|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
385-712 |
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: 534.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 385 KGNIRVIARVRPVTKedGEGPEATNAVTFDADDDSIIHLLHKG-KPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFN 463
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 464 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 540
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 541 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 620
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 621 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 700
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 973353098 701 LKFAERVRSVEL 712
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
393-710 |
4.28e-150 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 441.24 E-value: 4.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 393 RVRPVTKEDGEGPEATNAVTFDADDDSI--IHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVCIFAY 469
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 470 GQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 549
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 550 VPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 626
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 627 G-AEGSRLREAQHINKSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 704
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 973353098 705 ERVRSV 710
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
387-714 |
1.10e-143 |
|
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: 425.06 E-value: 1.10e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVTKEDGEGPEAtNAVTFDADDDSIIHLLHKGKPV---SFELDKVFSPQASQQDVFQEVQA-LVTSCIDGF 462
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 463 NVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 542
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 543 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 620
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 621 ERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 698
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 973353098 699 YSLKFAERVRSVELGP 714
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
387-708 |
2.53e-124 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 374.67 E-value: 2.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPvtKEDGEGPEATNAVTFDADDDSIIHL--LHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFN 463
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 464 VCIFAYGQTGAGKTYTMEGTAEN-PGINQRALQLLFSEVQE-KASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 541
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 542 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 619
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 620 SERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 698
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 973353098 699 YSLKFAERVR 708
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
387-710 |
1.15e-105 |
|
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: 326.73 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVT-KEDGEGpeATNAVTFDADDDSIIhlLHKGK------PVSFELDKVFSPQASQQDVFQE-VQALVTSC 458
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 459 IDGFNVCIFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEK 535
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 536 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 611
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 612 LNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 690
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 973353098 691 EKNTSETLYSLKFAERVRSV 710
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
388-711 |
5.47e-104 |
|
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: 322.74 E-value: 5.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 388 IRVIARVRPVT-KEDGEGPEatNAVTFDADDDSIIhllhKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 465
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 466 IFAYGQTGAGKTYTMEGTA------ENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIR 539
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 540 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 609
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 610 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 686
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 973353098 687 VSPVEKNTSETLYSLKFAERVRSVE 711
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
387-710 |
5.90e-94 |
|
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: 296.56 E-value: 5.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDADDDSIIHLL----------HKGKPVSFELDKVFSPQASQQDVFQ 449
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 450 E-VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLL 528
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 529 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 607
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 608 --TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 682
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 973353098 683 MVVQVSPVEKNTSETLYSLKFAERVRSV 710
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
387-710 |
2.22e-92 |
|
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: 291.54 E-value: 2.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVTKEDgegPEATNAVTFDADDDSIIHllHKGKPVSFELDKVFSPQASQQDVFQEV-QALVTSCIDGFNVC 465
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 466 IFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkASDWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 545
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 546 GQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT---GKLNLVDLAGSER 622
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvrvSTLNLIDLAGSER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 623 VGKSGAEGSRLREAQHINKSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 700
Cdd:cd01374 232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
330
....*....|
gi 973353098 701 LKFAERVRSV 710
Cdd:cd01374 312 LKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
387-710 |
1.47e-91 |
|
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: 289.61 E-value: 1.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVTKEDGEGPeatNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSCIDGFNVC 465
Cdd:cd01369 3 NIKVVCRFRPLNELEVLQG---SKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFaAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 466 IFAYGQTGAGKTYTMEGTAENP---GINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGkepQEKLEIRLCP 542
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 543 DGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSER 622
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 623 VGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSL 701
Cdd:cd01369 237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316
|
....*....
gi 973353098 702 KFAERVRSV 710
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
387-710 |
1.84e-87 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 279.98 E-value: 1.84e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVTKEDgegPEATNAVTFDADDDS----IIHLLHKGKPV--SFELDKVFSPQASQQDVFQEVQA-LVTSCI 459
Cdd:cd01364 3 NIQVVVRCRPFNLRE---RKASSHSVVEVDPVRkevsVRTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 460 DGFNVCIFAYGQTGAGKTYTMEG--------TAENP---GINQRALQLLFSEVQEkaSDWEYTITVSAAEIYNEVLRDLL 528
Cdd:cd01364 80 MGYNCTIFAYGQTGTGKTYTMEGdrspneeyTWELDplaGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 529 GKEPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG- 605
Cdd:cd01364 158 SPSSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 606 --LRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLM 683
Cdd:cd01364 238 eeLVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340
....*....|....*....|....*..
gi 973353098 684 VVQVSPVEKNTSETLYSLKFAERVRSV 710
Cdd:cd01364 318 IATISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
386-710 |
9.53e-87 |
|
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: 278.47 E-value: 9.53e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 386 GNIRVIARVRPVTKEDGEGPeATNAVTFDADDDSIIHL--------LHKGKPVSFELDKVF-------SPQASQQDVFQE 450
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 451 VQA-LVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASD-WEYTITVSAAEIYNEVLRDLL 528
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 529 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 603
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 604 TGLRT--TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 673
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 973353098 674 SLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 710
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
371-711 |
6.45e-79 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 264.29 E-value: 6.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 371 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdadDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQE 450
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 451 -VQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLG 529
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 530 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 609
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 610 GKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 687
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 973353098 688 SPVEKNTSETLYSLKFAERVRSVE 711
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
387-708 |
6.71e-78 |
|
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: 254.74 E-value: 6.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVTKEDGEGpEATNAVTFDADDDSIihlLHKGKPVSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVC 465
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 466 IFAYGQTGAGKTYTMEGTAENP--------GINQRALQLLFSEVQ---EKASD-WEYTITVSAAEIYNEVLRDLLgKEPQ 533
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL-DPAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 534 EKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTTg 610
Cdd:cd01373 157 RNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 611 KLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 686
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340
....*....|....*....|..
gi 973353098 687 VSPVEKNTSETLYSLKFAERVR 708
Cdd:cd01373 314 VHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
388-705 |
1.54e-77 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 253.47 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 388 IRVIARVRPVTKEDGEGPEA-------TNAVTFDADDDSIIHLLHKG---KPVSFELDKVFSPQASQQDVFQEV-QALVT 456
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 457 SCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEkasdweYTITVSAAEIYNEVLRDLL----GKEP 532
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 533 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 607
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 608 ---TTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 679
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 973353098 680 KTLMVVQVSPVEKNTSETLYSLKFAE 705
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
387-708 |
2.92e-72 |
|
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: 238.56 E-value: 2.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVtkEDGEGPEATNAVTFDADDDSII--HLLHKGKPVSFELDKVFSPQASQQDVF-QEVQALVTSCIDGFN 463
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 464 VCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKAsdWEYTITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 543
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 544 GSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 622
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 623 VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 702
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 973353098 703 FAERVR 708
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
388-708 |
2.96e-72 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 239.02 E-value: 2.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 388 IRVIARVRPVTKEDGEGpeatnaVTFDADDDSI-IHLL---------HKGKPVSFELDKVFSpQASQQDVFQEV-QALVT 456
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLH-NASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 457 SCIDGFNVCIFAYGQTGAGKTYTMEGTAEN---PGINQRALQLLFSEVQEKASDwEYTITVSAAEIYNEVLRDLLGKEPQ 533
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 534 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 608
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 609 TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 687
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 973353098 688 SPVEKNTSETLYSLKFAERVR 708
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
387-707 |
1.38e-66 |
|
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: 223.71 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 387 NIRVIARVRPVTKEDgEGPEATNAVTFDADDDSIIH-------LLHKGKPVSFELDKVFSPQASQQDVFQE-VQALVTSC 458
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 459 IDGFNVCIFAYGQTGAGKTYTMEG----TAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLgkepQE 534
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 535 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 614
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 615 VDLAGSER-VGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 692
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 973353098 693 NTSETLYSLKFAERV 707
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
388-711 |
1.03e-56 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 210.95 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 388 IRVIARVRPVTKeDGEGPEATNAVTFDAdddsiihLLHKGKpvSFELDKVFSPQASQQDVFQEVQA-LVTSCIDGFNVCI 466
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 467 FAYGQTGAGKTYTMEGTA----------ENPGINQRALQLLF---SEVQEKASDWE--YTITVSAAEIYNEVLRDLLGKE 531
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLLDPS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 532 pQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT- 608
Cdd:PLN03188 250 -QKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSSf 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 609 -TGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKTL 682
Cdd:PLN03188 327 kTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLA 406
|
330 340
....*....|....*....|....*....
gi 973353098 683 MVVQVSPVEKNTSETLYSLKFAERVRSVE 711
Cdd:PLN03188 407 MVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
367-528 |
8.12e-43 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 151.99 E-value: 8.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 367 YRRELQLRKKCHNELVRLKGNIRVIARVRPvtkedgegpEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQD 446
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRP---------ELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 447 VFQEVQALVTSCIDGFNVCIFAYGQTGAGktytmegtaENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRD 526
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 973353098 527 LL 528
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
435-654 |
1.76e-23 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 97.80 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 435 DKVFSPQASQQDVFQEVQALVTSCIDGFNV-CIFAYGQTGAGKTYTMEgtaenpGINQRALQLLFSEVQEKASDWEYTIT 513
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 514 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfghTNRTTEfTNLNEHSSRSHALL 593
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353098 594 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegsrlreaqhINKSLSALGDVIAALR 654
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-356 |
7.21e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 18 QLQEELVVLQ-ERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCE 96
Cdd:COG1196 217 ELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 97 AELQELRTkpagpcpGCEHSQE-SAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERL 175
Cdd:COG1196 295 AELARLEQ-------DIARLEErRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 176 SRRLRDSHETIaslraqsppvkyviktvevessktkQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQ 255
Cdd:COG1196 368 LEAEAELAEAE-------------------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 256 IAMYESELERAHGQMLEEMQSLEEDKNRA--IEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 333
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340
....*....|....*....|...
gi 973353098 334 FPLLLQEALRSVKAEIGQAIEEV 356
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-331 |
4.71e-13 |
|
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: 73.18 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 2 VLRMVEAMSQLQDEKTQLQEELVVLQERL-ALRD--SDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhr 78
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLdELSQelSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--------- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 79 DLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaESKGMLSELNLEVQQKTDRLAEVE 158
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLH------KLEEALNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 159 LRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVL 235
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 236 KEMEQQLQS---------SHQLTARLRAQIAMYE-SELERAHGQMLE--------------------EMQSLEEDKNRAI 285
Cdd:TIGR02169 899 RELERKIEEleaqiekkrKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLAI 978
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 973353098 286 E--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 331
Cdd:TIGR02169 979 QeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-295 |
2.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 11 QLQDEKTQLQEELVVLQERLALRDSDQQ---ATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENER 87
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 88 LRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 167
Cdd:COG1196 314 LEERLEELEEELAELE-------------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 168 KAQEEERLSRRLRDSHETIASLRAQsppvKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQ 247
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 973353098 248 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 295
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-355 |
3.72e-12 |
|
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: 70.09 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 43 QLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQL 122
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 123 RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLS----------RRLRDSHETIASLRAQ 192
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltllnEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 193 sppVKYVIKTVEvESSKTKQALSESQARNQHLQEQvamQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErahgQMLE 272
Cdd:TIGR02168 833 ---IAATERRLE-DLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELE----ELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 273 EMQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND-YNGLKRQVRGFPLLLQEALRSVKaEIGQ 351
Cdd:TIGR02168 902 ELRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLK-RLEN 979
|
....
gi 973353098 352 AIEE 355
Cdd:TIGR02168 980 KIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-268 |
6.71e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 2 VLRMVEA---MSQLQDEKTQLQEELVVLQERLALRDSDQQAT---STQLQNQVEHLKEKLISQAQEVSRlrselggtdLE 75
Cdd:TIGR02168 231 VLRLEELreeLEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISR---------LE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 76 KHRDLLMVENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 155
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLD------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 156 EVE---LRLKDCLAEKAQEE--------------ERLSRRLRDSHETIASLRAQspPVKYVIKTVEVESSKTKQALSESQ 218
Cdd:TIGR02168 376 ELEeqlETLRSKVAQLELQIaslnneierlearlERLEDRRERLQQEIEELLKK--LEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 973353098 219 ARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHG 268
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-293 |
1.50e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQ---ERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 83
Cdd:COG1196 246 AELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELN---LEVQQKTDRLAEVELR 160
Cdd:COG1196 324 ELAELEEELEELEEELEELE-------------EELEEAEEELEEAEAELAEAEEALLEAEaelAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 161 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQ 240
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 973353098 241 QLQSSHQLTARLRAQIAMYESELERAHGQ--MLEEMQSLEEDKNRAIEEAFARAQ 293
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-358 |
1.52e-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: 68.16 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 44 LQNQVEHLKEKlISQAQEVSRLRSELGgtdlEKHRDLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaqlr 123
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE-------------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 124 DKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKA---QEEERLSRRLRDSHETIASLRAQsppvkyvI 200
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQ-------L 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 201 KTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT--------------ARLRAQIAMYESELER- 265
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERl 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 266 -AHGQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRS 344
Cdd:TIGR02168 406 eARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDA 479
|
330
....*....|....
gi 973353098 345 VKAEIGQAIEEVNS 358
Cdd:TIGR02168 480 AERELAQLQARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-279 |
2.15e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.35 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 26 LQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMvenerlrQEMRRCEAELQELRTk 105
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-------QQLSELESQLAEARA- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 106 pagpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 183
Cdd:COG3206 234 ------------ELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 184 ETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSshqlTARLRAQIAMYESE 262
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLERE 359
|
250
....*....|....*..
gi 973353098 263 LERAHGQMLEEMQSLEE 279
Cdd:COG3206 360 VEVARELYESLLQRLEE 376
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
12-369 |
8.02e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 12 LQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLMVENERL 88
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDLG--NAEDFLEELREERDEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 89 RQEMRRCEAELQELRTK--------PAGPCPGC-------EHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDr 153
Cdd:PRK02224 425 REREAELEATLRTARERveeaeallEAGKCPECgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 154 LAEVELRLKDcLAEKAqeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQ 233
Cdd:PRK02224 504 LVEAEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 234 VLKEMEQQLQSSHQLTARLrAQIAMYESELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENL 303
Cdd:PRK02224 580 KLAELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDK 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353098 304 AGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 369
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-388 |
9.84e-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: 62.38 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 89 RQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEmaeskgmLSELNLEVQQKTDRLAEVELRLkdclAEK 168
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL----ARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 169 AQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQL 248
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 249 TARLRAQIAMYESELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK 328
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 329 RQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 388
Cdd:TIGR02168 887 EAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-366 |
2.77e-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: 60.85 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 10 SQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVENERLR 89
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL--EKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 90 QEMRRCEAELQELRtkpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdclaeka 169
Cdd:TIGR02169 272 QLLEELNKKIKDLG------------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI-------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 170 qeeERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLT 249
Cdd:TIGR02169 332 ---DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 250 ARLRAQIAMYESELERAHgqmlEEMQSLEEDKNrAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR 329
Cdd:TIGR02169 409 DRLQEELQRLSEELADLN----AAIAGIEAKIN-ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350
....*....|....*....|....*....|....*....
gi 973353098 330 QVRGfpllLQEALRSVKAEIGQAIEEVNSN--NQELLRK 366
Cdd:TIGR02169 484 ELSK----LQRELAEAEAQARASEERVRGGraVEEVLKA 518
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
369-653 |
3.59e-09 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 60.14 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 369 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDADDDSIihllhKGKPV------------SFELDK 436
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 437 VFSPQASQQDVFQEVQALVTSCIDGfnvcIFAYGQTGAGKTYTMEgtAENPGINQRALQLLFSEVQ-EKASDWEYTITVS 515
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 516 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvddinkvfEFGHTNRTTEFTNLNEHSSRS 589
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--------EKASKLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353098 590 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGSRLREAQHINKSLSALGDVIAAL 653
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-192 |
1.72e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQE-RLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMVEN 85
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL--DALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 86 --------ERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEV 157
Cdd:COG4913 333 rgnggdrlEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|....*
gi 973353098 158 ELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ 192
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
7-363 |
1.97e-08 |
|
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: 58.21 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERL--ALRDSDQ-QATSTQLQNQVE------HLKEKLISQAQEVS-RLRSELGGTDLEK 76
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELteARTERDQfSQESGNLDDQLQklladlHKREKELSLEKEQNkRLWDRDTGNSITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 77 hrDLLMVENERLRQEMRRCEAELQELRTKpagpCPGCEHSQESA-----QLRDKLSQLQLEMAESKGMLSELNLEVQQKT 151
Cdd:pfam15921 415 --DHLRRELDDRNMEVQRLEALLKAMKSE----CQGQMERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 152 DRLAEVELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQARNQHLQEQVAM 230
Cdd:pfam15921 489 MTLESSERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 231 QRQVLKEMEQQLQSSHQLTA---RLRAQIAMYESELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH--- 300
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGqhgRTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvn 639
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353098 301 ---ENLAGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 363
Cdd:pfam15921 640 agsERLRAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
9-393 |
1.43e-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: 55.12 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 9 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGT------DLEKHRDLLM 82
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTvsqlrsELREAKRMYE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 83 VENERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKgmlSELNLEVQQKT----------- 151
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERD------QFSQESGNLDDQLQKLLADLHKRE---KELSLEKEQNKrlwdrdtgnsi 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 152 ----------DRLAEVElRLKDCL-AEKAQEEERLSRRL------RDSHETIASLRAQSPPVKYVIKTVEVESSKTKQAL 214
Cdd:pfam15921 413 tidhlrreldDRNMEVQ-RLEALLkAMKSECQGQMERQMaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 215 SESQARNQHLQEQvamqrqvLKEMEQQLQSSHQLTARLRAQIAMYESELE--RAHGQMLEEMQSLEE-------DKNRAI 285
Cdd:pfam15921 492 ESSERTVSDLTAS-------LQEKERAIEATNAEITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEalklqmaEKDKVI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 286 EeaFARAQVE----MKAVHENLAGvrtnllTLQPALRTLTNDYNGLKRQVRGFPLLLQE---ALRSVKAEIG----QAIE 354
Cdd:pfam15921 565 E--ILRQQIEnmtqLVGQHGRTAG------AMQVEKAQLEKEINDRRLELQEFKILKDKkdaKIRELEARVSdlelEKVK 636
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 973353098 355 EVNSNNQEL--LRKYRRE----LQLRKKCHNELVRLKGNIRVIAR 393
Cdd:pfam15921 637 LVNAGSERLraVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKR 681
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-389 |
1.51e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 2 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRDSDQQA--TSTQLQNQVEHLKEKLisQAQEVSRLRSELggTDLEKHRD 79
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRL--TGLTPEKLEKEL--EELEKAKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 80 LLMVENERLRQEMRRCEAELQELRT------KPAGPCPGC------EH---------------SQESAQLRDKLSQLQLE 132
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKaieelkKAKGKCPVCgrelteEHrkelleeytaelkriEKELKEIEEKERKLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 133 MAESKGMLSELNLEVQQKT--DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIASLRAQsppvkyvIKTVEVESSKT 210
Cdd:PRK03918 482 LRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIKLKGE-------IKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 211 KQALSESQARNQHLQEQVAMQRQVLKEMEQQ-LQSSHQLTARLRaqiamyesELERAHGQMLEEMQSleEDKNRAIEEAF 289
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLK--------ELEPFYNEYLELKDA--EKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 290 ARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVKAEIGQA---IEEVNSNNQEL-- 363
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELekrREEIKKTLEKLke 701
|
410 420 430
....*....|....*....|....*....|
gi 973353098 364 ----LRKYRRELQLRKKCHNELVRLKGNIR 389
Cdd:PRK03918 702 eleeREKAKKELEKLEKALERVEELREKVK 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
84-299 |
1.71e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 ENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 163
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 164 CLAEKAQEEERLSRRLR-----DSHETIASLRAQSPP---------VKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 229
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 230 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 299
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
82-356 |
3.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 82 MVEN----ERLRQEMRRCEAELQELRtkpagpcPGCEHSQESAQLRDKLSQLQLemaeskgMLSELNLEVQQKTDRLAEV 157
Cdd:COG4913 230 LVEHfddlERAHEALEDAREQIELLE-------PIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 158 EL-RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqALSESQARNQHLQEQVAMQRQVLK 236
Cdd:COG4913 296 ELeELRAELARLEAELERLEARLDALREELDELEAQ--------------------IRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 237 EMEQQLQSSHQLTARLRAQIAMYESELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 316
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 973353098 317 LRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 356
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
4-372 |
5.75e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 4 RMVEAMSQlQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 83
Cdd:PRK04863 339 LVQTALRQ-QEKIERYQADLEELEERLE----EQNEVVEEADEQQEENEARAEAAEEEVDELKSQL--ADYQQALDVQQT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 ENERLRQEMRRCEaELQELRTKPAgpcpgcehsqesaqlrdklsqlqLEMAESKGMLSELNLEVQQKTDRLAEVELRLKD 163
Cdd:PRK04863 412 RAIQYQQAVQALE-RAKQLCGLPD-----------------------LTADNAEDWLEEFQAKEQEATEELLSLEQKLSV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 164 CLAEKAQEEERLsrrlrdshETIASLRAQSPPvkyviktvEVESSKTKQALSesQARNQ-HLQEQVAMQRQVLKEMEQQL 242
Cdd:PRK04863 468 AQAAHSQFEQAY--------QLVRKIAGEVSR--------SEAWDVARELLR--RLREQrHLAEQLQQLRMRLSELEQRL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 243 QSSHQLTARLR----AQIAMY--ESELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLAGVRTNLLTLQ 314
Cdd:PRK04863 530 RQQQRAERLLAefckRLGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLAARAPAWLAAQ 609
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353098 315 PA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 372
Cdd:PRK04863 610 DAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7-266 |
7.94e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrdllmvenE 86
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQEL----------------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 87 RLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQlQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdcLA 166
Cdd:COG4942 80 ALEAELAELEKEIAELR-------------AELEAQKEELAE-LLRALYRLGRQPPLALLLSPEDFLDAVRRLQY---LK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 167 EKAQEEERLSRRLRDSHETIASLRAQsppvkyviktVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSH 246
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAE----------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|
gi 973353098 247 QLTARLRAQIAMYESELERA 266
Cdd:COG4942 213 AELAELQQEAEELEALIARL 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-385 |
1.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 153 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQR 232
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 233 QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 310
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973353098 311 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 385
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
74-355 |
3.37e-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: 50.94 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 74 LEKHRDLLMVENERLRQEMR--------------RCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGM 139
Cdd:pfam01576 375 LEKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQARLS------ESERQRAELAEKLSKLQSELESVSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 140 LSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALS 215
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 216 ESQARnqhlQEQVAMQRQVLKEMEQQLQS-SHQLTARLRAQIAMYEsELERAHGQMLEEMQSL--EEDKNRAIEEAFARA 292
Cdd:pfam01576 528 DMKKK----LEEDAGTLEALEEGKKRLQReLEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvDLDHQRQLVSNLEKK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 293 Q-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKAEIGQAIE 354
Cdd:pfam01576 603 QkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQLRAEM-EDLVSSKDDVGKNVH 681
|
.
gi 973353098 355 E 355
Cdd:pfam01576 682 E 682
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
9-385 |
3.75e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.07 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 9 MSQLQDEKTQLQEELVVLQERLALRDSDQQATS------TQLQNQVEHLKEKL--ISQAQEVSRLRSElggtDLEKHRDL 80
Cdd:pfam05622 23 VSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 81 LMVENERLR---QEMRRCEAELQELRtkpagpcpgcehsqESAqlrDKLSQLQLEMAESKGMLSELN-LEVQQKTdrlae 156
Cdd:pfam05622 99 LQHRNEELTslaEEAQALKDEMDILR--------------ESS---DKVKKLEATVETYKKKLEDLGdLRRQVKL----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 157 velrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSE---SQARNQHLQ---EQVAM 230
Cdd:pfam05622 157 ----LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQkekERLII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 231 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELErAHGQMLEEMQSLEedknraIEEAFARAQVEMKAVHENLAGvrtNL 310
Cdd:pfam05622 233 ERDTLRETNEELRCAQLQQAELSQADALLSPSSD-PGDNLAAEIMPAE------IREKLIRLQHENKMLRLGQEG---SY 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973353098 311 LTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRsvkaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 385
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNRLANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-386 |
4.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 6 VEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEK------LISQAQEVSRLR---------SELG 70
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKVKELKELKekaeeyiklSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 71 GTDLEKHRDlLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNlEVQQK 150
Cdd:PRK03918 303 EEYLDELRE-IEKRLSRLEEEINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELYE-EAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 151 TDRLAEVELRLKDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTV-----EVESSKTKQALSESQARNQHL 224
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELkkaieELKKAKGKCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 225 QEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELER-----AHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAV 299
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 300 HENLAGVRTNLLTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHN 379
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
....*..
gi 973353098 380 ELVRLKG 386
Cdd:PRK03918 603 EYLELKD 609
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-393 |
7.27e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 52 KEKLISQAQEVSRLRSELGGTDLEKHR--DLLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsqesaQLRDKLSQL 129
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELE-----------------ELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 130 QLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEKAQEEERLSR-------RLRDSHETIASLRAQS 193
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 194 PPVKYVIKTVEVESSK---TKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAH--- 267
Cdd:PRK03918 324 NGIEERIKELEEKEERleeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeei 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 268 -------GQMLEEMQSLEEDKNRAIEEaFARAQVE----------------MKAVHENLAGVRTNLLTLQPALRTLTNDY 324
Cdd:PRK03918 404 eeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973353098 325 NGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKchnELVRLKGNIRVIAR 393
Cdd:PRK03918 483 RELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7-195 |
7.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLIS--QAQEVSRLRSELGGTDLEKH-RDLLMV 83
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAvRRLQYL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 E--NERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRL 161
Cdd:COG4942 142 KylAPARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|....
gi 973353098 162 KDCLAEKAQEEERLSRRLRDSHETIASLRAQSPP 195
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
120-397 |
9.64e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 120 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyv 199
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 200 iktvevessktKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEE 279
Cdd:COG4913 677 -----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 280 DKNRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAI 353
Cdd:COG4913 746 ELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYL 818
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 973353098 354 EEVNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 397
Cdd:COG4913 819 ALLDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
10-376 |
1.01e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 10 SQLQDEKTQLQEELVVLQERLALRDSDQQATSTQL---QNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENE 86
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 87 RLRQEmrrceaelqelrtkpagpcpgcehsqesaqlRDKLSQLQLEMAESKGMLSELNLEVQQktdrlaevelrLKDCLA 166
Cdd:TIGR04523 315 ELKNQ-------------------------------EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 167 EKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQssh 246
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 247 qltaRLRAQIAMYESELERahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNG 326
Cdd:TIGR04523 430 ----RLKETIIKNNSEIKD-----LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 973353098 327 LKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 376
Cdd:TIGR04523 501 LNEEKK----ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
3-287 |
1.37e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 3 LRMVEAMSQLQDEKTQLQEELVVLQERLALRDSdQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGG--TDLEKHRDL 80
Cdd:PLN02939 152 LQALEDLEKILTEKEALQGKINILEMRLSETDA-RIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLcvHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 81 LMVENERLRQEMRRCEAELQELrtkpagpcpgcehsqesAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELR 160
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEV-----------------AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 161 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEvESSKTKQALSESqarnqhlQEQVAMQRQVLKEMEQ 240
Cdd:PLN02939 294 QYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE-ASLKEANVSKFS-------SYKVELLQQKLKLLEE 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 973353098 241 QLQSSHQltaRLRAQIAMYESELERAHgqmlEEMQSL-EEDKNRAIEE 287
Cdd:PLN02939 366 RLQASDH---EIHSYIQLYQESIKEFQ----DTLSKLkEESKKRSLEH 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
11-374 |
1.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 11 QLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQN-----QVEHLKEKLISQAQEVSRLRSELggtdleKHRDLLMVEN 85
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 86 ERLRQEMRRCEAELQELRTKPAGpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLkdcl 165
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 166 aEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQARNQHLQEQVA 229
Cdd:COG4717 237 -EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 230 MQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEMKAVHENLAgvrt 308
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVEDEEELRAAL---- 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353098 309 nllTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 374
Cdd:COG4717 392 ---EQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10-298 |
2.18e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 10 SQLQDEKTQLQEELVVLQERLA---LRDSDQQATSTQLQNQ------VEHLKEKLISQAQEVSRLRSELggTDLEKHRDl 80
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGelkLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSEL--RQARKRRD- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 81 lmVENERLRQEMRRCE---AELQELRTKpAGPCPGCEH---SQESAQLRDKLSQL-QLEMAESKGMLSELNLEVQQKTDR 153
Cdd:pfam12128 503 --QASEALRQASRRLEerqSALDELELQ-LFPQAGTLLhflRKEAPDWEQSIGKViSPELLHRTDLDPEVWDGSVGGELN 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 154 LAEVELRLKDCLA-EKAQEEERLSRR-------LRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQAR----- 220
Cdd:pfam12128 580 LYGVKLDLKRIDVpEWAASEEELRERldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlf 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 221 NQHLQEQVAMQRQV---LKEMEQQLQS-SHQLTARLRAQIAMYES---ELERAHGQMLEEMQSLEEDKNRA---IEEAFA 290
Cdd:pfam12128 660 DEKQSEKDKKNKALaerKDSANERLNSlEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVVEGALDAQlalLKAAIA 739
|
....*...
gi 973353098 291 RAQVEMKA 298
Cdd:pfam12128 740 ARRSGAKA 747
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
15-295 |
3.77e-05 |
|
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: 47.04 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 15 EKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHL--KEKLISQAQEVSRLRSelggtdlekhrdllmVENERLRQEM 92
Cdd:pfam17380 241 ESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIvqHQKAVSERQQQEKFEK---------------MEQERLRQEK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 93 RRCEAELQELRTkpagpcpgCEHSQESAQLR-DKLSQLQLEMaESKGMLSELNLEVQQKTDRLAEVELRLKDCLA---EK 168
Cdd:pfam17380 306 EEKAREVERRRK--------LEEAEKARQAEmDRQAAIYAEQ-ERMAMERERELERIRQEERKRELERIRQEEIAmeiSR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 169 AQEEERL-------SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARN-QHLQEQVA--MQRQVLKEM 238
Cdd:pfam17380 377 MRELERLqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAreMERVRLEEQ 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973353098 239 EQQLQSS---HQLTARLRAQIAMYESELERAHGQMLEEM---QSLEEDKNRAIEEAFARAQVE 295
Cdd:pfam17380 457 ERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-192 |
3.82e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 2 VLRMVEAMSQLQDEKTQLQEELVVLQERLAL---RDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggTDLEKHR 78
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL--LEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 79 DLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 158
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQ----------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190
....*....|....*....|....*....|....
gi 973353098 159 LRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ 192
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
72-193 |
5.33e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 72 TDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAG-------------PCPGCEhSQESAQLRDKLSQLQLEMAESKG 138
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDAleeelrqlkqledELEDCD-PTELDRAKEKLKKLLQEIMIKVK 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 973353098 139 MLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 193
Cdd:smart00787 226 KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-178 |
8.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 3 LRMVEAMSQLQDEKTQLQEEL---VVLQERLALRDSDQQATSTQLQNQVEHlKEKLISQAQEVSRLRSELGGTDLEKHRD 79
Cdd:COG4717 343 LDRIEELQELLREAEELEEELqleELEQEIAALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQLEELLGELEEL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 80 LLMVENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQL--QLEMAESKGMLSELNLEVQQKTDRLAEV 157
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELE-------------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELREL 488
|
170 180
....*....|....*....|....*.
gi 973353098 158 E-----LRLKDCLAEKAQEEERLSRR 178
Cdd:COG4717 489 AeewaaLKLALELLEEAREEYREERL 514
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
10-287 |
9.55e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 10 SQLQDEKTQLQ---EELVVlqERLALRDSDQqaTSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrDLLMVENE 86
Cdd:pfam15921 468 AQLESTKEMLRkvvEELTA--KKMTLESSER--TVSDLTASLQEKERAIEATNAEITKLRSRV---------DLKLQELQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 87 RLRQE---MRRCEAELQELRTKPAGPCPGCE---------------HSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQ 148
Cdd:pfam15921 535 HLKNEgdhLRNVQTECEALKLQMAEKDKVIEilrqqienmtqlvgqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 149 QKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLRAQSPPVK--YVIKTVEVESSK 209
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKrnFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 210 TKQALSESQArnqhlQEQVAMQRQVLKEMEQQ--------LQSSHQLTARlRAQIAMYESE---LERAHGQMLEEMQSLE 278
Cdd:pfam15921 695 NKLKMQLKSA-----QSELEQTRNTLKSMEGSdghamkvaMGMQKQITAK-RGQIDALQSKiqfLEEAMTNANKEKHFLK 768
|
....*....
gi 973353098 279 EDKNRAIEE 287
Cdd:pfam15921 769 EEKNKLSQE 777
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
4-257 |
1.03e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 4 RMVEAMSQLQDEKTQLQEElvvlQERlALRDSDQQATSTQLQNQVEhlkeKLISQAQevSRLRSELGGTDLEKHRDLLMV 83
Cdd:PRK10929 110 EILQVSSQLLEKSRQAQQE----QDR-AREISDSLSQLPQQQTEAR----RQLNEIE--RRLQTLGTPNTPLAQAQLTAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 ENERLRQEMRRCEAELQELrtkpagpcpgcehsqeSAQLRDKLSQLQLEMAESK---------GMLSELNLEVQQKTDR- 153
Cdd:PRK10929 179 QAESAALKALVDELELAQL----------------SANNRQELARLRSELAKKRsqqldaylqALRNQLNSQRQREAERa 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 154 LAEVELrlkdcLAEKAQE-EERLSRRLRDSHETIASLRAQSppvkyviKTVEVESSKTKQALSESQarnqhlqeQVamqR 232
Cdd:PRK10929 243 LESTEL-----LAEQSGDlPKSIVAQFKINRELSQALNQQA-------QRMDLIASQQRQAASQTL--------QV---R 299
|
250 260
....*....|....*....|....*...
gi 973353098 233 QVL---KEMEQQLQSSHQLTARLRAQIA 257
Cdd:PRK10929 300 QALntlREQSQWLGVSNALGEALRAQVA 327
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
5-296 |
1.09e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 5 MVEAMSQLQDEKTQLQEELVVLQERLALRdSDQQATSTQlqnQVEHLKEKLISQAQEVSRLRSELggtdlekhrDLLMVE 84
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETL-TNQNSDCKQ---HIEVLKESLTAKEQRAAILQTEV---------DALRLR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 85 NERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRD--------KLSQLQLEMAESKGMLSELNLEV---QQKTDR 153
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKErkinvlqkKIENLQEQLRDKDKQLAGLKERVkslQTDSSN 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 154 LAEVELRLKDCLAEKAQEEERL----SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVA 229
Cdd:pfam10174 434 TDTALTTLEEALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973353098 230 MQRQVLKEMEQQLQSSHQLTARLRAQI--AMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEM 296
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEES-GKAQAEV 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-374 |
1.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 166 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALsesqarnqhLQEQVAMQRQVLKEMEQQLQSS 245
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 246 HQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 311
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353098 312 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 374
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-369 |
1.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 2 VLRMVEAMSQLQDEKTQLQEELVVLQERLALRdSDQQATSTQLQNQVEHLKEKLiSQAQEVSRLRSELGGTDLEKHRDLL 81
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEEL-EELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 82 MVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDK------------LSQLQLEMAESKGMLSELNLEVQQ 149
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallaLLGLGGSLLSLILTIAGVLFLVLG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 150 KTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktVEVESSKTKQALSESQARNQHLQEQVA 229
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA----------LGLPPDLSPEELLELLDRIEELQELLR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 230 MQRQVLKEMEQQlQSSHQLTARLRAQIAMYESELERAHGQmLEEMQSLEEDKNRAIEE-AFARAQVEMKAVHENLAGVRT 308
Cdd:COG4717 355 EAEELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQlEELLGELEELLEALDEEELEE 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353098 309 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVK-AEIGQAIEEVNSNNQELLRKYRR 369
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAA 494
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
52-251 |
1.37e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.75 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 52 KEKLISQAQEVSRLRSELGGT-------DLEKHRDLLMVENERLRQEMRRCEAELQELRTkpagpcpgcEHSQESAQLRD 124
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEA---------QQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 125 KLSQLQLEMAESKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 204
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 973353098 205 VESSKTKQALSESQARNQHLQEQVAMQRQV----LKEMEQQLQSSHQLTAR 251
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQGEGSN 216
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
3-374 |
1.92e-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: 44.94 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 3 LRMVEAMSQLQDEKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtDLEKHRDLLM 82
Cdd:COG3096 336 LNLVQTALRQQEKIERYQEDLEELTERLE----EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 83 VENERLRQEMRRCEaELQELrtkpagpcpgCEhsqesaqlrdkLSQLQLEMAEskGMLSELNLEVQQKTDRLAEVELRLK 162
Cdd:COG3096 410 TRAIQYQQAVQALE-KARAL----------CG-----------LPDLTPENAE--DYLAAFRAKEQQATEEVLELEQKLS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 163 DCLAEKAQEEERLsrrlrdshetiASLRAQSPPVkyviktVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQL 242
Cdd:COG3096 466 VADAARRQFEKAY-----------ELVCKIAGEV------ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 243 QSSH-------QLTARLRAQIAMYEsELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVHENLAGVRTNLLTLQP 315
Cdd:COG3096 529 RQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARAP 602
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353098 316 ALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 374
Cdd:COG3096 603 AWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
86-357 |
2.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 86 ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQ--LEMAESKGMLSELNLEVQQKTDRLAEVEL---- 159
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE------ALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 160 --RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQARNQHLQEQV--AM 230
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 231 QRQVLKEMEQQLQSShqlTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 310
Cdd:COG4913 760 GDAVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 973353098 311 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 357
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
15-370 |
2.99e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 15 EKTQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLE---KHRDLLMVENERLRQE 91
Cdd:pfam07111 243 ERQELLDTMQHLQEDRA----DLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkKCRSLLNRWREKVFAL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 92 MRRCEAelQELrtkpagpcpgcEHSQESAQLRDKLSQLQ-------------------------LEMAESKGMLSELNLE 146
Cdd:pfam07111 319 MVQLKA--QDL-----------EHRDSVKQLRGQVAELQeqvtsqsqeqailqralqdkaaeveVERMSAKGLQMELSRA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 147 VQ---QKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQH 223
Cdd:pfam07111 386 QEarrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 224 ---------LQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQiamyesELERAHGQMLEEMQSLEEDKNRaIEEAFARAQv 294
Cdd:pfam07111 466 cpppppappVDADLSLELEQLREERNRLDAELQLSAHLIQQ------EVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353098 295 emkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 370
Cdd:pfam07111 538 ------ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-167 |
3.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQ-----LQNQVEHLKE---KLISQAQEVSRLRSELggTDLEKHR 78
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDAssdDLAALEEQLEELEAEL--EELEEEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 79 DLLMVENERLRQEMRRCEAELQELRTKpAGPCPGCEHSQESAQLRDKLSQLQLEMAESKgMLSELNLEVQQKTDRLAEVE 158
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDR-LEAAEDLARLELRALLEERFAAALGDAVERE-LRENLEERIDALRARLNRAE 786
|
....*....
gi 973353098 159 LRLKDCLAE 167
Cdd:COG4913 787 EELERAMRA 795
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
19-275 |
3.44e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 19 LQEELVVLQERLALRDSDQQATStqLQNQVEhlKEKLISQAQEVSRLRSELG-----GTDLEKHRDLLMVENERLR---- 89
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIK--LQKTIK--REKKLRETEEVEFSLKAEVliqkfGRSLKAKKRFSLLKKETIYlqsa 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 90 QEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAE-SKGMLSELNLEVQQKTDRLAEVE--LRLKDCLA 166
Cdd:COG5022 875 QRVELAERQLQELK----------IDVKSISSLKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKklLNNIDLEE 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 167 EKAQEEERLSRRLRDsHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQV----AMQRQV--LKEMEQ 240
Cdd:COG5022 945 GPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPV 1023
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 973353098 241 QLQSSHQLTARLRA-----QIAMYESELERAHGQMLEEMQ 275
Cdd:COG5022 1024 EVAELQSASKIISSestelSILKPLQKLKGLLLLENNQLQ 1063
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
18-331 |
3.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 18 QLQEELVVLQERLALRDSDQQatstQLQNQVEHLKEKLISQ---------AQEVSRLRSELG--GTDLEKHRDllmvENE 86
Cdd:PRK04863 790 QLRAEREELAERYATLSFDVQ----KLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRVelERALADHES----QEQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 87 RLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQL-RDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVElRLKDCL 165
Cdd:PRK04863 862 QQRSQLEQAKEGLSALN----------RLLPRLNLLaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE-PIVSVL 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 166 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE-------VESSKTKQALSES-QARNQHLQEQVAMQRQVLKE 237
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQ 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 238 MEQQLQSSHQLTARLRAQIamyeseleRAHGQMLEE-MQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRT-------- 308
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAEERARARRDELHARLSANRSrrnqlekq 1082
|
330 340
....*....|....*....|....*....
gi 973353098 309 ------NLLTLQPALRTLTNDYNGLKRQV 331
Cdd:PRK04863 1083 ltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
117-293 |
5.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 117 QESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 189
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 190 RAQSPP-----VKYViKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 264
Cdd:COG3883 110 GSESFSdfldrLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 973353098 265 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 293
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
7-181 |
6.05e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERLALrdsdQQATSTQLQNQVEHLKEKLISQAQEVSRLRSEL-----GGTDLEKHRDLL 81
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 82 MVENERLRQEMRRCEAELQELRtkpagpcpgcehsQESAQLRDKLSQLQ--LEMAESKGmlselnlevQQKTDRLAEVEL 159
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLN-------------QQIAALRRQLAALEaaLDASEKRD---------RESQAKIADLGR 179
|
170 180
....*....|....*....|....*....
gi 973353098 160 RLKDCLAEKAQEeerLSR-------RLRD 181
Cdd:PRK09039 180 RLNVALAQRVQE---LNRyrseffgRLRE 205
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
9-283 |
6.52e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 9 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEK---LISQAQEVSRLRSELGGTDL----------E 75
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKdkqLAGLKERVKSLQTDSSNTDTalttleealsE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 76 KHRDLLMVENERLRQEMRRCEaELQELRtkpagpcpgcehsQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 155
Cdd:pfam10174 448 KERIIERLKEQREREDRERLE-ELESLK-------------KENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 156 EVELRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAqSPPVKYVIKTVEVESSKTKQALSESQARNQHLQE---QVA 229
Cdd:pfam10174 514 KKDSKLKSLeiaVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRIRLLEQEVARYKEESGKAQAEVERLLGilrEVE 592
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 973353098 230 MQR----QVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNR 283
Cdd:pfam10174 593 NEKndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
7-373 |
7.26e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQ---NQVEHLKEKLISQAQEVSRLRS--ELGGTDLEKH---- 77
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAahSFVVTEFEATtcsl 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 78 RDLLMVENERLRQEMRRCEAELQELRTKpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELN--LEVQQKTDRLA 155
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKK----------SSELEEMTKFKNNKEVELEELKKILAEDEklLDEKKQFEKIA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 156 EvELrlkdclaeKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEvessKTKQALSESQARNQHLQEQVAMqr 232
Cdd:pfam05483 432 E-EL--------KGKEQELiflLQAREKEIHDLEIQLTAIKTSEEHYLKEVE----DLKTELEKEKLKNIELTAHCDK-- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 233 qVLKEMEQQLQSSHQLTARLRAQ---IAMYESELERahgqMLEEMQSLEE------DKNRAIEEAFARAQVEMKA----V 299
Cdd:pfam05483 497 -LLLENKELTQEASDMTLELKKHqedIINCKKQEER----MLKQIENLEEkemnlrDELESVREEFIQKGDEVKCkldkS 571
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973353098 300 HENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQL 373
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
6-252 |
8.36e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 6 VEAMSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELG--GTDLEKHRDLLMV 83
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAqrDTQVLQLQDTITT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 ENERLRQEMRRcEAELQELRTKPAGPCPGCEHSQESAQ-LRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLK 162
Cdd:pfam07888 218 LTQKLTTAHRK-EAENEALLEELRSLQERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 163 DCLAEKAQEEERLSRRLRDSHETIASLRA---------QSPPVKYVIKTVEVESSKTKQALSESQARNQhLQEQVAMQRQ 233
Cdd:pfam07888 297 EGRARWAQERETLQQSAEADKDRIEKLSAelqrleerlQEERMEREKLEVELGREKDCNRVQLSESRRE-LQELKASLRV 375
|
250 260
....*....|....*....|....*.
gi 973353098 234 VLKEMEQQ-------LQSSHQLTARL 252
Cdd:pfam07888 376 AQKEKEQLqaekqelLEYIRQLEQRL 401
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
178-385 |
8.63e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 178 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQAR--------NQHLQEQVAMQRQVLK-EMEQQLQS 244
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 245 SH-----QLTARLRAQIAMYESELE--RAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 312
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973353098 313 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 385
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
116-380 |
1.01e-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: 42.73 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 116 SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLRAQS 193
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 194 PPVKYVIKTVEVESS-------KTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERa 266
Cdd:TIGR00606 663 AVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 267 hgqMLEEMQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLT---LQPALRTLTNDYNGLKRQVRGFPlllQEALR 343
Cdd:TIGR00606 742 ---KEKEIPELRN-KLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMERFQMELKDVERKIA---QQAAK 814
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 973353098 344 SVKAEIGQAIEEVNSNNQELLRKYRR---ELQLRKKCHNE 380
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTvvsKIELNRKLIQD 854
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
90-357 |
1.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 90 QEMRRCEAELQELRTKPAgpcpgcehsqESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 167
Cdd:COG4717 71 KELKELEEELKEAEEKEE----------EYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 168 KAQEEERLsRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQARNQhlQEQVAMQRQVLKEMEQQLQSSHQ 247
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE------------------LEELEAELAELQ--EELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 248 LTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGL 327
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270
....*....|....*....|....*....|
gi 973353098 328 KRQVRGFPLLLQEALRSVKAEIGQAIEEVN 357
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
7-316 |
1.12e-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: 42.63 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELvvlqerlalrdSDQQATSTQLQNQVEHLKEKLisqaQEVSRLRSELGGTDLEKHRDLLmvenE 86
Cdd:COG3096 836 AELAALRQRRSELEREL-----------AQHRAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLADRL----E 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 87 RLRQEMRRCEAELQELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAEskgmLSELNLEVQQKTDRLAEVELRLkDCLA 166
Cdd:COG3096 897 ELREELDAAQEAQAFIQ----------QHGKALAQLEPLVAVLQSDPEQ----FEQLQADYLQAKEQQRRLKQQI-FALS 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 167 EKAQEEERLSrrLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQAR-NQHLQEQVAMQ------RQVLKEME 239
Cdd:COG3096 962 EVVQRRPHFS--YEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQySQYNQVLASLKssrdakQQTLQELE 1039
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 240 QQLQ-------SSHQLTARLR-------------------AQIAMYESELERAHGQMLEemqsLEED---KNRAIEEAFA 290
Cdd:COG3096 1040 QELEelgvqadAEAEERARIRrdelheelsqnrsrrsqleKQLTRCEAEMDSLQKRLRK----AERDykqEREQVVQAKA 1115
|
330 340
....*....|....*....|....*.
gi 973353098 291 RAQVEMKAVHENlaGVRTNLLTLQPA 316
Cdd:COG3096 1116 GWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
7-320 |
1.25e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEK------TQLQEELVVLQERLAlrdsDQQATSTQLQNQVEHLKEKLISQAQEVSrlrselggtdlEKHRDL 80
Cdd:PRK10246 413 AALAQHAEQRplrqrlVALHGQIVPQQKRLA----QLQVAIQNVTQEQTQRNAALNEMRQRYK-----------EKTQQL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 81 LMVENeRLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAqlrdkLSQLQ-LEMAESKGMLSELNLEVQQKTDRLAEVEL 159
Cdd:PRK10246 478 ADVKT-ICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPA-----VEAYQaLEPGVNQSRLDALEKEVKKLGEEGAALRG 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 160 RLkDCLAEKAQEEERLSRRLRDSHETIaslraqsppvkyviktvevesSKTKQALSESQARNQHLQEQVAMQRQVLKEME 239
Cdd:PRK10246 552 QL-DALTKQLQRDESEAQSLRQEEQAL---------------------TQQWQAVCASLNITLQPQDDIQPWLDAQEEHE 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 240 QQLqssHQLTAR--LRAQIAMYESELERAHGQMLEEMQSLEEDKNR----------------AIEEAFARAQvemkAVHE 301
Cdd:PRK10246 610 RQL---RLLSQRheLQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSWQ----QRQN 682
|
330
....*....|....*....
gi 973353098 302 NLAGVRTNLLTLQPALRTL 320
Cdd:PRK10246 683 ELTALQNRIQQLTPLLETL 701
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
10-288 |
1.65e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 10 SQLQDEKTQLQEelvvLQERLalrdSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSElggtdlekhRDLLMVENERLR 89
Cdd:pfam05622 183 GQLETYKRQVQE----LHGKL----SEESKKADKLEFEYKKLEEKLEALQKEKERLIIE---------RDTLRETNEELR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 90 qemrrCeAELQELRTKPAGPCPGCEHSQE--------SAQLRDKLSQLQLEmaesKGMLSELnlEVQQKTDRLAEVELRL 161
Cdd:pfam05622 246 -----C-AQLQQAELSQADALLSPSSDPGdnlaaeimPAEIREKLIRLQHE----NKMLRLG--QEGSYRERLTELQQLL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 162 KDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVESSKT------KQALSESQARNQHLQEQVAMQRQVL 235
Cdd:pfam05622 314 ED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHEAQSELQKKKEQI 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 973353098 236 KEMEQQLQSSHQLTArlraqiamyeSELERAHGQMLEEMQSLEEDKNRAIEEA 288
Cdd:pfam05622 387 EELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-143 |
1.70e-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: 41.97 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 4 RMVEAMSQLQDEKTQLQEELVVLQE---RLALRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELggtdlekhrDL 80
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL---------EE 898
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973353098 81 LMVENERLRQEMRRCEAELQELRTKpagpcpgcehsqeSAQLRDKLSQLQLEMAESKGMLSEL 143
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREK-------------LAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
120-374 |
1.78e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 120 AQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERLSRRLRDSHETIASLRAQSPPVKYV 199
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 200 IKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQsleE 279
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE---A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 280 DKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSN 359
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*
gi 973353098 360 NQELLRKYRRELQLR 374
Cdd:COG4372 260 IEELELAILVEKDTE 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-235 |
1.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 21 EELVVLQERLALRDsDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQ 100
Cdd:COG4717 71 KELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 101 ELRtkpagpcpgcEHSQESAQLRDKLSQLQLEMAESKgmlselnlevQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLR 180
Cdd:COG4717 150 ELE----------ERLEELRELEEELEELEAELAELQ----------EELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 973353098 181 DSHETIASLRAqsppvkyviktvEVESSKTKQALSESQARNQHLQEQVAMQRQVL 235
Cdd:COG4717 210 ELEEELEEAQE------------ELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
119-306 |
2.31e-03 |
|
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: 40.37 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 119 SAQLRDKLSQLQLEMAESKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 192
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 193 SPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIamyESELERAhgqmle 272
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKEFEEVSELI---KSELERF------ 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 973353098 273 EMQSLEEDKNrAIE---EAFARAQVEMKAVHENLAGV 306
Cdd:cd07627 181 ERERVEDFRN-SVEiylESAIESQKELIELWETFYQR 216
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
80-309 |
2.82e-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: 41.26 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 80 LLMVENERLRQEMRRcEAELQELRTKPAGPCPGCEH-SQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVE 158
Cdd:pfam05557 11 LSQLQNEKKQMELEH-KRARIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 159 LRLKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQARNQHLQEQVAMQRQVLKEM 238
Cdd:pfam05557 90 KKLN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973353098 239 EQ---QLQSSHQLTARLRAQIAMYESELErahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTN 309
Cdd:pfam05557 152 EQlrqNLEKQQSSLAEAEQRIKELEFEIQ------SQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN 219
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-278 |
2.84e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 7 EAMSQLQDEKTQLQEELVVLQERLALRD--SDQQATSTQLQNQVEHLKE--KLISQAQEVSRLR------SELGGTDLEK 76
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQllKQLRARIEELRAQEAVLEEtqERINRARKAAPLAahikavTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 77 HRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESaQLRDKLSQLQLEMAESKGMLSELN--LEVQQKTDRL 154
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI-HIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 155 AEVELRLKDCL----AEKAQEEERLSRRlRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQARNQHLQEqvam 230
Cdd:TIGR00618 392 TQKLQSLCKELdilqREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE---- 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 973353098 231 QRQVLKEMEQQLQSSHQLTARlraqiamyESELERAHGQMLEEMQSLE 278
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEP 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
125-287 |
3.23e-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: 39.91 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 125 KLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRR---LRDSHETIASLRAQSPPVK---- 197
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 198 YVIKTVEVESSKTKQALSESQARNqhLQEQVAMQRQVLKEMEQQLqsshqltARLRAQIAMYESELERAHGQMLEEMQSL 277
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 973353098 278 EEDKNRAIEE 287
Cdd:COG1579 162 EAEREELAAK 171
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-323 |
3.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 29 RLALRD--SDQQATSTQLQNQVEHLKEKLISQAqeVSRLRSELGGTDLEKHRdllmVENERLRQEMRRCEAE--LQELRt 104
Cdd:PRK02224 175 RLGVERvlSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIER----YEEQREQARETRDEADevLEEHE- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 105 kpagpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAqeeerlsrrLRDSHE 184
Cdd:PRK02224 248 ---------ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG---------LDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 185 TIASLRaqsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 264
Cdd:PRK02224 310 EAVEAR---------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973353098 265 RAHGQMLE---EMQSLEEDKNRAiEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 323
Cdd:PRK02224 381 DRREEIEEleeEIEELRERFGDA-PVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-316 |
3.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 122 LRDKLSQLQLEMAESKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVI 200
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 201 KTVEV--ESSKTKQALSESQARNQHLQEQVamqrQVLKEMEQQLQsshqltaRLRAQIAMYESELERAHGQ----MLEEM 274
Cdd:COG4717 126 QLLPLyqELEALEAELAELPERLEELEERL----EELRELEEELE-------ELEAELAELQEELEELLEQlslaTEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 973353098 275 QSLEEDKNRA------IEEAFARAQVEMKAVHENLAGVRTNLLTLQPA 316
Cdd:COG4717 195 QDLAEELEELqqrlaeLEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-186 |
4.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 11 QLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQnQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVEN----- 85
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELE-QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAverel 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 86 --------ERLRQEMRRCEAELQELRT--KPAGPCPGCEHSQESAQLRDKLSQLQlemaeskgmlselnlevQQKTDRLA 155
Cdd:COG4913 768 renleeriDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYLALLD-----------------RLEEDGLP 830
|
170 180 190
....*....|....*....|....*....|..
gi 973353098 156 EVELRLKDCLAEKAQEE-ERLSRRLRDSHETI 186
Cdd:COG4913 831 EYEERFKELLNENSIEFvADLLSKLRRAIREI 862
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
9-180 |
4.41e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 9 MSQLQDEKTQLQEELVVLQERLALRDSDQQATSTQLQnQVEHLKEKLISQAQEVSRLRSELGGTDLEkhrdllmvenerl 88
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP-KLRDRKDALEEELRQLKQLEDELEDCDPT------------- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 89 rqEMRRCEAELQELrtkpagpcpgcehSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK 168
Cdd:smart00787 205 --ELDRAKEKLKKL-------------LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFT 269
|
170
....*....|..
gi 973353098 169 AQEEERLSRRLR 180
Cdd:smart00787 270 FKEIEKLKEQLK 281
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
89-293 |
5.09e-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: 40.32 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 89 RQEMRRCEAELQElrtkpagpcpgcehsQESAQLRdKLSQLQLEMAESkgMLSELNLEVQQKTDRLAEVELRLKDclAEK 168
Cdd:pfam15709 342 RAEMRRLEVERKR---------------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 169 AQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQA---RNQHLQEQVAMQRQVLKEMEQQlqss 245
Cdd:pfam15709 402 RQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAEE---- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 973353098 246 hqltARLRAQIAMYESElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 293
Cdd:pfam15709 475 ----ERLEYQRQKQEAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-395 |
5.35e-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: 40.43 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 231 QRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVhENLAGVRTNl 310
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQ- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 311 ltLQPALRTLTNDYNGLKRQVRGFPLLLQEALR---SVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGN 387
Cdd:TIGR02168 752 --LSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
....*...
gi 973353098 388 IRVIARVR 395
Cdd:TIGR02168 830 ERRIAATE 837
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
89-376 |
5.44e-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: 40.42 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 89 RQEMRRCEAELQELRTKPAGPCpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLA-- 166
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKAC----------EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKld 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 167 -EKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQL--- 242
Cdd:TIGR00606 269 nEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELlve 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 243 QSSHQLTA-RLRAQIAMYESelERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQP 315
Cdd:TIGR00606 349 QGRLQLQAdRHQEHIRARDS--LIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973353098 316 ALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQLRKK 376
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEK 492
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
33-311 |
6.00e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 33 RDSDQQATStqLQNQVEHLKEKLISQAQEVSRLRsELGGTDLEKHRDLLmvenERLRQEMRrceaelqelrtkpagpcpg 112
Cdd:PHA02562 177 RELNQQIQT--LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 113 cEHSQESAQLRDKLSQLQLEMAESKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrlrdsh 183
Cdd:PHA02562 231 -TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 184 etiaslraqsppvkyvIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESEL 263
Cdd:PHA02562 304 ----------------IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 973353098 264 ERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 311
Cdd:PHA02562 368 EELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-430 |
6.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 3 LRMVEAMSQLQDEKTQLQEELVVLQErlALRDSDQQATSTQLQNQVEHLK--EKLISQAQEVSRLRSELGGTDLEKHRDL 80
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 81 LMVENERLRQEMRrcEAELQELRTKPAGPCPGCEHSQESAQLR---DKLSQLQLEMAESKGMLSELnlevqQKTDRLAEV 157
Cdd:PTZ00121 1488 AKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADEL-----KKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 158 ELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVEVESS-KTKQALSESQARNQhlQEQVAMQRQVLK 236
Cdd:PTZ00121 1561 EEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIK--AEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 237 EMEQ-------------QLQSSHQLTARLRAQIAMYESELERAhgqmLEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnl 303
Cdd:PTZ00121 1634 KVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE-- 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 304 agvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 383
Cdd:PTZ00121 1707 -------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 973353098 384 LKGNIRVIARV---RPVTKEDGEGPEATNAVTFDADDDS--IIHLLHKGKPV 430
Cdd:PTZ00121 1769 KAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFanIIEGGKEGNLV 1820
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
4-222 |
7.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 4 RMVEAMSQLQDEKTQLQEELVVLQERLAlrdsdqqatstQLQNQVEHLKEKLISQAQEVSRLRSELGGTDLekhrdLLMV 83
Cdd:COG3883 48 ELNEEYNELQAELEALQAEIDKLQAEIA-----------EAEAEIEERREELGERARALYRSGGSVSYLDV-----LLGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 84 EN--------ERLRQEMRRCEAELQELRTKPAgpcpgcEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLA 155
Cdd:COG3883 112 ESfsdfldrlSALSKIADADADLLEELKADKA------ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973353098 156 EVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQ 222
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
6-192 |
7.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 6 VEAMSQLQDEKTQLQEELVVLQERLA-----LRDSDQQATSTQLQNQVEHLKEKLISQAQEVSRLRSELGgtdlEKHRDL 80
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAalraqLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT----PNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 81 LmveneRLRQEMRRCEAELQElrtkpagpcpgcehsqesaQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEvelr 160
Cdd:COG3206 294 I-----ALRAQIAALRAQLQQ-------------------EAQRILASLEAELEALQAREASLQAQLAQLEARLAE---- 345
|
170 180 190
....*....|....*....|....*....|..
gi 973353098 161 lkdcLAEKAQEEERLSRRLRDSHETIASLRAQ 192
Cdd:COG3206 346 ----LPELEAELRRLEREVEVARELYESLLQR 373
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
4-132 |
8.29e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 4 RMVEAMSQLQDEKTQLQEELVVLQErlaLRDSDQQATSTQLQNqvehLKEKLISQAQEVSRLRSELggTDLEKHRDLLMV 83
Cdd:smart00787 169 LLNSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELDR----AKEKLKKLLQEIMIKVKKL--EELEEELQELES 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 973353098 84 ENERLRQEMRRCEAELQELRTKPAgPCPGCEHSqESAQLRDKLSQLQLE 132
Cdd:smart00787 240 KIEDLTNKKSELNTEIAEAEKKLE-QCRGFTFK-EIEKLKEQLKLLQSL 286
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
140-264 |
8.54e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 140 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQA 219
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 973353098 220 RNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELE 264
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
4-357 |
9.13e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.43 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 4 RMVEAMSQL-------QDEKTQLQEELVVLQERLALRDSDQQATSTQLQNQVEHLKEKLisqaQEVSRLRSElgGTDLEK 76
Cdd:PRK04778 123 QILEELQELleseeknREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTES--GDYVEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 77 HRDLLMVENE--RLRQEMRRCEAELQELRTKpagpcpgcehsqesaqLRDKLSQLQL---EMAESKGMLSELNL--EVQQ 149
Cdd:PRK04778 197 REILDQLEEElaALEQIMEEIPELLKELQTE----------------LPDQLQELKAgyrELVEEGYHLDHLDIekEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 150 KTDRLAEVELRLKDC-LAEKAQEEERLSRRLRDSHETIAslraqsppvKYVI--KTVEVESSKTKQALSESQARNQHLQE 226
Cdd:PRK04778 261 LKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDILE---------REVKarKYVEKNSDTLPDFLEHAKEQNKELKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 227 QVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQ-----MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHE 301
Cdd:PRK04778 332 EIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRK 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973353098 302 NLAGVRTNLLTLQPALRTltndyngLKRQVR-----GFPLLLQEALRSVKAEIGQAIEEVN 357
Cdd:PRK04778 412 DELEAREKLERYRNKLHE-------IKRYLEksnlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
123-275 |
9.82e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 123 RDK-LSQLQLEMAESKGMLS-------ELNLEVQQKTDRLAEVEL---RLKDCLAEKAQEEERLSRRLRDSHETIASLRA 191
Cdd:PRK09039 51 KDSaLDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973353098 192 QSppvkyviktvevessktkqalSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQML 271
Cdd:PRK09039 131 VS---------------------ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....
gi 973353098 272 EEMQ 275
Cdd:PRK09039 190 QELN 193
|
|
| |
