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Conserved domains on  [gi|973353102|ref|NP_001305642|]
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kinesin-like protein KIFC3 isoform 7 [Homo sapiens]

Protein Classification

kinesin family protein( domain architecture ID 13526913)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to carboxy-terminal kinesins that contains a C-terminal domain responsible for the motor activity (it hydrolyzes ATP and binds microtubules)

CATH:  3.40.850.10
Gene Ontology:  GO:0007018|GO:0003777|GO:0005524|GO:0016887|GO:0005871
PubMed:  9368744|1618910|32842864
SCOP:  4004055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 304-628 0e+00

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: 523.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 304 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQD---EVQALVTSCIDGFN 379
Cdd:cd01366    1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDvfeEVSPLVQSALDGYN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 380 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 456
Cdd:cd01366   79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 457 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 536
Cdd:cd01366  159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 537 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 616
Cdd:cd01366  238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                        330
                 ....*....|..
gi 973353102 617 LKFAERVRSVEL 628
Cdd:cd01366  318 LRFASKVNSCEL 329
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-301 2.47e-13

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     3 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNL-------EVQQKTDRLAe 75
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALA------ELRKELEELEEELEQLRKELEELSRQISALRKdlarleaEVEQLEERIA- 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    76 velRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLK 155
Cdd:TIGR02168  751 ---QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   156 EMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 235
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353102   236 LRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELV 301
Cdd:TIGR02168  903 LRELESKRSELRRELE----ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
 
Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 304-628 0e+00

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: 523.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 304 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQD---EVQALVTSCIDGFN 379
Cdd:cd01366    1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDvfeEVSPLVQSALDGYN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 380 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 456
Cdd:cd01366   79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 457 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 536
Cdd:cd01366  159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 537 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 616
Cdd:cd01366  238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                        330
                 ....*....|..
gi 973353102 617 LKFAERVRSVEL 628
Cdd:cd01366  318 LRFASKVNSCEL 329
Kinesin pfam00225
Kinesin motor domain;
312-626 8.86e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 8.86e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  312 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDE----VQALVTSCIDGFNVCIFAY 385
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVyeetAKPLVESVLEGYNVTIFAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  386 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 465
Cdd:pfam00225  81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  466 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 542
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  543 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 620
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320


                  ....*.
gi 973353102  621 ERVRSV 626
Cdd:pfam00225 321 SRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 306-630 7.22e-141

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: 415.05  E-value: 7.22e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   306 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDE----VQALVTSCIDGF 378
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVfeetAAPLVDSVLEGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   379 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 458
Cdd:smart00129  80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   459 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 536
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   537 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 614
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316

                          330
                   ....*....|....*.
gi 973353102   615 YSLKFAERVRSVELGP 630
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
290-627 2.60e-78

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 260.83  E-value: 2.60e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 290 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDE--- 366
Cdd:COG5059    7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVyee 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 367 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 445
Cdd:COG5059   77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 446 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 525
Cdd:COG5059  157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 526 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 603
Cdd:COG5059  234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                        330       340
                 ....*....|....*....|....
gi 973353102 604 SPVEKNTSETLYSLKFAERVRSVE 627
Cdd:COG5059  314 SPSSNSFEETINTLKFASRAKSIK 337
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 307-627 3.62e-55

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 204.40  E-value: 3.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  307 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDEVQ----ALVTSCIDGFNVCI 382
Cdd:PLN03188  100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQlvgaPLVENCLAGFNSSV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  383 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLGKE 447
Cdd:PLN03188  170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLLDPS 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  448 pQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT- 524
Cdd:PLN03188  250 -QKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSSf 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  525 -TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKTL 598
Cdd:PLN03188  327 kTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLA 406

                         330       340
                  ....*....|....*....|....*....
gi 973353102  599 MVVQVSPVEKNTSETLYSLKFAERVRSVE 627
Cdd:PLN03188  407 MVCAISPSQSCKSETFSTLRFAQRAKAIK 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-301 2.47e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     3 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNL-------EVQQKTDRLAe 75
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALA------ELRKELEELEEELEQLRKELEELSRQISALRKdlarleaEVEQLEERIA- 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    76 velRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLK 155
Cdd:TIGR02168  751 ---QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   156 EMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 235
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353102   236 LRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELV 301
Cdd:TIGR02168  903 LRELESKRSELRRELE----ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-292 3.06e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRlkd 82
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELE------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--- 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  83 cLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQ 162
Cdd:COG1196  297 -LARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 163 SSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLT 240
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 973353102 241 NDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 292
Cdd:COG1196  449 EEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 10-282 5.79e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 53.20  E-value: 5.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    10 EMRRCEAELQELRTKpagpCPGCEHSQESA-----QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcL 84
Cdd:pfam15921  427 EVQRLEALLKAMKSE----CQGQMERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD-L 501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    85 AEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQARNQHLQEQVAMQRQVLKEMEQQLQS 163
Cdd:pfam15921  502 TASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   164 SHQLTA---RLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENLAGV----- 225
Cdd:pfam15921  574 MTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERLRAVkdikq 653

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353102   226 -RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 282
Cdd:pfam15921  654 eRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
3-288 9.43e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 9.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQELRTK--------PAGPCPGC-------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQ 67
Cdd:PRK02224 420 ERDELREREAELEATLRTARERveeaeallEAGKCPECgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  68 QKTDrLAEVELRLKDcLAEKAqeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV 147
Cdd:PRK02224 500 RAED-LVEAEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 148 AMQRQVLKEMEQQLQSSHQLTARLrAQIAMYESELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkA 217
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--E 650

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353102 218 VHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 288
Cdd:PRK02224 651 AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 5-112 4.74e-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: 42.70  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     5 ERLRQEMRRCEAELQELR--TKPAGPCPgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 82
Cdd:smart00787 175 PKLRDRKDALEEELRQLKqlEDELEDCD----PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSE 250

                           90       100       110
                   ....*....|....*....|....*....|.
gi 973353102    83 CLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 112
Cdd:smart00787 251 LNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 38-225 8.44e-04

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 41.14  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  38 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 111
Cdd:cd07627   30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 112 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 191
Cdd:cd07627  110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 973353102 192 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 225
Cdd:cd07627  181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
 
Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 304-628 0e+00

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: 523.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 304 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQD---EVQALVTSCIDGFN 379
Cdd:cd01366    1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDvfeEVSPLVQSALDGYN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 380 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 456
Cdd:cd01366   79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 457 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 536
Cdd:cd01366  159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 537 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 616
Cdd:cd01366  238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317

                        330
                 ....*....|..
gi 973353102 617 LKFAERVRSVEL 628
Cdd:cd01366  318 LRFASKVNSCEL 329
Kinesin pfam00225
Kinesin motor domain;
312-626 8.86e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 8.86e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  312 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDE----VQALVTSCIDGFNVCIFAY 385
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVyeetAKPLVESVLEGYNVTIFAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  386 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 465
Cdd:pfam00225  81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  466 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 542
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  543 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 620
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320


                  ....*.
gi 973353102  621 ERVRSV 626
Cdd:pfam00225 321 SRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 306-630 7.22e-141

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: 415.05  E-value: 7.22e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   306 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDE----VQALVTSCIDGF 378
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVfeetAAPLVDSVLEGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   379 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 458
Cdd:smart00129  80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   459 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 536
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   537 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 614
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316

                          330
                   ....*....|....*.
gi 973353102   615 YSLKFAERVRSVELGP 630
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 306-624 8.67e-122

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: 365.81  E-value: 8.67e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPvtKEDGEGPEATNAVTFDADDDSIIHL--LHKGKPVSFELDKVFSPQASQQD----EVQALVTSCIDGFN 379
Cdd:cd00106    1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEvyegTAKPLVDSALEGYN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 380 VCIFAYGQTGAGKTYTMEGTAEN-PGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 457
Cdd:cd00106   79 GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 458 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 535
Cdd:cd00106  157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 536 SERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 614
Cdd:cd00106  237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316

                        330
                 ....*....|
gi 973353102 615 YSLKFAERVR 624
Cdd:cd00106  317 STLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 306-626 6.84e-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: 319.79  E-value: 6.84e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVT-KEDGEGpeATNAVTFDADDDSIIhlLHKGK------PVSFELDKVFSPQASQQDEVQA----LVTSC 374
Cdd:cd01371    2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtarpLVDSV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 375 IDGFNVCIFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEK 451
Cdd:cd01371   78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 452 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 527
Cdd:cd01371  158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 528 LNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 606
Cdd:cd01371  235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314

                        330       340
                 ....*....|....*....|
gi 973353102 607 EKNTSETLYSLKFAERVRSV 626
Cdd:cd01371  315 DYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 307-627 1.58e-102

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: 316.58  E-value: 1.58e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 307 IRVIARVRPVT-KEDGEGPEatNAVTFDADDDSIIhllhKGKPVSFELDKVFSPQASQQ----DEVQALVTSCIDGFNVC 381
Cdd:cd01372    3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEevynTCVAPLVDGLFEGYNAT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 382 IFAYGQTGAGKTYTMEGTA------ENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIR 455
Cdd:cd01372   77 VLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 456 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 525
Cdd:cd01372  157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 526 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 602
Cdd:cd01372  237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316

                        330       340
                 ....*....|....*....|....*
gi 973353102 603 VSPVEKNTSETLYSLKFAERVRSVE 627
Cdd:cd01372  317 VSPADSNFEETLNTLKYANRARNIK 341
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 306-626 1.08e-91

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: 288.47  E-value: 1.08e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDADDDSIIHLL----------HKGKPVSFELDKVFSPQASQQD--- 365
Cdd:cd01370    1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEvye 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 366 -EVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLL 444
Cdd:cd01370   81 eTTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 445 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 523
Cdd:cd01370  161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 524 --TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 598
Cdd:cd01370  238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317

                        330       340
                 ....*....|....*....|....*...
gi 973353102 599 MVVQVSPVEKNTSETLYSLKFAERVRSV 626
Cdd:cd01370  318 MIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 306-626 1.39e-90

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: 285.00  E-value: 1.39e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVTKEDgegPEATNAVTFDADDDSIIHllHKGKPVSFELDKVFSPQASQQD----EVQALVTSCIDGFNVC 381
Cdd:cd01374    1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREvyelIAKPVVKSALEGYNGT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 382 IFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkASDWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 461
Cdd:cd01374   76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 462 GQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT---GKLNLVDLAGSER 538
Cdd:cd01374  152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvrvSTLNLIDLAGSER 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 539 VGKSGAEGSRLREAQHINKSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 616
Cdd:cd01374  232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311

                        330
                 ....*....|
gi 973353102 617 LKFAERVRSV 626
Cdd:cd01374  312 LKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 306-626 1.61e-90

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: 284.99  E-value: 1.61e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVTKEDGEGPeatNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDEVQALVTSCID----GFNVC 381
Cdd:cd01369    3 NIKVVCRFRPLNELEVLQG---SKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDdvlnGYNGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 382 IFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGkepQEKLEIRLCP 458
Cdd:cd01369   80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVHE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 459 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSER 538
Cdd:cd01369  157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 539 VGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSL 617
Cdd:cd01369  237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316


                 ....*....
gi 973353102 618 KFAERVRSV 626
Cdd:cd01369  317 RFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 306-626 1.05e-85

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: 273.43  E-value: 1.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVTKEDgegPEATNAVTFDADDDS----IIHLLHKGKPV--SFELDKVFSPQASQQDEVQALVTSCID--- 376
Cdd:cd01364    3 NIQVVVRCRPFNLRE---RKASSHSVVEVDPVRkevsVRTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCPILDevl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 377 -GFNVCIFAYGQTGAGKTYTMEG--------TAENP---GINQRALQLLFSEVQEkaSDWEYTITVSAAEIYNEVLRDLL 444
Cdd:cd01364   80 mGYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDplaGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 445 GKEPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG- 521
Cdd:cd01364  158 SPSSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDg 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 522 --LRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLM 599
Cdd:cd01364  238 eeLVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSI 317

                        330       340
                 ....*....|....*....|....*..
gi 973353102 600 VVQVSPVEKNTSETLYSLKFAERVRSV 626
Cdd:cd01364  318 IATISPASVNLEETLSTLEYAHRAKNI 344
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 305-626 2.24e-84

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: 269.99  E-value: 2.24e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 305 GNIRVIARVRPVTKEDGEGPeATNAVTFDADDDSIIHL--------LHKGKPVSFELDKVF-------SPQASQ----QD 365
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQeqvyED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 366 EVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASD-WEYTITVSAAEIYNEVLRDLL 444
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 445 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 519
Cdd:cd01365  160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 520 TGLRT--TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 589
Cdd:cd01365  238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 973353102 590 SLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 626
Cdd:cd01365  318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
290-627 2.60e-78

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 260.83  E-value: 2.60e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 290 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDE--- 366
Cdd:COG5059    7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVyee 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 367 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 445
Cdd:COG5059   77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 446 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 525
Cdd:COG5059  157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 526 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 603
Cdd:COG5059  234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                        330       340
                 ....*....|....*....|....
gi 973353102 604 SPVEKNTSETLYSLKFAERVRSVE 627
Cdd:COG5059  314 SPSSNSFEETINTLKFASRAKSIK 337
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 307-621 6.25e-76

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: 247.31  E-value: 6.25e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 307 IRVIARVRPVTKEDGEGPEA-------TNAVTFDADDDSIIHLLHKG---KPVSFELDKVFSPQASQ----QDEVQALVT 372
Cdd:cd01368    3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQkeffQGTALPLVQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 373 SCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkasdweYTITVSAAEIYNEVLRDLL----GKEP 448
Cdd:cd01368   83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 449 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 523
Cdd:cd01368  157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 524 ---TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 595
Cdd:cd01368  237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316

                        330       340
                 ....*....|....*....|....*.
gi 973353102 596 KTLMVVQVSPVEKNTSETLYSLKFAE 621
Cdd:cd01368  317 KASMIVNVNPCASDYDETLHVMKFSA 342
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 306-624 2.10e-75

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: 246.27  E-value: 2.10e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVTKEDGEGpEATNAVTFDADDDSIihlLHKGKPVSFELDKVFSPQASQQDEVQA----LVTSCIDGFNVC 381
Cdd:cd01373    2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSvgkpIVESCLSGYNGT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 382 IFAYGQTGAGKTYTMEGTAENP--------GINQRALQLLFSEVQ---EKASD-WEYTITVSAAEIYNEVLRDLLgkEP- 448
Cdd:cd01373   78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 449 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 525
Cdd:cd01373  156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 526 gKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 601
Cdd:cd01373  234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312

                        330       340
                 ....*....|....*....|...
gi 973353102 602 QVSPVEKNTSETLYSLKFAERVR 624
Cdd:cd01373  313 NVHPSSKCFGETLSTLRFAQRAK 335
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 307-624 2.58e-71

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


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 234.78  E-value: 2.58e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 307 IRVIARVRPVTKEDGEGpeatnaVTFDADDDSI-IHLL---------HKGKPVSFELDKVFSpQASQQDEVQAL----VT 372
Cdd:cd01375    2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLH-NASQELVYETVakdvVS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 373 SCIDGFNVCIFAYGQTGAGKTYTMEGTAEN---PGINQRALQLLFSEVQEKASDwEYTITVSAAEIYNEVLRDLLGKEPQ 449
Cdd:cd01375   75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 450 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 524
Cdd:cd01375  154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 525 TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 603
Cdd:cd01375  234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313

                        330       340
                 ....*....|....*....|.
gi 973353102 604 SPVEKNTSETLYSLKFAERVR 624
Cdd:cd01375  314 YGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 306-624 3.29e-71

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: 233.93  E-value: 3.29e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVtkEDGEGPEATNAVTFDADDDSII--HLLHKGKPVSFELDKVFSPQASQQD----EVQALVTSCIDGFN 379
Cdd:cd01376    1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDiyarEVQPIVPHLLEGQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 380 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKAsdWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 459
Cdd:cd01376   79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 460 GSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 538
Cdd:cd01376  154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 539 VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 618
Cdd:cd01376  234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313


                 ....*.
gi 973353102 619 FAERVR 624
Cdd:cd01376  314 FAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 306-623 4.71e-65

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: 217.93  E-value: 4.71e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 306 NIRVIARVRPVTKEDgEGPEATNAVTFDADDDSIIH-------LLHKGKPVSFELDKVFSPQASQQD----EVQALVTSC 374
Cdd:cd01367    1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETvyrsTVKPLVPHI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 375 IDGFNVCIFAYGQTGAGKTYTMEG----TAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLgkepQE 450
Cdd:cd01367   80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 451 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 530
Cdd:cd01367  156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 531 VDLAGSER-VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 608
Cdd:cd01367  233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312

                        330
                 ....*....|....*
gi 973353102 609 NTSETLYSLKFAERV 623
Cdd:cd01367  313 SCEHTLNTLRYADRV 327
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 307-627 3.62e-55

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 204.40  E-value: 3.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  307 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDEVQ----ALVTSCIDGFNVCI 382
Cdd:PLN03188  100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQlvgaPLVENCLAGFNSSV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  383 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLGKE 447
Cdd:PLN03188  170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLLDPS 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  448 pQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT- 524
Cdd:PLN03188  250 -QKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSSf 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  525 -TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKTL 598
Cdd:PLN03188  327 kTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLA 406

                         330       340
                  ....*....|....*....|....*....
gi 973353102  599 MVVQVSPVEKNTSETLYSLKFAERVRSVE 627
Cdd:PLN03188  407 MVCAISPSQSCKSETFSTLRFAQRAKAIK 435
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 286-444 8.06e-39

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 140.05  E-value: 8.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  286 YRRELQLRKKCHNELVRLKGNIRVIARVRPvtkedgegpEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQD 365
Cdd:pfam16796   1 LEEEETLRRKLENSIQELKGNIRVFARVRP---------ELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQED 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  366 ---EVQALVTSCIDGFNVCIFAYGQTGAGktytmegtaENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRD 442
Cdd:pfam16796  72 vfqEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142


                  ..
gi 973353102  443 LL 444
Cdd:pfam16796 143 LL 144
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 354-570 3.11e-20

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: 88.17  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 354 DKVFSPQASQQD---EVQALVTSCIDGFNV-CIFAYGQTGAGKTYTMEgtaenpGINQRALQLLFSEVQEKASDWEYTIT 429
Cdd:cd01363   23 YRGFRRSESQPHvfaIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 430 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfghTNRTTEfTNLNEHSSRSHALL 509
Cdd:cd01363   97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353102 510 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegsrlreaqhINKSLSALGDVIAALR 570
Cdd:cd01363  135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-301 2.47e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     3 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNL-------EVQQKTDRLAe 75
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALA------ELRKELEELEEELEQLRKELEELSRQISALRKdlarleaEVEQLEERIA- 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    76 velRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLK 155
Cdd:TIGR02168  751 ---QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   156 EMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 235
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353102   236 LRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELV 301
Cdd:TIGR02168  903 LRELESKRSELRRELE----ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-277 5.43e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 5.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    36 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA---QEEERLSRRLRDSHETIASLRAQs 112
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQ- 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   113 ppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT--------------ARLRAQIAMY 178
Cdd:TIGR02168  325 ------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   179 ESELER--AHGQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplL 256
Cdd:TIGR02168  399 NNEIERleARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----E 472

                          250       260
                   ....*....|....*....|.
gi 973353102   257 LQEALRSVKAEIGQAIEEVNS 277
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDS 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-307 2.42e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 2.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     8 RQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELRLkdclAEK 87
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL----ARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    88 AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQL 167
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   168 TARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK 247
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   248 RQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 307
Cdd:TIGR02168  887 EAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-292 3.06e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRlkd 82
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELE------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--- 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  83 cLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQ 162
Cdd:COG1196  297 -LARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 163 SSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLT 240
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 973353102 241 NDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 292
Cdd:COG1196  449 EEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-275 3.06e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQELRTkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD------RLAEV 76
Cdd:COG1196  254 ELEELEAELAELEAELEELRL---------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRREleerleELEEE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  77 ELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKE 156
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 157 MEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA--IEEAFARAQVEMKAVHENLAGVRTNLLTLQP 234
Cdd:COG1196  405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEaeLEEEEEALLELLAELLEEAALLEAALAELLE 484

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 973353102 235 ALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 275
Cdd:COG1196  485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
5-198 1.95e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 60.80  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   5 ERLRQEMRRCEAELQELRTKPAGPCPGCE---HSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE---- 77
Cdd:COG3206  185 PELRKELEEAEAALEEFRQKNGLVDLSEEaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspv 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  78 -LRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQARNQHLQEQVAMQRQVLK 155
Cdd:COG3206  265 iQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLA 337

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 973353102 156 EMEQQLQSshqlTARLRAQIAMYESELERAHGQMLEEMQSLEE 198
Cdd:COG3206  338 QLEARLAE----LPELEAELRRLEREVEVARELYESLLQRLEE 376
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-274 2.89e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     3 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKd 82
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELE-------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD- 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    83 claEKAQEEERLSRRLRDSHETIASLRAQsppVKYVIKTVEvESSKTKQALSESQARNQHLQEQvamQRQVLKEMEQQLQ 162
Cdd:TIGR02168  807 ---ELRAELTLLNEEAANLRERLESLERR---IAATERRLE-DLEEQIEELSEDIESLAAEIEE---LEELIEELESELE 876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   163 SSHQLTARLRAQIAMYESELErahgQMLEEMQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 242
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELE----ELSEELRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951

                          250       260       270
                   ....*....|....*....|....*....|...
gi 973353102   243 -YNGLKRQVRGFPLLLQEALRSVKaEIGQAIEE 274
Cdd:TIGR02168  952 tLEEAEALENKIEDDEEEARRRLK-RLENKIKE 983
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-250 3.16e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.47  E-value: 3.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     2 VENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaESKGMLSELNLEVQQKTDRLAEVELRLK 81
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLH------KLEEALNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLN 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    82 DCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEME 158
Cdd:TIGR02169  823 RLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   159 QQLQS---------SHQLTARLRAQIAMYE-SELERAHGQMLE--------------------EMQSLEEDKNRAIE--E 206
Cdd:TIGR02169  903 RKIEEleaqiekkrKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLAIQeyE 982

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 973353102   207 AFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 250
Cdd:TIGR02169  983 EVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-314 1.66e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  40 QLRDKLSQLQLEMAESKgmLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIaslraqsppvkyvi 119
Cdd:COG1196  217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEEL-------------- 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 120 ktvEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEED 199
Cdd:COG1196  280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 200 KN--RAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNS 277
Cdd:COG1196  357 EAelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAE 432

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 973353102 278 NNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVR 314
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 3-218 4.77e-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: 55.54  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 82
Cdd:COG4942   28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  83 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPP---------VKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 148
Cdd:COG4942   95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 149 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 218
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1-275 9.74e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    1 MVEN----ERLRQEMRRCEAELQELRtkpagpcPGCEHSQESAQLRDKLSQLQLemaeskgMLSELNLEVQQKTDRLAEV 76
Cdd:COG4913   230 LVEHfddlERAHEALEDAREQIELLE-------PIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   77 EL-RLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyviktvevessktkQALSESQARNQHLQEQVAMQRQVLK 155
Cdd:COG4913   296 ELeELRAELARLEAELERLEARLDALREELDELEA--------------------QIRGNGGDRLEQLEREIERLERELE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  156 EMEQQLQSSHQLTARLRAQIAMYESELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 235
Cdd:COG4913   356 ERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 973353102  236 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 275
Cdd:COG4913   421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
288-569 1.75e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 54.36  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 288 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDADDDSIihllhKGKPVSFELDKVFSPQA------ 361
Cdd:COG5059  289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQVNSSSDSSREIEeikfdl 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 362 -SQQDEVQALVTSCIDGFN----VCIFAYGQTGAGKTYTMEgtAENPGINQRALQLLFSEVQ-EKASDWEYTITVSAAEI 435
Cdd:COG5059  360 sEDRSEIEILVFREQSQLSqsslSGIFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQFLRI 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 436 Y----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvddinkvfEFGHTNRTTEFTNLNEHSSRSHall 509
Cdd:COG5059  438 EidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--------EKASKLRSSASTKLNLRSSRSH--- 506

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353102 510 ivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGSRLREAQHINKSLSALGDVIAAL 569
Cdd:COG5059  507 --SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 10-282 5.79e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 53.20  E-value: 5.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    10 EMRRCEAELQELRTKpagpCPGCEHSQESA-----QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcL 84
Cdd:pfam15921  427 EVQRLEALLKAMKSE----CQGQMERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD-L 501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    85 AEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQARNQHLQEQVAMQRQVLKEMEQQLQS 163
Cdd:pfam15921  502 TASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   164 SHQLTA---RLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENLAGV----- 225
Cdd:pfam15921  574 MTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERLRAVkdikq 653

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353102   226 -RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 282
Cdd:pfam15921  654 eRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
46-268 9.92e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 9.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  46 SQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK-----AQEEERLSRRLRDSHETIASLRAQSPPVKYVIK 120
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 121 TVEVESSKTKQALSESQA--RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSlEE 198
Cdd:COG3206  244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA-EL 322

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 199 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpLLLQEALRSVKAEI 268
Cdd:COG3206  323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVRV 390
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 12-274 1.36e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 51.71  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    12 RRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEE 91
Cdd:pfam01576  408 KKLEGQLQELQARLS------ESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEE 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    92 ER----LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARnqhlQEQVAMQRQVLKEMEQQLQS-SHQ 166
Cdd:pfam01576  481 TRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQReLEA 556

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   167 LTARLRAQIAMYEsELERAHGQMLEEMQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR----------- 226
Cdd:pfam01576  557 LTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaeareke 635

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 973353102   227 TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKAEIGQAIEE 274
Cdd:pfam01576  636 TRALSLARALEEALEAKEELERTNKQLRAEM-EDLVSSKDDVGKNVHE 682
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
39-316 2.93e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   39 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyv 118
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE------- 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  119 iktvevessktKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEE 198
Cdd:COG4913   677 -----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  199 DKNRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAI 272
Cdd:COG4913   746 ELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYL 818

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 973353102  273 EEVNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 316
Cdd:COG4913   819 ALLDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 70-284 3.64e-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: 50.44  E-value: 3.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    70 TDRLAEVELRLK--DCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYviKTVEVESSKTKQALSESQARNQHLQEQV 147
Cdd:TIGR02168  192 EDILNELERQLKslERQAEKAERYKELKAELRELELALLVLRLEELREEL--EELQEELKEAEEELEELTAELQELEEKL 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   148 AMQRQVLKEMEQQ-------LQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEmkavhE 220
Cdd:TIGR02168  270 EELRLEVSELEEEieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE-----E 344

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973353102   221 NLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQELLR 284
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIER 404
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
3-288 9.43e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 9.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQELRTK--------PAGPCPGC-------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQ 67
Cdd:PRK02224 420 ERDELREREAELEATLRTARERveeaeallEAGKCPECgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  68 QKTDrLAEVELRLKDcLAEKAqeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV 147
Cdd:PRK02224 500 RAED-LVEAEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 148 AMQRQVLKEMEQQLQSSHQLTARLrAQIAMYESELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkA 217
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--E 650

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353102 218 VHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 288
Cdd:PRK02224 651 AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
mukB PRK04863
chromosome partition protein MukB;
36-291 3.38e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.26  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   36 QESAQLRDKLSQL----QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE--RLSRRLRDshetiaslr 109
Cdd:PRK04863  417 QQAVQALERAKQLcglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAG--------- 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  110 aqsppvkyviktvEVESSKTKQALSE--SQARNQ-HLQEQVAMQRQVLKEMEQQLQSSHQLTARLR----AQIAMY--ES 180
Cdd:PRK04863  488 -------------EVSRSEAWDVAREllRRLREQrHLAEQLQQLRMRLSELEQRLRQQQRAERLLAefckRLGKNLddED 554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  181 ELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLAGVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPL 255
Cdd:PRK04863  555 ELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLAARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQ 634

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 973353102  256 LLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 291
Cdd:PRK04863  635 QLLERERELT----VERDELAARKQALDEEIERLSQ 666
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-276 6.10e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    5 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ--LEMAESKGMLSELNLEVQQKTDRLAEVEL---- 78
Cdd:COG4913   613 AALEAELAELEEELAEAEERLE------ALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   79 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQARNQHLQEQV--AM 149
Cdd:COG4913   687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  150 QRQVLKEMEQQLQSShqlTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 229
Cdd:COG4913   760 GDAVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 973353102  230 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 276
Cdd:COG4913   830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
39-293 1.39e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  39 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYV 118
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 119 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQsleE 198
Cdd:COG4372  103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE---A 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 199 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSN 278
Cdd:COG4372  180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259

                        250
                 ....*....|....*
gi 973353102 279 NQELLRKYRRELQLR 293
Cdd:COG4372  260 IEELELAILVEKDTE 274
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 5-312 1.39e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.49  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     5 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKgmlSELNLEVQQKT-------------- 70
Cdd:pfam15921  345 EELEKQLVLANSELTEARTERD------QFSQESGNLDDQLQKLLADLHKRE---KELSLEKEQNKrlwdrdtgnsitid 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    71 -------DRLAEVElRLKDCL-AEKAQEEERLSRRL------RDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSES 136
Cdd:pfam15921  416 hlrreldDRNMEVQ-RLEALLkAMKSECQGQMERQMaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   137 QARNQHLQEQvamqrqvLKEMEQQLQSSHQLTARLRAQIAMYESELE--RAHGQMLEEMQSLEE-------DKNRAIEea 207
Cdd:pfam15921  495 ERTVSDLTAS-------LQEKERAIEATNAEITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEalklqmaEKDKVIE-- 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   208 FARAQVE----MKAVHENLAGvrtnllTLQPALRTLTNDYNGLKRQVRGFPLLLQE---ALRSVKAEIG----QAIEEVN 276
Cdd:pfam15921  566 ILRQQIEnmtqLVGQHGRTAG------AMQVEKAQLEKEINDRRLELQEFKILKDKkdaKIRELEARVSdlelEKVKLVN 639

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 973353102   277 SNNQEL--LRKYRRE----LQLRKKCHNELVRLKGNIRVIAR 312
Cdd:pfam15921  640 AGSERLraVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKR 681
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-302 1.62e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   9 QEMRRCEAELQELRTKPAgpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 86
Cdd:COG4717   71 KELKELEEELKEAEEKEE----------EYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  87 KAQEEERLsRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQARNQhlQEQVAMQRQVLKEMEQQLQSSHQ 166
Cdd:COG4717  141 LAELPERL-EELEERLEELRELEEE------------------LEELEAELAELQ--EELEELLEQLSLATEEELQDLAE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 167 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGL 246
Cdd:COG4717  200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353102 247 KRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 302
Cdd:COG4717  279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-308 1.65e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   6 RLRQEMRRCEAELQELRtKPAGPCPGC------EH---------------SQESAQLRDKLSQLQLEMAESKGMLSELNL 64
Cdd:PRK03918 416 ELKKEIKELKKAIEELK-KAKGKCPVCgrelteEHrkelleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESE 494

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  65 EVQQKT--DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQH 142
Cdd:PRK03918 495 LIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIKLKGE-------IKSLKKELEKLEELKKKLAELEKK 564

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 143 LQEQVAMQRQVLKEMEQQ-LQSSHQLTARLRaqiamyesELERAHGQMLEEMQSleEDKNRAIEEAFARAQVEMKAVHEN 221
Cdd:PRK03918 565 LDELEEELAELLKELEELgFESVEELEERLK--------ELEPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEE 634

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 222 LAGVRTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVKAEIGQA---IEEVNSNNQEL------LRKYRRELQ 291
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELekrREEIKKTLEKLkeeleeREKAKKELE 714

                        330
                 ....*....|....*..
gi 973353102 292 LRKKCHNELVRLKGNIR 308
Cdd:PRK03918 715 KLEKALERVEELREKVK 731
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-212 1.88e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  36 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 108
Cdd:COG3883   30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 109 RAQSPP-----VKYViKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 183
Cdd:COG3883  110 GSESFSdfldrLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188

                        170       180
                 ....*....|....*....|....*....
gi 973353102 184 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 212
Cdd:COG3883  189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 35-299 2.63e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    35 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 112
Cdd:TIGR00606  583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   113 PPVKYVIKTVEVESS-------KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERa 185
Cdd:TIGR00606  663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   186 hgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALRT---LTNDYNGLKRqvrgfpllLQEALR 262
Cdd:TIGR00606  742 ---KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMER--------FQMELK 802

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 973353102   263 SVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 299
Cdd:TIGR00606  803 DVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
mukB PRK04863
chromosome partition protein MukB;
9-250 2.76e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    9 QEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELN-LEVQQKTDRLAEVELRLKDCLAEK 87
Cdd:PRK04863  837 AELRQLNRRRVELERALA------DHESQEQQQRSQLEQAKEGLSALNRLLPRLNlLADETLADRVEEIREQLDEAEEAK 910

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   88 A-----------------------QEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE-------VESSKTKQALSES- 136
Cdd:PRK04863  911 RfvqqhgnalaqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKNSDLNEKl 990

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  137 QARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyeseleRAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEM 215
Cdd:PRK04863  991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAEERARARR 1062

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 973353102  216 KAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 250
Cdd:PRK04863 1063 DELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 33-239 3.57e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  33 EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 112
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 113 PPVKYVIKTVEVESSKTKQAL-------SESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAmyesELERA 185
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA----ELEAL 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 973353102 186 HGQMLEEMQSLEEDKNRAiEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTL 239
Cdd:COG4942  180 LAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
46 PHA02562
endonuclease subunit; Provisional
 97-304 4.01e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.46  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  97 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQAR--------NQHLQEQVAMQRQVLK-EMEQQLQS 163
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDELLNlVMDIEDPS 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 164 SH-----QLTARLRAQIAMYESELE--RAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 231
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973353102 232 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 304
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
7-312 4.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   7 LRQEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC--- 83
Cdd:PRK03918 212 ISSELPELREELEKLE----------KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeek 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  84 ------LAEKAQEEERLSR-------RLRDSHETIASLRAQSPPVKYVIKTVEVESSK---TKQALSESQARNQHLQEQV 147
Cdd:PRK03918 282 vkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEERH 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 148 AMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE--- 214
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpv 440

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 215 -------------MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQE 281
Cdd:PRK03918 441 cgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLE 518

                        330       340       350
                 ....*....|....*....|....*....|.
gi 973353102 282 LLRKYRRELQLRKKchnELVRLKGNIRVIAR 312
Cdd:PRK03918 519 ELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 5-112 4.74e-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: 42.70  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     5 ERLRQEMRRCEAELQELR--TKPAGPCPgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 82
Cdd:smart00787 175 PKLRDRKDALEEELRQLKqlEDELEDCD----PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSE 250

                           90       100       110
                   ....*....|....*....|....*....|.
gi 973353102    83 CLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 112
Cdd:smart00787 251 LNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 2-214 4.88e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    2 VENERLRQEMRRCEAELQELRTkpagpcpgCEHSQESAQLR-DKLSQLQLEMaESKGMLSELNLEVQQKTDRLAEVELRL 80
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRK--------LEEAEKARQAEmDRQAAIYAEQ-ERMAMERERELERIRQEERKRELERIR 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   81 KDCLA---EKAQEEERL-------SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARN-QHLQEQVA- 148
Cdd:pfam17380 367 QEEIAmeiSRMRELERLqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAr 446

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973353102  149 -MQRQVLKEMEQQLQSS---HQLTARLRAQIAMYESELERAHGQMLEEM---QSLEEDKNRAIEEAFARAQVE 214
Cdd:pfam17380 447 eMERVRLEEQERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-310 5.94e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   85 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALsesqarnqhLQEQVAMQRQVLKEMEQQLQSS 164
Cdd:COG4913   244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  165 HQLTARLRAQIAMYESELERAHGQMLE----EMQSLEEDKNRaIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLT 240
Cdd:COG4913   315 EARLDALREELDELEAQIRGNGGDRLEqlerEIERLERELEE-RERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  241 NDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEvnsnnqellrkyRRELQlrkkchNELVRLKGNIRVI 310
Cdd:COG4913   394 EALEEELEA-------LEEALAEAEAALRDLRRE------------LRELE------AEIASLERRKSNI 438
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
41-235 6.73e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  41 LRDKLSQLQLEMAESKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 119
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 120 KTVEV--ESSKTKQALSESQARNQHLQEQVamqrQVLKEMEQQLQsshqltaRLRAQIAMYESELERAHGQ----MLEEM 193
Cdd:COG4717  126 QLLPLyqELEALEAELAELPERLEELEERL----EELRELEEELE-------ELEAELAELQEELEELLEQlslaTEEEL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 973353102 194 QSLEEDKNRA------IEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 235
Cdd:COG4717  195 QDLAEELEELqqrlaeLEEELEEAQEELEELEEELEQLENELEAAALE 242
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 38-225 8.44e-04

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 41.14  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  38 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 111
Cdd:cd07627   30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 112 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 191
Cdd:cd07627  110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 973353102 192 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 225
Cdd:cd07627  181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 15-250 9.33e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   15 EAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESK--------------GMLSELNL---------------- 64
Cdd:COG3096   835 EAELAALR-------------QRRSELERELAQHRAQEQQLRqqldqlkeqlqllnKLLPQANLladetladrleelree 901

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   65 ---------EVQQKTDRLAEVElRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVES-SKTKQALS 134
Cdd:COG3096   902 ldaaqeaqaFIQQHGKALAQLE-PLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSyEDAVGLLG 980

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  135 ESQARNQHLQEQ-VAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESelERAHGQMLEE-MQSLEEDKNRAIEEAFARAQ 212
Cdd:COG3096   981 ENSDLNEKLRARlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS--RDAKQQTLQElEQELEELGVQADAEAEERAR 1058

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 973353102  213 VEMKAVHENL---AGVRTNLLT-----------LQPALRTLTNDYNGLKRQV 250
Cdd:COG3096  1059 IRRDELHEELsqnRSRRSQLEKqltrceaemdsLQKRLRKAERDYKQEREQV 1110
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 8-295 1.35e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     8 RQEMRRCEAELQELRTKPAGPCpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE------LRLK 81
Cdd:TIGR00606  199 GQKVQEHQMELKYLKQYKEKAC----------EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlskiMKLD 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    82 D---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEME 158
Cdd:TIGR00606  269 NeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   159 QQL---QSSHQLTA-RLRAQIAMYESelERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMKAVHENLAGVRTN 228
Cdd:TIGR00606  343 TELlveQGRLQLQAdRHQEHIRARDS--LIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK 420

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353102   229 LLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQLRKK 295
Cdd:TIGR00606  421 ERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEK 492
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 2-228 1.46e-03

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: 41.65  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    2 VENERLRQEMRRcEAELQELRTKPAGPCPGCEH-SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRL 80
Cdd:pfam05557  14 LQNEKKQMELEH-KRARIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   81 KdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQARNQHLQEQVAMQRQVLKEMEQ- 159
Cdd:pfam05557  93 N----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQl 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353102  160 --QLQSSHQLTARLRAQIAMYESELErahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTN 228
Cdd:pfam05557 155 rqNLEKQQSSLAEAEQRIKELEFEIQ------SQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN 219
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 8-212 1.50e-03

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: 41.86  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    8 RQEMRRCEAELQElrtkpagpcpgcehsQESAQLRdKLSQLQLEMAESkgMLSELNLEVQQKTDRLAEVELRLKDclAEK 87
Cdd:pfam15709 342 RAEMRRLEVERKR---------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQ 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   88 AQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQA---RNQHLQEQVAMQRQVLKEMEQQlqss 164
Cdd:pfam15709 402 RQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAEE---- 474

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 973353102  165 hqltARLRAQIAMYESElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 212
Cdd:pfam15709 475 ----ERLEYQRQKQEAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-314 2.22e-03

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: 41.58  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   150 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVhENLAGVRTNl 229
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQ- 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   230 ltLQPALRTLTNDYNGLKRQVRGFPLLLQEALR---SVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGN 306
Cdd:TIGR02168  752 --LSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829


                   ....*...
gi 973353102   307 IRVIARVR 314
Cdd:TIGR02168  830 ERRIAATE 837
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
3-308 3.34e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   3 ENERLRQEMRRCEAELQelrtkpagpcpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVElrlkd 82
Cdd:COG4372   46 ELEQLREELEQAREELE--------------------QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  83 claekaQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQ 162
Cdd:COG4372  101 ------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 163 SshQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 242
Cdd:COG4372  175 A--LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353102 243 YNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIR 308
Cdd:COG4372  253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-206 3.36e-03

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: 40.87  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    33 EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLS 95
Cdd:pfam15921  580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLL 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    96 RRLRDSHETIASLRAQSPPVK--YVIKTVEVESSKTKQALSESQArnqhlQEQVAMQRQVLKEMEQQ--------LQSSH 165
Cdd:pfam15921  660 NEVKTSRNELNSLSEDYEVLKrnFRNKSEEMETTTNKLKMQLKSA-----QSELEQTRNTLKSMEGSdghamkvaMGMQK 734

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 973353102   166 QLTARlRAQIAMYESE---LERAHGQMLEEMQSLEEDKNRAIEE 206
Cdd:pfam15921  735 QITAK-RGQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQE 777
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 5-215 3.63e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 39.26  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   5 ERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQktdRLAEVELRLKDCL 84
Cdd:cd07596    7 EEAKDYILKLEEQLKKLSKQ----------AQRLVKRRRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  85 AEKAQEEERLSRR--------LRDSHETIASLRAqsppvkyVIKT-----VEVESSKtkQALSESQARNQHLQEQVAMQR 151
Cdd:cd07596   74 EELSSLSEAQANQelvkllepLKEYLRYCQAVKE-------TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKP 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353102 152 QVLKEMEQQLQSSHQLTARLRAqiamyesELERAHGQMLEEMQSLEEDKNRAIEEA---FARAQVEM 215
Cdd:cd07596  145 AKVEELEEELEEAESALEEARK-------RYEEISERLKEELKRFHEERARDLKAAlkeFARLQVQY 204
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 5-287 3.65e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   5 ERLRQEMRRCEAELQELRTKPAgpcpgcehSQESAQLRDKL----SQLQLEMAESKgmlselnlEVQQKTDRLAEVELRL 80
Cdd:PRK04778 259 QDLKEQIDENLALLEELDLDEA--------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPDFLEHA 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  81 KDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVesskTKQALSESQARNQHLQEQVAMQRQVLKEME-Q 159
Cdd:PRK04778 323 KEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDE----ITERIAEQEIAYSELQEELEEILKQLEEIEkE 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 160 QLQSSHQLtarlraqIAMYESELErAHgQMLEEMQSLEEDKNRAIE------------EAFARAQVEMKAVHENLAGVRT 227
Cdd:PRK04778 399 QEKLSEML-------QGLRKDELE-AR-EKLERYRNKLHEIKRYLEksnlpglpedylEMFFEVSDEIEALAEELEEKPI 469

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973353102 228 NLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRKYR 287
Cdd:PRK04778 470 NMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFREYD 534
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 15-292 3.90e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   15 EAELQEL-RTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRL---------AEVELR-LKDC 83
Cdd:pfam05483 334 EAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELeemtkfknnKEVELEeLKKI 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   84 LAEKA------QEEERLSRRLRDS-HETIASLRAQSPPVK------YVIKTVEVESSKTKQALsESQARNQHLQ--EQVA 148
Cdd:pfam05483 414 LAEDEklldekKQFEKIAEELKGKeQELIFLLQAREKEIHdleiqlTAIKTSEEHYLKEVEDL-KTELEKEKLKniELTA 492

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  149 MQRQVLKEMEQQLQSSHQLTARLRAQ---IAMYESELERahgqMLEEMQSLEE------DKNRAIEEAFARAQVEMKA-- 217
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHqedIINCKKQEER----MLKQIENLEEkemnlrDELESVREEFIQKGDEVKCkl 568

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353102  218 --VHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 292
Cdd:pfam05483 569 dkSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 6-160 3.92e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   6 RLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLA 85
Cdd:COG1579   21 RLEHRLKELPAELAELE-------------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  86 EK-----AQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARnqhLQEQVAMQRQVLKEMEQQ 160
Cdd:COG1579   88 NKeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 3-293 4.20e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    3 ENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESA-QLRDKLSQLQlemaESKGMLSELNLEVQQKTDRLAEVELRlk 81
Cdd:COG3096   376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiQYQQAVQALE----KARALCGLPDLTPENAEDYLAAFRAK-- 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   82 dclaEKAQEEERLS--RRLRDSHETIASLRAQSPPVKYVIKTVEVES--SKTKQALSesQARNQ-HLQEQVAMQRQVLKE 156
Cdd:COG3096   450 ----EQQATEEVLEleQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLR--RYRSQqALAQRLQQLRAQLAE 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  157 MEQQLQSSH-------QLTARLRAQIAMYEsELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNL 229
Cdd:COG3096   524 LEQRLRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQLEQLRARIKEL 597

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353102  230 LTLQPALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 293
Cdd:COG3096   598 AARAPAWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
PRK09039 PRK09039
peptidoglycan -binding protein;
59-183 4.31e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  59 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQA 138
Cdd:PRK09039  55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 973353102 139 RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 183
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
PRK09039 PRK09039
peptidoglycan -binding protein;
42-194 4.96e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.56  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  42 RDK-LSQLQLEMAESKGMLS-------ELNLEVQQKTDRLAEVEL---RLKDCLAEKAQEEERLSRRLRDSHETIASLRA 110
Cdd:PRK09039  51 KDSaLDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 111 QSppvkyviktvevessktkqalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML 190
Cdd:PRK09039 131 VS---------------------ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189


                 ....
gi 973353102 191 EEMQ 194
Cdd:PRK09039 190 QELN 193
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-223 5.07e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102     3 ENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRdkLSQLQLEMAESKgmlSELNLEVQqktdRLAEVELRLKD 82
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR--RDKLTEEYAELK---EELEDLRA----ELEEVDKEFAE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102    83 CLAEKAQEEERLS---RRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQ 159
Cdd:TIGR02169  383 TRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973353102   160 QLQSSHQLTARLRAQIAMYESELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 223
Cdd:TIGR02169  463 DLSKYEQELYDLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 41-276 6.37e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  41 LRDKLSQLQL---EMAESKGMLSELNL--EVQQKTDRLAEVELRLKDC-LAEKAQEEERLSRRLRDSHETIAslraqspp 114
Cdd:PRK04778 228 LPDQLQELKAgyrELVEEGYHLDHLDIekEIQDLKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDILE-------- 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 115 vKYVI--KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQ---- 188
Cdd:PRK04778 300 -REVKarKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQeiay 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 189 -MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTltndyngLKRQVR-----GFPLLLQEALR 262
Cdd:PRK04778 379 sELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHE-------IKRYLEksnlpGLPEDYLEMFF 451

                        250
                 ....*....|....
gi 973353102 263 SVKAEIGQAIEEVN 276
Cdd:PRK04778 452 EVSDEIEALAEELE 465
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-295 6.66e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   43 DKLSQLQLEMAESKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTV 122
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  123 EVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQsshqltaRLRAQIAMYESELERahgqmLEEMQSLEEDKNR 202
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-------RLKETIIKNNSEIKD-----LTNQDSVKELIIK 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  203 AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQEL 282
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK----ELEEKVKDLTKKISSLKEKIEKLESEK 533

                         250
                  ....*....|...
gi 973353102  283 LRKYRRELQLRKK 295
Cdd:TIGR04523 534 KEKESKISDLEDE 546
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
37-296 8.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  37 ESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSppvk 116
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 117 yviKTVEVESSKTKQALSESQARNQHL----------QEQVAMQRQVLKEMEQQLQSSHQlTARLRAQiaMYESELERAh 186
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE-ECRVAAQ--AHNEEAESL- 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102 187 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 266
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422

                        250       260       270
                 ....*....|....*....|....*....|..
gi 973353102 267 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 296
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 40-195 8.17e-03

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 39.28  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   40 QLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 119
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQ-------VRTLREEKERSVSQVQELETSLAELKNQAAVPPAEE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  120 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVlkemeqQLQSSHQLTaRLRAQIAMYESELERA----------HGQM 189
Cdd:pfam15070  74 EQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQA------QVQDNEQLS-RLNQEQEQRLLELERAaerwgeqaedRKQI 146


                  ....*.
gi 973353102  190 LEEMQS 195
Cdd:pfam15070 147 LEDMQS 152
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 33-289 8.64e-03

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: 39.35  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   33 EHSQESAQLRDKLSQLQ-------------------------LEMAESKGMLSELNLEVQ---QKTDRLAEVELRLKDCL 84
Cdd:pfam07111 328 EHRDSVKQLRGQVAELQeqvtsqsqeqailqralqdkaaeveVERMSAKGLQMELSRAQEarrRQQQQTASAEEQLKFVV 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102   85 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQH---------LQEQVAMQRQVLK 155
Cdd:pfam07111 408 NAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScpppppappVDADLSLELEQLR 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353102  156 EMEQQLQSSHQLTARLRAQiamyesELERAHGQMLEEMQSLEEDKNRaIEEAFARAQvemkavhENLAGVRTNLLTLQPA 235
Cdd:pfam07111 488 EERNRLDAELQLSAHLIQQ------EVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-------ESLASVGQQLEVARQG 553

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 973353102  236 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 289
Cdd:pfam07111 554 QQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
 
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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