|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
548-875 |
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: 533.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 548 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 626
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 627 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 703
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 704 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 783
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 784 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 863
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 568956232 864 LRFAERVRSVEL 875
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
556-873 |
1.68e-147 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 439.70 E-value: 1.68e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 556 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 632
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 633 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 712
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 713 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 789
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 790 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFA 867
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 568956232 868 ERVRSV 873
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
550-877 |
1.18e-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: 427.37 E-value: 1.18e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 625
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 626 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 705
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 706 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 783
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 784 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 861
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 568956232 862 YSLRFAERVRSVELGP 877
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
550-871 |
1.52e-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: 377.37 E-value: 1.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 626
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 627 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 704
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 705 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 782
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 783 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 861
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 568956232 862 YSLRFAERVR 871
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
550-873 |
8.11e-106 |
|
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: 331.35 E-value: 8.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 621
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 622 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 698
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 699 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 774
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 775 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 853
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 568956232 854 EKNTSETLYSLRFAERVRSV 873
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
551-874 |
6.67e-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: 323.90 E-value: 6.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 551 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 628
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 629 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 702
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 703 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 772
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 773 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 849
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 568956232 850 VSPVEKNTSETLYSLRFAERVRSVE 874
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
550-873 |
3.90e-94 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 301.19 E-value: 3.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 612
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 613 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 691
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 692 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 770
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 771 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 845
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 568956232 846 MVVQVSPVEKNTSETLYSLRFAERVRSV 873
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
550-873 |
4.35e-91 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 292.31 E-value: 4.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 627
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 628 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 704
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 705 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 784
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 785 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 863
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 568956232 864 LRFAERVRSV 873
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
549-873 |
1.22e-89 |
|
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: 289.64 E-value: 1.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 549 GNIRVIARVRPVTKEDGEGPeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQE 613
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 614 VQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDLL 691
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 692 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 766
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 767 TGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 836
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 568956232 837 SLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSV 873
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
550-873 |
8.63e-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: 285.77 E-value: 8.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 628
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 629 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 708
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 709 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 784
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 785 RVGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 862
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 568956232 863 SLRFAERVRSV 873
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
550-873 |
3.15e-86 |
|
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: 280.37 E-value: 3.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 624
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 625 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 693
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 694 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 768
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 769 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 848
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 568956232 849 QVSPVEKNTSETLYSLRFAERVRSV 873
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
534-874 |
8.93e-81 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 272.77 E-value: 8.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 534 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 613
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 614 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 692
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 693 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 772
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 773 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 850
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 568956232 851 SPVEKNTSETLYSLRFAERVRSVE 874
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
551-868 |
3.96e-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: 255.40 E-value: 3.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 551 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 619
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 620 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 695
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 696 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 770
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 771 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 842
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 568956232 843 KTLMVVQVSPVEKNTSETLYSLRFAE 868
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
550-871 |
1.44e-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: 253.97 E-value: 1.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 628
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 629 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgkEP- 695
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 696 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 772
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 773 gKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 848
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 568956232 849 QVSPVEKNTSETLYSLRFAERVR 871
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
550-871 |
2.46e-71 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 238.94 E-value: 2.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 626
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 627 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 706
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 707 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 785
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 786 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLR 865
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 568956232 866 FAERVR 871
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
551-871 |
1.14e-70 |
|
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: 237.48 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 551 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 619
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 620 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 696
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 697 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 771
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 772 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 850
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 568956232 851 SPVEKNTSETLYSLRFAERVR 871
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
550-870 |
2.40e-66 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 225.64 E-value: 2.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 550 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 621
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 622 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 697
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 698 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 777
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 778 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 855
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 568956232 856 NTSETLYSLRFAERV 870
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
551-874 |
1.06e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 216.34 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 551 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 629
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 630 FAYGQTGAGKTYTMEGtPENP-----------GINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLgk 693
Cdd:PLN03188 170 FAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 694 EP-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLR 770
Cdd:PLN03188 247 DPsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 771 T--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSK 843
Cdd:PLN03188 325 SfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAK 404
|
330 340 350
....*....|....*....|....*....|.
gi 568956232 844 TLMVVQVSPVEKNTSETLYSLRFAERVRSVE 874
Cdd:PLN03188 405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
530-691 |
2.21e-42 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 151.22 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 530 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 609
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 610 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 689
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 568956232 690 LL 691
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
598-817 |
7.01e-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: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 598 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 676
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 677 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 756
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956232 757 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 817
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-494 |
8.43e-14 |
|
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: 75.87 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 181 QLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELRRCEV 260
Cdd:TIGR02169 671 SEPAELQRLRERLE-----------GLKRELSSLQSELRRIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 261 ELQELRAQ--------PVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLS------------ELNLEVQQKTDRLAEV 320
Cdd:TIGR02169 738 RLEELEEDlssleqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 321 ELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV 397
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 398 LKEMEQQLQ---------NSHQLTVQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEEDKNRA 447
Cdd:TIGR02169 898 LRELERKIEeleaqiekkRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLA 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568956232 448 IE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 494
Cdd:TIGR02169 978 IQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-534 |
6.86e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 207 LQNQVENLKEKlISQAQEVSRLRSELggtdAEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLR 286
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAEL----RELELALLVLRLEELREELEELQEELKEAE-------------EELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 287 DKLSQLQLEVAENKGMLSELNLEVQQKTDRLaeveLRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTV 366
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 367 EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT--------------VQLRAQIAMYEAELER--AH 430
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 431 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 510
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330 340
....*....|....*....|....*.
gi 568956232 511 EIGQAIEEVNS--NNQELLRKYRREL 534
Cdd:TIGR02168 483 ELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-458 |
3.85e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELR 256
Cdd:COG1196 246 AELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 257 RCEVELQELRAQpvvpcegcehsqeSSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 336
Cdd:COG1196 320 ELEEELAELEEE-------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 337 RLSRRLRDSHETIASLRAQsppvKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 416
Cdd:COG1196 387 ELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568956232 417 AQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 458
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-451 |
4.81e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 70.05 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 189 LRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQ 268
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 269 pvvpcegcehsqessqlrdkLSQLQLEVAENKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 346
Cdd:COG3206 242 --------------------LAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 347 ETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAe 425
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV- 362
|
250 260
....*....|....*....|....*.
gi 568956232 426 LERAHGQMLEEMQSLEEDKNRAIEEA 451
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-536 |
1.89e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 204 TTQLQNQVENLKEKLiSQAQEVSRLRSELGGTDAE---KHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehsq 280
Cdd:COG1196 195 LGELERQLEPLERQA-EKAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAE------------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 281 essqlrdkLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvk 360
Cdd:COG1196 262 --------LAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEE----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 361 yvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSL 440
Cdd:COG1196 325 --LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 441 EEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEE 518
Cdd:COG1196 403 EELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAA 478
|
330
....*....|....*...
gi 568956232 519 VNSNNQELLRKYRRELQL 536
Cdd:COG1196 479 LAELLEELAEAAARLLLL 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
177-526 |
6.67e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTT---QLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHR--DRLM---VEN 248
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTerdQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlwDRDTgnsITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRCEVELQELRAQPVVPCEGCEHSQE--------SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEV 320
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMErqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 321 ELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQRQVLK 399
Cdd:pfam15921 495 ERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 400 EMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENL 466
Cdd:pfam15921 566 ILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERL 645
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 467 AGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 526
Cdd:pfam15921 646 RAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-456 |
2.08e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELR 256
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERLEELEEEL---------AELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 257 RCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 336
Cdd:COG1196 341 ELEEELEEAEEE----------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 337 RLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 416
Cdd:COG1196 411 ALLERLERLEEELEELEEA-------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568956232 417 AQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFARAQ 456
Cdd:COG1196 484 EELAEAAARLL-----LLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-355 |
3.14e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTTQL-QNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN------- 248
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARL--DALREELDELEAQIrgnggdr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 -EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC 327
Cdd:COG4913 340 lEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 568956232 328 LAEKAQEEERLSRRLRDSHETIASLRAQ 355
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-580 |
4.37e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 279 SQESSQL--RDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 356
Cdd:TIGR02168 667 KTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 357 PPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG----- 431
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanl 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 432 ----QMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRS 507
Cdd:TIGR02168 823 rerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRS 894
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956232 508 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI-RVIARVRPVTKEDGEGPEA-TNAVTFDPDD 580
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEAlENKIEDDEEE 969
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
188-556 |
9.06e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 188 VLRERLALHDSDR-----QATTTQLQNQVENLkEKLISQAQEVSRLRSELGGTDAEKHR--DRLMVENEQLRQELRRCEV 260
Cdd:PRK03918 150 VVRQILGLDDYENayknlGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 261 ELQELRAqpvvpcegcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEK 331
Cdd:PRK03918 229 EVKELEE-----------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 332 AQEEERLSR-------RLRDSHETIASLRAQSPPVKYVIKtvevESSKTKQALSESQTRNQHLQEQVAmqrqVLKEMEQQ 404
Cdd:PRK03918 292 AEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 405 LQNSHQLTVQ---LRAQIAMYEAE--------LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----- 458
Cdd:PRK03918 364 YEEAKAKKEElerLKKRLTGLTPEklekeleeLEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcg 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 459 -----------MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELL 527
Cdd:PRK03918 443 relteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEEL 520
|
410 420
....*....|....*....|....*....
gi 568956232 528 RKYRRELQLRKKchnELVRLKGNIRVIAR 556
Cdd:PRK03918 521 EKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
532-816 |
2.22e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 57.83 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 532 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 599
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 600 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 678
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 679 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 752
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956232 753 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 816
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
172-549 |
2.27e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 172 VHRTVEAMSQLQEELVVLRERLALHDSDR---QATTTQLQNQVENLKEKLISQAQEVSRLRsELGGtDAEKHRdRLMVEN 248
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELK-ELKE-KAEEYI-KLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRCEVEL----QELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNlEVQQKTDRLAEVELRL 324
Cdd:PRK03918 303 EEYLDELREIEKRLsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 325 KDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTV-----EVESSKTKQALSESQTRNQHLQEQVAMQRQVL 398
Cdd:PRK03918 382 TGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELkkaieELKKAKGKCPVCGRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 399 KEMEQQLQNSHQLTVQLRAQIAMYEAELER-----AHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNL 473
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956232 474 LTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKG 549
Cdd:PRK03918 542 KSLKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-537 |
4.35e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 173 HRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQN-----QVENLKEKLISQAQEVSRLRSELggtdaeKHRDRLMVE 247
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 248 NEQLRQELRRCEVELQELRAQPVVpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdc 327
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 328 laEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQTRNQHLQEQV 391
Cdd:COG4717 237 --EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 392 AMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVemkavhENLAGVR 470
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGV------EDEEELR 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956232 471 tNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 537
Cdd:COG4717 389 -AALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
206-429 |
5.33e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 206 QLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLmvenEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQL 285
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQL-----AALERRI----AALARRIRALEQELAALE-------------AELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 286 RDKLSQLQLEVAENKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLRAQSPP 358
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956232 359 VKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERA 429
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-453 |
5.54e-08 |
|
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: 56.99 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 172 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLqnqvENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQL 251
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELAEELAELEEKL---------EELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 252 RQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLaevelrlkdclaEK 331
Cdd:TIGR02168 357 EAELEELEAELEELESRLE------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR------------ER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 332 AQEEERLSRRLRDSHEtiaslraqsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQnshql 411
Cdd:TIGR02168 419 LQQEIEELLKKLEEAE---------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD----- 478
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568956232 412 tvQLRAQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFA 453
Cdd:TIGR02168 479 --AAERELAQLQARLD-----SLERLQENLEGFSEGVKALLK 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
216-518 |
6.38e-08 |
|
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: 56.72 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 216 EKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELR--------------RCEVELQELRAQpvvpceGCEHSQE 281
Cdd:pfam01576 359 EELTEQLEQAKRNKANL-----EKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQAR------LSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 282 SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSP 357
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 358 PVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQLTVQLRAQIAMYEaELERAHGQMLEE 436
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYD-KLEKTKNRLQQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 437 MQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRG 496
Cdd:pfam01576 582 LDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQ 661
|
330 340
....*....|....*....|..
gi 568956232 497 FPLLLqEALRSVKAEIGQAIEE 518
Cdd:pfam01576 662 LRAEM-EDLVSSKDDVGKNVHE 682
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-535 |
7.07e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 199 DRQATTtqLQNQVENLKEKLISQAQEVSRLRSELG---------GTDAEKHRDRLMVENEQLRQE--LRRCEVELQELRA 267
Cdd:PRK04863 285 LEEALE--LRRELYTSRRQLAAEQYRLVEMARELAelneaesdlEQDYQAASDHLNLVQTALRQQekIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 268 QPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKD 326
Cdd:PRK04863 363 RLEEQNEVVEEADEQqEENEARAEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 327 CLAE-KAQEEERLSRRLR-----DSHETIASLRAQSppVKYVIKTV-EVESSKTKQALSE--SQTRNQ-HLQEQVAMQRQ 396
Cdd:PRK04863 443 WLEEfQAKEQEATEELLSleqklSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 397 VLKEMEQQLQNsHQLTVQLRAQ-----IAMY--EAELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLA 467
Cdd:PRK04863 521 RLSELEQRLRQ-QQRAERLLAEfckrlGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956232 468 GVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 535
Cdd:PRK04863 600 ARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-431 |
1.22e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 173 HRTVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLR 252
Cdd:COG1196 291 YELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEEL---------EEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 253 QELRRCEVELQELRAQpvvpcegcEHSQESSQLRDKLSQLQLEVAEnkgmlSELNLEVQQKTDRLAEVELRLKDCLAEKA 332
Cdd:COG1196 358 AELAEAEEALLEAEAE--------LAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 333 QEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT 412
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEA------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250
....*....|....*....
gi 568956232 413 VQLRAQIAMYEAELERAHG 431
Cdd:COG1196 487 AEAAARLLLLLEAEADYEG 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
237-468 |
1.49e-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: 54.77 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 237 AEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDR 316
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 317 LAEVELRLKDCLAEKAQEEERLSRRLR-----DSHETIASLRAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQH 386
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 387 LQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENL 466
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERT 243
|
..
gi 568956232 467 AG 468
Cdd:COG4942 244 PA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
243-519 |
2.16e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 243 RLMVENeqlRQELRRCEVELQELRAQpvvpcegCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVEL 322
Cdd:COG4913 228 DALVEH---FDDLERAHEALEDAREQ-------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 323 -RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQRQVLKE 400
Cdd:COG4913 298 eELRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 401 MEQQLQNSHQLTVQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPAL 480
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956232 481 RTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 519
Cdd:COG4913 422 RELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
210-356 |
2.81e-07 |
|
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: 53.48 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 210 QVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvPCEGCEhSQESSQLRDKL 289
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLL-----MKELELLNSIKPKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956232 290 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 356
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
198-539 |
3.14e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 198 SDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQ------------LRQELRRCEVELQEL 265
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeLEKQLNQLKSEISDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 266 RAQPVVPCEGCEHSQESSQlRDKLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDS 345
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 346 HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIamyeAE 425
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 426 LErahgqmlEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQ 502
Cdd:TIGR04523 445 LT-------NQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK----ELE 509
|
330 340 350
....*....|....*....|....*....|....*..
gi 568956232 503 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 539
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
162-479 |
4.42e-07 |
|
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: 54.19 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 162 LSGAPGPDPVvhrtvEAMSQLQEELVVLRERLALHdsdrQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHR 241
Cdd:COG3096 826 LAVAFAPDPE-----AELAALRQRRSELERELAQH----RAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLA 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 242 DRLmvenEQLRQELRRCEVELQELRaqpvvpcegcEHSQESSQLRDKLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVE 321
Cdd:COG3096 893 DRL----EELREELDAAQEAQAFIQ----------QHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLK 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 322 LRLkDCLAEKAQEEERLS-----RRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTR-NQHLQEQVAMQ- 394
Cdd:COG3096 955 QQI-FALSEVVQRRPHFSyedavGLLGENSDLNEKLRAR-------LEQAEEARREAREQLRQAQAQySQYNQVLASLKs 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 395 -----RQVLKEMEQ--------------------------QLQNSHQLTVQLRAQIAMYEAELERAHGQMLEemqsLEED 443
Cdd:COG3096 1027 srdakQQTLQELEQeleelgvqadaeaeerarirrdelheELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK----AERD 1102
|
330 340 350
....*....|....*....|....*....|....*....
gi 568956232 444 ---KNRAIEEAFARAQVEMKAVHENlaGVRTNLLTLQPA 479
Cdd:COG3096 1103 ykqEREQVVQAKAGWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
157-504 |
1.09e-06 |
|
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: 52.81 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 157 GRCSSLSGAPGPDPVVHRTVEAMSQLQEELVVlrERLALHDSDRQAT--TTQLQN----------QVENLKEKLISQAQE 224
Cdd:pfam15921 455 GKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSdlTASLQEkeraieatnaEITKLRSRVDLKLQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 225 VSRLRSElggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQ--PVVPCEGcEHSQESSQLRDKLSQLQLEVAENKGM 302
Cdd:pfam15921 533 LQHLKNE------GDHLRNVQTECEALKLQMAEKDKVIEILRQQieNMTQLVG-QHGRTAGAMQVEKAQLEKEINDRRLE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 303 LSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLRAQSPPVKYVIKT 365
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 366 ----VEVESSKTKQALSESQTrnqhlqeQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELErahgQMLEEMQSLE 441
Cdd:pfam15921 686 kseeMETTTNKLKMQLKSAQS-------ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLE 754
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956232 442 EDKNRAIEEAFARAQvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEA 504
Cdd:pfam15921 755 EAMTNANKEKHFLKE-EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
174-487 |
1.48e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 174 RTVEAMSQLQEElvvlrERLALHDSDRQATTTQLQNQVENLKEKLISQAQ------EVSRLRSELGGTDAEKHRD--RLM 245
Cdd:pfam17380 310 REVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERELERIRqeerkrELERIRQEEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 246 VE----NEQLRQELRRC------EVELQELRAQPVVPCEGCEHSQESSQLRDkLSQLQLEVAENKGMLSELNLEVQQKTD 315
Cdd:pfam17380 385 MErqqkNERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 316 RL--AEVELRLKDCLAEKAQEEERLSRRLRDshetiaslraqsppvkyviKTVEVESSKTKQALSESQTRNQHLQEQVAM 393
Cdd:pfam17380 464 RLrqQEEERKRKKLELEKEKRDRKRAEEQRR-------------------KILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 394 QRQVLKEMEQQlqnshqltvqlraqiamYEAELERAHGQMLEEMQSLEEDKNRAIEE-----AFARAQVEMKAVHENLAG 468
Cdd:pfam17380 525 RQKAIYEEERR-----------------REAEEERRKQQEMEERRRIQEQMRKATEErsrleAMEREREMMRQIVESEKA 587
|
330 340
....*....|....*....|....
gi 568956232 469 -----VRTNLLTLQPALRTLTNDY 487
Cdd:pfam17380 588 raeyeATTPITTIKPIYRPRISEY 611
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
316-548 |
1.78e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 316 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 395
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 396 QVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 473
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956232 474 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 548
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
215-410 |
2.34e-06 |
|
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: 50.53 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 215 KEKLISQAQEVSRLRSELGGT-------DAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegceHSQESSQLRD 287
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEAQ---------QQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 288 KLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 367
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568956232 368 VESSKTKQALSESQTRNQHLQEQVAMQRQV----LKEMEQQLQNSHQ 410
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQG 212
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
177-465 |
5.64e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLmvenEQLRQELR 256
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ----QQRSQLEQAKEGL----SALNRLLPRLNLLADETLADRV----EEIREQLD 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 257 RCEVELQELRAQPVVpCEGCEhsQESSQLR---DKLSQLQLEVAENKGMLSElnleVQQKTDRLAEVELRL--------K 325
Cdd:PRK04863 905 EAEEAKRFVQQHGNA-LAQLE--PIVSVLQsdpEQFEQLKQDYQQAQQTQRD----AKQQAFALTEVVQRRahfsyedaA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 326 DCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEM---- 401
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQ-------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpa 1050
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956232 402 ---------------EQQLQNSHQLTVQLRAQIAMYEAELERAHGQmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHEN 465
Cdd:PRK04863 1051 dsgaeerararrdelHARLSANRSRRNQLEKQLTFCEAEMDNLTKK-LRKLERDYHEMREQVVNAKAGWCAVLRLVKDN 1128
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-355 |
5.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQ 253
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 254 ELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQ 333
Cdd:TIGR02168 888 ALALLRSELEELSEELR------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
170 180
....*....|....*....|..
gi 568956232 334 EEERLSRRLRDShetIASLRAQ 355
Cdd:TIGR02168 962 KIEDDEEEARRR---LKRLENK 980
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
173-537 |
5.65e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 173 HRTVEAMSQLQEELVVLRERLALHDSDR--------QATTTQLQNQVENLKEKLISQAQEVSRLR---SELGGTDA---- 237
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKlekeleelEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 238 ------EKHRDRLM----VENEQLRQELRRCEVELQELRAQpVVPCEGcEHSQESSQLRDKLSQLQLEVAENKgmLSELN 307
Cdd:PRK03918 441 cgreltEEHRKELLeeytAELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESELIKLKELAEQLKELEEK--LKKYN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 308 LEVQQKTDRLAEvelRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppVKYVIKTVEVESSKTKQALSES-----QT 382
Cdd:PRK03918 517 LEELEKKAEEYE---KLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELgfesvEE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 383 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMK 460
Cdd:PRK03918 590 LEERLKELEPFYNEYleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 461 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAE---IGQAIEEVnSNNQELLRKYRRELQLR 537
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKElekLEKALERV-EELREKVKKYKALLKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-358 |
5.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 174 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLIS--QAQEVSRLRSELGGTDAEKHRDRLMVE---N 248
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLkylA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 328
Cdd:COG4942 146 PARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|
gi 568956232 329 AEKAQEEERLSRRLRDSHETIASLRAQSPP 358
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
179-451 |
8.71e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.30 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 179 MSQLQEE-LVVLRERLALHDSDRQATTtqLQNQVENLKEklisQAQEV-SRLRSELGGTD---------------AEKHR 241
Cdd:pfam05622 154 VKLLEERnAEYMQRTLQLEEELKKANA--LRGQLETYKR----QVQELhGKLSEESKKADklefeykkleekleaLQKEK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 242 DRLMVENEQLRQ---ELRRCEVELQELRAQPVVPCEGCEHSQE------SSQLRDKLSQLQLEvaeNKgMLSELnlEVQQ 312
Cdd:pfam05622 228 ERLIIERDTLREtneELRCAQLQQAELSQADALLSPSSDPGDNlaaeimPAEIREKLIRLQHE---NK-MLRLG--QEGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 313 KTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVESSKT------KQALSESQTRNQH 386
Cdd:pfam05622 302 YRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956232 387 LQEQVAMQRQVLKEMEQQLQNSHQLTVqlraqiamyeAELERAHGQMLEEMQSLEEDKNRAIEEA 451
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-537 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 329 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 408
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 409 HQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 474
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956232 475 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 537
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
259-537 |
1.35e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 259 EVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQlEVAENkgmLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERL 338
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEE---LEQLREELEQAREELEQLEEELE----QARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 339 SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQ 418
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 419 IAMYEAELERAHGQMLEEMQsleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFP 498
Cdd:COG4372 159 LESLQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956232 499 LLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 537
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
184-441 |
1.67e-05 |
|
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: 48.81 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 184 EELVVLRERLALHDSDRQATTTQLQNQvENLKEKLISQAQEVSRLRSELggtdaekhrdrlmvenEQLRQELRRCEVELQ 263
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI----------------EEQRRLLQTLHSQEI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 264 ELRAQPVVPCEGCEHSQESSQLRDKLSQLQlevaENKGMLSELNLEVQQKTDRLAEvelrlkdclaEKAQEEERLSRRlR 343
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKELDILQR----------EQATIDTRTSAF-R 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 344 DSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQTRNQHLQEqvamQRQVLKEMEQQLQNSHQLTVQlraqiamyE 423
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE----SAQSLKEREQQLQTKEQIHLQ--------E 485
|
250
....*....|....*...
gi 568956232 424 AELERAHGQMLEEMQSLE 441
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEP 503
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
173-541 |
1.88e-05 |
|
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: 48.81 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 173 HRTVEAMSQLQEELVVLRERLALHDSDRQATTtQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQL- 251
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR--DLQGQLa 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 252 ----RQELRRCEVELQELRAQPVVPCEGCE--HSQESSQ-LRDKLSQLQ-----LEVAENKGMLSELNLEVQQKTDRLAE 319
Cdd:TIGR00618 428 hakkQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQsLKEREQQLQtkeqiHLQETRKKAVVLARLLELQEEPCPLC 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 320 VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyVIKTVEVE-SSKTKQA--LSESQTRNQHLQEQVAMQRQ 396
Cdd:TIGR00618 508 GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET-------SEEDVYHQlTSERKQRasLKEQMQEIQQSFSILTQCDN 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 397 VLKEMEQQLQNshqLTVQLRAQIAMyEAELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAgvrtnLLTL 476
Cdd:TIGR00618 581 RSKEDIPNLQN---ITVRLQDLTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK-----LTAL 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956232 477 QPALRTLTNDYNGLK-RQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCH 541
Cdd:TIGR00618 649 HALQLTLTQERVREHaLSIRVLPKELLAsrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
246-494 |
2.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 246 VENEQLRQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQlevaenkGMLSELN-LEVQQKTDRLAEVELRL 324
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ------QQRSQLEQAKEGLSALN-------RLLPRLNlLADETLADRVEEIREQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 325 KDclAEKAQ-----------EEERLSRRLRDSHETIASLRAQSPPVKYVIKTV--------EVESSKTKQALSESQ---T 382
Cdd:PRK04863 904 DE--AEEAKrfvqqhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAkqqafaltEVVQRRAHFSYEDAAemlA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 383 RNQHLQEQVamqRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE------RAHGQMLEE-MQSLEEDKNRAIEEAFARA 455
Cdd:PRK04863 982 KNSDLNEKL---RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLAslkssyDAKRQMLQElKQELQDLGVPADSGAEERA 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568956232 456 QVEMKAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 494
Cdd:PRK04863 1059 RARRDELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
177-467 |
2.62e-05 |
|
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: 48.14 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVEN----LKEKLISQAQEVSRLRSELggtdAEKHRdrlmvENEQLR 252
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSI----AEKER-----ELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 253 QELRRCEVELQELRAQpvvpCEGCEHSQESSQLRdkLSQLQLEVAENKgmlSELNLEVQqktdRLAEVELRLKDCLAEKA 332
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAE----IEELEREIEEERKR--RDKLTEEYAELK---EELEDLRA----ELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 333 QEEERLS---RRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSH 409
Cdd:TIGR02169 389 DYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956232 410 QLTVQLRAQIAMYEAELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 467
Cdd:TIGR02169 469 QELYDLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
170-533 |
3.26e-05 |
|
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: 47.82 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 170 PVVHRtvEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRdrlmvene 249
Cdd:pfam07111 233 PEVHS--QTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPK-------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 250 QLRQELRRCEVELQELRAQpvVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 329
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQ--LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQM 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 330 E--KAQEEERLSRRLRDS--------------------------HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQ 381
Cdd:pfam07111 381 ElsRAQEARRRQQQQTASaeeqlkfvvnamsstqiwlettmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 382 TRNQHLQEQVA---MQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQve 458
Cdd:pfam07111 461 LRQESCPPPPPappVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956232 459 mkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 533
Cdd:pfam07111 538 -----ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
175-544 |
3.58e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 175 TVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSE---------LGGTDAE---KHRD 242
Cdd:PRK02224 242 VLEEHEERREELETLEAEIE----DLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagLDDADAEaveARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 243 RLMVENEQLRQELRRCEVELQELRAQPVVPCEGC-EHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 321
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDAdDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 322 LRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE--------------VESSKTKQALSESQTRN 384
Cdd:PRK02224 398 ERFGDApvdLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERV 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 385 QHLQEQVAMQRQVLKEMEQQLQNSHQLtVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIE--------EAFARAQ 456
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEElreraaelEAEAEEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 457 VE-MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRqvrgfplllQEALRSVKAEIGQAIEEVNSNNQEL--LRKYRRE 533
Cdd:PRK02224 557 REaAAEAEEEAEEAREEVAELNSKLAELKERIESLER---------IRTLLAAIADAEDEIERLREKREALaeLNDERRE 627
|
410
....*....|..
gi 568956232 534 -LQLRKKCHNEL 544
Cdd:PRK02224 628 rLAEKRERKREL 639
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
119-456 |
3.72e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 119 KEDELPKRQAPAPRRDREAPEAGGTMNVENTGGRL---------FGIGRCSSLSGAPGPDPvvhrtvEAMSQLQEELVVL 189
Cdd:pfam15709 220 KSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVinsketedaSERGAFSSDSVVEDPWL------SSKYDAEESQVSI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 190 RERLAlhdSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSElggtdaeKHRDRLMVEneqlRQELRRCEVELQElraqp 269
Cdd:pfam15709 294 DGRSS---PTQTFVVTGNMESEEERSEEDPSKALLEKREQEK-------ASRDRLRAE----RAEMRRLEVERKR----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 270 vvpcegcehsQESSQLRdKLSQLQLEVAENkgMLSELNLEVQQKTDRLAEVELRLKDclAEKAQEEERLSRRLRdshETI 349
Cdd:pfam15709 355 ----------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQ---LQA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 350 ASLRAQSPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQVLKEMEQQlqnsHQLTVQLRAQiamyEAEl 426
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKRLMEMAEE----ERLEYQRQKQ----EAE- 487
|
330 340 350
....*....|....*....|....*....|
gi 568956232 427 ERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 456
Cdd:pfam15709 488 EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-356 |
4.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 181 QLQEELVVLRERLALHDSDRQATTTQLQ--NQVENLKEKLI---SQAQEVSRLRSELggTDAEKHRDRLmvenEQLRQEL 255
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIdvaSAEREIAELEAEL--ERLDASSDDL----AALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 256 RRCEVELQELRAQpvvpCEGCEhsQESSQLRDKLSQLQLEVAENKGMLSElnLEVQQKTDRLAEVELRLKDCLAEKAqeE 335
Cdd:COG4913 695 EELEAELEELEEE----LDELK--GEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERFAAALGDAV--E 764
|
170 180
....*....|....*....|.
gi 568956232 336 ERLSRRLRDSHETIASLRAQS 356
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
162-541 |
5.20e-05 |
|
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: 47.27 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 162 LSGAPGPD-PVVHRTVEAMSQLQEELVVLRERLalhDSDRQaTTTQLQNQVENLKEKLISQAQEVSRLRSELGGT----- 235
Cdd:TIGR00618 519 DIDNPGPLtRRMQRGEQTYAQLETSEEDVYHQL---TSERK-QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnitv 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 236 DAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKtD 315
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK-E 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 316 RLAEVELRLkdclaekaQEEERLSRRLRDSHETIAslraQSPPVKYVIKTVEVESSKTKQALS------------ESQTR 383
Cdd:TIGR00618 674 LLASRQLAL--------QKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIEnassslgsdlaaREDAL 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 384 NQHLQEQVAMQRQVLKEME-QQLQNSHQLTV--QLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMK 460
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTeAHFNNNEEVTAalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE-IGQEIPSDEDILN 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 461 AVHENLAGVRTNLLTLqpaLRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIGQAIEEVNSNNQ-------ELLRKYR 531
Cdd:TIGR00618 821 LQCETLVQEEEQFLSR---LEEKSATLGEITHQLLKYEECSKqlAQLTQEQAKIIQLSDKLNGINQikiqfdgDALIKFL 897
|
410
....*....|
gi 568956232 532 RELQLRKKCH 541
Cdd:TIGR00618 898 HEITLYANVR 907
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
177-545 |
6.09e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQLRQELR 256
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS--SELEEMTKFKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 257 RCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclAEKAQEEE 336
Cdd:pfam05483 402 NKEVELEELKKI----------LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 337 RLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 416
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 417 AQIAMYEAELERAHGQMLEEMQSLEEDKnRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 496
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568956232 497 fpllLQEALRSVKAEIGQAIEEVNSNNQ---ELLRKYRRELQLRKKCHNELV 545
Cdd:pfam05483 627 ----ENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
181-543 |
6.46e-05 |
|
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: 46.96 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 181 QLQEELVVLRERLALHDSDRQATTTQ-----LQNQVENLKEKLISQAQEVSRL-RSELGGTDAEKHRDRLMVENEQLRQE 254
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKkevksLQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 255 LRRCEVELQELRA----QPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 330
Cdd:TIGR00606 555 KSRHSDELTSLLGyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 331 KAQEE--ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEM 401
Cdd:TIGR00606 635 QDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 402 EQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALR 481
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDL----KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEE 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 482 T---LTNDYNGLKRqvrgfpllLQEALRSVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 543
Cdd:TIGR00606 783 SakvCLTDVTIMER--------FQMELKDVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
280-456 |
6.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 280 QESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 352
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 353 RAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEA---ELE 427
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 568956232 428 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 456
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-352 |
1.13e-04 |
|
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: 46.20 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELGgtDAEKHRDRLMVENEQLRQELR 256
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAA----NLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 257 RCEVELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 336
Cdd:TIGR02168 870 ELESELEALLN------ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
170
....*....|....*.
gi 568956232 337 RLSRRLRDSHETIASL 352
Cdd:TIGR02168 944 RLSEEYSLTLEEAEAL 959
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
183-537 |
1.22e-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: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 183 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEkLISQAQEVSRLRSELGgTDAEKHRDRLMVENEQLRQE--LRRCEV 260
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLE-QDYQAASDHLNLVQTALRQQekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 261 ELQELRAQPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENKGMLSELN--LEVQQK--------TDRLAEVELRL----- 324
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYQqaLDVQQTraiqyqqaVQALEKARALCglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 325 -----KDCLAE-KAQEEER------LSRRLRDSHETIASLRAQSPPVKYVIKTVEVES--SKTKQALSESQTRnQHLQEQ 390
Cdd:COG3096 435 tpenaEDYLAAfRAKEQQAteevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ-QALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 391 VAMQRQVLKEMEQQLQNSH-------QLTVQLRAQIAMYEaELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVH 463
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQL 587
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956232 464 ENLAGVRTNLLTLQPALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 537
Cdd:COG3096 588 EQLRARIKELAARAPAWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
189-546 |
1.31e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 189 LRERLALHDSDRQATTTQLQ---NQ-------VENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRC 258
Cdd:pfam10174 294 LKQELSKKESELLALQTKLEtltNQnsdckqhIEVLKESLTAKEQRAAILQTEV---------DALRLRLEEKESFLNKK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 259 EVELQELRAQpvvpcEGCEhSQESSQLRD--------------KLSQLQLEVAENKGMLSELNLEVQQ-KTDR------L 317
Cdd:pfam10174 365 TKQLQDLTEE-----KSTL-AGEIRDLKDmldvkerkinvlqkKIENLQEQLRDKDKQLAGLKERVKSlQTDSsntdtaL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 318 AEVElrlkDCLAEKAQEEERL----SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAM 393
Cdd:pfam10174 439 TTLE----EALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 394 QRQVLKEMEQQLQNSHQLTVQLRAQI--AMYEAELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMkavhENLAGvrt 471
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEES-GKAQAEV----ERLLG--- 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956232 472 nlltlqpALRTLTNDYNGLKRQVRGFPLLlqeALRSVKaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 546
Cdd:pfam10174 587 -------ILREVENEKNDKDKKIAELESL---TLRQMK-EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
177-344 |
1.38e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL-----GGTDAEKHRDRLMVENEQL 251
Cdd:PRK09039 53 SALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 252 RQELRRCEVELQELRAQpvvpcegcehsqeSSQLRDKLSQLQ--LEVAENKGmlselnlevQQKTDRLAEVELRLKDCLA 329
Cdd:PRK09039 129 KQVSARALAQVELLNQQ-------------IAALRRQLAALEaaLDASEKRD---------RESQAKIADLGRRLNVALA 186
|
170 180
....*....|....*....|..
gi 568956232 330 EKAQEeerLSR-------RLRD 344
Cdd:PRK09039 187 QRVQE---LNRyrseffgRLRE 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-538 |
1.44e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 174 RTVEAMSQLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKL-ISQAQEVSRLRSELggtdaekhrDRLMVENEQLR 252
Cdd:COG4717 153 ERLEELRELEEELEELEAELA-----------ELQEELEELLEQLsLATEEELQDLAEEL---------EELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 253 QELRRCEVELQELRAQpvvpCEGCEHSQESSQLRDKLSQLQL----------------EVAENKGMLSELNLEVQQKTDR 316
Cdd:COG4717 213 EELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAGVLFLVLGLLAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 317 LAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ-----SPPVKYVIKTVEvESSKTKQALSESQTRNQHLQEQV 391
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppDLSPEELLELLD-RIEELQELLREAEELEEELQLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 392 AMQRQV----------LKEMEQQLQNSHQLtVQLRAQIAMYEAELERAHGQMLEEMQSLEEDknrAIEEAFARAQVEMKA 461
Cdd:COG4717 368 LEQEIAallaeagvedEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEE 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956232 462 VHENLAGVRTNLLTLQPALRTLTNDynGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNN--QELLRKYRRELQLRK 538
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED--GELAE-------LLQELEELKAELRELAEEWAALKlaLELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
234-520 |
1.55e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 234 GTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQlEVAENKGMLSELNLEVQQK 313
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAE----------LDALQERREALQRLA-EYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 314 TDRLAEVEL------RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQT 382
Cdd:COG4913 674 EAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 383 RNQHLQEQV--AMQRQVLKEMEQQLQNSHQltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMK 460
Cdd:COG4913 747 LRALLEERFaaALGDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYL 818
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 461 AVHENLagVRTNLLTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 520
Cdd:COG4913 819 ALLDRL--EEDGLPEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
172-476 |
1.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 172 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQL---QNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN 248
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 328
Cdd:COG4372 111 EELQEELEELQKERQDLE-------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 329 AEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVamQRQVLKEMEQQLQN 407
Cdd:COG4372 178 EAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA--LELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956232 408 SHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTL 476
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
183-555 |
2.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 183 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRCEVEL 262
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL---------EQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 263 QELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRL 342
Cdd:COG4372 83 EELNEQLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 343 RDSHETIASLRAQSPPVKYVIKtvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMY 422
Cdd:COG4372 157 EQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 423 EAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 502
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568956232 503 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIA 555
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-341 |
2.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 174 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENL---------KEKLISQAQEVSRLRSELGGTDAEKHRDRL 244
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleqAEEYQELKEELEELEEQLEELLGELEELLE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 245 MVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQL--QLEVAENKGMLSELNLEVQQKTDRLAEVE- 321
Cdd:COG4717 424 ALDEEELEEELEELEEELEELE-------------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAe 490
|
170 180
....*....|....*....|....
gi 568956232 322 ----LRLKDCLAEKAQEEERLSRR 341
Cdd:COG4717 491 ewaaLKLALELLEEAREEYREERL 514
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
212-476 |
2.72e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 212 ENLKEKLISQAQEVSRLRSELggtdaekhRDRLMVENEQLRQELRRcevELQELRAQpvvpcegcehSQESSQLRDKLSQ 291
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFSLLK--------KETIYLQSAQRVELAER---QLQELKID----------VKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 292 LQLEVAENKGML-SELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLRAQSPPVKYVIKTVEV 368
Cdd:COG5022 904 LESEIIELKKSLsSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTI 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 369 ESSKTKQALSESQTRNQHLQEQV----AMQRQV--LKEMEQQLQNSHQLTVQLRA-----QIAMYEAELERAHgqMLEEM 437
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQKLKGLL--LLENN 1060
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956232 438 QSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 476
Cdd:COG5022 1061 QLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
174-338 |
3.05e-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: 42.97 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 174 RTVEAMSQLQEELVVLRERLALHDSDRQAtttqlqnqVENLKEKLisqaqevsrlrselggTDAEKHRDRLMVENEQLRQ 253
Cdd:pfam13851 58 RLTEPLQKAQEEVEELRKQLENYEKDKQS--------LKNLKARL----------------KVLEKELKDLKWEHEVLEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 254 ELRRCEVELQELRAQpvvpCEGCEHS-QESSQLRD-----KLSQLQlEVAENK-----GMLSELNLEvqqkTDRLAEVEL 322
Cdd:pfam13851 114 RFEKVERERDELYDK----FEAAIQDvQQKTGLKNlllekKLQALG-ETLEKKeaqlnEVLAAANLD----PDALQAVTE 184
|
170
....*....|....*.
gi 568956232 323 RLKDCLAEKAQEEERL 338
Cdd:pfam13851 185 KLEDVLESKNQLIKDL 200
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
175-462 |
3.44e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 175 TVEAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSElggtdAEKHRDRlmveneqlRQE 254
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRD----ELNEELKELAEKRDELNAQVKELREE-----AQELREK--------RDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 255 LRRcevELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELN--------LEVQQKTDRL-AEVELRLK 325
Cdd:COG1340 69 LNE---KVKELKE------ERDELNEKLNELREELDELRKELAELNKAGGSIDklrkeierLEWRQQTEVLsPEEEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 326 DCLAEKAQEEERLsRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQL 405
Cdd:COG1340 140 EKIKELEKELEKA-KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956232 406 QNSHQLTVQLRAQIAMYEAELErahgQMLEEMQSLEE------DKNRAIEEAFARAQVEMKAV 462
Cdd:COG1340 212 DELHKEIVEAQEKADELHEEII----ELQKELRELRKelkklrKKQRALKREKEKEELEEKAE 270
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
282-444 |
3.79e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 42.68 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 282 SSQLRDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 355
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 356 SPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLE 435
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASE--------------LKKEFEEVSELIKS 175
|
....*....
gi 568956232 436 EMQSLEEDK 444
Cdd:cd07627 176 ELERFERER 184
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
177-410 |
5.22e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL------------GGTDAEKHRDRL 244
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLidlkehasslasSGLKKDSKLKSL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 245 MVENEQLRQELRRCEVELQelRAQpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRl 324
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLK--KAH-----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 325 KDCLAEKAQE-EERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQ--RQVLKEM 401
Cdd:pfam10174 595 KNDKDKKIAElESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEktRQELDAT 674
|
....*....
gi 568956232 402 EQQLQNSHQ 410
Cdd:pfam10174 675 KARLSSTQQ 683
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
210-593 |
5.67e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 210 QVENLKEKL--ISQAQEVSRLRSELGGTDAEKHRDRlmvENEQLRQELRRCEVELQelRAQPVVPCEGCEHSQESSQLRD 287
Cdd:PTZ00121 1458 KAEEAKKKAeeAKKADEAKKKAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 288 KLSQLQLEVAENKGMLSELnlevqQKTDRLAEVELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVE 367
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL-----KKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 368 VESS-KTKQALSESQTRNQhlQEQVAMQRQVLKEMEQ-------------QLQNSHQLTVQLRAQIAMYEAELERAhgqm 433
Cdd:PTZ00121 1603 EEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK---- 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 434 LEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIG 513
Cdd:PTZ00121 1677 AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEA 1735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 514 QAIEEVNSNNQELLRKYRRE----LQLRKKCHNELVRLKGNIRVIARvRPVTKEDGEGPEATNAVTFDPDDDS--IIHLL 587
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGG 1814
|
....*.
gi 568956232 588 HKGKPV 593
Cdd:PTZ00121 1815 KEGNLV 1820
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
207-450 |
5.80e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 207 LQNQV-ENLKEKL-ISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcEGCEHSQESSQ 284
Cdd:pfam07888 32 LQNRLeECLQERAeLLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE---ELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 285 LRDKLSQ----LQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkDCLAEKAqeeERLSRRLRDSHETIASLRAQSPPVK 360
Cdd:pfam07888 109 SSEELSEekdaLLAQRAAHEARIRELEEDIKTLTQRVLERETEL-ERMKERA---KKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 361 YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAElERAHGQMLEEMQSL 440
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS-ERKVEGLGEELSSM 263
|
250
....*....|
gi 568956232 441 EEDKNRAIEE 450
Cdd:pfam07888 264 AAQRDRTQAE 273
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
177-531 |
6.06e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLMVENEQLRQE-- 254
Cdd:PRK04778 140 EEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTESGDYVEAREILDQLEEELAALEQIme 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 255 -----LRRCEVE----LQELRAqpvvpceGCEHSQESS------QLRDKLSQLQLEVAENKGMLSELNL--------EVQ 311
Cdd:PRK04778 216 eipelLKELQTElpdqLQELKA-------GYRELVEEGyhldhlDIEKEIQDLKEQIDENLALLEELDLdeaeekneEIQ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 312 QKTDRL-----AEVELRlKDCLAEKAQEEERLSRRLRDSHETIASLR--AQSppvkYVIKTVEVESSKTKQA-LSESQTR 383
Cdd:PRK04778 289 ERIDQLydileREVKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEIDrvKQS----YTLNESELESVRQLEKqLESLEKQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 384 NQHLQEQVAMQRQV-------LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHgQMLEEMQS-LEEDKnRAIE------ 449
Cdd:PRK04778 364 YDEITERIAEQEIAyselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR-EKLERYRNkLHEIK-RYLEksnlpg 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 450 ------EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQ 514
Cdd:PRK04778 442 lpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAE 521
|
410
....*....|....*..
gi 568956232 515 AIEEVnsnnQELLRKYR 531
Cdd:PRK04778 522 ALNEA----ERLFREYD 534
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
191-411 |
7.19e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 191 ERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLR-QELRRCEVELQELRAQP 269
Cdd:pfam07888 160 KKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlTTAHRKEAENEALLEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 270 VVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHET 348
Cdd:pfam07888 240 RSLQERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDR 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956232 349 IASLRA---------QSPPVKYVIKTVEVESSKTKQALSESQTRNQhLQEQVAMQRQVLKEMEQQLQNSHQL 411
Cdd:pfam07888 320 IEKLSAelqrleerlQEERMEREKLEVELGREKDCNRVQLSESRRE-LQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-526 |
7.74e-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: 43.57 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 179 MSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLK-------EKLISQAQ-EVSRL--RSELGGTDAEKHRDRLMVEN 248
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLqqhqdriEQLISEHEvEITGLteKASSARSQANSIQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRCEVELQELRAQPvvpcegcehSQESSQLR-------DKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 321
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTV---------SQLRSELReakrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 322 LRLKDCLAEKAQEEERLS------RRLRDSHE----TIASLRAQSPPvkyviKTVEVESSKTKQALSESQTRNQHLQEQV 391
Cdd:pfam15921 377 DQLQKLLADLHKREKELSlekeqnKRLWDRDTgnsiTIDHLRRELDD-----RNMEVQRLEALLKAMKSECQGQMERQMA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 392 AMQ-----RQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEdKNRAIEEAFA-----RAQVEMKA 461
Cdd:pfam15921 452 AIQgknesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAeitklRSRVDLKL 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956232 462 VH--------ENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKA---EIGQAIEEVNSNNQEL 526
Cdd:pfam15921 531 QElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqvEKAQLEKEINDRRLEL 606
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
178-355 |
1.04e-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: 41.83 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 178 AMSQLQEELvvlrerLALHDSDRQATttQLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLmvenEQLRQELRR 257
Cdd:COG1579 1 AMPEDLRAL------LDLQELDSELD--RLEHRLKELPAELAELEDELAALEARL-----EAAKTEL----EDLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 258 CEVELQELRAQPVvpcegcEHSQESSQLRD--KLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE 335
Cdd:COG1579 64 LELEIEEVEARIK------KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
170 180
....*....|....*....|
gi 568956232 336 ERLSRRLRDSHETIASLRAQ 355
Cdd:COG1579 138 AELEEKKAELDEELAELEAE 157
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
249-563 |
1.14e-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: 42.81 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRCEVE----LQELRAQPVVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 323
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 324 LKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 403
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 404 ---QLQNSHQL--------------------------TVQLR-AQIAMYEAELERaHGQMLEEMQSLEEDKNRAIEEAFa 453
Cdd:pfam05557 154 lrqNLEKQQSSlaeaeqrikelefeiqsqeqdseivkNSKSElARIPELEKELER-LREHNKHLNENIENKLLLKEEVE- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 454 raqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL- 526
Cdd:pfam05557 232 ----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSAr 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568956232 527 -LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 563
Cdd:pfam05557 308 qLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
206-545 |
1.18e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 206 QLQNQVENLKEKLISQAQEVSRLRS-----ELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcegcEHSQ 280
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK------SKEK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 281 ESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVK 360
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN----------------LE 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 361 YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSL 440
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK----LSSIIKNI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 441 EEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQPALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIE 517
Cdd:TIGR04523 637 KSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKIKESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR 702
|
330 340 350
....*....|....*....|....*....|.
gi 568956232 518 evNSNNQELLRKYR---RELQLRKKCHNELV 545
Cdd:TIGR04523 703 --IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
337-460 |
1.27e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 337 RLSRRLRDshETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 406
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956232 407 -------NSHQLtVQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 460
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
307-535 |
1.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 307 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQ 375
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 376 ALSESQTRNQ--HLQEQVAMQRQVLKEMEQQLQnshqltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFA 453
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLA-------EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 454 RAQVEMKAvheNLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 530
Cdd:COG3206 270 AQLAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 568956232 531 RRELQ 535
Cdd:COG3206 340 EARLA 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-562 |
1.67e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 290 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDS-------HET 348
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKNltvepvkGSN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 349 IASLRAQSP-PVK-----------YVIKTVEVESSKTKQA--------------LSESQT-----RNQH----LQEQVAM 393
Cdd:COG3206 137 VIEISYTSPdPELaaavanalaeaYLEQNLELRREEARKAlefleeqlpelrkeLEEAEAaleefRQKNglvdLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 394 QRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQS--LEEDKNRAIEEAFARAQV---------EMKAV 462
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELsarytpnhpDVIAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 463 HENLAGVRTNLLT-LQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRkYRRELQLRKKCH 541
Cdd:COG3206 297 RAQIAALRAQLQQeAQRILASLEAELEALQARE--------ASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELY 367
|
330 340 350
....*....|....*....|....*....|..
gi 568956232 542 NELV-RLK----------GNIRVIARVRPVTK 562
Cdd:COG3206 368 ESLLqRLEearlaealtvGNVRVIDPAVVPLK 399
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
209-470 |
2.16e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 209 NQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRqELRRcevELQELRAQpvVPcegcEHSQESSQLRDK 288
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEI-----EELKEKRDELNEELK-ELAE---KRDELNAQ--VK----ELREEAQELREK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 289 LSQLQLEVAENKGMLSELNLEVQQKTDRLAEVElRLKDCLAEKAQEEERLSR---RLRDSHET--------------IAS 351
Cdd:COG1340 66 RDELNEKVKELKEERDELNEKLNELREELDELR-KELAELNKAGGSIDKLRKeieRLEWRQQTevlspeeekelvekIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 352 LRAQsppvkyvIKTVEVESSKTKQaLSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG 431
Cdd:COG1340 145 LEKE-------LEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956232 432 QMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVR 470
Cdd:COG1340 217 EIVEAQEKADE-----LHEEIIELQKELRELRKELKKLR 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
179-341 |
2.20e-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: 40.68 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 179 MSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDA--EKHRDRLM-VENEQLRQEL 255
Cdd:COG1579 19 LDRLEHRLKELPAELA----ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGnVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 256 RRcEVELQELRAqpvvpcegcehsqesSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE 335
Cdd:COG1579 95 QK-EIESLKRRI---------------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*.
gi 568956232 336 ERLSRR 341
Cdd:COG1579 159 EELEAE 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
341-548 |
2.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 341 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 407
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 408 SH-----QLTVQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 475
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956232 476 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 548
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
207-474 |
3.82e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 207 LQNQVENLKEKLISQAQEVSRLRsELGGTDAEKHRDRLmvenEQLRQELRrcevelqelraqpvvpcegcEHSQESSQLR 286
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK--------------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 287 DKLSQLQLEVAENKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrLRDSHETIAslraqsp 357
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK-IKDKLKELQ------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 358 pvkyviktvevessktkQALSESQTRNQHLQE---QVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQML 434
Cdd:PHA02562 313 -----------------HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568956232 435 EEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 474
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
286-459 |
4.13e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 39.65 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 286 RDKLSQLQLEVAENKGMLSELNLEVQQktdRLAEVELRLKDCLAEKAQEEERLSRR--------LRDSHETIASLRAqsp 357
Cdd:cd07596 34 RRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAAEELSSLSEAQANQelvkllepLKEYLRYCQAVKE--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 358 pvkyVIKT-----VEVESSKtkQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAqiamyeaELERAHGQ 432
Cdd:cd07596 108 ----TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARK-------RYEEISER 174
|
170 180 190
....*....|....*....|....*....|
gi 568956232 433 MLEEMQSLEEDKNRAIEEA---FARAQVEM 459
Cdd:cd07596 175 LKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
183-552 |
4.60e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 183 QEELVVLR-ERLALHDSDRQATTTQLQNQ------VENLKEKLISQAQEVSRLRSELggTDAEKHRDRlmvENEQLRQEL 255
Cdd:pfam12128 438 EEYRLKSRlGELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSEL--RQARKRRDQ---ASEALRQAS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 256 RRCE---VELQELRAQPVVPCEGCEH--SQESSQLRDKLSQL-QLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 329
Cdd:pfam12128 513 RRLEerqSALDELELQLFPQAGTLLHflRKEAPDWEQSIGKViSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 330 -EKAQEEERLSRR-------LRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTR-----NQHLQEQVAMQRQ 396
Cdd:pfam12128 593 pEWAASEEELRERldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKA 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 397 V---LKEMEQQLQN-SHQLTVQLRAQIAMYEA---ELERAHGQMLEEMQSLEEDKNRA---IEEAFARAQVEMKA----- 461
Cdd:pfam12128 673 LaerKDSANERLNSlEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVVEGALDAQlalLKAAIAARRSGAKAelkal 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 462 ---VHENLAGV---RTNLLTLQPALRTLT---NDYNGLKRQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQE 525
Cdd:pfam12128 753 etwYKRDLASLgvdPDVIAKLKREIRTLErkiERIAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNIERAISELQQQLAR 832
|
410 420 430
....*....|....*....|....*....|.
gi 568956232 526 LLRKYRRELQL----RKKCHNELVRLKGNIR 552
Cdd:pfam12128 833 LIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
176-548 |
4.78e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 176 VEAMSQLQEELVVLRERLALHDSDRQATT------TQLQNQVENLKEKL--ISQAQEVSRLRSElggtDAEKHRDRLMVE 247
Cdd:pfam05622 27 QEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLELQHR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 248 NEQLR---QELRRCEVELQELRaqpvvpcegcehsqESSqlrDKLSQLQLEVAENKGMLSELN-LEVQQKTdrlaevelr 323
Cdd:pfam05622 103 NEELTslaEEAQALKDEMDILR--------------ESS---DKVKKLEATVETYKKKLEDLGdLRRQVKL--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 324 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSE---SQTRNQHLQ---EQVAMQRQV 397
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQkekERLIIERDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 398 LKEMEQQLQNSHQLTVQLRAQIAMYEAELErAHGQMLEEMQSLEedknraIEEAFARAQVEMKAVHENLAGvrtNLLTLQ 477
Cdd:pfam05622 237 LRETNEELRCAQLQQAELSQADALLSPSSD-PGDNLAAEIMPAE------IREKLIRLQHENKMLRLGQEG---SYRERL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956232 478 PALRTLTNDYNGLKRQVRGFPLLLQEALRsvkaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 548
Cdd:pfam05622 307 TELQQLLEDANRRKNELETQNRLANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| BAR_Bin3 |
cd07590 |
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ... |
383-467 |
5.41e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153274 Cd Length: 225 Bit Score: 39.27 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 383 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAqIAMYEAELERAHGQMLEEMQSLEEDKNRAIE---EAFARAQV 457
Cdd:cd07590 117 REQSLQEYERLQAKVekLAEKEKTGPNLAKLEQAEKA-LAAARADFEKQNIKLLEELPKFYNGRTDYFQpcfEALIKSQV 195
|
90
....*....|....
gi 568956232 458 ----EMKAVHENLA 467
Cdd:cd07590 196 lyysQSTKIFTQLA 209
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
176-443 |
6.34e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.22 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 176 VEAMSqLQEELVVLRERLALHDSDRQATTTQLQNQVENLKE---KLISQAQEVSRLRSELGGTDaEKHRDRLMVEN---- 248
Cdd:PLN03229 479 VIAMG-LQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDefnKRLSRAPNYLSLKYKLDMLN-EFSRAKALSEKkska 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 249 EQLRQELRRcevELQELRAQPvvpcegcehsqessQLRDKLSQLQLEVAENK-GMLSELNLEVQQKTDRL-AEVELRLKD 326
Cdd:PLN03229 557 EKLKAEINK---KFKEVMDRP--------------EIKEKMEALKAEVASSGaSSGDELDDDLKEKVEKMkKEIELELAG 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 327 CLAEKAQEEERLSRRLRDSHETIAslraqSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEqvaMQRQVLKEMEQQLQ 406
Cdd:PLN03229 620 VLKSMGLEVIGVTKKNKDTAEQTP-----PPNLQEKIESLNEEINKKIERVIRSSDLKSKIEL---LKLEVAKASKTPDV 691
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568956232 407 NSHQLTVQLRAQI------AMYEAELERAHGQMLEEMQSLEED 443
Cdd:PLN03229 692 TEKEKIEALEQQIkqkiaeALNSSELKEKFEELEAELAAARET 734
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
239-539 |
6.54e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 239 KHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEgcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLA 318
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACE----------IRDQITSKEAQLESSREIVKSYENELDPLKNRLK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 319 EVE------LRLKD---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQTRNQHLQE 389
Cdd:TIGR00606 256 EIEhnlskiMKLDNeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 390 QVAMQRQVLKEMEQQLQNsHQLTVQLRA---QIAMYEAELERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMK 460
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLV-EQGRLQLQAdrhQEHIRARDSLIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 461 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQ 535
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELS 488
|
....
gi 568956232 536 LRKK 539
Cdd:TIGR00606 489 KAEK 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
285-486 |
6.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 285 LRDKLSQLQLEVAENKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyvi 363
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELRE--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 364 ktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqlTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 443
Cdd:COG4717 117 ---ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956232 444 KNRAIEEA---FARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 486
Cdd:COG4717 190 TEEELQDLaeeLEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
179-403 |
7.38e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 179 MSQLQEELVVLRERLALHDSDRqattTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQEL--- 255
Cdd:pfam15905 96 LQALEEELEKVEAKLNAAVREK----TSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLeak 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 256 -RRCEVELQELRAQPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENK---GMLSELNLEVQQKTDRLAEVEL---RLKDC 327
Cdd:pfam15905 172 mKEVMAKQEGMEGKLQVTQKNLEHSKGKvAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVEKYKLdiaQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 328 LAEKAQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSK-TKQALSESQTRN---QHLQEQVAMQRQVLKEMEQ 403
Cdd:pfam15905 252 LKEKNDEIESLKQSLE---EKEQELSKQIKDLNEKCKLLESEKEElLREYEEKEQTLNaelEELKEKLTLEEQEHQKLQQ 328
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
303-427 |
7.45e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 303 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQT 382
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568956232 383 RNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE 427
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
363-442 |
8.24e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.67 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 363 IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQMLEEMQS 439
Cdd:pfam12718 23 VKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNnenLTRKIQLLEEELEESDKRLKETTEK 102
|
...
gi 568956232 440 LEE 442
Cdd:pfam12718 103 LRE 105
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| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
177-483 |
8.31e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 177 EAMSQLQEELVvLRERL-ALHdsdrqATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQL---- 251
Cdd:PRK10246 413 AALAQHAEQRP-LRQRLvALH-----GQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL-----NEMRQRYKEKTQQLadvk 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 252 ---RQELRRCEVELQELRAQPVVPCEGCEHSQESSqlrdkLSQLQ-LEVAENKGMLSELNLEVQQKTDRLAEVELRLkDC 327
Cdd:PRK10246 482 ticEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPA-----VEAYQaLEPGVNQSRLDALEKEVKKLGEEGAALRGQL-DA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 328 LAEKAQEEERLSRRLRDSHETIaslraqsppvkyviktvevesSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLqn 407
Cdd:PRK10246 556 LTKQLQRDESEAQSLRQEEQAL---------------------TQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-- 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 408 sHQLT--VQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR----------------AIEEAFARAQvemkAVHENLAGV 469
Cdd:PRK10246 613 -RLLSqrHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSWQ----QRQNELTAL 687
|
330
....*....|....
gi 568956232 470 RTNLLTLQPALRTL 483
Cdd:PRK10246 688 QNRIQQLTPLLETL 701
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| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
222-343 |
8.72e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.44 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 222 AQEVSRLRSELGGTDAE-KHRDRLMVE-NEQLRQ---ELRRCEVELQELRAqpvvpcegcehsqESSQLRDKLSQLQLEV 296
Cdd:pfam06818 30 LNEIVALRAQLRELRAKlEEKEEQIQElEDSLRSktlELEVCENELQRKKN-------------EAELLREKVGKLEEEV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568956232 297 AENKGMLSELNLEVQQKTDRLAEVELRLK--DCLAEKAQEEERLSRRLR 343
Cdd:pfam06818 97 SGLREALSDVSPSGYESVYESDEAKEQRQeeADLGSLRREVERLRAELR 145
|
|
| Vps5 |
pfam09325 |
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
286-458 |
9.17e-03 |
|
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.
Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 38.80 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 286 RDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---QSPPV 359
Cdd:pfam09325 54 RKELASATGEFAKSLASLASLELStgLSRALSQLAEVEERIKELLERQALQDVLtLGETIDEYLRLIGSVKAvfnQRVKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 360 KYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLEEMQS 439
Cdd:pfam09325 134 WQSWQNAEQELSKKKEQLEKLLRANKSQNDKLQQAKKEVEELERRVQQ--------------AEKEFEDISELIKKELER 199
|
170 180
....*....|....*....|..
gi 568956232 440 LEEDKN---RAIEEAFARAQVE 458
Cdd:pfam09325 200 FELERVddfKNSVEIYLESAIE 221
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
169-295 |
9.87e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956232 169 DPVVHRTVEAMSQLQEELVVLRErlaLHDSDRQATTTQLQnqveNLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN 248
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELD----RAKEKLKKLLQEIMIKVKKL--EELEEELQELESKI 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568956232 249 EQLRQELRRCEVELQELRAQpVVPCEGCEHSqESSQLRDKLSQLQLE 295
Cdd:smart00787 242 EDLTNKKSELNTEIAEAEKK-LEQCRGFTFK-EIEKLKEQLKLLQSL 286
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