1600 4.47e-65

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 222.98  E-value: 4.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1292 EGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVST-SYIKVWDIRDSaK 1368
Cdd:cd00200     6 KGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDLETG-E 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1369 CIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGKLTGHIGPVMCLT 1447
Cdd:cd00200    85 CVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1448 VTQTasqHDLVVTGSKDHYVKMFELGecvtgTIGPTHNFEPpHYDGIECLAIQGD--ILFSGSRDNGIKKWDLDQQELIQ 1525
Cdd:cd00200   143 FSPD---GTFVASSSQDGTIKLWDLR-----TGKCVATLTG-HTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 1526 QIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:cd00200   214 TLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1189-1602 1.72e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.95  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1189 RDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDK 1268
Cdd:COG2319    11 AASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1269 GIISPVGGAKGAR---TAPLQCVSMAEGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKY 1343
Cdd:COG2319    91 RLLASASADGTVRlwdLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1344 cSHSG-LVFSVSTSY-IKVWDIrDSAKCIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-N 1420
Cdd:COG2319   171 -SPDGkLLASGSDDGtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1421 AVRIWELSRFQPVGKLTGHIGPVMCLTVTqtasqHD--LVVTGSKDHYVKMFELGecvTGTIGPTHnfePPHYDGIECLA 1498
Cdd:COG2319   227 TVRLWDLATGKLLRTLTGHSGSVRSVAFS-----PDgrLLASGSADGTVRLWDLA---TGELLRTL---TGHSGGVNSVA 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1499 I--QGDILFSGSRDNGIKKWDLDQQELIQQIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSP 1576
Cdd:COG2319   296 FspDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGA 374
                         410       420
                  ....*....|....*....|....*...
gi 355390331 1577 INAICTNA--KHIFTASSDLTVKFWSVR 1602
Cdd:COG2319   375 VTSVAFSPdgRTLASGSADGTVRLWDLA 402
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
929-1010 4.06e-43

regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.


Pssm-ID: 410203 [Multi-domain]  Cd Length: 82  Bit Score: 151.88  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22262     1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80

                  ..
gi 355390331 1009 TK 1010
Cdd:cd22262    81 TK 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
633-842 9.25e-14

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 74.80  E-value: 9.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV---LQNLSTMECYTEEKANKIKAD 709
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  710 YEKRLR---------------------EMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE 768
Cdd:COG4942   106 LAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355390331  769 EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRlAKPMSERVAGRAGLKPP 842
Cdd:COG4942   186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLPWP 258
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
472-1064 9.17e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  472 EAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSpyslgaspaapafggspassmEDASEVIRRAKQDLERL 551
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL---------------------EEAQAEEYELLAELARL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  552 KKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKE-- 629
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEee 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  630 -VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteekankika 708
Cdd:COG1196   381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL---------------- 444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  709 dyEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQMREEQQ-----RRRLVETKRNRE 783
Cdd:COG1196   445 --EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRG 521
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  784 IAQLKKEQRRQEF----QIRALESQKRQQemVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSASTTSSEA 859
Cdd:COG1196   522 LAGAVAVLIGVEAayeaALEAALAAALQN--IVVEDDEVAAAAIEYLK---AAKAGRATFLPLDKIRARAALAAALARGA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  860 ESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARkkfqkkgasqsfskaARLKWQSLERRIIDIVMQRMTIVNLEAD 939
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE---------------AALRRAVTLAGRLREVTLEGEGGSAGGS 661
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  940 MERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDgitdcQATIVQLEETKEELDSTDTS 1019
Cdd:COG1196   662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER-----LEEELEEEALEEQLEAEREE 736
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 355390331 1020 VVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1064
Cdd:COG1196   737 LLE---ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
383-1094 3.31e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 3.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   383 QQISALRAEIARLQMELMEYKAGKRVIGEDgaegYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANL 462
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   463 LlakagDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAApafggspASSMEDASEVIR 542
Cdd:TIGR02168  315 E-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-------ESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   543 RAKQDLERLKKKE----VRQRRKSPEKEAFKKR-AKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEES 617
Cdd:TIGR02168  383 TLRSKVAQLELQIaslnNEIERLEARLERLEDRrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   618 LVDSDSDPEEKevnfQADLADLTCEIEIKQKLIDELENSQRRLQTLkhqYEEKLILLQNKIRDTQLeRDRVLQNLSTMEC 697
Cdd:TIGR02168  463 LEELREELEEA----EQALDAAERELAQLQARLDSLERLQENLEGF---SEGVKALLKNQSGLSGI-LGVLSELISVDEG 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   698 Y------------------TEEKANK-IKADYEKRLREMN---RDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEM 755
Cdd:TIGR02168  535 YeaaieaalggrlqavvveNLNAAKKaIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   756 KKA----------------KVALMKQMREEQQ--------------------RRRLVETKRNREIAQLKKEQRRQEFQIR 799
Cdd:TIGR02168  615 RKAlsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIA 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   800 ALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVagraglkppmldSGAEVSASTTSSEAESGARSVSSIVRQWNRKINH 879
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQI------------SALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   880 FLGDHpaptvngtrparkkfQKKGASQSFSKAARLKWQSLERRIidivmQRMTIvNLEADMERLIKKREELFLLQEALRR 959
Cdd:TIGR02168  763 IEELE---------------ERLEEAEEELAEAEAEIEELEAQI-----EQLKE-ELKALREALDELRAELTLLNEEAAN 821
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   960 KRER---LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQAtivQLEETKEELDSTDTSVVISSCSLAEARLLLDN 1036
Cdd:TIGR02168  822 LRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEE 898
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355390331  1037 FlkasiDKGLQVAQKEAQiRLLEGRLRQTDMAGSSQNHL---------LLDALREK----AEAHPELQALI 1094
Cdd:TIGR02168  899 L-----SEELRELESKRS-ELRRELEELREKLAQLELRLeglevridnLQERLSEEysltLEEAEALENKI 963
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
632-1230 4.57e-10

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 64.75  E-value: 4.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   632 FQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYE 711
Cdd:pfam15921  315 YMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----DQLQKLLADLH 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   712 KRLREMNrdLQKLQAaQKEHARLLKNQ---SRYERELKKLQAEVAEMKkakvALMKQMREEQQrrrlveTKRNREIAQLK 788
Cdd:pfam15921  388 KREKELS--LEKEQN-KRLWDRDTGNSitiDHLRRELDDRNMEVQRLE----ALLKAMKSECQ------GQMERQMAAIQ 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   789 KEQRRQEfQIRALESQKRQQEMVLRRKTQEVSAlRRLAKPMSERVAG-------------------------RAGLKPPM 843
Cdd:pfam15921  455 GKNESLE-KVSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVSdltaslqekeraieatnaeitklrsRVDLKLQE 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   844 L----DSGAEVSASTTSSEA----ESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFS-- 909
Cdd:pfam15921  533 LqhlkNEGDHLRNVQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKil 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   910 ---KAARLKwqSLERRIIDIVMQRMTIVNleADMERLIKKREelfllqeaLRRKRERLQAESPEEEKGLQELAEEIEVLA 986
Cdd:pfam15921  613 kdkKDAKIR--ELEARVSDLELEKVKLVN--AGSERLRAVKD--------IKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   987 ANIDYINDGI-TDCQATIVQLEETKEELDSTDTSVVISSCSLAEArllldnfLKASIDKGLQVAQKEAQIRLLEGRLRQT 1065
Cdd:pfam15921  681 RNFRNKSEEMeTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA-------MKVAMGMQKQITAKRGQIDALQSKIQFL 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1066 DMAGSSQN---HLLLDalrEKAEAHPELQALiynVQQENGYASTDEEISefsegsfSQSFTMKGSTSHDDFKFKsepKLS 1142
Cdd:pfam15921  754 EEAMTNANkekHFLKE---EKNKLSQELSTV---ATEKNKMAGELEVLR-------SQERRLKEKVANMEVALD---KAS 817
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1143 AQMkavsAECLGPPLDISTKNITKSLASLVEIKE-DGVGFSvRDPYYRDRVSRTVSLPTRGSTFPR-QSRATETSPLTRR 1220
Cdd:pfam15921  818 LQF----AECQDIIQRQEQESVRLKLQHTLDVKElQGPGYT-SNSSMKPRLLQPASFTRTHSNVPSsQSTASFLSHHSRK 892
                          650
                   ....*....|
gi 355390331  1221 KSYDRGQPIR 1230
Cdd:pfam15921  893 TNALKEDPTR 902
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
642-818 3.76e-09

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 61.68  E-value: 3.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   642 EIEIKQKLIDELEnsqrRLQTLKHQYEEKL---ILLQNKIRDTQLERDR-VLQNLSTMECYTEEKAN----KIKADYEKR 713
Cdd:pfam17380  369 EIAMEISRMRELE----RLQMERQQKNERVrqeLEAARKVKILEEERQRkIQQQKVEMEQIRAEQEEarqrEVRRLEEER 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   714 LREMNRDLQKLQAAQKEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQ----RRRLVETKRNREIAQLKK 789
Cdd:pfam17380  445 AREMERVRLEEQERQQQVERL--RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKLLEKEM 522
                          170       180       190
                   ....*....|....*....|....*....|....
gi 355390331   790 EQRR----QEFQIRALESQKR-QQEMVLRRKTQE 818
Cdd:pfam17380  523 EERQkaiyEEERRREAEEERRkQQEMEERRRIQE 556
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
633-1014 5.61e-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: 61.23  E-value: 5.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcYTEEKANKIKADYEK 712
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   713 RLREMNRDLQKLQAAQKEHarllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQR----RRLVETKRNReIAQLK 788
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEA----------EAEIEELEAQIEQLKEELKALREALDELRAEltllNEEAANLRER-LESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   789 KEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPpmldsgaevSASTTSSEAESGARSVSS 868
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------SLEEALALLRSELEELSE 901
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   869 IVRQWNRKInhflgdhpaptvngtRPARKKFQKKGASQSfskAARLKWQSLERRIIDIVMQRMTIVNLEADMerLIKKRE 948
Cdd:TIGR02168  902 ELRELESKR---------------SELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEE--AEALEN 961
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331   949 ELFLLQEALRRKRERLQAEspeeekgLQELA-------EEIEVLAANIDYINDGITDCQATIVQLEETKEELD 1014
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENK-------IKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
362-982 2.32e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  362 KYANRARNIKNKVVVNQDK---TSQQISALRAEIARLQMELMEYKAGKRVIgEDGAEGYSDLFRENAMLQKENGALRLRV 438
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKI 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  439 KAMQEAIDAINNRVTQLMSQEANLL-LAKAGDGNEAIGALIQNY---IREIEELRTKLleseamnESLRRSLSRasarsp 514
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKeLKEKAEEYIKLSEFYEEYldeLREIEKRLSRL-------EEEINGIEE------ 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  515 yslgaspaapafggspasSMEDASEVIRRakqdLERLKKKEVRQRRkspEKEAFKKRAKLQQENSEETDENEAEEEEEER 594
Cdd:PRK03918  329 ------------------RIKELEEKEER----LEELKKKLKELEK---RLEELEERHELYEEAKAKKEELERLKKRLTG 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  595 DESGCEEEEGredededsgseESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKlill 674
Cdd:PRK03918  384 LTPEKLEKEL-----------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE---- 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  675 qnkirdtqlERDRVlqnlstMECYTEEKAN--KIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRY------ERELK 746
Cdd:PRK03918  449 ---------HRKEL------LEEYTAELKRieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkelEEKLK 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  747 KLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRK----TQEV-SA 821
Cdd:PRK03918  514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELeER 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  822 LRRLAKPMSERVAgraglkppMLDSGAEV--------SASTTSSEAESGARSVSSIVRQWNRKINHFLGDHpapTVNGTR 893
Cdd:PRK03918  594 LKELEPFYNEYLE--------LKDAEKELereekelkKLEEELDKAFEELAETEKRLEELRKELEELEKKY---SEEEYE 662
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  894 PARKKFQKKgASQSFSKAARLKwqSLERRIIDIvmqRMTIVNLEADMERLIKKREELFLLQ------EALRRKRERLQAE 967
Cdd:PRK03918  663 ELREEYLEL-SRELAGLRAELE--ELEKRREEI---KKTLEKLKEELEEREKAKKELEKLEkalervEELREKVKKYKAL 736
                         650
                  ....*....|....*...
gi 355390331  968 spEEEKGL---QELAEEI 982
Cdd:PRK03918  737 --LKERALskvGEIASEI 752
PRK12704 PRK12704
phosphodiesterase; Provisional
673-818 1.28e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  673 LLQNKIRDTQLERDRVLQNLST-MECYTEEK-------ANKIKADYEKRLREMNRDLQKLQAaqkehaRLLKNQSRYERE 744
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKeAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEK------RLLQKEENLDRK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  745 LKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR------EIAQLKKEQRRQEfQIRALESQKRQQEMVLRRKTQE 818
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqeleRISGLTAEEAKEI-LLEKVEEEARHEAAVLIKEIEE 180
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1563-1600 1.08e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 1.08e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 355390331   1563 NFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1286-1321 1.33e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 1.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 355390331  1286 QCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1321
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
645-788 1.52e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 45.78  E-value: 1.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    645 IKQKLIDELENSQRRLQTLKhQYEEKLILLQNKIRDTQ--LERD-RVLQNLstmecytEEKANKIKADYEKRLREmnrdl 721
Cdd:smart00787  145 LKEGLDENLEGLKEDYKLLM-KELELLNSIKPKLRDRKdaLEEElRQLKQL-------EDELEDCDPTELDRAKE----- 211
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331    722 qKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLK 788
Cdd:smart00787  212 -KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLK 277
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
379-539 1.81e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  379 DKTSQQISALRAEIARLQMELME-----YKAGKRVIGED---GAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINN 450
Cdd:COG3883    68 DKLQAEIAEAEAEIEERREELGEraralYRSGGSVSYLDvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  451 RVTQLMSQEANL--LLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGG 528
Cdd:COG3883   148 KKAELEAKLAELeaLKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
                         170
                  ....*....|.
gi 355390331  529 SPASSMEDASE 539
Cdd:COG3883   228 AAAAAAAAAAA 238
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
651-822 3.46e-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: 41.41  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  651 DELENSQRRLQ-TLKHQYEEklILLQNKirDTQLER-DRVLQNLS-TME---------------CYTEEKaNKIKADYEK 712
Cdd:cd16269    86 DEDQKFQKKLMeQLEEKKEE--FCKQNE--EASSKRcQALLQELSaPLEekisqgsysvpggyqLYLEDR-EKLVEKYRQ 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  713 RLR---EMNRDLQK-LQAAQKEHARLLK-NQSRYERELKKLqaevAEMKKAKVALMKQMREEQQRRRLVETKRNRE---- 783
Cdd:cd16269   161 VPRkgvKAEEVLQEfLQSKEAEAEAILQaDQALTEKEKEIE----AERAKAEAAEQERKLLEEQQRELEQKLEDQErsye 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 355390331  784 --IAQLKKE-----QRRQEFQIRALESQKRQQEMVLRRKTQEVSAL 822
Cdd:cd16269   237 ehLRQLKEKmeeerENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
919-1021 4.14e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  919 LERRIIDIVMQRMTIVNL--EADMERLIKKREELFLLQEALRRKRERLQAEspeeekglQELAEEIEVLAANIDYINDGI 996
Cdd:COG0542   416 LERRLEQLEIEKEALKKEqdEASFERLAELRDELAELEEELEALKARWEAE--------KELIEEIQELKEELEQRYGKI 487
                          90       100
                  ....*....|....*....|....*
gi 355390331  997 TDCQATIVQLEETKEELDSTDTSVV 1021
Cdd:COG0542   488 PELEKELAELEEELAELAPLLREEV 512
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
7-371 0e+00

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


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 597.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    7 CCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   87 GQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDSTRdpd 166
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPET--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  167 trHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVN 246
Cdd:cd01372   150 --DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  247 eavtglpdgtpPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSK 326
Cdd:cd01372   228 -----------ADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 355390331  327 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 371
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-377 1.33e-138

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


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 430.84  E-value: 1.33e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331      9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVL-------LGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNA 81
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNA 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331     82 TVLAYGQTGAGKTYTMGTgfdmatSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDS 161
Cdd:smart00129   82 TIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNP 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    162 trdpdtrhRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMrmctq 241
Cdd:smart00129  148 --------SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQK----- 214
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    242 pdlvneavtglpdGTPPSSEyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVvHVP 321
Cdd:smart00129  215 -------------IKNSSSG-SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR-HIP 279
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331    322 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 377
Cdd:smart00129  280 YRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
14-370 2.85e-137

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 426.99  E-value: 2.85e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    14 RIRPQLSKEKIEGCHICTSVTPGEPQVLL-------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    87 GQTGAGKTYTMGTgfdmatSEEEQGIIPRAIAHLFGGIAERKRRaqeqgvagPEFKVSAQFLELYNEEILDLFDSTRDPD 166
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPSNKNK 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   167 TrhrrsNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRmctqpdlvn 246
Cdd:pfam00225  147 R-----KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRN--------- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   247 eavtglpdgTPPSSEYETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRDS 325
Cdd:pfam00225  213 ---------RSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK--HIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 355390331   326 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
9-368 2.41e-124

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


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 392.00  E-value: 2.41e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKiEGCHICTSVTPG------EPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:cd00106     2 VRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   83 VLAYGQTGAGKTYTMgtgfdMATSEEEQGIIPRAIAHLFggiaerkRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd00106    81 IFAYGQTGSGKTYTM-----LGPDPEQRGIIPRALEDIF-------ERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  163 RdpdtrhrRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMctqp 242
Cdd:cd00106   149 P-------KKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNR---- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  243 DLVNEAVTGlpdgtppsseyetltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPY 322
Cdd:cd00106   218 EKSGESVTS---------------SKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPY 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 355390331  323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 368
Cdd:cd00106   281 RDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
8-370 5.58e-104

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


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 335.58  E-value: 5.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    8 CVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKA--------FTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGY 79
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   80 NATVLAYGQTGAGKTYTMGtGFDmaTSEEEQGIIPRAIAHLFGGIAerkrRAQEQgvagPEFKVSAQFLELYNEEILDLF 159
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTME-GKR--EDPELRGIIPNSFAHIFGHIA----RSQNN----QQFLVRVSYLEIYNEEIRDLL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  160 DStrdpDTRHRrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrMC 239
Cdd:cd01371   151 GK----DQTKR---LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----EC 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  240 TQPDLVNEAVTGLpdgtppsseyetltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqsKKVVH 319
Cdd:cd01371   220 SEKGEDGENHIRV--------------GKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD--GKSTH 283
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 355390331  320 VPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01371   284 IPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
8-372 3.96e-103

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


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 333.02  E-value: 3.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    8 CVKVAVRIRPQLSKEKIE-GCHICTSVTPGEPQVLLGKD---KAFTYDFVFDLDTWQEQIYSTcVSKLIEGCFEGYNATV 83
Cdd:cd01366     3 NIRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   84 LAYGQTGAGKTYTM-GTgfdmatsEEEQGIIPRAIAHLFGGIAERKrraqEQGVagpEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd01366    82 FAYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELK----EKGW---SYTIKASMLEIYNETIRDLLAPG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  163 RDPDTRHrrsNIKiHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrmctqp 242
Cdd:cd01366   148 NAPQKKL---EIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  243 dlvneavtglpDGTPPSSEyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdqSKKVVHVPY 322
Cdd:cd01366   215 -----------SGRNLQTG-EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPY 279
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 355390331  323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 372
Cdd:cd01366   280 RNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
9-370 4.00e-101

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


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 328.15  E-value: 4.00e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEGCHICTSVT--------PGEPQVLL--------------GKDKAFTYDFVFDLDTWQEQIYST 66
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   67 CVSKLIEGCFEGYNATVLAYGQTGAGKTYTM-GTgfdmatsEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSA 145
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLK--------DEKEFEVSM 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  146 QFLELYNEEILDLFDSTRDPdtrhrrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRS 225
Cdd:cd01370   147 SYLEIYNETIRDLLNPSSGP--------LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRS 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  226 HAIFTIHLCQMrmcTQPDLVNEAVTglpdgtppsseyetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGN 305
Cdd:cd01370   219 HAVLQITVRQQ---DKTASINQQVR---------------QGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGN 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355390331  306 VISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01370   281 CINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
9-377 1.96e-99

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


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 323.92  E-value: 1.96e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEGC--------HICTSVTPGEPQVLLGKDKAFTYDFVFDLDTW-----------QEQIYSTCVS 69
Cdd:cd01365     3 VKVAVRVRPFNSREKERNSkcivqmsgKETTLKNPKQADKNNKATREVPKSFSFDYSYWshdsedpnyasQEQVYEDLGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   70 KLIEGCFEGYNATVLAYGQTGAGKTYTMgtgfdMATsEEEQGIIPRAIAHLFggiaERKRRAQEQGVagpEFKVSAQFLE 149
Cdd:cd01365    83 ELLQHAFEGYNVCLFAYGQTGSGKSYTM-----MGT-QEQPGIIPRLCEDLF----SRIADTTNQNM---SYSVEVSYME 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  150 LYNEEILDLFDstrdPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIF 229
Cdd:cd01365   150 IYNEKVRDLLN----PKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  230 TIHLCQMRMctqpdlvnEAVTGLPdgtppsseyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 309
Cdd:cd01365   226 TIVLTQKRH--------DAETNLT---------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISA 288
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331  310 LGDQSKKV-----VHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 377
Cdd:cd01365   289 LADMSSGKskkksSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
9-379 4.95e-96

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


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 313.68  E-value: 4.95e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGK-DKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYG 87
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   88 QTGAGKTYTM--GTGFDMATSEEEQGIIPRAIAHLFGGIaerkRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRdp 165
Cdd:cd01373    83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLI----QREKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPAS-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  166 dtrhrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqMRMCTQPDLV 245
Cdd:cd01373   157 ------RNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  246 NeavtglpdgtppsseyeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSK-KVVHVPYRD 324
Cdd:cd01373   229 N-----------------IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRD 291
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 355390331  325 SKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQD 379
Cdd:cd01373   292 SKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
6-370 6.51e-95

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


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 309.65  E-value: 6.51e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    6 DCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKD--KAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATV 83
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   84 LAYGQTGAGKTYTM-GTGFDmatsEEEQGIIPRAIAHLFGGIaerkrraqEQGVAGPEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd01369    81 FAYGQTSSGKTYTMeGKLGD----PESMGIIPRIVQDIFETI--------YSMDENLEFHVKVSYFEIYMEKIRDLLDVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  163 RDpdtrhrrsNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQp 242
Cdd:cd01369   149 KT--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETE- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  243 dlvneavtglpdgtppsseyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqsKKVVHVPY 322
Cdd:cd01369   220 --------------------KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPY 277
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 355390331  323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01369   278 RDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
9-379 8.16e-94

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


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 307.72  E-value: 8.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLL--------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYN 80
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   81 ATVLAYGQTGAGKTYTMgTGfDMATSE-------EEQGIIPRAIAHLFggiaerkrraQEQGVAGPEFKVSAQFLELYNE 153
Cdd:cd01364    84 CTIFAYGQTGTGKTYTM-EG-DRSPNEeytweldPLAGIIPRTLHQLF----------EKLEDNGTEYSVKVSYLEIYNE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  154 EILDLFDStrDPDTRHRrsnIKIHEDAN--GGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTI 231
Cdd:cd01364   152 ELFDLLSP--SSDVSER---LRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSI 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  232 HLcqmrmctqpdLVNEAvtglpdgtppSSEYETL--TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 309
Cdd:cd01364   227 TI----------HIKET----------TIDGEELvkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITA 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  310 LGDQSKkvvHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQD 379
Cdd:cd01364   287 LVERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
9-370 1.55e-89

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


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 294.24  E-value: 1.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQ 88
Cdd:cd01374     2 ITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   89 TGAGKTYTMgTGfdmatSEEEQGIIPRAIAHLFGGIAERKRRaqeqgvagpEFKVSAQFLELYNEEILDLFDSTRdpdtr 168
Cdd:cd01374    82 TSSGKTFTM-SG-----DEDEPGIIPLAIRDIFSKIQDTPDR---------EFLLRVSYLEIYNEKINDLLSPTS----- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  169 hrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcQMRMCTQPDlvNEA 248
Cdd:cd01374   142 ---QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELE--EGT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  249 VTglpdgtppsseYETLTakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqSKKVVHVPYRDSKLT 328
Cdd:cd01374   216 VR-----------VSTLN----LIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLT 279
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 355390331  329 RLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01374   280 RILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
43-507 6.99e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 298.58  E-value: 6.99e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   43 GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGtgfdmaTSEEEQGIIPRAIAHLFG 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMS------GTEEEPGIIPLSLKELFS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  123 GIAERKRRAqeqgvagpEFKVSAQFLELYNEEILDLFDSTRDPdtrhrrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQ 202
Cdd:COG5059   127 KLEDLSMTK--------DFAVSISYLEIYNEKIYDLLSPNEES--------LNIREDSLLGVKVAGLTEKHVSSKEEILD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  203 CLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrmctqpdlvneavtglpDGTPPSSEYeTLTAKFHFVDLAGSERLKR 282
Cdd:COG5059   191 LLRKGEKNRTTASTEINDESSRSHSIFQIEL--------------------ASKNKVSGT-SETSKLSLVDLAGSERAAR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  283 TGATGERAKEGISINCGLLALGNVISALGDQsKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLK 362
Cdd:COG5059   250 TGNRGTRLKEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  363 YANRARNIKNKVVVNQDK-TSQQISALRAEIARLQMELMEYKAGKRVIGEDgaegySDLFRENAMLQKengaLRLRVKAM 441
Cdd:COG5059   329 FASRAKSIKNKIQVNSSSdSSREIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQS----LKKETETL 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  442 QEAIDAINNRVTQLMSQEANLLLAKaGDGNEAIGALIQNYI----REIEELRTKLLESEAMNESLRRSLS 507
Cdd:COG5059   400 KSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIdrllLLREEELSKKKTKIHKLNKLRHDLS 468
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
9-368 3.20e-69

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


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 235.86  E-value: 3.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEGCHICTSVTpGEPQVLL------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   83 VLAYGQTGAGKTYTMgtgfdmATSEEEQGIIPRAIAHLFggiaerkRRAQEQGVAGpefKVSAQFLELYNEEILDLFDSt 162
Cdd:cd01376    81 VFAYGSTGAGKTFTM------LGSPEQPGLMPLTVMDLL-------QMTRKEAWAL---SFTMSYLEIYQEKILDLLEP- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  163 rdpdtrhRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQmrmctQP 242
Cdd:cd01376   144 -------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQ-----RE 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  243 DLVNeavtglpdgtppsseYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdqSKKVVHVPY 322
Cdd:cd01376   212 RLAP---------------FRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 355390331  323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 368
Cdd:cd01376   274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
45-368 9.77e-69

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


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 235.17  E-value: 9.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   45 DKAFTYDFVFDlDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGfdmATSEEEQGIIPRAIAHLFGGI 124
Cdd:cd01375    47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGG---TENYKHRGIIPRALQQVFRMI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  125 AERKRRAqeqgvagpeFKVSAQFLELYNEEILDLFDSTrdPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCL 204
Cdd:cd01375   123 EERPTKA---------YTVHVSYLEIYNEQLYDLLSTL--PYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  205 KQGALSRTTASTQMNVQSSRSHAIFTIHLcQMRMCTqpdlvneavtglpdgtpPSSEyETLTAKFHFVDLAGSERLKRTG 284
Cdd:cd01375   192 FLGETNRIIASHTMNKNSSRSHCIFTIHL-EAHSRT-----------------LSSE-KYITSKLNLVDLAGSERLSKTG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  285 ATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 364
Cdd:cd01375   253 VEGQVLKEATYINKSLSFLEQAIIALSDKDRT--HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330

                  ....
gi 355390331  365 NRAR 368
Cdd:cd01375   331 SRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
9-366 2.73e-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 [Multi-domain]  Cd Length: 328  Bit Score: 233.73  E-value: 2.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKIEG-CHICTSVTPGEPQVLLGKDK----------AFTYDFVFDLDTWQEQIYSTCVSKLIEGCFE 77
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   78 GYNATVLAYGQTGAGKTYTMGTGFdmATSEEEQGIIPRAIAHLFGGIAERKRRAQeqgvagpeFKVSAQFLELYNEEILD 157
Cdd:cd01367    82 GGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDN--------LGVTVSFFEIYGGKVFD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  158 LFdstrdpdtrHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmr 237
Cdd:cd01367   152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  238 mctqpdlvneavtglpdgtpPSSEYETLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDQSkk 316
Cdd:cd01367   219 --------------------RDRGTNKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 355390331  317 vVHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 366
Cdd:cd01367   277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
9-364 1.40e-67

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


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 232.28  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    9 VKVAVRIRPQLSKEKI---EGC-HI--CTSVTPGEPQVLLG---------KDKAFTYDFVFDLDTWQEQIYSTCVSKLIE 73
Cdd:cd01368     3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   74 GCFEGYNATVLAYGQTGAGKTYTMgTGfdmatSEEEQGIIPRAIAHLFGGIaerkrraqeqgvagPEFKVSAQFLELYNE 153
Cdd:cd01368    83 DLLHGKNGLLFTYGVTNSGKTYTM-QG-----SPGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  154 EILDLFDSTRDPDTRHRRSnIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHL 233
Cdd:cd01368   143 YIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  234 CQmrmctqpdlvneavtgLPDGTPPSSEYET---LTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 310
Cdd:cd01368   222 VQ----------------APGDSDGDVDQDKdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVL 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331  311 GDQ--SKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 364
Cdd:cd01368   286 RENqlQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-404 3.75e-65

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 244.07  E-value: 3.75e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    3 GQGDCCVKVAVRIRPQLSKEKIEgchicTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:PLN03188   94 GVSDSGVKVIVRMKPLNKGEEGE-----MIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   83 VLAYGQTGAGKTYTM----GTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVagpEFKVSAQFLELYNEEILDL 158
Cdd:PLN03188  169 VFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQIKHADRQL---KYQCRCSFLEIYNEQITDL 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  159 FDSTRdpdtrhrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTihlcqmrm 238
Cdd:PLN03188  246 LDPSQ--------KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT-------- 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  239 CtqpdLVNEAVTGLPDGTppsSEYETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD--QSKK 316
Cdd:PLN03188  310 C----VVESRCKSVADGL---SSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisQTGK 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  317 VVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDkTSQQISALRAEIARLQ 396
Cdd:PLN03188  381 QRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLR 459

                  ....*...
gi 355390331  397 MELMEYKA 404
Cdd:PLN03188  460 DELQRVKA 467
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1292-1600 4.47e-65

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 222.98  E-value: 4.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1292 EGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVST-SYIKVWDIRDSaK 1368
Cdd:cd00200     6 KGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDLETG-E 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1369 CIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGKLTGHIGPVMCLT 1447
Cdd:cd00200    85 CVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1448 VTQTasqHDLVVTGSKDHYVKMFELGecvtgTIGPTHNFEPpHYDGIECLAIQGD--ILFSGSRDNGIKKWDLDQQELIQ 1525
Cdd:cd00200   143 FSPD---GTFVASSSQDGTIKLWDLR-----TGKCVATLTG-HTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 1526 QIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:cd00200   214 TLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1189-1602 1.72e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.95  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1189 RDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDK 1268
Cdd:COG2319    11 AASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1269 GIISPVGGAKGAR---TAPLQCVSMAEGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKY 1343
Cdd:COG2319    91 RLLASASADGTVRlwdLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1344 cSHSG-LVFSVSTSY-IKVWDIrDSAKCIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-N 1420
Cdd:COG2319   171 -SPDGkLLASGSDDGtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1421 AVRIWELSRFQPVGKLTGHIGPVMCLTVTqtasqHD--LVVTGSKDHYVKMFELGecvTGTIGPTHnfePPHYDGIECLA 1498
Cdd:COG2319   227 TVRLWDLATGKLLRTLTGHSGSVRSVAFS-----PDgrLLASGSADGTVRLWDLA---TGELLRTL---TGHSGGVNSVA 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1499 I--QGDILFSGSRDNGIKKWDLDQQELIQQIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSP 1576
Cdd:COG2319   296 FspDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGA 374
                         410       420
                  ....*....|....*....|....*...
gi 355390331 1577 INAICTNA--KHIFTASSDLTVKFWSVR 1602
Cdd:COG2319   375 VTSVAFSPdgRTLASGSADGTVRLWDLA 402
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
929-1010 4.06e-43

regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.


Pssm-ID: 410203 [Multi-domain]  Cd Length: 82  Bit Score: 151.88  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22262     1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80

                  ..
gi 355390331 1009 TK 1010
Cdd:cd22262    81 TK 82
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1399-1602 5.61e-36

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 139.01  E-value: 5.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1399 EHQINQIALSPSGTMLYAASGNA-VRIWELSRFQPVGKLTGHIGPVMCLTVTqtaSQHDLVVTGSKDHYVKMFEL--GEC 1475
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPVRDVAAS---ADGTYLASGSSDKTIRLWDLetGEC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1476 VtgtigptHNFEPpHYDGIECLAIQ--GDILFSGSRDNGIKKWDLDQQELIQQIpNAHKDWVCALAFIPGRPMLLSACRA 1553
Cdd:cd00200    86 V-------RTLTG-HTSYVSSVAFSpdGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 355390331 1554 GVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWSVR 1602
Cdd:cd00200   157 GTIKLWDLRTGKCVATLTGHTGEVNSVAfsPDGEKLLSSSSDGTIKLWDLS 207
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
929-1010 2.63e-28

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 109.63  E-value: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                  ..
gi 355390331 1009 TK 1010
Cdd:cd22263    81 AK 82
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
929-1010 6.17e-27

regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410202 [Multi-domain]  Cd Length: 81  Bit Score: 105.36  E-value: 6.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKgLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22248     1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKDESV-LRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79

                  ..
gi 355390331 1009 TK 1010
Cdd:cd22248    80 SK 81
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
7-158 2.52e-17

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 80.34  E-value: 2.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331     7 CCVKVAVRIRPQLSKEkiegCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCvSKLIEGCFEGYNATVLAY 86
Cdd:pfam16796   20 GNIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAY 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355390331    87 GQTGAGKTYTMgtgfdmatseeeqgiIPRAIAHLFGGIAERKRraqeqgvaGPEFKVSAQFLELYNEEILDL 158
Cdd:pfam16796   95 GQTGSGSNDGM---------------IPRAREQIFRFISSLKK--------GWKYTIELQFVEIYNESSQDL 143
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
11-309 1.47e-14

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: 73.15  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   11 VAVRIRPQLSKEKIEGCHICTSvtpgepqvllgkdkaftyDFVFDLDTWQEQIYSTCvSKLIEGCFEGYN-ATVLAYGQT 89
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVF------------------YRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   90 GAGKTYTMgtgfdmatseeeQGIIPRAIAHLFGGIaerkrraqeqgvagpefkvsaqflelyneeildlfdstrdpdtrh 169
Cdd:cd01363    62 GAGKTETM------------KGVIPYLASVAFNGI--------------------------------------------- 84
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  170 rrsnikiheDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRtTASTQMNVQSSRSHAIFTIhlcqmrmctqpdlvneav 249
Cdd:cd01363    85 ---------NKGETEGWVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  250 tglpdgtppsseyetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 309
Cdd:cd01363   137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
633-842 9.25e-14

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 74.80  E-value: 9.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV---LQNLSTMECYTEEKANKIKAD 709
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  710 YEKRLR---------------------EMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE 768
Cdd:COG4942   106 LAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355390331  769 EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRlAKPMSERVAGRAGLKPP 842
Cdd:COG4942   186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLPWP 258
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
642-1085 1.30e-13

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 75.96  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  642 EIEIKQKLIDELENSQRRLQTL---KHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANkikadyEKRLREMN 718
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL------EAELAELP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  719 RDLQKLQAAQKEHARLlknqsryERELKKLQAEVAEMKKAKVALMKQMREEqQRRRLVETKRNRE-----IAQLKKEQRR 793
Cdd:COG4717   146 ERLEELEERLEELREL-------EEELEELEAELAELQEELEELLEQLSLA-TEEELQDLAEELEelqqrLAELEEELEE 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  794 QEFQIRALESQKRQ--QEMVLRRKTQEVSALRRLAKPMS----------------ERVAG----RAGLKPPMLDSGAEVS 851
Cdd:COG4717   218 AQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAallallglggsllsliLTIAGvlflVLGLLALLFLLLAREK 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  852 ASTTSSEAESGARSVSSIVRQwnRKINHFLGDHPAPTVNGTRPARKKFQ-----KKGASQSFSKAARLKWQSLERRIIDI 926
Cdd:COG4717   298 ASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDrieelQELLREAEELEEELQLEELEQEIAAL 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  927 VmqRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQ-----ELAEEIEVLAANIDYINDGITDCQA 1001
Cdd:COG4717   376 L--AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELRE 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1002 TIVQLEETKEELDSTDTsvvisscsLAEARllldnflkasidkgLQVAQKEAQIRLLEGRLRQTDMAGSsqnhlLLDALR 1081
Cdd:COG4717   454 ELAELEAELEQLEEDGE--------LAELL--------------QELEELKAELRELAEEWAALKLALE-----LLEEAR 506

                  ....
gi 355390331 1082 EKAE 1085
Cdd:COG4717   507 EEYR 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
472-1064 9.17e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  472 EAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSpyslgaspaapafggspassmEDASEVIRRAKQDLERL 551
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL---------------------EEAQAEEYELLAELARL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  552 KKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKE-- 629
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEee 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  630 -VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteekankika 708
Cdd:COG1196   381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL---------------- 444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  709 dyEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQMREEQQ-----RRRLVETKRNRE 783
Cdd:COG1196   445 --EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRG 521
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  784 IAQLKKEQRRQEF----QIRALESQKRQQemVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSASTTSSEA 859
Cdd:COG1196   522 LAGAVAVLIGVEAayeaALEAALAAALQN--IVVEDDEVAAAAIEYLK---AAKAGRATFLPLDKIRARAALAAALARGA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  860 ESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARkkfqkkgasqsfskaARLKWQSLERRIIDIVMQRMTIVNLEAD 939
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE---------------AALRRAVTLAGRLREVTLEGEGGSAGGS 661
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  940 MERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDgitdcQATIVQLEETKEELDSTDTS 1019
Cdd:COG1196   662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER-----LEEELEEEALEEQLEAEREE 736
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 355390331 1020 VVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1064
Cdd:COG1196   737 LLE---ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
383-1094 3.31e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 3.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   383 QQISALRAEIARLQMELMEYKAGKRVIGEDgaegYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANL 462
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   463 LlakagDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAApafggspASSMEDASEVIR 542
Cdd:TIGR02168  315 E-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-------ESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   543 RAKQDLERLKKKE----VRQRRKSPEKEAFKKR-AKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEES 617
Cdd:TIGR02168  383 TLRSKVAQLELQIaslnNEIERLEARLERLEDRrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   618 LVDSDSDPEEKevnfQADLADLTCEIEIKQKLIDELENSQRRLQTLkhqYEEKLILLQNKIRDTQLeRDRVLQNLSTMEC 697
Cdd:TIGR02168  463 LEELREELEEA----EQALDAAERELAQLQARLDSLERLQENLEGF---SEGVKALLKNQSGLSGI-LGVLSELISVDEG 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   698 Y------------------TEEKANK-IKADYEKRLREMN---RDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEM 755
Cdd:TIGR02168  535 YeaaieaalggrlqavvveNLNAAKKaIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   756 KKA----------------KVALMKQMREEQQ--------------------RRRLVETKRNREIAQLKKEQRRQEFQIR 799
Cdd:TIGR02168  615 RKAlsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIA 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   800 ALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVagraglkppmldSGAEVSASTTSSEAESGARSVSSIVRQWNRKINH 879
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQI------------SALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   880 FLGDHpaptvngtrparkkfQKKGASQSFSKAARLKWQSLERRIidivmQRMTIvNLEADMERLIKKREELFLLQEALRR 959
Cdd:TIGR02168  763 IEELE---------------ERLEEAEEELAEAEAEIEELEAQI-----EQLKE-ELKALREALDELRAELTLLNEEAAN 821
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   960 KRER---LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQAtivQLEETKEELDSTDTSVVISSCSLAEARLLLDN 1036
Cdd:TIGR02168  822 LRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEE 898
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355390331  1037 FlkasiDKGLQVAQKEAQiRLLEGRLRQTDMAGSSQNHL---------LLDALREK----AEAHPELQALI 1094
Cdd:TIGR02168  899 L-----SEELRELESKRS-ELRRELEELREKLAQLELRLeglevridnLQERLSEEysltLEEAEALENKI 963
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
632-1230 4.57e-10

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 64.75  E-value: 4.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   632 FQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYE 711
Cdd:pfam15921  315 YMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----DQLQKLLADLH 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   712 KRLREMNrdLQKLQAaQKEHARLLKNQ---SRYERELKKLQAEVAEMKkakvALMKQMREEQQrrrlveTKRNREIAQLK 788
Cdd:pfam15921  388 KREKELS--LEKEQN-KRLWDRDTGNSitiDHLRRELDDRNMEVQRLE----ALLKAMKSECQ------GQMERQMAAIQ 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   789 KEQRRQEfQIRALESQKRQQEMVLRRKTQEVSAlRRLAKPMSERVAG-------------------------RAGLKPPM 843
Cdd:pfam15921  455 GKNESLE-KVSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVSdltaslqekeraieatnaeitklrsRVDLKLQE 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   844 L----DSGAEVSASTTSSEA----ESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFS-- 909
Cdd:pfam15921  533 LqhlkNEGDHLRNVQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKil 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   910 ---KAARLKwqSLERRIIDIVMQRMTIVNleADMERLIKKREelfllqeaLRRKRERLQAESPEEEKGLQELAEEIEVLA 986
Cdd:pfam15921  613 kdkKDAKIR--ELEARVSDLELEKVKLVN--AGSERLRAVKD--------IKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   987 ANIDYINDGI-TDCQATIVQLEETKEELDSTDTSVVISSCSLAEArllldnfLKASIDKGLQVAQKEAQIRLLEGRLRQT 1065
Cdd:pfam15921  681 RNFRNKSEEMeTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA-------MKVAMGMQKQITAKRGQIDALQSKIQFL 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1066 DMAGSSQN---HLLLDalrEKAEAHPELQALiynVQQENGYASTDEEISefsegsfSQSFTMKGSTSHDDFKFKsepKLS 1142
Cdd:pfam15921  754 EEAMTNANkekHFLKE---EKNKLSQELSTV---ATEKNKMAGELEVLR-------SQERRLKEKVANMEVALD---KAS 817
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1143 AQMkavsAECLGPPLDISTKNITKSLASLVEIKE-DGVGFSvRDPYYRDRVSRTVSLPTRGSTFPR-QSRATETSPLTRR 1220
Cdd:pfam15921  818 LQF----AECQDIIQRQEQESVRLKLQHTLDVKElQGPGYT-SNSSMKPRLLQPASFTRTHSNVPSsQSTASFLSHHSRK 892
                          650
                   ....*....|
gi 355390331  1221 KSYDRGQPIR 1230
Cdd:pfam15921  893 TNALKEDPTR 902
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
701-1092 1.69e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  701 EKANKIKADYEKR--------LREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKAKVALMKQMREEQQR 772
Cdd:COG1196   213 ERYRELKEELKELeaellllkLRELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEEAQAE 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  773 RRLVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSA 852
Cdd:COG1196   290 EYELL----AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  853 STTSSEAESGARsvSSIVRQWNRKinhflgdhpaptvngtrpARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMT 932
Cdd:COG1196   363 AEEALLEAEAEL--AEAEEELEEL------------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  933 IVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEE 1012
Cdd:COG1196   423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1013 LDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQA 1092
Cdd:COG1196   503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
702-1015 2.29e-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: 2.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   702 KANKIKAdyEKRLREMNRDLQKLQAAQKEHARLLKN---QSRYERELKKLQAEVAEMKKAKVAL-MKQMREEQQRRRLVE 777
Cdd:TIGR02168  171 KERRKET--ERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELALLVLrLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   778 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA-GRAGLKPpmlDSGAEVSASTTS 856
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQiLRERLAN---LERQLEELEAQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   857 SEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQsfskAARLKWQSLERRIIDIVMQ----RMT 932
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLELQiaslNNE 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   933 IVNLEADMERLIKKREELFLLQEALRRK-----RERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLE 1007
Cdd:TIGR02168  402 IERLEARLERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481

                   ....*...
gi 355390331  1008 ETKEELDS 1015
Cdd:TIGR02168  482 RELAQLQA 489
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
642-818 3.76e-09

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 61.68  E-value: 3.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   642 EIEIKQKLIDELEnsqrRLQTLKHQYEEKL---ILLQNKIRDTQLERDR-VLQNLSTMECYTEEKAN----KIKADYEKR 713
Cdd:pfam17380  369 EIAMEISRMRELE----RLQMERQQKNERVrqeLEAARKVKILEEERQRkIQQQKVEMEQIRAEQEEarqrEVRRLEEER 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   714 LREMNRDLQKLQAAQKEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQ----RRRLVETKRNREIAQLKK 789
Cdd:pfam17380  445 AREMERVRLEEQERQQQVERL--RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKLLEKEM 522
                          170       180       190
                   ....*....|....*....|....*....|....
gi 355390331   790 EQRR----QEFQIRALESQKR-QQEMVLRRKTQE 818
Cdd:pfam17380  523 EERQkaiyEEERRREAEEERRkQQEMEERRRIQE 556
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
633-1014 5.61e-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: 61.23  E-value: 5.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcYTEEKANKIKADYEK 712
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   713 RLREMNRDLQKLQAAQKEHarllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQR----RRLVETKRNReIAQLK 788
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEA----------EAEIEELEAQIEQLKEELKALREALDELRAEltllNEEAANLRER-LESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   789 KEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPpmldsgaevSASTTSSEAESGARSVSS 868
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------SLEEALALLRSELEELSE 901
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   869 IVRQWNRKInhflgdhpaptvngtRPARKKFQKKGASQSfskAARLKWQSLERRIIDIVMQRMTIVNLEADMerLIKKRE 948
Cdd:TIGR02168  902 ELRELESKR---------------SELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEE--AEALEN 961
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331   949 ELFLLQEALRRKRERLQAEspeeekgLQELA-------EEIEVLAANIDYINDGITDCQATIVQLEETKEELD 1014
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENK-------IKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
626-1084 7.93e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 7.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  626 EEKEVNFQADLADLTCEIEIKQKLIDELEnsqRRLQTLKHQYEE----KLILLQNKIRDTQLERDRVLQNLSTME--CYT 699
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALR---EELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEalLAA 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  700 -EEKANKIKADYEKRLREMNRDLQKLQ----AAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRR 774
Cdd:COG4913   371 lGLPLPASAEEFAALRAEAAALLEALEeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDA 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  775 LVETKRNREIA--------QLKKEQRRQEFQI-RALESQK-------RQQEMVLRrktqevsALRRLakPMSERVAGRaG 838
Cdd:COG4913   449 LAEALGLDEAElpfvgeliEVRPEEERWRGAIeRVLGGFAltllvppEHYAAALR-------WVNRL--HLRGRLVYE-R 518
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  839 LKPpmldsgAEVSASTTSSEAESGARSVS---SIVRQW-NRKINHF-----------LGDHP-APTVNG------TRpAR 896
Cdd:COG4913   519 VRT------GLPDPERPRLDPDSLAGKLDfkpHPFRAWlEAELGRRfdyvcvdspeeLRRHPrAITRAGqvkgngTR-HE 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  897 KKFQKKGASQS---FSKAARLKWqsLERRIidivmqrmtiVNLEADMERLIKKREELFLLQEALRRKRERLQ--AESPEE 971
Cdd:COG4913   592 KDDRRRIRSRYvlgFDNRAKLAA--LEAEL----------AELEEELAEAEERLEALEAELDALQERREALQrlAEYSWD 659
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  972 EKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDstdtsvvisscslaEARLLLDNFLKASIDKGLQVAQK 1051
Cdd:COG4913   660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE--------------ELEEELDELKGEIGRLEKELEQA 725
                         490       500       510
                  ....*....|....*....|....*....|...
gi 355390331 1052 EAQIRLLEGRLRQTDMAGSSQNHLLLDALREKA 1084
Cdd:COG4913   726 EEELDELQDRLEAAEDLARLELRALLEERFAAA 758
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
623-896 9.36e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.46  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  623 SDPEEKEVnfQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEklilLQNKIRDTQLERDRVLQNLSTmecyTEEK 702
Cdd:COG3883    14 ADPQIQAK--QKELSELQAEL---EAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAE----AEAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  703 ANKIKADYEKRLREMNRD----------------------LQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 760
Cdd:COG3883    81 IEERREELGERARALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  761 ALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLK 840
Cdd:COG3883   161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331  841 PPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPAR 896
Cdd:COG3883   241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
484-822 1.65e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.70  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   484 EIEELRTKLLESEAMNESLRRSLSRASARSpyslgaspaapafgGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSP 563
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRL--------------DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   564 EKEAFKKraKLQQEnseetdeneaeeeeeerdesgceeeegrededeDSGSEESLVDSDSDPEEKE---VNFQADLADLt 640
Cdd:TIGR02169  741 ELEEDLS--SLEQE---------------------------------IENVKSELKELEARIEELEedlHKLEEALNDL- 784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   641 cEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLER---DRVLQNLSTMECYTEEKANKIKADYE---KRL 714
Cdd:TIGR02169  785 -EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKK 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   715 REMNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKkakvalmKQMREEQQRRRLVETKRNRE---IAQLKKEQ 791
Cdd:TIGR02169  864 EELEEELEELEAALRD----------LESRLGDLKKERDELE-------AQLRELERKIEELEAQIEKKrkrLSELKAKL 926
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 355390331   792 RRQEFQIRALESQKRQQE-------------MVLRRKTQEVSAL 822
Cdd:TIGR02169  927 EALEEELSEIEDPKGEDEeipeeelsledvqAELQRVEEEIRAL 970
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
670-1062 4.62e-08

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 57.60  E-value: 4.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   670 KLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKAD---YEKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELK 746
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRVAELK---EELRQSREKHEELEEKYK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   747 KLQAEVAEMKKAKVALMKQMREEQQRRRLVE----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKT 816
Cdd:pfam07888  105 ELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   817 QEvsaLRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTS------SEAESGA-----RSVSSIVRQWNRKINhFLGDHP 885
Cdd:pfam07888  185 EE---LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEAlleelRSLQERLNASERKVE-GLGEEL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   886 APTVNgtrparkkfqKKGASQSFSKAARLKWQSLERRIIDIVMQ-----------RMTIV-NLEADMERLIKkreelflL 953
Cdd:pfam07888  261 SSMAA----------QRDRTQAELHQARLQAAQLTLQLADASLAlregrarwaqeRETLQqSAEADKDRIEK-------L 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   954 QEALRRKRERLQAESPEEEKGLQELAEEievlaanidyindgiTDCqaTIVQLEETKEELDStdtsvvisscslaearll 1033
Cdd:pfam07888  324 SAELQRLEERLQEERMEREKLEVELGRE---------------KDC--NRVQLSESRRELQE------------------ 368
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 355390331  1034 ldnfLKASidkgLQVAQKEAQ------------IRLLEGRL 1062
Cdd:pfam07888  369 ----LKAS----LRVAQKEKEqlqaekqelleyIRQLEQRL 401
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
633-838 9.07e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.31  E-value: 9.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  633 QADLADLTCEIEIKQKLIDELENsqrRLQTLKHQYEEKLILLQNKIRDTQLE----RDRVLQNLSTMECYteekaNKIKA 708
Cdd:COG4942    75 EQELAALEAELAELEKEIAELRA---ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYL-----KYLAP 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  709 DYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLK 788
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-------AELAELQ 219
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 355390331  789 KEQRRQEFQIRALESQKRQQEmvLRRKTQEVSALR-RLAKPMSERVAGRAG 838
Cdd:COG4942   220 QEAEELEALIARLEAEAAAAA--ERTPAAGFAALKgKLPWPVSGRVVRRFG 268
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
702-1105 1.13e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  702 KANKIKAdyEKRLREMNRDLQKLQAAQKEharlLKNQsryereLKKL--QAEVA--------EMKKAKVALM-KQMREEQ 770
Cdd:COG1196   171 KERKEEA--ERKLEATEENLERLEDILGE----LERQ------LEPLerQAEKAeryrelkeELKELEAELLlLKLRELE 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  771 QRRRLVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRrlakpmservagraglkppmldsGAEV 850
Cdd:COG1196   239 AELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-----------------------AEEY 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  851 SASTTSSEAEsgarsvssivrqwnrkinhflgdhpaptvngtrpARKKFQKKGASQSFSKAARLKWQ--SLERRIIDIVM 928
Cdd:COG1196   292 ELLAELARLE----------------------------------QDIARLEERRRELEERLEELEEElaELEEELEELEE 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  929 QRMT----IVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIV 1004
Cdd:COG1196   338 ELEEleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1005 QLEETKEELDStdtsvvisscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKA 1084
Cdd:COG1196   418 RLEEELEELEE----------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
                         410       420
                  ....*....|....*....|.
gi 355390331 1085 EAHPELQALIYNVQQENGYAS 1105
Cdd:COG1196   488 EAAARLLLLLEAEADYEGFLE 508
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
626-834 1.47e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   626 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDtqLERDRVLQNLSTMECYTEeKANK 705
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELS-KLEE 805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   706 IKADYEKRLREMNRDLQKL----QAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRn 781
Cdd:TIGR02169  806 EVSRIEARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL- 884
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 355390331   782 reiAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 834
Cdd:TIGR02169  885 ---GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
665-841 2.22e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 55.63  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  665 HQYEEKLILLQNKI-RDTQLE--RDRVLQNLS----------TMECYTEEKANKIKADYEKRLREMNRDLQKLQ---AAQ 728
Cdd:COG2433   346 DAYKNKFERVEKKVpPDVDRDevKARVIRGLSieealeelieKELPEEEPEAEREKEHEERELTEEEEEIRRLEeqvERL 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  729 KEHARLLKNQSR-YERELKKLQAEVAEMKKakvalmkQMREEQQRRRLVeTKRNREIAQLKKEQRRQEFQIRALESQ--- 804
Cdd:COG2433   426 EAEVEELEAELEeKDERIERLERELSEARS-------EERREIRKDREI-SRLDREIERLERELEEERERIEELKRKler 497
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 355390331  805 -KRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKP 841
Cdd:COG2433   498 lKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKE 535
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
362-982 2.32e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  362 KYANRARNIKNKVVVNQDK---TSQQISALRAEIARLQMELMEYKAGKRVIgEDGAEGYSDLFRENAMLQKENGALRLRV 438
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKI 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  439 KAMQEAIDAINNRVTQLMSQEANLL-LAKAGDGNEAIGALIQNY---IREIEELRTKLleseamnESLRRSLSRasarsp 514
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKeLKEKAEEYIKLSEFYEEYldeLREIEKRLSRL-------EEEINGIEE------ 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  515 yslgaspaapafggspasSMEDASEVIRRakqdLERLKKKEVRQRRkspEKEAFKKRAKLQQENSEETDENEAEEEEEER 594
Cdd:PRK03918  329 ------------------RIKELEEKEER----LEELKKKLKELEK---RLEELEERHELYEEAKAKKEELERLKKRLTG 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  595 DESGCEEEEGredededsgseESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKlill 674
Cdd:PRK03918  384 LTPEKLEKEL-----------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE---- 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  675 qnkirdtqlERDRVlqnlstMECYTEEKAN--KIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRY------ERELK 746
Cdd:PRK03918  449 ---------HRKEL------LEEYTAELKRieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkelEEKLK 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  747 KLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRK----TQEV-SA 821
Cdd:PRK03918  514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELeER 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  822 LRRLAKPMSERVAgraglkppMLDSGAEV--------SASTTSSEAESGARSVSSIVRQWNRKINHFLGDHpapTVNGTR 893
Cdd:PRK03918  594 LKELEPFYNEYLE--------LKDAEKELereekelkKLEEELDKAFEELAETEKRLEELRKELEELEKKY---SEEEYE 662
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  894 PARKKFQKKgASQSFSKAARLKwqSLERRIIDIvmqRMTIVNLEADMERLIKKREELFLLQ------EALRRKRERLQAE 967
Cdd:PRK03918  663 ELREEYLEL-SRELAGLRAELE--ELEKRREEI---KKTLEKLKEELEEREKAKKELEKLEkalervEELREKVKKYKAL 736
                         650
                  ....*....|....*...
gi 355390331  968 spEEEKGL---QELAEEI 982
Cdd:PRK03918  737 --LKERALskvGEIASEI 752
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
642-824 3.83e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.03  E-value: 3.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   642 EIEIKQKLIDELENSQRRLQTLKHQYEEKLILL-------QNKIRDTQLERDRVLQNLSTMECYTE-------------E 701
Cdd:TIGR04523  146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeklniQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqiselkK 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   702 KANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKR 780
Cdd:TIGR04523  226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKE 305
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 355390331   781 NREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRR 824
Cdd:TIGR04523  306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
PTZ00121 PTZ00121
MAEBL; Provisional
482-1017 3.86e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  482 IREIEELR-----TKLLESEAMNESLRRSlsrASARSPYSLGASPAAPAFGGSPASSMEDASEV-----IRRA--KQDLE 549
Cdd:PTZ00121 1229 VKKAEEAKkdaeeAKKAEEERNNEEIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKkkadeAKKAeeKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  550 RLKKKEVRQRRKSPEK---EAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPE 626
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  627 EKEVNFQADLADLTCEiEIKQKlIDEL---ENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTmECYTEEKA 703
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAE-EDKKK-ADELkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEA 1462
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  704 NKiKADYEKRLREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVAlmKQMREEQQRRRLVET 778
Cdd:PTZ00121 1463 KK-KAEEAKKADEAKKKAEEAKKADEakkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEA 1539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  779 KRNREIA---QLKK-EQRRQEFQIRALESQKRQQE---MVLRR----KTQEVSALRRLAKPMSERVAGRAGLKPPMLDSG 847
Cdd:PTZ00121 1540 KKAEEKKkadELKKaEELKKAEEKKKAEEAKKAEEdknMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  848 AEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKA---ARLKWQSLERRii 924
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEALKKE-- 1697
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  925 diVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEiEVLAANIDYINDGITDCQATIV 1004
Cdd:PTZ00121 1698 --AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIR 1774
                         570
                  ....*....|....*
gi 355390331 1005 QLEET--KEELDSTD 1017
Cdd:PTZ00121 1775 KEKEAviEEELDEED 1789
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
626-855 5.18e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 5.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   626 EEKEVNFQADLADLTCEIEIKQKLIDELEN-SQRRLQTL-------KHQYEEKLILLQNKIRDTQLERdrvlqnlstmec 697
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKrLEEIEQLLeelnkkiKDLGEEEQLRVKEKIGELEAEI------------ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   698 yteEKANKIKADYEKRLREMNRDLQKLQAaqkEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVE 777
Cdd:TIGR02169  304 ---ASLERSIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 355390331   778 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTT 855
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
724-1024 1.13e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.84  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  724 LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRRLVETkrNREIAQLKKEQRRQEFQIRALES 803
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAAL--ARRIRALEQELAALEAELAELEK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  804 QKRQQEMVLRRKTQEVSalRRLakpmseRVAGRAGLKPPMLdsgaevsasttsseaesgarsvssivrqwnrkinhFLgd 883
Cdd:COG4942    91 EIAELRAELEAQKEELA--ELL------RALYRLGRQPPLA-----------------------------------LL-- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  884 hpaptvngtrparkkFQKKGASQSFSKAARLKwQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRER 963
Cdd:COG4942   126 ---------------LSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355390331  964 LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISS 1024
Cdd:COG4942   190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
649-827 1.25e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  649 LIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKLQAAQ 728
Cdd:COG4372    25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL--------EQARSELEQLEEELEELNEQLQAAQAEL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  729 KEHARLLKnqsRYERELKKLQAEVAEMKKAKVALM---KQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALEsqK 805
Cdd:COG4372    97 AQAQEELE---SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE--Q 171
                         170       180
                  ....*....|....*....|..
gi 355390331  806 RQQEMVLRRKTQEVSALRRLAK 827
Cdd:COG4372   172 ELQALSEAEAEQALDELLKEAN 193
PRK12704 PRK12704
phosphodiesterase; Provisional
673-818 1.28e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  673 LLQNKIRDTQLERDRVLQNLST-MECYTEEK-------ANKIKADYEKRLREMNRDLQKLQAaqkehaRLLKNQSRYERE 744
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKeAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEK------RLLQKEENLDRK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  745 LKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR------EIAQLKKEQRRQEfQIRALESQKRQQEMVLRRKTQE 818
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqeleRISGLTAEEAKEI-LLEKVEEEARHEAAVLIKEIEE 180
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
644-810 1.30e-06

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 50.92  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   644 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnkirdTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQK 723
Cdd:pfam14988   22 KLWNQYVQECEEIERRRQELASRYTQQTAELQ-----TQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   724 LQAA-----QKEHARLLKNQSRYERELKKLQA-EVAEMKKAKVALMKQMREEQQRRRLVETKRN--REIAQLKKEQRRQE 795
Cdd:pfam14988   97 VRAEtaekdREAHLQFLKEKALLEKQLQELRIlELGERATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQLI 176
                          170
                   ....*....|....*
gi 355390331   796 FQIRALESQKRQQEM 810
Cdd:pfam14988  177 QETQALEAIKSKLEN 191
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
643-831 1.51e-06

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 52.37  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   643 IEIKQ---KLIDELENSQRRLQTLKHQyeeklillQNKIRDTQLERDRVLQNLSTMECYTE----EKANKIKADyEKRLr 715
Cdd:pfam15742   62 AELKQaqqKLLDSTKMCSSLTAEWKHC--------QQKIRELELEVLKQAQSIKSQNSLQEklaqEKSRVADAE-EKIL- 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   716 emnrDLQKlqaaQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETK-----------RNREi 784
Cdd:pfam15742  132 ----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNvnelqqqvrslQDKE- 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 355390331   785 AQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSE 831
Cdd:pfam15742  203 AQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSS 249
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
650-804 1.61e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.08  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  650 IDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKaDYEKRLrEMNRDLQKLQAAQK 729
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQL-GNVRNNKEYEALQK 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355390331  730 EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQ 804
Cdd:COG1579    97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
PTZ00121 PTZ00121
MAEBL; Provisional
364-1029 2.03e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  364 ANRARNIKNKVVVNQDKTSQQI-SALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRvKAMQ 442
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  443 EAIDAINNRVTQLMSQEANLL--LAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNES------LRRSLSRASARSP 514
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeAKKKADAAKKKAE 1339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  515 YSLGASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEK---EAFKKRA----KLQQENSEETDENEA 587
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDEAKKKAeedkKKADELKKAAAAKKK 1419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  588 EEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQY 667
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  668 EEKLILLQNKIRDTQL---ERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERE 744
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAkkaEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  745 LKKLQAEVA-EMKKAKVALMKQMREEQQRRRLVETKRNREiAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALR 823
Cdd:PTZ00121 1578 MALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  824 RLAKPMSERVAGRAglkppmldSGAEVSASTTSSEAESGARSVSSIVRQwnrkinhflgdhpaptvngTRPARKKFQ-KK 902
Cdd:PTZ00121 1657 EENKIKAAEEAKKA--------EEDKKKAEEAKKAEEDEKKAAEALKKE-------------------AEEAKKAEElKK 1709
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  903 GASQSFSKAARLKWQSLERRIidivmqrmTIVNLEADMERLIKKREELFLLQE-----ALRRKRERLQAESPEEEKGL-- 975
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKI--------KAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAEEIRKEKEAvi 1781
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331  976 -QELAEEIEVLAANIDYINDGITDCQATIVQ--------LEETKEELDSTDTSVVISSCSLAE 1029
Cdd:PTZ00121 1782 eEELDEEDEKRRMEVDKKIKDIFDNFANIIEggkegnlvINDSKEMEDSAIKEVADSKNMQLE 1844
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
646-834 2.09e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   646 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLsTMECYTEEKANKIKADYEKRlREMNRDLQKLQ 725
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL-YQEEQERKERQKEREEAEKK-ARQRQELQQAR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   726 AAQKEHARLLKnqsryerelkklQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQefqiraLESQK 805
Cdd:pfam13868  242 EEQIELKERRL------------AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ------IEERE 303
                          170       180
                   ....*....|....*....|....*....
gi 355390331   806 RQQEMVLRRKTQEVSALRRLAKPMSERVA 834
Cdd:pfam13868  304 EQRAAEREEELEEGERLREEEAERRERIE 332
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
652-832 2.18e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 52.43  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   652 ELENSQRRLQTLKhqyEEKLILLQNKIRDT---QLER----DRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKL 724
Cdd:pfam17380  354 RQEERKRELERIR---QEEIAMEISRMRELerlQMERqqknERVRQEL--------EAARKVKILEEERQRKIQQQKVEM 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   725 QA--AQKEHAR---LLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKEQRRqefQIR 799
Cdd:pfam17380  423 EQirAEQEEARqreVRRLEEERAREMERVRLEEQE-RQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQRR---KIL 497
                          170       180       190
                   ....*....|....*....|....*....|...
gi 355390331   800 ALESQKRQQEMVlrrktQEVSALRRLAKPMSER 832
Cdd:pfam17380  498 EKELEERKQAMI-----EEERKRKLLEKEMEER 525
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
741-1062 2.72e-06

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: 52.37  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   741 YERELKKLQAEVAEM--------KKAKVALMKQMREEQQRRRLVETKR--NREIAQLKKEQRRQEFQIRALESQKRQQEM 810
Cdd:TIGR02168  675 RRREIEELEEKIEELeekiaeleKALAELRKELEELEEELEQLRKELEelSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   811 VLRRKT-QEVSALRRLAKPMSERVAG---RAGLKPPMLDSGAEVSASttsseaESGARSVSSIVRQWNRKINhflgdhpa 886
Cdd:TIGR02168  755 ELTELEaEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKAL------REALDELRAELTLLNEEAA-------- 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   887 ptvngtrparkkfqkkgasqsfskAARLKWQSLERRIID----IVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRE 962
Cdd:TIGR02168  821 ------------------------NLRERLESLERRIAAterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   963 RLQAESPEEE-------KGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSvvISSCSLAEARLLLD 1035
Cdd:TIGR02168  877 ALLNERASLEealallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN--LQERLSEEYSLTLE 954
                          330       340
                   ....*....|....*....|....*..
gi 355390331  1036 NFLKASIDKGLQVAQKEAQIRLLEGRL 1062
Cdd:TIGR02168  955 EAEALENKIEDDEEEARRRLKRLENKI 981
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
656-837 3.14e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 52.05  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   656 SQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQK--EHAR 733
Cdd:pfam17380  285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERkrELER 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   734 LLKNQSRYE----RELKKLQ-----------AEVAEMKKAKV-------------ALMKQMREEQqrrrlvETKRNREIA 785
Cdd:pfam17380  365 IRQEEIAMEisrmRELERLQmerqqknervrQELEAARKVKIleeerqrkiqqqkVEMEQIRAEQ------EEARQREVR 438
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 355390331   786 QLKKEQRRQEFQIRaLESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRA 837
Cdd:pfam17380  439 RLEEERAREMERVR-LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
714-830 3.33e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.82  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  714 LREMNRDLQKLQAAQkehARLLKNQSRYERELKKLQAEVAEMKK-------------AKVALMKQMREEQQRRRLvetkr 780
Cdd:COG1842    32 IRDMEEDLVEARQAL---AQVIANQKRLERQLEELEAEAEKWEEkarlalekgredlAREALERKAELEAQAEAL----- 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 355390331  781 NREIAQLKKEQRRQEFQIRALESQ----KRQQEMVL-RRKTQEvsALRRLAKPMS 830
Cdd:COG1842   104 EAQLAQLEEQVEKLKEALRQLESKleelKAKKDTLKaRAKAAK--AQEKVNEALS 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
911-1112 4.14e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  911 AARLKWQSLERRIIDivmQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANID 990
Cdd:COG1196   229 LLLLKLRELEAELEE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  991 YINDGITDCQATIVQLEETKEELDSTDTSVVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGS 1070
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 355390331 1071 SQNHLLLDALREKAEAHPELQALIynvQQENGYASTDEEISE 1112
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEE 421
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
650-833 4.20e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  650 IDELENSQRRLQTLKHQY-----EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKL 724
Cdd:COG4913   264 YAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  725 QA----AQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQrrrlvetkrnrEIAQLKKEQRRQEFQIRA 800
Cdd:COG4913   344 EReierLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE-----------ALEEELEALEEALAEAEA 412
                         170       180       190
                  ....*....|....*....|....*....|...
gi 355390331  801 LESQKRQQemvLRRKTQEVSALRRLAKPMSERV 833
Cdd:COG4913   413 ALRDLRRE---LRELEAEIASLERRKSNIPARL 442
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
712-832 5.84e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  712 KRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK--AKVALMKQMREEQQRRRLVETKRNREIAQLKK 789
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 355390331  790 EQRRQEfQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 832
Cdd:COG4717   151 LEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
626-818 7.05e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.92  E-value: 7.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   626 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstMECYTEEKANK 705
Cdd:pfam13868   41 EERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV--ERIQEEDQAEA 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   706 IKADYEKR-----LREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRl 775
Cdd:pfam13868  119 EEKLEKQRqlreeIDEFNEEQAEWKELEKeeereEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ- 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 355390331   776 vETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQE 818
Cdd:pfam13868  198 -DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQ 239
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
719-1084 2.04e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 49.45  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   719 RDLQKLQAAQKEHARLLKNQSRYErELKKLQAEVAEMKKAKVALMKQMREEQQRRrlvetkrnreiaqlKKEQRRQEFQI 798
Cdd:pfam12128  228 RDIQAIAGIMKIRPEFTKLQQEFN-TLESAELRLSHLHFGYKSDETLIASRQEER--------------QETSAELNQLL 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   799 RALESQKRQqemVLRRKTQEVSALR-RLAKPMSERVAGRAGLKPpMLDSGAEvsasTTSSEAESgARSVSSIVRQWNRKI 877
Cdd:pfam12128  293 RTLDDQWKE---KRDELNGELSAADaAVAKDRSELEALEDQHGA-FLDADIE----TAAADQEQ-LPSWQSELENLEERL 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   878 NHFLGDHpaptvngtRPARKKFQK---KGASQSFSKAARLKwQSLERriidivmQRMTIVNLEADMERLIKKreelflLQ 954
Cdd:pfam12128  364 KALTGKH--------QDVTAKYNRrrsKIKEQNNRDIAGIK-DKLAK-------IREARDRQLAVAEDDLQA------LE 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   955 EALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLL 1034
Cdd:pfam12128  422 SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRR 501
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 355390331  1035 DNFLkasidkglqVAQKEAQIRLLE--GRLRQTDMAGSSQNHLLLDALREKA 1084
Cdd:pfam12128  502 DQAS---------EALRQASRRLEErqSALDELELQLFPQAGTLLHFLRKEA 544
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
631-836 2.60e-05

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: 48.95  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   631 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNK---IRDTQLErdrvLQNLSTMECYTEEKANKIK 707
Cdd:pfam05483  402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeIHDLEIQ----LTAIKTSEEHYLKEVEDLK 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   708 ADYEK-RLR--EMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvETKRNREI 784
Cdd:pfam05483  478 TELEKeKLKniELTAHCDKLLLENKE---LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----EMNLRDEL 550
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331   785 AQLKKE--QRRQEFQIRALESQK--RQQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:pfam05483  551 ESVREEfiQKGDEVKCKLDKSEEnaRSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
631-805 2.74e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   631 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEE-KANKIKAD 709
Cdd:TIGR04523  479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKEN 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   710 YEKRLREMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreeqqrrrlveTKRNREIAQLKK 789
Cdd:TIGR04523  559 LEKEIDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----------SSLEKELEKAKK 624
                          170
                   ....*....|....*.
gi 355390331   790 EQRRQEFQIRALESQK 805
Cdd:TIGR04523  625 ENEKLSSIIKNIKSKK 640
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
717-827 3.62e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 45.26  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   717 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLKKE-QRRQE 795
Cdd:pfam03938    7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKE-------QELQKKEQElQQLQQ 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 355390331   796 FQIRALesQKRQQEMVLRRKTQEVSALRRLAK 827
Cdd:pfam03938   80 KAQQEL--QKKQQELLQPIQDKINKAIKEVAK 109
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
671-823 3.86e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.58  E-value: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   671 LILLQNKIRDTQLERDRVLQNLstmecytEEKANKIKADYE---KRLREMNRDLQKLQaaQKEHARLLKNQSRYERELKK 747
Cdd:pfam05557   11 LSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDresDRNQELQKRIRLLE--KREAEAEEALREQAELNRLK 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355390331   748 LQAEVAEMKKAKvalmKQMREEQQRRRLVETKRNrEIAQLKKEQRRQEFQIRALESQK---RQQEMVLRRKTQEVSALR 823
Cdd:pfam05557   82 KKYLEALNKKLN----EKESQLADAREVISCLKN-ELSELRRQIQRAELELQSTNSELeelQERLDLLKAKASEAEQLR 155
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
654-818 4.12e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.84  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  654 ENSQRRLQTLkHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyTE-EKANKIKADYEKRLREMNRDLQKLQAAQKEHA 732
Cdd:COG1579     3 PEDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALE--ARlEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  733 RLLkNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-----EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQ 807
Cdd:COG1579    80 EQL-GNVRNNKEYEALQKEIESLKRRISDLEDEILElmeriEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
                         170
                  ....*....|.
gi 355390331  808 QEMVLRRKTQE 818
Cdd:COG1579   159 EELEAEREELA 169
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
378-827 4.36e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  378 QDKTSQQISALRAEIARLQMELMEYKAgkrvigedgAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMS 457
Cdd:COG4717    97 LEELEEELEELEAELEELREELEKLEK---------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  458 QEANlllakagdgneaigalIQNYIREIEELRTKLLESEAMN-ESLRRSLSRASARspyslgaspaapafggspassMED 536
Cdd:COG4717   168 LEAE----------------LAELQEELEELLEQLSLATEEElQDLAEELEELQQR---------------------LAE 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  537 ASEVIRRAKQDLERLKKKEvrqRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEE 616
Cdd:COG4717   211 LEEELEEAQEELEELEEEL---EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  617 SLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTME 696
Cdd:COG4717   288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  697 CYTEEKA--NKIKADYEKRLREMNRDLQKLQAAQKEHARLlknQSRYERELKKLQAEVAEMKKAkvALMKQMREEQQRRR 774
Cdd:COG4717   368 LEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEEL---EEQLEELLGELEELLEALDEE--ELEEELEELEEELE 442
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 355390331  775 LVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEvSALRRLAK 827
Cdd:COG4717   443 ELE----EELEELREELAELEAELEQLEEDGELAELLQELEELK-AELRELAE 490
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
701-823 4.55e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.52  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   701 EKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKakvalmKQMREEQQRRRLVETKR 780
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE---ELEEERRQAEEEAERLEQ------KRQEAEEEKERLEESAE 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 355390331   781 NREiaqlkKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALR 823
Cdd:pfam20492   73 MEA-----EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
369-1060 5.41e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.04  E-value: 5.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   369 NIKNKVVVNQDKTSQQIsALRAEIARLQMElmEYKAGKRVIgEDGAEGYSDLFRENAMLQKENGALRLrvkamqeaidaI 448
Cdd:pfam02463  131 SPEAYNFLVQGGKIEII-AMMKPERRLEIE--EEAAGSRLK-RKKKEALKKLIEETENLAELIIDLEE-----------L 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   449 NNRVTQLMSQEANLL-----LAKAGDGNEAIGALIQNYIRE--IEELRTKLLESEAMNESLRRSLSRA---SARSPYSLG 518
Cdd:pfam02463  196 KLQELKLKEQAKKALeyyqlKEKLELEEEYLLYLDYLKLNEerIDLLQELLRDEQEEIESSKQEIEKEeekLAQVLKENK 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   519 ASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESG 598
Cdd:pfam02463  276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   599 CEEEEGREDEDEDSGSEESLVDSDSdpeEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKI 678
Cdd:pfam02463  356 EEEEELEKLQEKLEQLEEELLAKKK---LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-EI 431
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   679 RDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKA 758
Cdd:pfam02463  432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   759 KVALMKQMR------EEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 832
Cdd:pfam02463  512 LLALIKDGVggriisAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   833 VAGRAGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINH-FLGDHPAPTVNGTRPARKKFQKKGASQSFSKA 911
Cdd:pfam02463  592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   912 ARLKWQSLErRIIDIVMQRMTIVNLEADME----RLIKKREELFLLQEALRRK---RERLQAESPEEEKGLQELAEEIEV 984
Cdd:pfam02463  672 TKELLEIQE-LQEKAESELAKEEILRRQLEikkkEQREKEELKKLKLEAEELLadrVQEAQDKINEELKLLKQKIDEEEE 750
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331   985 LAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEG 1060
Cdd:pfam02463  751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
700-989 5.84e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  700 EEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK---AKVALMKQMREEQQRRRLV 776
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEqlqAAQAELAQAQEELESLQEE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  777 ETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTS 856
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  857 SEAESGArsVSSIVRQWNRKINHFLGDHPAptvnGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNL 936
Cdd:COG4372   190 KEANRNA--EKEEELAEAEKLIESLPRELA----EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 355390331  937 EADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANI 989
Cdd:COG4372   264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
715-819 6.21e-05

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: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 47.64  E-value: 6.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   715 REMNRDL-QKLQAAQKEHARLLKNQSRYER-ELKKLQAEVAEMKKakvalmkQMREE----QQRR----RLVETKRNREI 784
Cdd:pfam15709  328 REQEKASrDRLRAERAEMRRLEVERKRREQeEQRRLQQEQLERAE-------KMREEleleQQRRfeeiRLRKQRLEEER 400
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 355390331   785 AQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEV 819
Cdd:pfam15709  401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL 435
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
646-826 7.25e-05

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: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 47.25  E-value: 7.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   646 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNlstmecyTEEKANKIKADYEK---------RLR- 715
Cdd:pfam15709  321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQE-------QLERAEKMREELELeqqrrfeeiRLRk 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   716 -------------EMNRDLQkLQAAQkEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR 782
Cdd:pfam15709  394 qrleeerqrqeeeERKQRLQ-LQAAQ-ERARQ--QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLM 469
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 355390331   783 EIAqlkkEQRRQEFQIRALESQ-KRQQEMVLRRKTQEVSAlrRLA 826
Cdd:pfam15709  470 EMA----EEERLEYQRQKQEAEeKARLEAEERRQKEEEAA--RLA 508
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
651-825 7.77e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 7.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  651 DELENSQRRLQTLKhqyeeklilLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYEKRLREMNRDLQKLQAAQKE 730
Cdd:COG3206   189 KELEEAEAALEEFR---------QKNGLVDLSEEAKLLLQQLSELE----SQLAEARAELAEAEARLAALRAQLGSGPDA 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  731 HARLLKNQ--SRYERELKKLQAEVAEMK-------------KAKVA-LMKQMREEQQrRRLVETKRNREIAQLKK---EQ 791
Cdd:COG3206   256 LPELLQSPviQQLRAQLAELEAELAELSarytpnhpdvialRAQIAaLRAQLQQEAQ-RILASLEAELEALQAREaslQA 334
                         170       180       190
                  ....*....|....*....|....*....|....
gi 355390331  792 RRQEFQIRALESQKRQQEmvLRRKTQEVSALRRL 825
Cdd:COG3206   335 QLAQLEARLAELPELEAE--LRRLEREVEVAREL 366
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1563-1600 1.08e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 1.08e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 355390331   1563 NFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
651-798 1.09e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  651 DELENSQRRLQTLKHQYEEKLILLQNKIRDTqlerDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK-LQAAQK 729
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEA----EKLKEEL-------EEKKEKLQEEEDKLLEEAEKEAQQaIKEAKK 584
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355390331  730 EHARLLknqsryeRELKKLQAEVAEMKKAKVAlmkqmreEQQRRRLVETKRNREIAQLKKEQRRQEFQI 798
Cdd:PRK00409  585 EADEII-------KELRQLQKGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKV 639
WD40 pfam00400
WD domain, G-beta repeat;
1286-1321 1.33e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 1.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 355390331  1286 QCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1321
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
645-788 1.52e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 45.78  E-value: 1.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    645 IKQKLIDELENSQRRLQTLKhQYEEKLILLQNKIRDTQ--LERD-RVLQNLstmecytEEKANKIKADYEKRLREmnrdl 721
Cdd:smart00787  145 LKEGLDENLEGLKEDYKLLM-KELELLNSIKPKLRDRKdaLEEElRQLKQL-------EDELEDCDPTELDRAKE----- 211
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331    722 qKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLK 788
Cdd:smart00787  212 -KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLK 277
PTZ00121 PTZ00121
MAEBL; Provisional
483-901 1.60e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  483 REIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDASEVIRRA--KQDLERLKKKEvrQRR 560
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAeeAKKADEAKKAE--EAK 1534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  561 KSPE-KEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADL 639
Cdd:PTZ00121 1535 KADEaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  640 TCEIEIKQKLIDELENSQRRLQTLKHQYEEKlillqnKIRDTQLERdrvlqnlstmecytEEKANKIKADYEKRLREmnR 719
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEE------KKKAEELKK--------------AEEENKIKAAEEAKKAE--E 1672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  720 DLQKLQAAQKEHarllKNQSRYERELKKLQAEvaemkKAKVALMKQMREEQQRR----RLVETKRNREIAQLKKEQrrqe 795
Cdd:PTZ00121 1673 DKKKAEEAKKAE----EDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKaeelKKAEEENKIKAEEAKKEA---- 1739
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  796 fqiralESQKRQQEMvLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAESGARSV---SSIVRQ 872
Cdd:PTZ00121 1740 ------EEDKKKAEE-AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFANIIE 1812
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 355390331  873 WNRKINHFLGDHP----------APTVNGTRPARKKFQK 901
Cdd:PTZ00121 1813 GGKEGNLVINDSKemedsaikevADSKNMQLEEADAFEK 1851
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1529-1560 1.73e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 40.37  E-value: 1.73e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 355390331   1529 NAHKDWVCALAFIPGRPMLLSACRAGVIKVWN 1560
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
277-796 1.84e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   277 SERLKRTGATGERAKEGISINCGLLALGNVISALGDQSK-KVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRdfm 355
Cdd:pfam02463  528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN--- 604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   356 eTLNTLKYANRARNIKNKVVVNQDKTSQQISALRAE-IARLQMELMEYKAGKRVIGEDGAEGYSDL--------FRENAM 426
Cdd:pfam02463  605 -LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKSEVKASLSeltkelleIQELQE 683
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   427 LQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSL 506
Cdd:pfam02463  684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   507 SRASARSPYSLGASpaapafggspassmEDASEVIRRAKQDLERLKKKEV---RQRRKSPEKEAFKKRAKLQQENSEETD 583
Cdd:pfam02463  764 EEKSELSLKEKELA--------------EEREKTEKLKVEEEKEEKLKAQeeeLRALEEELKEEAELLEEEQLLIEQEEK 829
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   584 ENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDpEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTL 663
Cdd:pfam02463  830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ-ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   664 KHQYEEKLILLQNKIrdtQLERDRVLQNLStmECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYER 743
Cdd:pfam02463  909 LNLLEEKENEIEERI---KEEAEILLKYEE--EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 355390331   744 ELKKLQAEVAEMKKAKvalMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEF 796
Cdd:pfam02463  984 EEKEERYNKDELEKER---LEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
543-1110 1.87e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   543 RAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEE--EEEERDESGCEEEEGREDEDedsgSEESLVD 620
Cdd:pfam02463  235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKklQEEELKLLAKEEEELKSELL----KLERRKV 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   621 SDSDPEEKEVNfqadladltcEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTE 700
Cdd:pfam02463  311 DDEEKLKESEK----------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   701 EKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKR 780
Cdd:pfam02463  381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   781 NREIAQLKKEqRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSAST--TSSE 858
Cdd:pfam02463  461 LKDELELKKS-EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlgVAVE 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   859 AESGARSVSSIVRQWNRKINHFLGDHpapTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQrmtiVNLEA 938
Cdd:pfam02463  540 NYKVAISTAVIVEVSATADEVEERQK---LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ----LDKAT 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   939 DMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDT 1018
Cdd:pfam02463  613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1019 SVVISSCSLAEARL---LLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSsqnhLLLDALREKAEAHPELQALIY 1095
Cdd:pfam02463  693 EILRRQLEIKKKEQrekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE----EEEEEEKSRLKKEEKEEEKSE 768
                          570
                   ....*....|....*
gi 355390331  1096 NVQQENGYASTDEEI 1110
Cdd:pfam02463  769 LSLKEKELAEEREKT 783
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
626-836 2.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  626 EEKEVNFQADLAdltceieikQKLIDELENSQRRLQTLKHQYEeklILLQnkIRDTQLERDRVLQNLSTmecyteekank 705
Cdd:COG4913   219 EEPDTFEAADAL---------VEHFDDLERAHEALEDAREQIE---LLEP--IRELAERYAAARERLAE----------- 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  706 ikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRR--RLvetkrNRE 783
Cdd:COG4913   274 --LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleQL-----ERE 346
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 355390331  784 IAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:COG4913   347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
708-963 2.49e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  708 ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSR------YERELKKLQAEVAEMKKAKVALMK-QMREEQQRRRLVETKr 780
Cdd:COG4913   627 AEAEERLEALEAELDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDDLAAlEEQLEELEAELEELE- 705
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  781 nREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVS-ALRRLAKPMSERVAGRAglkppmldSGAEVSASTTSSEA 859
Cdd:COG4913   706 -EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAALGDA--------VERELRENLEERID 776
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  860 ESGARsVSSIVRQWNRKINHFLGDHPAPTVNGTRparkkfqkkgasqsfSKAARLKWQSLERRIIDIVmqrmtIVNLEAD 939
Cdd:COG4913   777 ALRAR-LNRAEEELERAMRAFNREWPAETADLDA---------------DLESLPEYLALLDRLEEDG-----LPEYEER 835
                         250       260
                  ....*....|....*....|....*.
gi 355390331  940 MERLIKKREELFL--LQEALRRKRER 963
Cdd:COG4913   836 FKELLNENSIEFVadLLSKLRRAIRE 861
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
717-827 2.67e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 43.29  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  717 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvetKRNREIAQLKKE--QRRQ 794
Cdd:COG2825    31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQ------KKERELQKKQQElqRKQQ 104
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 355390331  795 EFQiRALesQKRQQEMV--LRRKTQEvsALRRLAK 827
Cdd:COG2825   105 EAQ-QDL--QKRQQELLqpILEKIQK--AIKEVAK 134
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1284-1321 2.72e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.99  E-value: 2.72e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 355390331   1284 PLQCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1321
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
676-832 2.84e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   676 NKIRDTQLERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRyERELKKLQAEVAEM 755
Cdd:pfam13868   21 NKERDAQIAEKKRIKAEEKEE--ERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKL 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331   756 KKakvalmKQMREEQQRRRLVETKRNREiaqlKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 832
Cdd:pfam13868   98 QE------REQMDEIVERIQEEDQAEAE----EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
642-1110 3.28e-04

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 45.51  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   642 EIEIKQKLIDELENSQRRLQTLKHQYEEKLIL----LQNKIRdtqLERDRV-LQNLSTMECYTEEKANKIKADY------ 710
Cdd:pfam07111   54 ELEGSQALSQQAELISRQLQELRRLEEEVRLLretsLQQKMR---LEAQAMeLDALAVAEKAGQAEAEGLRAALagaemv 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   711 EKRLREMN-RDLQKLQAAQKEHARLLKNQsrYERELKKLQAEVAEMKKAKVALmkQMREEQQRRRLVETKRNREI--AQL 787
Cdd:pfam07111  131 RKNLEEGSqRELEEIQRLHQEQLSSLTQA--HEEALSSLTSKAEGLEKSLNSL--ETKRAGEAKQLAEAQKEAELlrKQL 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   788 KKEQRRQEFQIRALES-QKRQQEMVLRRKTQEVSALRR--LAKPMSERVAGRAGLKPPMLDSGAEVSAST--TSSEAESG 862
Cdd:pfam07111  207 SKTQEELEAQVTLVESlRKYVGEQVPPEVHSQTWELERqeLLDTMQHLQEDRADLQATVELLQVRVQSLThmLALQEEEL 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   863 ARSVS--------------SIVRQWNRKINHFLGDHPAP------TVNGTRPARKKFQKKGASQSFSKAarLKWQSLERR 922
Cdd:pfam07111  287 TRKIQpsdslepefpkkcrSLLNRWREKVFALMVQLKAQdlehrdSVKQLRGQVAELQEQVTSQSQEQA--ILQRALQDK 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   923 IIDIVMQRMTIVNLEADMERLikkreelfllQEAlrRKRERLQAESPEEEkglqelaeeievLAANIDYINDGITDCQAT 1002
Cdd:pfam07111  365 AAEVEVERMSAKGLQMELSRA----------QEA--RRRQQQQTASAEEQ------------LKFVVNAMSSTQIWLETT 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1003 IVQLEETKEELDStdtsvvisscslaearllLDNFLKASIDK-----GLqVAQKE--AQIRLLEGRLRQTDMAGSSQNHL 1075
Cdd:pfam07111  421 MTRVEQAVARIPS------------------LSNRLSYAVRKvhtikGL-MARKValAQLRQESCPPPPPAPPVDADLSL 481
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 355390331  1076 LLDALR-EKAEAHPELQALIYNVQQENGYASTDEEI 1110
Cdd:pfam07111  482 ELEQLReERNRLDAELQLSAHLIQQEVGRAREQGEA 517
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
643-814 3.29e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 42.59  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  643 IEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteekankikadyekRLREMNRDLQ 722
Cdd:COG2882    11 LDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAA----------------QLRNYQQFIA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  723 KLQAAQKEHARLLKN-QSRYERELKKLQaevaemkkakvalmkqmrEEQQRRRLVETKRNREIAQLKKEQRRQEfqiral 801
Cdd:COG2882    75 RLDEAIEQQQQQVAQaEQQVEQARQAWL------------------EARQERKALEKLKERRREEERQEENRRE------ 130
                         170
                  ....*....|...
gi 355390331  802 esQKRQQEMVLRR 814
Cdd:COG2882   131 --QKELDELASRR 141
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
642-813 3.65e-04

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: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.94  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   642 EIEIKQKLIDELENSQRR----LQTLKHQYEEKlillqnKIRDTQLERDRVLQnlstmECYTEEKANKIKADYEKRLREM 717
Cdd:pfam15709  367 QLERAEKMREELELEQQRrfeeIRLRKQRLEEE------RQRQEEEERKQRLQ-----LQAAQERARQQQEEFRRKLQEL 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   718 NRDLQKlQAAQKEHARllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnreiAQLKKEQRRQ--E 795
Cdd:pfam15709  436 QRKKQQ-EEAERAEAE--------KQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK----ARLEAEERRQkeE 502
                          170
                   ....*....|....*....
gi 355390331   796 FQIR-ALESQKRQQEMVLR 813
Cdd:pfam15709  503 EAARlALEEAMKQAQEQAR 521
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
644-809 4.09e-04

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 44.83  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   644 EIKQKLIDELENSQRRLQTL--KHQY-EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKI--KADYEKRLRemn 718
Cdd:pfam15066  318 EVLQKLKHTNRKQQMQIQDLqcSNLYlEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVIleKNDINKTLQ--- 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   719 rDLQKLQAAQKEHARllknQSRYERELkkLQAEVAEMKKAKVALMKQ-MREEQQRRRLVE---------TKRNREIAQLK 788
Cdd:pfam15066  395 -NLQEILANTQKHLQ----ESRKEKET--LQLELKKIKVNYVHLQERyITEMQQKNKSVSqclemdktlSKKEEEVERLQ 467
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 355390331   789 --------------------KEQRRQEFQIRALESQKRQQE 809
Cdd:pfam15066  468 qlkgelekattsaldllkreKETREQEFLSLQEEFQKHEKE 508
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
633-802 4.70e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.50  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   633 QADLADLTCEIEIKQKLIDELENSQ---RRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIkAD 709
Cdd:pfam07888  212 QDTITTLTQKLTTAHRKEAENEALLeelRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL-AD 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   710 YEKRLREMNRDLQK-----LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQ-----MREEQQRRRLVETK 779
Cdd:pfam07888  291 ASLALREGRARWAQeretlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELK 370
                          170       180
                   ....*....|....*....|....*...
gi 355390331   780 RNREIAQLKKEQRRQEFQ-----IRALE 802
Cdd:pfam07888  371 ASLRVAQKEKEQLQAEKQelleyIRQLE 398
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
708-836 4.72e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 43.51  E-value: 4.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   708 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEVAEM-KKAKVALMKQmrEEQQRRRLVETKRNRE-- 783
Cdd:pfam04012   21 EDPEKMLEQAIRDMQSeLVKARQALAQTIARQKQLERRLEQQTEQAKKLeEKAQAALTKG--NEELAREALAEKKSLEkq 98
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 355390331   784 --------------IAQLKKEQRRQEFQIRALESQKR-----------QQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:pfam04012   99 aealetqlaqqrsaVEQLRKQLAALETKIQQLKAKKNllkarlkaakaQEAVQTSLGSLSTSSATDSFERIEEKIEER 176
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
636-809 5.93e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   636 LADLTCEIEIKQKLIDELENS----QRRLQTLKHQYEEKLILL--------QNKIRDTQLERDRVLQNLSTMEcyteEKA 703
Cdd:TIGR04523  269 LSEKQKELEQNNKKIKELEKQlnqlKSEISDLNNQKEQDWNKElkselknqEKKLEEIQNQISQNNKIISQLN----EQI 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   704 NKIK-------ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLV 776
Cdd:TIGR04523  345 SQLKkeltnseSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 355390331   777 E----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQE 809
Cdd:TIGR04523  425 EkeierlketiIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
PRK12704 PRK12704
phosphodiesterase; Provisional
700-822 6.26e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  700 EEKANKIKADYEKRLREMNRDlqKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKaKValmkQMREEQQRRRLVE-T 778
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAIKKE--ALLEAKEE---IHKLRNEFEKELRERRNELQKLEK-RL----LQKEENLDRKLELlE 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 355390331  779 KRNREIAQLKK--EQRRQEFQIRALESQKRQQEMvlRRKTQEVSAL 822
Cdd:PRK12704  107 KREEELEKKEKelEQKQQELEKKEEELEELIEEQ--LQELERISGL 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
767-1116 6.41e-04

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: 44.67  E-value: 6.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   767 REEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKppMLDS 846
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER--QLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   847 GAEVSASTTSSEAESGARSVS--SIVRQWNRKINHfLGDHPAPTVngtrparkkfQKKGASQSfSKAARLkwqsleRRII 924
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEieQLLEELNKKIKD-LGEEEQLRV----------KEKIGELE-AEIASL------ERSI 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   925 DIVMQRM-----TIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDC 999
Cdd:TIGR02169  311 AEKERELedaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  1000 QATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQ----KEAQIRLLEGRLRQT--DMAGSSQN 1073
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEekedKALEIKKQEWKLEQLaaDLSKYEQE 470
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 355390331  1074 HL------------LLDALREKAEAHPELQALiynVQQENGYASTDEEISEFSEG 1116
Cdd:TIGR02169  471 LYdlkeeydrvekeLSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQG 522
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
379-819 6.81e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.33  E-value: 6.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   379 DKTSQQISALRAEIARLQMEL-----------MEYKAGKRVIGEDgaegySDLFRENAMLQKENGALRlrvKAMQEAIDA 447
Cdd:pfam05483  373 EKNEDQLKIITMELQKKSSELeemtkfknnkeVELEELKKILAED-----EKLLDEKKQFEKIAEELK---GKEQELIFL 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   448 INNRVTQLMSQEANLLLAKAGDgneaigaliQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPyslgaspaapafg 527
Cdd:pfam05483  445 LQAREKEIHDLEIQLTAIKTSE---------EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK------------- 502
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   528 gSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEafKKRAKLQQEnseetdeneaeeeeeERDESGCEEEEGRED 607
Cdd:pfam05483  503 -ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE--EKEMNLRDE---------------LESVREEFIQKGDEV 564
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   608 EDEDSGSEESLVDSDSDPEEKEVN---FQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLE 684
Cdd:pfam05483  565 KCKLDKSEENARSIEYEVLKKEKQmkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   685 RDRVLQNLSTMeCYTEEKANKIKADYEKRLREmnrDLQKLQAAQKEHARLLKNQSryerelKKLQAEVAEMkkakVALMK 764
Cdd:pfam05483  645 LASAKQKFEEI-IDNYQKEIEDKKISEEKLLE---EVEKAKAIADEAVKLQKEID------KRCQHKIAEM----VALME 710
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331   765 qmREEQQRRRLVEtKRNREIAQLKKEQRRQEFQIRALESQ--KRQQEMVLRRKTQEV 819
Cdd:pfam05483  711 --KHKHQYDKIIE-ERDSELGLYKNKEQEQSSAKAALEIElsNIKAELLSLKKQLEI 764
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
682-947 7.01e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.26  E-value: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  682 QLERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVA 761
Cdd:COG3064    38 EAEEERLAELEAKRQ--AEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  762 LMKQMREEQQRRRLVETKRN-----REIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:COG3064   116 AAEKEKAEEAKRKAEEEAKRkaeeeRKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADT 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  837 AGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKW 916
Cdd:COG3064   196 AAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275
                         250       260       270
                  ....*....|....*....|....*....|.
gi 355390331  917 QSLERRIIDIVMQRMTIVNLEADMERLIKKR 947
Cdd:COG3064   276 SGLVVVAAALAGLAAAAAGLVLDDSAALAAE 306
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
624-827 8.06e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  624 DPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEeklillqnKIRDTQLERDRVLQnlstmecyTEEKA 703
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVAS--------AEREI 670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  704 nkikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAkvalMKQMREEQQR-RRLVETKRNR 782
Cdd:COG4913   671 ----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDElQDRLEAAEDL 742
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 355390331  783 EIAQLKK--EQRRQEFQIRALESQKRQQemVLRRKTQEVSALRRLAK 827
Cdd:COG4913   743 ARLELRAllEERFAAALGDAVERELREN--LEERIDALRARLNRAEE 787
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
626-1016 8.88e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 8.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   626 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRlqtlkhqyeeklilLQNKIRDTQLERDRVLQNLSTME--------C 697
Cdd:pfam01576  544 EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR--------------LQQELDDLLVDLDHQRQLVSNLEkkqkkfdqM 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   698 YTEEKA-------NKIKADYEKRLRE-----MNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKKAKVALMKQ 765
Cdd:pfam01576  610 LAEEKAisaryaeERDRAEAEAREKEtralsLARALEEALEAKEE----------LERTNKQLRAEMEDLVSSKDDVGKN 679
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   766 MREEQQRRRLVETkrnrEIAQLKKEQRRQEFQIRALESQKRQQEMVLRR-KTQEVSALRRLAKPMSERvaGRAGLKppml 844
Cdd:pfam01576  680 VHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRLEVNMQAlKAQFERDLQARDEQGEEK--RRQLVK---- 749
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   845 dsgaEVSASTTSSEAESGARSVSSIVRqwnRKINHFLGDHPAPTvngtrparkKFQKKGASQSFSKAARLKWQ--SLERR 922
Cdd:pfam01576  750 ----QVRELEAELEDERKQRAQAVAAK---KKLELDLKELEAQI---------DAANKGREEAVKQLKKLQAQmkDLQRE 813
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   923 IIDIVMQRMTIVNLEADMERLIKKRE-ELFLLQEALR-RKRERLQAESPEEekglqELAEEIEVLAANIDYINDGITDCQ 1000
Cdd:pfam01576  814 LEEARASRDEILAQSKESEKKLKNLEaELLQLQEDLAaSERARRQAQQERD-----ELADEIASGASGKSALQDEKRRLE 888
                          410
                   ....*....|....*.
gi 355390331  1001 ATIVQLEETKEELDST 1016
Cdd:pfam01576  889 ARIAQLEEELEEEQSN 904
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
711-834 8.97e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  711 EKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKE 790
Cdd:COG1579    23 EHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEA-RIKKYEEQLGNVRNNKEYEALQKE 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 355390331  791 QRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 834
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
701-872 1.39e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.91  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   701 EKANKIKADYEKRLREMNRDLQKLQAAQK--EHARLLKNQSRYERELK-------KLQAEVAEMKKAKVALMKQMREEQQ 771
Cdd:TIGR02794   78 EEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKakqaaeaKAKAEAEAERKAKEEAAKQAEEEAK 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   772 RRRLVETKRNREIAQLKKEQ------------RRQEFQIRALESQKRQQEMVLRRKTQEVSALRRL---AKPMSERVAGR 836
Cdd:TIGR02794  158 AKAAAEAKKKAEEAKKKAEAeakakaeaeakaKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAeaeRKADEAELGDI 237
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 355390331   837 AGLkppMLDSGAEVSASTTSSEAESGARSVSSIVRQ 872
Cdd:TIGR02794  238 FGL---ASGSNAEKQGGARGAAAGSEVDKYAAIIQQ 270
WD40 pfam00400
WD domain, G-beta repeat;
1564-1600 1.51e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 1.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 355390331  1564 FTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
644-832 1.63e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   644 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKIRDTQLERDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK 723
Cdd:TIGR00618  676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR-ELETHIEEYDREFNEI-------ENASSSLGSDLAAREDALNQSLKE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   724 LQAAQKEHARLLKNqsryERELKKLQAEVAEMKKAKVALMKQmrEEQQRRRLVETkRNREIAQLKKE---QRRQEFQIRA 800
Cdd:TIGR00618  748 LMHQARTVLKARTE----AHFNNNEEVTAALQTGAELSHLAA--EIQFFNRLREE-DTHLLKTLEAEigqEIPSDEDILN 820
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 355390331   801 LESQKRQQEM-----VLRRKTQEVSALRRLAKPMSER 832
Cdd:TIGR00618  821 LQCETLVQEEeqflsRLEEKSATLGEITHQLLKYEEC 857
Caldesmon pfam02029
Caldesmon;
535-847 1.71e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   535 EDASEVIRRAKQDLERLKKKE-----VRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDED 609
Cdd:pfam02029    6 EAARERRRRAREERRRQKEEEepsgqVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALER 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   610 EDSGSEESLVDSDSDPEEKEVNFQADLADLT---------CEIEIKQKLIDELENSQRRLQTLKHQYEEKLillqNKIRD 680
Cdd:pfam02029   86 QKEFDPTIADEKESVAERKENNEEEENSSWEkeekrdsrlGRYKEEETEIREKEYQENKWSTEVRQAEEEG----EEEED 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   681 TQLERDRVLQNLSTMECYTEEKANKIKADYEKRL----REMNRDLQKLQAAQ--------KEHARLLKNQSRYERELKKL 748
Cdd:pfam02029  162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKvfldQKRGHPEVKSQNGEeevtklkvTTKRRQGGLSQSQEREEEAE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   749 QAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR--EIAQLKK--EQRRqefQIRALESQKRQQEMvLRRKTQEVSALRR 824
Cdd:pfam02029  242 VFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAelELEELKKkrEERR---KLLEEEEQRRKQEE-AERKLREEEEKRR 317
                          330       340
                   ....*....|....*....|...
gi 355390331   825 LAKPMSERVAGRAGLKPPMLDSG 847
Cdd:pfam02029  318 MKEEIERRRAEAAEKRQKLPEDS 340
WD40 pfam00400
WD domain, G-beta repeat;
1529-1560 1.73e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 1.73e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 355390331  1529 NAHKDWVCALAFIPGRPMLLSACRAGVIKVWN 1560
Cdd:pfam00400    8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
379-539 1.81e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  379 DKTSQQISALRAEIARLQMELME-----YKAGKRVIGED---GAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINN 450
Cdd:COG3883    68 DKLQAEIAEAEAEIEERREELGEraralYRSGGSVSYLDvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  451 RVTQLMSQEANL--LLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGG 528
Cdd:COG3883   148 KKAELEAKLAELeaLKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
                         170
                  ....*....|.
gi 355390331  529 SPASSMEDASE 539
Cdd:COG3883   228 AAAAAAAAAAA 238
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
714-842 2.49e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  714 LREMNRDLQKLQAaQKEHARLLKNQSRYEReLKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnREIAQLKKEQRR 793
Cdd:COG0542   413 LDELERRLEQLEI-EKEALKKEQDEASFER-LAELRDELAELEEELEALKARWEAEKELIEEIQELK-EELEQRYGKIPE 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  794 QEFQIRALESQKRQQEMVLR-------------RKT---------QEVSALRRLAKPMSERVAG---------------R 836
Cdd:COG0542   490 LEKELAELEEELAELAPLLReevteediaevvsRWTgipvgklleGEREKLLNLEEELHERVIGqdeaveavadairrsR 569

                  ....*.
gi 355390331  837 AGLKPP 842
Cdd:COG0542   570 AGLKDP 575
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
708-994 2.49e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   708 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEvaeMKKAKVALmKQMREEQqrRRLVETKRNreiaq 786
Cdd:pfam12128  596 AASEEELRERLDKAEEaLQSAREKQAAAEEQLVQANGELEKASRE---ETFARTAL-KNARLDL--RRLFDEKQS----- 664
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   787 lkkEQRRQEfqiRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRA-GLKPPMLDSGAEVSASTTSSEA------ 859
Cdd:pfam12128  665 ---EKDKKN---KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKrEARTEKQAYWQVVEGALDAQLAllkaai 738
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   860 ---ESGARSVSSIVRQWNRKinhflgDHPAPTVNGTRPARKKFQKKGASQSFSKAAR-----LKWQSLERRIIDIVMQRM 931
Cdd:pfam12128  739 aarRSGAKAELKALETWYKR------DLASLGVDPDVIAKLKREIRTLERKIERIAVrrqevLRYFDWYQETWLQRRPRL 812
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355390331   932 --TIVNLEADMERLikkREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYIND 994
Cdd:pfam12128  813 atQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
616-1012 2.49e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   616 ESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQT----LKHQYEEklilLQNKIRDTQLERDRVLQN 691
Cdd:pfam01576  646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQqveeMKTQLEE----LEDELQATEDAKLRLEVN 721
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   692 LSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAA----QKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMR 767
Cdd:pfam01576  722 MQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAEledeRKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLK 801
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   768 EEQqrrrlvetkrnreiAQLKKEQR--------RQEFQIRALESQKRQQ--EMVLRRKTQEVSALRRLAK-------PMS 830
Cdd:pfam01576  802 KLQ--------------AQMKDLQReleearasRDEILAQSKESEKKLKnlEAELLQLQEDLAASERARRqaqqerdELA 867
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   831 ERVAGRAGLKPPMLDSGAEVSASTTSSEAE-SGARSVSSIVRQWNRKINhflgdHPAPTVNGTRPARKKFQKK--GASQS 907
Cdd:pfam01576  868 DEIASGASGKSALQDEKRRLEARIAQLEEElEEEQSNTELLNDRLRKST-----LQVEQLTTELAAERSTSQKseSARQQ 942
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   908 F---SKAARLKWQSLERRIIDivMQRMTIVNLEADMERLikkreELFLLQEAlrrkRERLQAES--PEEEKGLQELAEEI 982
Cdd:pfam01576  943 LerqNKELKAKLQEMEGTVKS--KFKSSIAALEAKIAQL-----EEQLEQES----RERQAANKlvRRTEKKLKEVLLQV 1011
                          410       420       430
                   ....*....|....*....|....*....|....
gi 355390331   983 EVLAANIDYINDGITDCQATIV----QLEETKEE 1012
Cdd:pfam01576 1012 EDERRHADQYKDQAEKGNSRMKqlkrQLEEAEEE 1045
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
717-834 2.62e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.87  E-value: 2.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331    717 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQqrrrlvETKRNREIAQLKKEQRRQef 796
Cdd:smart00935    6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA------REKKEKELQKKVQEFQRK-- 77
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 355390331    797 qiraleSQKRQQEMVlRRKTQEVSALRRLAKPMSERVA 834
Cdd:smart00935   78 ------QQKLQQDLQ-KRQQEELQKILDKINKAIKEVA 108
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
644-773 2.75e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.50  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   644 EIKQKLIDELENSQRRLQTLKH-QYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA---NKIKADYEKRLRE-MN 718
Cdd:pfam10174  629 EMKKKGAQLLEEARRREDNLADnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghlTNLRAERRKQLEEiLE 708
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 355390331   719 RDLQKLQAAQKEH----ARLLKNQSRYerelKKLQAEVAEMKKAKVALMKQMREEQQRR 773
Cdd:pfam10174  709 MKQEALLAAISEKdaniALLELSSSKK----KKTQEEVMALKREKDRLVHQLKQQTQNR 763
PRK11281 PRK11281
mechanosensitive channel MscK;
625-817 3.08e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.21  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  625 PEEKEVNFQADLADLTCEIEIKQKL-IDELENSQRRLQTLKhQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA 703
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLLEAEDKLvQQDLEQTLALLDKID-RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  704 NKIKADY-----EKRLREMNRDLQKLQAAQKE-HARLLKNQSRYERelkkLQAEVAEMkkakvalmkQMREEQQRRRLVE 777
Cdd:PRK11281  115 RETLSTLslrqlESRLAQTLDQLQNAQNDLAEyNSQLVSLQTQPER----AQAALYAN---------SQRLQQIRNLLKG 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 355390331  778 TKRNREiaQLKKEQRRQ-EFQIRALESQKRQQEMVLRRKTQ 817
Cdd:PRK11281  182 GKVGGK--ALRPSQRVLlQAEQALLNAQNDLQRKSLEGNTQ 220
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
378-577 3.20e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  378 QDKTSQQISALRAEIARLQMELMEYKAGKRvigedgaegysDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLms 457
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEK-----------ALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  458 qeanlllakagdgneaigaliqnyIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDA 537
Cdd:COG4942    89 ------------------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 355390331  538 SEVIRRA----KQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQE 577
Cdd:COG4942   145 APARREQaeelRADLAELAALRAELEAERAELEALLAELEEERA 188
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
918-1100 3.25e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  918 SLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEAL--------RRKRERLQAESPEEEKGLQELAEEIEVLAANI 989
Cdd:COG4913   239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAELARLEAELERLEARL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  990 DYINDGITDCQATI-----VQLEETKEELDSTDTSvvisscsLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1064
Cdd:COG4913   319 DALREELDELEAQIrgnggDRLEQLEREIERLERE-------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 355390331 1065 TDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQE 1100
Cdd:COG4913   392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
615-824 3.32e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   615 EESLVDSDSDPEEKE---VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLK-------HQYEEKLILLQNKIRDTQLE 684
Cdd:pfam01576   74 EEILHELESRLEEEEersQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteakiKKLEEDILLLEDQNSKLSKE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   685 RDRVLQNLSTMECY---TEEKA---NKIK-------ADYEKRLREMNRDLQKLQAA-----------QKEHARL------ 734
Cdd:pfam01576  154 RKLLEERISEFTSNlaeEEEKAkslSKLKnkheamiSDLEERLKKEEKGRQELEKAkrklegestdlQEQIAELqaqiae 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   735 LKNQ-SRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKRNREIAQLKKEQRRQEF--QIRAL--------E 802
Cdd:pfam01576  234 LRAQlAKKEEELQAALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAEKQRRDLgeELEALkteledtlD 313
                          250       260
                   ....*....|....*....|..
gi 355390331   803 SQKRQQEMVLRRKtQEVSALRR 824
Cdd:pfam01576  314 TTAAQQELRSKRE-QEVTELKK 334
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
651-822 3.46e-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: 41.41  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  651 DELENSQRRLQ-TLKHQYEEklILLQNKirDTQLER-DRVLQNLS-TME---------------CYTEEKaNKIKADYEK 712
Cdd:cd16269    86 DEDQKFQKKLMeQLEEKKEE--FCKQNE--EASSKRcQALLQELSaPLEekisqgsysvpggyqLYLEDR-EKLVEKYRQ 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  713 RLR---EMNRDLQK-LQAAQKEHARLLK-NQSRYERELKKLqaevAEMKKAKVALMKQMREEQQRRRLVETKRNRE---- 783
Cdd:cd16269   161 VPRkgvKAEEVLQEfLQSKEAEAEAILQaDQALTEKEKEIE----AERAKAEAAEQERKLLEEQQRELEQKLEDQErsye 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 355390331  784 --IAQLKKE-----QRRQEFQIRALESQKRQQEMVLRRKTQEVSAL 822
Cdd:cd16269   237 ehLRQLKEKmeeerENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
712-842 3.72e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  712 KRLREMNRDLQKLQAAQKEHARL--LKNQSRY---ERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVEtkrnREIAQ 786
Cdd:COG4913   252 ELLEPIRELAERYAAARERLAELeyLRAALRLwfaQRRLELLEAELEELRAELARLEAELERLEARLDALR----EELDE 327
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331  787 LKKEQRRQEFQ-IRALESQKRQQEMVLRRKTQEVSALRRLAKpmservagRAGLKPP 842
Cdd:COG4913   328 LEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLA--------ALGLPLP 376
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
722-808 3.79e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 40.30  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   722 QKLQAAQKEHARL-LKN---QSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRR--------------------LVE 777
Cdd:pfam06391   68 KKIEQYEKENKDLiLKNkmkLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKekakqelidelmtsnkdaeeIIA 147
                           90       100       110
                   ....*....|....*....|....*....|.
gi 355390331   778 TKRNReIAQLKKEQRRQEFQIRALESQKRQQ 808
Cdd:pfam06391  148 QHKKT-AKKRKSERRRKLEELNRVLEQKPTQ 177
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
919-1021 4.14e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  919 LERRIIDIVMQRMTIVNL--EADMERLIKKREELFLLQEALRRKRERLQAEspeeekglQELAEEIEVLAANIDYINDGI 996
Cdd:COG0542   416 LERRLEQLEIEKEALKKEqdEASFERLAELRDELAELEEELEALKARWEAE--------KELIEEIQELKEELEQRYGKI 487
                          90       100
                  ....*....|....*....|....*
gi 355390331  997 TDCQATIVQLEETKEELDSTDTSVV 1021
Cdd:COG0542   488 PELEKELAELEEELAELAPLLREEV 512
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
664-824 4.75e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 40.73  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   664 KHQYEEKLI-LLQNK----IRDTQLERDR----VLQNLST-ME---------------CYTEEKaNKIKADYEKRLREMN 718
Cdd:pfam02841   94 NQEFQKELVeLLEAKkddfLKQNEEASSKycsaLLQDLSEpLEekisqgtfskpggykLFLEER-DKLEAKYNQVPRKGV 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   719 RDLQKLQaaqkehaRLLKNQSRYERELkkLQAEvaemkKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQI 798
Cdd:pfam02841  173 KAEEVLQ-------EFLQSKEAVEEAI--LQTD-----QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQE 238
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 355390331   799 RALESQKRQ---------------QEMVLRRKTQEVSALRR 824
Cdd:pfam02841  239 RSYQEHVKQliekmeaereqllaeQERMLEHKLQEQEELLK 279
PRK11637 PRK11637
AmiB activator; Provisional
633-837 5.75e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  633 QADLADLTCEIEIKQKLIdeLENSQRR---LQTLKHQyEEKLILLQNKIRDTQlerdrvlQNLSTMEcyteekankikad 709
Cdd:PRK11637   46 RDQLKSIQQDIAAKEKSV--RQQQQQRaslLAQLKKQ-EEAISQASRKLRETQ-------NTLNQLN------------- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  710 yeKRLREMNRDLQKLQAAQKEHARLLKNQ----------------------SRYER-----------------ELKKLQA 750
Cdd:PRK11637  103 --KQIDELNASIAKLEQQQAAQERLLAAQldaafrqgehtglqlilsgeesQRGERilayfgylnqarqetiaELKQTRE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  751 EVAEMKKAKVAlmKQmreEQQRRRLVETKRnreiAQLKKEQRRQEFQ--IRALES--QKRQQEMVLRRktQEVSALR--- 823
Cdd:PRK11637  181 ELAAQKAELEE--KQ---SQQKTLLYEQQA----QQQKLEQARNERKktLTGLESslQKDQQQLSELR--ANESRLRdsi 249
                         250
                  ....*....|....*...
gi 355390331  824 ----RLAKPMSERVAGRA 837
Cdd:PRK11637  250 araeREAKARAEREAREA 267
WD40 pfam00400
WD domain, G-beta repeat;
1430-1471 6.62e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 6.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 355390331  1430 FQPVGKLTGHIGPVMCLTVTQTasqHDLVVTGSKDHYVKMFE 1471
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPD---GKLLASGSDDGTVKVWD 39
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
673-841 7.37e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.76  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   673 LLQNKIRDTQLERDRV-LQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKeHARLLKNQSRYERELKKLQAE 751
Cdd:pfam05262  186 LREDNEKGVNFRRDMTdLKERESQE--DAKRAQQLKEELDKKQIDADKAQQKADFAQD-NADKQRDEVRQKQQEAKNLPK 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   752 VAEMKKAKVAlmKQMREEQQR---RRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVL--RRKTQEVSA-LRRL 825
Cdd:pfam05262  263 PADTSSPKED--KQVAENQKReieKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELeaQKKREPVAEdLQKT 340
                          170       180
                   ....*....|....*....|.
gi 355390331   826 -----AKPMSERVAGRAGLKP 841
Cdd:pfam05262  341 kpqveAQPTSLNEDAIDSSNP 361
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
632-797 7.68e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.74  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  632 FQADLADLTCEIE----IKQKLIDEL----ENSQRRLQTLKHQYEEKLILLQNkiRDTQLERDRVLQNLST----MECYT 699
Cdd:cd00176    45 LEAELAAHEERVEalneLGEQLIEEGhpdaEEIQERLEELNQRWEELRELAEE--RRQRLEEALDLQQFFRdaddLEQWL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  700 EEKANKIKADyekrlrEMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALmkqmREEQQRRRLVETK 779
Cdd:cd00176   123 EEKEAALASE------DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD----ADEEIEEKLEELN 192
                         170
                  ....*....|....*...
gi 355390331  780 RNREIAQLKKEQRRQEFQ 797
Cdd:cd00176   193 ERWEELLELAEERQKKLE 210
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
710-815 8.61e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 39.69  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331   710 YEKRLREMNRDLQKLQAAQKEharllknQSRYERELKKLQAEVAEMK-----------KAKVALMKQMREEQQRRRLVET 778
Cdd:pfam13904   57 YENWLAAKQRQRQKELQAQKE-------EREKEEQEAELRKRLAKEKyqewlqrkarqQTKKREESHKQKAAESASKSLA 129
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 355390331   779 KRNREIAQ-----------LKKEQRRQEFQIRALESQKRQQEMVLRRK 815
Cdd:pfam13904  130 KPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
646-915 9.29e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.80  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  646 KQKLIDELENSQRRLQT----LKHQYEEKLILlqNKIRDTQLERDRVLQNLSTMECYTEEKANKIKA------------- 708
Cdd:PTZ00108  997 KEYLLGKLERELARLSNkvrfIKHVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAeeeegaeeddead 1074
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  709 ------------DYEKRLR--------EMNRDLQK-LQAAQKEHARLLKN--QSRYERELKKLQAEVAEMKKAKVALMKQ 765
Cdd:PTZ00108 1075 deddeeelgaavSYDYLLSmpiwsltkEKVEKLNAeLEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAK 1154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  766 MREEQQRRRLVETKRNREIAQLKKEQRRQefqirALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLD 845
Cdd:PTZ00108 1155 EQRLKSKTKGKASKLRKPKLKKKEKKKKK-----SSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDE 1229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355390331  846 SGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFSKAARLK 915
Cdd:PTZ00108 1230 EQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGkpknAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
PRK12705 PRK12705
hypothetical protein; Provisional
658-857 9.58e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  658 RRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQnlstmecyteEKANKIKADYEKRLREMNRDLQKLQaaqKEHARLLKN 737
Cdd:PRK12705   23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALL----------EAKELLLRERNQQRQEARREREELQ---REEERLVQK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331  738 QSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnREIAQLKKEQRRQEFqIRALESQKRQQemvlrrKTQ 817
Cdd:PRK12705   90 EEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNEL-YRVAGLTPEQARKLL-LKLLDAELEEE------KAQ 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 355390331  818 EVSALRRLAKPMSERVAgRAGLKPPMLDSGAEVSASTTSS 857
Cdd:PRK12705  162 RVKKIEEEADLEAERKA-QNILAQAMQRIASETASDLSVS 200
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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