|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
370-697 |
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: 527.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 370 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 448
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 449 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 525
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 526 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 605
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 606 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 685
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 1958746520 686 LKFAERVRSVEL 697
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
378-695 |
4.80e-147 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 434.31 E-value: 4.80e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 378 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 454
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 455 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 534
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 535 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 611
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 612 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 689
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 1958746520 690 ERVRSV 695
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
372-699 |
2.41e-142 |
|
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: 422.75 E-value: 2.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 447
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 448 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 527
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 528 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 605
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 606 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 683
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 1958746520 684 YSLKFAERVRSVELGP 699
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
372-693 |
5.91e-123 |
|
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: 372.36 E-value: 5.91e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 448
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 449 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 526
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 527 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 604
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 605 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 683
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 1958746520 684 YSLKFAERVR 693
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
372-695 |
2.76e-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: 2.76e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 443
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 444 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 520
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 521 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 596
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 597 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 675
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 1958746520 676 EKNTSETLYSLKFAERVRSV 695
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
373-696 |
1.47e-103 |
|
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: 1.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 373 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 450
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 451 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 524
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 525 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 594
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 595 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 671
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 1958746520 672 VSPVEKNTSETLYSLKFAERVRSVE 696
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
372-695 |
5.27e-95 |
|
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: 300.42 E-value: 5.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 434
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 435 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 513
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 514 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 592
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 593 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 667
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 1958746520 668 MVVQVSPVEKNTSETLYSLKFAERVRSV 695
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
372-695 |
7.53e-90 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 286.15 E-value: 7.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 449
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 450 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 526
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 527 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 606
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 607 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 685
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 1958746520 686 LKFAERVRSV 695
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
372-695 |
9.89e-89 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 283.07 E-value: 9.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 450
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 451 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 530
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 531 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT---GKLNLVDLAGSER 607
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvrvSTLNLIDLAGSER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 608 VGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 685
Cdd:cd01374 232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
330
....*....|
gi 1958746520 686 LKFAERVRSV 695
Cdd:cd01374 312 LKFASRAKKI 321
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
371-695 |
1.42e-88 |
|
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: 284.24 E-value: 1.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 371 GNIRVIARVRPVTKEDGEGPeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQE 435
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 436 VQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDLL 513
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 514 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 588
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 589 TGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 658
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958746520 659 SLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 695
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
372-695 |
1.08e-85 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 276.13 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 446
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 447 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 515
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 516 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 590
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 591 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 670
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 1958746520 671 QVSPVEKNTSETLYSLKFAERVRSV 695
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
356-696 |
7.43e-78 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 262.37 E-value: 7.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 356 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 435
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 436 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 514
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 515 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 594
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 595 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 672
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 1958746520 673 SPVEKNTSETLYSLKFAERVRSVE 696
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
373-690 |
7.58e-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: 252.31 E-value: 7.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 373 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 441
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 442 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 517
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 518 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 592
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 593 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 664
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 1958746520 665 KTLMVVQVSPVEKNTSETLYSLKFAE 690
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
372-693 |
2.06e-76 |
|
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: 251.27 E-value: 2.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 450
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 451 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgKEPQ 518
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL-DPAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 519 EKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTTg 595
Cdd:cd01373 157 RNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 596 KLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 671
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340
....*....|....*....|..
gi 1958746520 672 VSPVEKNTSETLYSLKFAERVR 693
Cdd:cd01373 314 VHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
372-693 |
8.69e-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: 238.17 E-value: 8.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 448
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 449 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 528
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 529 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 607
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 608 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 687
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 1958746520 688 FAERVR 693
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
373-693 |
1.74e-69 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 232.47 E-value: 1.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 373 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 441
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 442 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 518
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 519 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 593
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 594 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 672
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 1958746520 673 SPVEKNTSETLYSLKFAERVR 693
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
372-692 |
1.05e-65 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 221.79 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 372 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 443
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 444 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 519
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 520 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 599
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 600 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 677
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 1958746520 678 NTSETLYSLKFAERV 692
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
373-696 |
1.28e-56 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 211.33 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 373 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 451
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 452 FAYGQTGAGKTYTMEG----------TPENPGINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLGKE 516
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLLDPS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 517 pQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLRT- 593
Cdd:PLN03188 250 -QKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLSSf 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 594 -TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSKTL 667
Cdd:PLN03188 327 kTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLA 406
|
330 340
....*....|....*....|....*....
gi 1958746520 668 MVVQVSPVEKNTSETLYSLKFAERVRSVE 696
Cdd:PLN03188 407 MVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
352-513 |
3.66e-41 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 147.37 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 352 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 431
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 432 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 511
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 1958746520 512 LL 513
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
420-639 |
5.89e-22 |
|
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: 93.56 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 420 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 498
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 499 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 578
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746520 579 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 639
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-341 |
4.85e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLR-ERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCE 81
Cdd:COG1196 217 ELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 82 AELQELRaqpvvpcQGCEHSQE-STQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERL 160
Cdd:COG1196 295 AELARLE-------QDIARLEErRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 161 SRRLRDSHETIASLKAQsppvKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQ 240
Cdd:COG1196 368 LEAEAELAEAEEELEEL----AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 241 iamyEAELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRG 318
Cdd:COG1196 444 ----LEEAAEEEAELEEEEEALLELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalLLAG 518
|
330 340
....*....|....*....|....*
gi 1958746520 319 FPLLLQE--ALRSVKAEIGQAIEEV 341
Cdd:COG1196 519 LRGLAGAvaVLIGVEAAYEAALEAA 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-367 |
4.97e-14 |
|
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: 76.25 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 58 DVEKHRDRLMVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTD 137
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELE-------------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 138 RLAevelRLKDCLAEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 217
Cdd:TIGR02168 748 RIA----QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 218 QVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLT 297
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 298 LQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELV 367
Cdd:TIGR02168 899 LSEELRELESKRSELRRELE----ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-316 |
6.79e-12 |
|
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: 69.33 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCEA 82
Cdd:TIGR02169 671 SEPAELQRLRERLE-----------GLKRELSSLQSELRRIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAQPVVPCQGCEHS-QESTQLRDRLSQLQLEVAENK-------------------GMLSELNLEVQQKTDRLAEV 142
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVkSELKELEARIEELEEDLHKLEealndlearlshsripeiqAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 143 ELRLKDCLAEKAQEEER---LSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV 219
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 220 LKEMEQQLQ---------NSHQLTIQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEEDKNRA 269
Cdd:TIGR02169 898 LRELERKIEeleaqiekkRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLA 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958746520 270 IE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 316
Cdd:TIGR02169 978 IQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-343 |
8.57e-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: 68.93 E-value: 8.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 29 LQNQVENLKEKlISQAQEVSRLRSELGgtdvEKHRDRLMVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLR 108
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE-------------EELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 109 DRLSQLQLEVAENKGMLSELNLEVQQKTDRLaeveLRLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvIKTV 188
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 189 EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT--------------IQLRAQIAMYEAELER--AH 252
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 253 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 332
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330
....*....|.
gi 1958746520 333 EIGQAIEEVNS 343
Cdd:TIGR02168 483 ELAQLQARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
11-273 |
1.19e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 68.12 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 11 LRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRLMVENEQLRQELRRCEAELQELRAq 90
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 91 pvvpcqgcehsqestqlrdRLSQLQLEVAENKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 168
Cdd:COG3206 241 -------------------RLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 169 ETIASLKAQsppvkyvIKTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAe 247
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV- 362
|
250 260
....*....|....*....|....*.
gi 1958746520 248 LERAHGQMLEEMQSLEEDKNRAIEEA 273
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-358 |
3.99e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 26 TTQLQNQVENLKEKLiSQAQEVSRLRSELGGTDVE---KHRDRLMVENEQLRQELRRCEAELQELRAQpvvpcqgcehsq 102
Cdd:COG1196 195 LGELERQLEPLERQA-EKAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAE------------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 103 estqlrdrLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkdcLAEKAQEEERLSRRLRDSHETIASLKAQsppvk 182
Cdd:COG1196 262 --------LAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEE----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 183 yvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSL 262
Cdd:COG1196 325 --LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 263 EEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEE 340
Cdd:COG1196 403 EELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAA 478
|
330
....*....|....*...
gi 1958746520 341 VNSNNQELLRKYRRELQL 358
Cdd:COG1196 479 LAELLEELAEAAARLLLL 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-356 |
6.75e-10 |
|
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: 62.78 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 42 SQAQEVSRLRSELGGTDVEKhrdrlmvenEQLRQELRRCEAELQELRAQPvvpcqgCEHSQESTQLRDRLSQLQLEVAEN 121
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKREL---------SSLQSELRRIENRLDELSQEL------SDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 122 KGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSrRLRDSHETIASLKAQSPpvkyvIKTVEVESSKtkqalse 201
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEARLSHSR-----IPEIQAELSK------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 202 sqtrnqhLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQV 279
Cdd:TIGR02169 803 -------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeELEEELEELEA 875
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746520 280 EMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRREL 356
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI--------EKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-361 |
5.48e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 71 EQLRQELRRCEAELQELRAQpvvpcqgCEH-SQESTQ------LRDRLSQLQLEVAENKgmLSELNLEVQQKTDRLAEVE 143
Cdd:COG1196 182 EATEENLERLEDILGELERQ-------LEPlERQAEKaeryreLKEELKELEAELLLLK--LRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 144 LRLKDCLAEKAQEE----------ERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQV 213
Cdd:COG1196 253 AELEELEAELAELEaeleelrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 214 AMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEafARAQVEMKAVHENLAGVRT 293
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746520 294 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 361
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-177 |
1.50e-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: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHDSDRQATTTQL-QNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVEN--------EQL 73
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARL--DALREELDELEAQIrgnggdrlEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 74 RQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEK 153
Cdd:COG4913 344 EREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
170 180
....*....|....*....|....
gi 1958746520 154 AQEEERLSRRLRDSHETIASLKAQ 177
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-348 |
4.61e-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: 57.05 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 1 MSQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVS-------RLRSELGGTDVEKhrDRLMVEN 70
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKELSlekeqnkRLWDRDTGNSITI--DHLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 71 EQLRQELRRCEAELQELRAQpvvpCQG-CEHSQESTQLR----DRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 145
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSE----CQGqMERQMAAIQGKneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 146 LKDcLAEKAQEEERlsrRLRDSHETIASLKAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQRQVLKEME 224
Cdd:pfam15921 498 VSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIEILR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 225 QQLQNSHQLTIQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENLAGV 291
Cdd:pfam15921 569 QQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERLRAV 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746520 292 ------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 348
Cdd:pfam15921 649 kdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-341 |
1.43e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 65 RLMVENeqlRQELRRCEAELQELRAQ-----PVVpcqgcEHSQESTQLRDRLSQLQLevaenkgMLSELNLEVQQKTDRL 139
Cdd:COG4913 228 DALVEH---FDDLERAHEALEDAREQiellePIR-----ELAERYAAARERLAELEY-------LRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 140 AEVEL-RLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQR 217
Cdd:COG4913 293 LEAELeELRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 218 QVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLT 297
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958746520 298 LQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 341
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
28-251 |
1.54e-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: 54.38 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 28 QLQNQVENLKEKLISQAQEVSRLRSELggtdvEKHRDRLmvenEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQL 107
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQL-----AALERRI----AALARRIRALEQELAALE-------------AELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 108 RDRLSQLQLEVAENKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLKAQSPP 180
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746520 181 VKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERA 251
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-373 |
1.74e-07 |
|
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: 55.06 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 108 RDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKT 187
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 188 VEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHG---------QMLEE 258
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlrerlESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 259 MQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAI 338
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRSELEELSEEL 903
|
250 260 270
....*....|....*....|....*....|....*
gi 1958746520 339 EEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI 373
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-253 |
1.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQLRQELRRCE 81
Cdd:COG1196 298 ARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEEL---------EEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 82 AELQELRAQpvvpcqgcEHSQESTQLRDRLSQLQLEVAEnkgmlSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLS 161
Cdd:COG1196 365 EALLEAEAE--------LAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 162 RRLRDSHETIASLKAQsppvkyviktvevessktKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQI 241
Cdd:COG1196 432 ELEEEEEEEEEALEEA------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250
....*....|..
gi 1958746520 242 AMYEAELERAHG 253
Cdd:COG1196 494 LLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-275 |
2.23e-07 |
|
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: 54.68 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQATTTQLqnqvENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQLRQELRRCE 81
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELAEELAELEEKL---------EELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 82 AELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLaevelrlkdclaEKAQEEERLS 161
Cdd:TIGR02168 365 AELEELESRLE------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR------------ERLQQEIEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 162 RRLRDSHEtiaslkaqsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQnshqltiQLRAQI 241
Cdd:TIGR02168 427 LKKLEEAE---------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD-------AAEREL 484
|
250 260 270
....*....|....*....|....*....|....
gi 1958746520 242 AMYEAELErahgqMLEEMQSLEEDKNRAIEEAFA 275
Cdd:TIGR02168 485 AQLQARLD-----SLERLQENLEGFSEGVKALLK 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
69-290 |
2.43e-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: 53.61 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 69 ENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKD 148
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 149 CLAEKAQEEERLSRRLR-----DSHETIASLKAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQ 218
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746520 219 VLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENLAG 290
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
21-357 |
2.60e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 21 DRQATTtqLQNQVENLKEKLISQAQEVSRLRSELG---------GTDVEKHRDRLMVENEQLRQ--ELRRCEAELQELRA 89
Cdd:PRK04863 285 LEEALE--LRRELYTSRRQLAAEQYRLVEMARELAelneaesdlEQDYQAASDHLNLVQTALRQqeKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 90 QPVVPCQGCEHSQES-TQLRDRLSQLQLEVAENKGMLSELN--LEVQQK--------TDRLAEVEL----------RLKD 148
Cdd:PRK04863 363 RLEEQNEVVEEADEQqEENEARAEAAEEEVDELKSQLADYQqaLDVQQTraiqyqqaVQALERAKQlcglpdltadNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 149 CLAE-KAQEEERLSRRLR-----DSHETIASLKAQSppVKYVIKTV-EVESSKTKQALSE--SQTRNQ-HLQEQVAMQRQ 218
Cdd:PRK04863 443 WLEEfQAKEQEATEELLSleqklSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 219 VLKEMEQQLQNSHQLTIQLR----AQIAMY--EAELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLAG 290
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAefckRLGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLAA 600
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 291 VRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 357
Cdd:PRK04863 601 RAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-378 |
4.56e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 10 VLRERLALHDSDR-----QATTTQLQNQVENLkEKLISQAQEVSRLRSELGG--TDVEKHRDRLMVENEQLRQELRRCEA 82
Cdd:PRK03918 150 VVRQILGLDDYENayknlGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKelEEVLREINEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAqpvvpcqgcehsqestqLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEK 153
Cdd:PRK03918 229 EVKELEE-----------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 154 AQEEERLSR-------RLRDSHETIASLKAQSPPVKYVIKTVEVESSK---TKQALSESQTRNQHLQEQV---AMQRQVL 220
Cdd:PRK03918 292 AEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEERHelyEEAKAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 221 KEMEQQLQNSHQLTIQ------LRAQIAMYEAELERAH-GQMLEEMQSLEEDKNRAIEEaFARAQVE------------- 280
Cdd:PRK03918 372 EELERLKKRLTGLTPEklekelEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehr 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 281 ---MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQ 357
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420
....*....|....*....|.
gi 1958746520 358 LRKKchnELVRLKGNIRVIAR 378
Cdd:PRK03918 529 KLKE---KLIKLKGEIKSLKK 546
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
354-638 |
5.91e-07 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 52.82 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 354 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 421
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 422 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 500
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 501 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 574
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746520 575 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 638
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
32-178 |
1.32e-06 |
|
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: 51.17 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 32 QVENLKEKLisqAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCEAELQELRAQPVvPCQGCEhSQESTQLRDRL 111
Cdd:smart00787 141 LLEGLKEGL---DENLEGLKEDY--KLLMKELELLNSIKPKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746520 112 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLKAQS 178
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3-354 |
1.98e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHDSDRQATTTQL---QNQVENLKEKLISQAQEVSRLRSELGgtDVEKHRDRLMVENEQLRQELRR 79
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDLG--NAEDFLEELREERDELREREAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 80 CEAELQELR------------------AQPVvpcQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDrLAE 141
Cdd:PRK02224 431 LEATLRTARerveeaealleagkcpecGQPV---EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 142 VELRLKDcLAEKAqeeERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLK 221
Cdd:PRK02224 507 AEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 222 EMEQQLQNSHQLTIQLrAQIAMYEAELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHENLAGV 291
Cdd:PRK02224 583 ELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EAREDKERA 658
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746520 292 RTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 354
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-370 |
2.10e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 138 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 217
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 218 QVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 295
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746520 296 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 370
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-359 |
2.76e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQATTTQLQN-----QVENLKEKLISQAQEVSRLRSELggtdveKHRDRLMVENEQLRQE 76
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 77 LRRCEAELQELRAQPVVpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclaEKAQE 156
Cdd:COG4717 172 LAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 157 EERLSRRLRD--SHETIASLKAQSPPVKYVIKTV--------------EVESSKTKQALSESQTRNQHLQEQVAMQRQVL 220
Cdd:COG4717 242 EERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 221 KEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEMKAVHENLAgvrtnllTLQ 299
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVEDEEELRAAL-------EQA 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746520 300 PALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 359
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-340 |
5.50e-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: 50.17 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 38 EKLISQAQEVSRLRSELggtdvEKHRDRLMVENEQLRQELR--------------RCEAELQELRAQpvvpcqGCEHSQE 103
Cdd:pfam01576 359 EELTEQLEQAKRNKANL-----EKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQAR------LSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 104 STQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLKAQSP 179
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 180 PVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQLTIQLRAQIAMYEaELERAHGQMLEE 258
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYD-KLEKTKNRLQQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 259 MQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRG 318
Cdd:pfam01576 582 LDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQ 661
|
330 340
....*....|....*....|..
gi 1958746520 319 FPLLLqEALRSVKAEIGQAIEE 340
Cdd:pfam01576 662 LRAEM-EDLVSSKDDVGKNVHE 682
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1-301 |
7.45e-06 |
|
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: 49.95 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 1 MSQLQEELVVLRERLALHdsdrQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDVEKHRDRLMVENEQL------R 74
Cdd:COG3096 838 LAALRQRRSELERELAQH----RAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLADRLEELREELdaaqeaQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 75 QELRRCEAELQELRAQPVV----PCQGCEHSQESTQLRDRLSQLQL------EVAENK---------GML---SELNLEV 132
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVlqsdPEQFEQLQADYLQAKEQQRRLKQqifalsEVVQRRphfsyedavGLLgenSDLNEKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 133 QQKTDRlAEVELRLKDCLAEKAQEeerlsrRLRDSHETIASLKAqsppvkyviktveveSSKTK-QALSESQTRNQHL-- 209
Cdd:COG3096 990 RARLEQ-AEEARREAREQLRQAQA------QYSQYNQVLASLKS---------------SRDAKqQTLQELEQELEELgv 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 210 ---QEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEemqsLEED---KNRAIEEAFARAQVEMKA 283
Cdd:COG3096 1048 qadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK----AERDykqEREQVVQAKAGWCAVLRL 1123
|
330
....*....|....*...
gi 1958746520 284 VHENlaGVRTNLLTLQPA 301
Cdd:COG3096 1124 ARDN--DVERRLHRRELA 1139
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
21-309 |
9.22e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 21 DRQATTTQLQNQVENLKEKLISQAQ------EVSRLRSELGGTDVEKHRD--RLMVE----NEQLRQELRRC------EA 82
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRqeerkrELERIRQEEIAMEISRMREleRLQMErqqkNERVRQELEAArkvkilEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAQPVVPCQGCEHSQESTQLRDrLSQLQLEVAENKGMLSELNLEVQQKTDRL--AEVELRLKDCLAEKAQEEERL 160
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKLELEKEKRDRKR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 161 SRRLRDshetiaslkaqsppvkyviKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQlqnshqltiqlraq 240
Cdd:pfam17380 489 AEEQRR-------------------KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-------------- 535
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746520 241 iamYEAELERAHGQMLEEMQSLEEDKNRAIEE-----AFARAQVEMKAVHENLAG-----VRTNLLTLQPALRTLTNDY 309
Cdd:pfam17380 536 ---REAEEERRKQQEMEERRRIQEQMRKATEErsrleAMEREREMMRQIVESEKAraeyeATTPITTIKPIYRPRISEY 611
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-277 |
1.24e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCEA 82
Cdd:COG1196 320 ELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEAL--LEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSR 162
Cdd:COG1196 394 AAAELAAQ----------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 163 RLRDSHETIASLKAQSppvkyvikTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIA 242
Cdd:COG1196 464 LLAELLEEAALLEAAL--------AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
250 260 270
....*....|....*....|....*....|....*
gi 1958746520 243 MYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARA 277
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-180 |
1.33e-05 |
|
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: 48.22 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLIS--QAQEVSRLRSELGGTDVEKHRDRLMVE---NEQLRQE 76
Cdd:COG4942 72 RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLkylAPARREQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 77 LRRCEAELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQE 156
Cdd:COG4942 152 AEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
170 180
....*....|....*....|....
gi 1958746520 157 EERLSRRLRDSHETIASLKAQSPP 180
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
68-316 |
2.17e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 68 VENEQLRQELRRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQlevaenkGMLSELN-LEVQQKTDRLAEVELRL 146
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ------QQRSQLEQAKEGLSALN-------RLLPRLNlLADETLADRVEEIREQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 147 KDCLAEKA-----------------------QEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVE-------VESSKTK 196
Cdd:PRK04863 904 DEAEEAKRfvqqhgnalaqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKN 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 197 QALSES-QTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIamyeaeleRAHGQMLEE-MQSLEEDKNRAIEEAF 274
Cdd:PRK04863 984 SDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAE 1055
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746520 275 ARAQVEMKAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 316
Cdd:PRK04863 1056 ERARARRDELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-273 |
3.00e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 14 RLALHD--SDRQATTTQLQNQVE-----NLKEKLISQAQEVSRLRSELGGTDVEKHR--------DRLMVENEQLRQELR 78
Cdd:PRK02224 175 RLGVERvlSDQRGSLDQLKAQIEekeekDLHERLNGLESELAELDEEIERYEEQREQaretrdeaDEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 79 RCEAELQELRAQpvvpCQGCEHSQE--STQLRDRLSQLQLEVAENKGMLSELNLE------VQQKTDRLAEVELRLKDCL 150
Cdd:PRK02224 255 TLEAEIEDLRET----IAETEREREelAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 151 AEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNs 230
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN- 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958746520 231 hqltiqLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEA 273
Cdd:PRK02224 410 ------AEDFLEELREERDELREREAELEATLRTARER-VEEA 445
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
37-232 |
3.40e-05 |
|
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: 46.67 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 37 KEKLISQAQEVSRLRSELGGT-------DVEKHRDRLMVENEQLRQELRRCEAELQELRAQpvvpcqgceHSQESTQLRD 109
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEAQ---------QQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 110 RLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLKAQSpPVKYVIKTVE 189
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958746520 190 VESSKTKQALSESQTRNQHLQEQVAMQRQV----LKEMEQQLQNSHQ 232
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQG 212
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
20-241 |
3.58e-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: 47.32 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 20 SDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRLMVENEQ------------LRQELRRCEAELQEL 87
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeLEKQLNQLKSEISDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 88 RAQPVVPCQGCEHSQESTQlRDRLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDS 167
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746520 168 HETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQI 241
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI 442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-178 |
4.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHDSDRQATTTQLQ--NQVENLKEKLI---SQAQEVSRLRSELggTDVEKHRDRLmvenEQLRQEL 77
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIdvaSAEREIAELEAEL--ERLDASSDDL----AALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 78 RRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSElnLEVQQKTDRLAEVELRLKDCLAEKAqeE 157
Cdd:COG4913 695 EELEAELEELEEELD------ELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERFAAALGDAV--E 764
|
170 180
....*....|....*....|.
gi 1958746520 158 ERLSRRLRDSHETIASLKAQS 178
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
23-281 |
4.32e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 23 QATTTQLQNQVENLKEKL----ISQ-----AQEVSRLRSELggtdVEKHRDRLMVENEQLRQEL---RRCEAELqelraq 90
Cdd:PRK10929 172 QAQLTALQAESAALKALVdeleLAQlsannRQELARLRSEL----AKKRSQQLDAYLQALRNQLnsqRQREAER------ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 91 pvvpcqgcehSQESTQLrdrlsqlqleVAENKGMLSELNLEvQQKTDRlaevelRLKDCLAEKAQEEERLSRRLRdsheT 170
Cdd:PRK10929 242 ----------ALESTEL----------LAEQSGDLPKSIVA-QFKINR------ELSQALNQQAQRMDLIASQQR----Q 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 171 IASlkaQSPPVKYVIKTVEVESsktkQALSESQTRNQHLQEQVAMqrqvLKEME--QQLQNShqlTIQLRAQIAMYEAEL 248
Cdd:PRK10929 291 AAS---QTLQVRQALNTLREQS----QWLGVSNALGEALRAQVAR----LPEMPkpQQLDTE---MAQLRVQRLRYEDLL 356
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958746520 249 ERAHGQM---LEEMQSLEEDKNRaIEEAFARAQVEM 281
Cdd:PRK10929 357 NKQPQLRqirQADGQPLTAEQNR-ILDAQLRTQREL 391
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1-273 |
7.01e-05 |
|
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: 46.22 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 1 MSQLQEE-LVVLRERLALHDSDRQATTtqLQNQVENLKEklisQAQEV-SRLRSELGGTD---------------VEKHR 63
Cdd:pfam05622 154 VKLLEERnAEYMQRTLQLEEELKKANA--LRGQLETYKR----QVQELhGKLSEESKKADklefeykkleekleaLQKEK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 64 DRLMVENEQLRQ---ELRRCEAELQELRAQPVVPCQGCEHSQE------STQLRDRLSQLQLEvaeNKgMLSELnlEVQQ 134
Cdd:pfam05622 228 ERLIIERDTLREtneELRCAQLQQAELSQADALLSPSSDPGDNlaaeimPAEIREKLIRLQHE---NK-MLRLG--QEGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 135 KTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLKAQsppVKYVIKTVEVESSKT------KQALSESQTRNQH 208
Cdd:pfam05622 302 YRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746520 209 LQEQVAMQRQVLKEMEQQLQNSHQLTIqlraqiamyeAELERAHGQMLEEMQSLEEDKNRAIEEA 273
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-177 |
7.14e-05 |
|
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: 46.59 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELR 78
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEEALA 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 79 RCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 158
Cdd:TIGR02168 891 LLRSELEELSEELR------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
170
....*....|....*....
gi 1958746520 159 RLSRRLRDShetIASLKAQ 177
Cdd:TIGR02168 965 DDEEEARRR---LKRLENK 980
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
151-359 |
7.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 151 AEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 230
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 231 HQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 296
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746520 297 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 359
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-342 |
8.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 71 EQLRQELRRCEAELQELRAQpvvpCQGCEhsQESTQLRDRLSQLQ--LEVAENKGMLSELNLEVQQKTDRLAEVEL---- 144
Cdd:COG4913 613 AALEAELAELEEELAEAEER----LEALE--AELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 145 --RLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSE-----SQTRNQHLQEQV--AM 215
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 216 QRQVLKEMEQQLQNSHQltiQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 295
Cdd:COG4913 760 GDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958746520 296 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 342
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
5-359 |
1.00e-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: 46.10 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 5 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEkLISQAQEVSRLRSELGgTDVEKHRDRLMVENEQLRQE--LRRCEA 82
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLE-QDYQAASDHLNLVQTALRQQekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAQPVVPCQGCEHSQES-TQLRDRLSQLQLEVAENKGMLSEL----------NLEVQQKTDRLAEVELRL----- 146
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYqqaldvqqtrAIQYQQAVQALEKARALCglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 147 -----KDCLAE-KAQEEER------LSRRLRDSHETIASLKAQSPPVKYVIKTVEVES--SKTKQALSESQTRnQHLQEQ 212
Cdd:COG3096 435 tpenaEDYLAAfRAKEQQAteevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ-QALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 213 VAMQRQVLKEMEQQLQNSHQLTIQLraqiamyeAELERAHGQMLEEMQSLEEDKNRAiEEAFARAQVEMKAVHENLAGVR 292
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLL--------EEFCQRIGQQLDAAEELEELLAEL-EAQLEELEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 293 TNLLTLQPALRTLtndynglkRQVRGFPLLLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 359
Cdd:COG3096 585 QQLEQLRARIKEL--------AARAPAWLAAQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-326 |
1.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 1 MSQLQEELVVlrERLALHDSDRQAT--TTQLQN----------QVENLKEKLISQAQEVSRLRSElggtdvEKHRDRLMV 68
Cdd:pfam15921 477 LRKVVEELTA--KKMTLESSERTVSdlTASLQEkeraieatnaEITKLRSRVDLKLQELQHLKNE------GDHLRNVQT 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 69 ENEQLRQELRRCEAELQELRAQPVVPCQGC-EHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLK 147
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 148 DCLAEKA-----------------QEEERLSRRLRDSHETIASLKAQSPPVKYVIKT----VEVESSKTKQALSESQTrn 206
Cdd:pfam15921 629 DLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMETTTNKLKMQLKSAQS-- 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 207 qhlqeQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELErahgQMLEEMQSLEEDKNRAIEEAFARAQvEMKAVHE 286
Cdd:pfam15921 707 -----ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNANKEKHFLKE-EKNKLSQ 776
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958746520 287 NLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEA 326
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-220 |
1.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHdsdrqattTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRLMVENEQLRQELRRCEA 82
Cdd:COG4717 75 ELEEELKEAEEKEEEY--------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKgmlselnlevQQKTDRLAEVELRLKDCLAEKAQEEERLSR 162
Cdd:COG4717 147 RLEELEER----------LEELRELEEELEELEAELAELQ----------EELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746520 163 RLRDSHETIASLKAqsppvkyviktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVL 220
Cdd:COG4717 207 RLAELEEELEEAQE------------ELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
5-355 |
1.47e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 5 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRdrlmveneQLRQELRRCEAEL 84
Cdd:pfam07111 244 RQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPK--------KCRSLLNRWREKV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 85 QELRAQpvVPCQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAE--KAQEEERLSR 162
Cdd:pfam07111 316 FALMVQ--LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsRAQEARRRQQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 163 RLRDS--------------------------HETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVA-- 214
Cdd:pfam07111 394 QQTASaeeqlkfvvnamsstqiwlettmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPap 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 215 -MQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQvemkavhENLAGVRT 293
Cdd:pfam07111 474 pVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-------ESLASVGQ 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746520 294 NLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 355
Cdd:pfam07111 546 QLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-382 |
2.17e-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: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 132 VQQKTDRLAEVELRLKDC--LAEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEvESSKTKQALSESQTRNQHL 209
Cdd:COG4913 612 LAALEAELAELEEELAEAeeRLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 210 QEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE------MKA 283
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDaverelREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 284 VHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAIEEVNS-NNQELLRKYRRELQLRKKC 362
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYLALLDRlEEDGLPEYEERFKELLNEN 843
|
250 260
....*....|....*....|....*.
gi 1958746520 363 HNELV-----RLKGNIRVI-ARVRPV 382
Cdd:COG4913 844 SIEFVadllsKLRRAIREIkERIDPL 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
75-342 |
2.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 75 QELRRCEAELQELRAQPvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 152
Cdd:COG4717 71 KELKELEEELKEAEEKE----------EEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 153 KAQEEERLsRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTR-NQHLQEQVAMQRQVLKEMEQQLQNSH 231
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE-------LEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 232 QLTIQLRAQIAMYEAELERAhgqmleEMQSLEEDKNRAIEEAFARAQVemkavhenlAGVRTNLLTLQPALRTLTNDYNG 311
Cdd:COG4717 213 EELEEAQEELEELEEELEQL------ENELEAAALEERLKEARLLLLI---------AAALLALLGLGGSLLSLILTIAG 277
|
250 260 270
....*....|....*....|....*....|.
gi 1958746520 312 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 342
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
29-365 |
2.98e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 29 LQNQVENLKEKLISQAQEVSRL-RSELGGTDVEKHRDRLMVENEQLRQELRRCEAELQELRA----QPVVPCQGCEHSQE 103
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpnKKQLEDWLHSKSKE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 104 STQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE--ERLSRRLRDSHETIASLKAQSPPV 181
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGATAVY 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 182 KYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERahgq 254
Cdd:TIGR00606 666 SQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL---- 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 255 MLEEMQSLEEdKNRAIEEAFARAQVEMKAVHENLAGVRTNLLT---LQPALRTLTNDYNGLKRQVRGFPlllQEALRSVK 331
Cdd:TIGR00606 742 KEKEIPELRN-KLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvCLTDVTIMERFQMELKDVERKIA---QQAAKLQG 817
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958746520 332 AEIGQAIEEVNSNNQELLRKYRR---ELQLRKKCHNE 365
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTvvsKIELNRKLIQD 854
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
102-278 |
3.86e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 102 QESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 174
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 175 KAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEA---ELE 249
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 1958746520 250 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 278
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-374 |
4.39e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQatttqLQNQVENLK--------EKLISQAQEVSRLRSElggtdVEKHRDRLMVENEQL 73
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKA-----KKEELERLKkrltgltpEKLEKELEELEKAKEE-----IEEEISKITARIGEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 74 RQELRRCEAELQELR-AQPVVPCQGCEHSQES-------------------TQLRDRLSQLQLEVAENKGMLSELNLEVQ 133
Cdd:PRK03918 418 KKEIKELKKAIEELKkAKGKCPVCGRELTEEHrkelleeytaelkriekelKEIEEKERKLRKELRELEKVLKKESELIK 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 134 QKT--DRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQE 211
Cdd:PRK03918 498 LKElaEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIKLKGE-------IKSLKKELEKLEELKKKLAELEKKLDE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 212 QVAMQRQVLKEMEQqLQNSHQLTIQLRAQiamyeaELERAHGQMLEEMQSleEDKNRAIEEAFARAQVEMKAVHENLAGV 291
Cdd:PRK03918 568 LEEELAELLKELEE-LGFESVEELEERLK------ELEPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEELAET 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 292 RTNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVKAEIGQA---IEEVNSNNQEL------LRKYRRELQLRKK 361
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELekrREEIKKTLEKLkeeleeREKAKKELEKLEK 718
|
410
....*....|...
gi 1958746520 362 CHNELVRLKGNIR 374
Cdd:PRK03918 719 ALERVEELREKVK 731
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1-160 |
5.36e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 1 MSQLQEELVVLRERLalhdsdrqattTQLQNQVENLKEKLISQAQEVSRL-RSELGGTDVEKHRDRLMVENEQLRQELRR 79
Cdd:pfam13851 49 MSEIQQENKRLTEPL-----------QKAQEEVEELRKQLENYEKDKQSLkNLKARLKVLEKELKDLKWEHEVLEQRFEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 80 CEAELQELRAQpvvpcqgCEHS----QESTQLRDRLSQLQL----EVAENKGM-LSELNLEVQQKTDRLAEVELRLKDCL 150
Cdd:pfam13851 118 VERERDELYDK-------FEAAiqdvQQKTGLKNLLLEKKLqalgETLEKKEAqLNEVLAAANLDPDALQAVTEKLEDVL 190
|
170
....*....|
gi 1958746520 151 AEKAQEEERL 160
Cdd:pfam13851 191 ESKNQLIKDL 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
106-272 |
7.96e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 106 QLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIASLKAqsppvkYVI 185
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNKE------YEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 186 KTVEVESSKTKQALSESQTRNqhLQEQVAMQRQVLKEMEQQLQnshqltiQLRAQIAMYEAELERAHGQMLEEMQSLEED 265
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 1958746520 266 KNRAIEE 272
Cdd:COG1579 165 REELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
49-374 |
9.73e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 49 RLRSELGGTDVEKHRDRLMVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSEL 128
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 129 NLEVQQKTDRLAEVElrlkdclaekaQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQH 208
Cdd:COG4372 86 NEQLQAAQAELAQAQ-----------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 209 LQEQVAMQRQVLKEMEQQLQNshQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENL 288
Cdd:COG4372 155 LEEQLESLQEELAALEQELQA--LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 289 AGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 368
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
....*.
gi 1958746520 369 LKGNIR 374
Cdd:COG4372 313 LEDALL 318
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-289 |
1.02e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHDSDRQATTTQLQNQVEN----LKEKLISQAQEVSRLRSELGgtdvEKHRdrlmvENEQLRQELR 78
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIA----EKER-----ELEDAEERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 79 RCEAELQELRAqpvvpcqgcehsqESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 158
Cdd:TIGR02169 326 KLEAEIDKLLA-------------EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 159 RLS---RRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTI 235
Cdd:TIGR02169 393 KLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958746520 236 QLRAQIAMYEAELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 289
Cdd:TIGR02169 473 DLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2-238 |
1.10e-03 |
|
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: 42.19 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSE---LGGT--DVEKHRDRLMVENEQLRQE 76
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERakkAGAQrkEEEAERKQLQAKLQQTEEE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 77 LRRCEAELQELR-AQPVVPCQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELN-------------------------- 129
Cdd:pfam07888 187 LRSLSKEFQELRnSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaserkveglgeelssmaaq 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 130 ------------LEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLKA---------QSPPVKYVIKTV 188
Cdd:pfam07888 267 rdrtqaelhqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAelqrleerlQEERMEREKLEV 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958746520 189 EVESSKTKQALSESQTRNQhLQEQVAMQRQVLKEMEQQLQNSHQLTIQLR 238
Cdd:pfam07888 347 ELGREKDCNRVQLSESRRE-LQELKASLRVAQKEKEQLQAEKQELLEYIR 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
72-249 |
1.16e-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: 41.45 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 72 QLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 151
Cdd:COG1579 21 RLEHRLKELPAELAELE-------------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 152 EK-----AQEEERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVamqRQVLKEMEQQ 226
Cdd:COG1579 88 NKeyealQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAE 157
|
170 180
....*....|....*....|...
gi 1958746520 227 LQnshqltiQLRAQIAMYEAELE 249
Cdd:COG1579 158 LE-------ELEAEREELAAKIP 173
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
11-232 |
1.20e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 11 LRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL------------GGTDVEKHRDRLMVENEQLRQELR 78
Cdd:pfam10174 455 LKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLidlkehasslasSGLKKDSKLKSLEIAVEQKKEECS 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 79 RCEAELQelRAQpvvpcQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlKDCLAEKAQE-E 157
Cdd:pfam10174 535 KLENQLK--KAH-----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE-KNDKDKKIAElE 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746520 158 ERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQ--RQVLKEMEQQLQNSHQ 232
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEktRQELDATKARLSSTQQ 683
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-163 |
1.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHDSDRQATTTQLQNQVENL---------KEKLISQAQEVSRLRSELGGTDVEKHRDRLMVENEQL 73
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 74 RQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQL--QLEVAENKGMLSELNLEVQQKTDRLAEVE-----LRL 146
Cdd:COG4717 431 EEELEELEEELEELE-------------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAeewaaLKL 497
|
170
....*....|....*..
gi 1958746520 147 KDCLAEKAQEEERLSRR 163
Cdd:COG4717 498 ALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
15-176 |
1.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 15 LALHDSDRQATTTQLQNQVENLKEKL--ISQAQEVSRLRSELGGTDVEKHRDRLMV--ENEQLRQELRRCEAELQELRAq 90
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDEEELRAALEQaeEYQELKEELEELEEQLEELLG- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 91 pvvPCQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEveLRLKDCLAEKAQEEERLSRRLRDSHET 170
Cdd:COG4717 417 ---ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELRELAEE 491
|
....*.
gi 1958746520 171 IASLKA 176
Cdd:COG4717 492 WAALKL 497
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3-367 |
2.12e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 3 QLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRlmVENEQLRQELRRCEA 82
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS--SELEEMTKFKNNKEV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 83 ELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclAEKAQEEERLSR 162
Cdd:pfam05483 406 ELEELKKI----------LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEEHYLK 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 163 RLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIA 242
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 243 MYEAELERAHGQMLEEMQSLEEDKnRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpll 322
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA---- 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958746520 323 LQEALRSVKAEIGQAIEEVNSNNQ---ELLRKYRRELQLRKKCHNELV 367
Cdd:pfam05483 627 ENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1-166 |
2.93e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 1 MSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGtdVEKHRDRLMVENEQLRQELRRC 80
Cdd:PRK09039 55 LDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLAE--LAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 81 EAELQELRAQPVVpcqgceHSQESTQLRDRLSQLQ--LEVAENKGmlselnlevQQKTDRLAEVELRLKDCLAEKAQEee 158
Cdd:PRK09039 129 KQVSARALAQVEL------LNQQIAALRRQLAALEaaLDASEKRD---------RESQAKIADLGRRLNVALAQRVQE-- 191
|
170
....*....|....*
gi 1958746520 159 rLSR-------RLRD 166
Cdd:PRK09039 192 -LNRyrseffgRLRE 205
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
20-325 |
3.09e-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: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 20 SDRQATTTQ----LQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRlmVENEQL-----RQELRRCEAELQELRAQ 90
Cdd:TIGR00618 371 SCQQHTLTQhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR--DLQGQLahakkQQELQQRYAELCAAAIT 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 91 PVVPCQGCE--HSQESTQ-LRDRLSQLQ-----LEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSR 162
Cdd:TIGR00618 449 CTAQCEKLEkiHLQESAQsLKEREQQLQtkeqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 163 RLRDSHETIASLKAqsppvkyVIKTVEVE-SSKTKQA--LSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqLTIQLRA 239
Cdd:TIGR00618 529 RMQRGEQTYAQLET-------SEEDVYHQlTSERKQRasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN---ITVRLQD 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 240 QIAMyEAELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAgvrtnLLTLQPALRTLTNDYNGLK-RQVRG 318
Cdd:TIGR00618 599 LTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK-----LTALHALQLTLTQERVREHaLSIRV 669
|
....*..
gi 1958746520 319 FPLLLQE 325
Cdd:TIGR00618 670 LPKELLA 676
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2-177 |
4.09e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLALHDSDRQATTtQLQNQVENLKEKLISQAQEVSRlRSELGGTDVEKHRDRLMVENEQLRQELRRCE 81
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFEQLKQDYQ-QAQQTQRDAKQQAFALTEVVQR-RAHFSYEDAAEMLAKNSDLNEKLRQRLEQAE 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 82 aelqelraqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC-------LAEKA 154
Cdd:PRK04863 999 --------------------QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgAEERA 1058
|
170 180
....*....|....*....|....
gi 1958746520 155 QE-EERLSRRLRDSHETIASLKAQ 177
Cdd:PRK04863 1059 RArRDELHARLSANRSRRNQLEKQ 1082
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
159-282 |
4.40e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 159 RLSRRLRDshETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 228
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746520 229 -------NSHQLtIQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 282
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
71-294 |
5.59e-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: 40.11 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 71 EQLRQELRRCEAE----LQELRAQPVVPCQGCEH-SQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 145
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 146 LKdclaEKAQEEErlsrrlrDSHETIASLKAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 225
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746520 226 ---QLQNSHQLTIQLRAQIAMYEAELErahgqmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTN 294
Cdd:pfam05557 154 lrqNLEKQQSSLAEAEQRIKELEFEIQ------SQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN 219
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
600-765 |
5.68e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 39.89 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 600 VDLAGSERVGKSG---AEGNRLreAQHInRSLS-ALGDVI---------------AALRSRQGHVPFrNSKLT-----YL 655
Cdd:PRK08276 3 VIMAPSGEVVTYGeleARSNRL--AHGL-RALGlREGDVVaillennpeffevywAARRSGLYYTPI-NWHLTaaeiaYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 656 LQDSlsgDSKtlmVVQVSPVEKNTSETLYS-LKFAERVRSVELGPGSRRTELGSWSSQEhlewePACQTPQPTARAHSAP 734
Cdd:PRK08276 79 VDDS---GAK---VLIVSAALADTAAELAAeLPAGVPLLLVVAGPVPGFRSYEEALAAQ-----PDTPIADETAGADMLY 147
|
170 180 190
....*....|....*....|....*....|.
gi 1958746520 735 GSGTSSRPGSIRRKLQPSEREETALSQAWRL 765
Cdd:PRK08276 148 SSGTTGRPKGIKRPLPGLDPDEAPGMMLALL 178
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
66-278 |
5.77e-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: 39.93 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 66 LMVENEQLRQELRRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENkgMLSELNLEVQQKTDRLAEVELR 145
Cdd:pfam15709 324 LLEKREQEKASRDRLRAERAEMRRLEV------ERKRREQEEQRRLQQEQLERAEK--MREELELEQQRRFEEIRLRKQR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 146 LKDclAEKAQEEERLSRRLRdshETIASLKAQSPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQVLKE 222
Cdd:pfam15709 396 LEE--ERQRQEEEERKQRLQ---LQAAQERARQQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKRLME 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746520 223 MEQQlqnsHQLTIQLRAQiamyEAElERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 278
Cdd:pfam15709 471 MAEE----ERLEYQRQKQ----EAE-EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
103-362 |
5.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 103 ESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLKAQSppvk 182
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 183 yviKTVEVESSKTKQALSESQTRNQHL----------QEQVAMQRQVLKEMEQQLQNSHQltiQLRAQIAMYEAELERAh 252
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE---ECRVAAQAHNEEAESL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 253 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 332
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422
|
250 260 270
....*....|....*....|....*....|..
gi 1958746520 333 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 362
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
34-260 |
7.34e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 34 ENLKEKLISQAQEVSRLRSELggtdvekhRDRLMVENEQLRQELRRceaELQELRAQpvvpcqgcehSQESTQLRDRLSQ 113
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFSLLK--------KETIYLQSAQRVELAER---QLQELKID----------VKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 114 LQLEVAENKGML-SELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLKAQSPPVKYVIKTVEV 190
Cdd:COG5022 904 LESEIIELKKSLsSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTI 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 191 ESSKTKQALSESQTRNQHLQEQV----AMQRQV--LKEMEQQLQNSHQLTIQLRA-----QIAMYEAELERAHGQMLEEM 259
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQKLKGLLLLENNQL 1062
|
.
gi 1958746520 260 Q 260
Cdd:COG5022 1063 Q 1063
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
108-233 |
7.46e-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: 38.82 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 108 RDRLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLKA---QSPPV 181
Cdd:cd07627 34 RKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQRQKL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958746520 182 KYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQL 233
Cdd:cd07627 114 WQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASELKKE 165
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
129-357 |
7.59e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 129 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQ 197
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 198 ALSESQTRNQ--HLQEQVAMQRQVLKEMEQQLQnshqltiQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFA 275
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLA-------EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 276 RAQVEMKAvheNLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 352
Cdd:COG3206 270 AQLAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 1958746520 353 RRELQ 357
Cdd:COG3206 340 EARLA 344
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-354 |
8.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 2 SQLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKL-ISQAQEVSRLRSELggtdvekhrDRLMVENEQLRQELRRC 80
Cdd:COG4717 159 RELEEELEELEAELA-----------ELQEELEELLEQLsLATEEELQDLAEEL---------EELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 81 EAELQELRAQpvvpCQGCEHSQESTQLRDRLSQLQL----------------EVAENKGMLSELNLEVQQKTDRLAEVEL 144
Cdd:COG4717 219 QEELEELEEE----LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 145 RLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyviktVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEME 224
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAA----------LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 225 QQLQNSHQLTIQLRAQIAMyEAELERAHGQmLEEMQSLEEDKNRAIEE-AFARAQVEMKAVHENLAGVRTNLLTLQPALR 303
Cdd:COG4717 365 LEELEQEIAALLAEAGVED-EEELRAALEQ-AEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELE 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958746520 304 TLTNDYNGLKRQVRGFPLLLQEALRSVK-AEIGQAIEEVNSNNQELLRKYRR 354
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAA 494
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
163-370 |
9.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 163 RLRDSHETIASLKAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 229
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 230 SH-----QLTIQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 297
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746520 298 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 370
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
5-377 |
9.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 5 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQLRQELRRCEAEL 84
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL---------EQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 85 QELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRL 164
Cdd:COG4372 83 EELNEQLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 165 RDSHETIASLKAQSPPVKYVIKtvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMY 244
Cdd:COG4372 157 EQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746520 245 EAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 324
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958746520 325 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIA 377
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| |
