|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
598-925 |
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 1958746508 598 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 676
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 677 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 753
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 754 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 833
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 834 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 913
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 1958746508 914 LKFAERVRSVEL 925
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
606-923 |
2.66e-147 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 440.47 E-value: 2.66e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 606 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 682
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 683 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 762
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 763 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 839
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 840 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFA 917
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 1958746508 918 ERVRSV 923
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
600-927 |
1.36e-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: 428.53 E-value: 1.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 675
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 676 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 755
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 756 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 833
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 834 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 911
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 1958746508 912 YSLKFAERVRSVELGP 927
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
600-921 |
4.37e-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: 4.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 676
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 677 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 754
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 755 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 832
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 833 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 911
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 1958746508 912 YSLKFAERVR 921
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
600-923 |
6.34e-105 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 330.19 E-value: 6.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 671
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 672 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 748
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 749 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 824
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 825 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 903
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 1958746508 904 EKNTSETLYSLKFAERVRSV 923
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
601-924 |
4.51e-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: 325.44 E-value: 4.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 601 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 678
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 679 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 752
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 753 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 822
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 823 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 899
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 1958746508 900 VSPVEKNTSETLYSLKFAERVRSVE 924
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
600-923 |
4.02e-95 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 304.65 E-value: 4.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 662
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 663 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 741
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 742 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 820
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 821 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 895
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 1958746508 896 MVVQVSPVEKNTSETLYSLKFAERVRSV 923
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
600-923 |
3.58e-90 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 290.39 E-value: 3.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 677
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 678 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 754
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 755 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 834
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 835 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 913
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 1958746508 914 LKFAERVRSV 923
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
600-923 |
5.20e-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: 287.31 E-value: 5.20e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 678
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 679 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 758
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 759 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 834
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 835 RVGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 912
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 1958746508 913 SLKFAERVRSV 923
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
599-923 |
1.33e-88 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 287.71 E-value: 1.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 599 GNIRVIARVRPVTK-EDGEGpeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQ 662
Cdd:cd01365 1 ANVKVAVRVRPFNSrEKERN--SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 663 EVQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDL 740
Cdd:cd01365 79 DLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 741 LGKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDC 815
Cdd:cd01365 159 LNPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 816 STGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQ 885
Cdd:cd01365 237 ETNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLK 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958746508 886 DSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSV 923
Cdd:cd01365 317 ENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
600-923 |
2.70e-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: 281.14 E-value: 2.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 674
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 675 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 743
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 744 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 818
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 819 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 898
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 1958746508 899 QVSPVEKNTSETLYSLKFAERVRSV 923
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
584-924 |
3.58e-81 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 274.31 E-value: 3.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 584 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 663
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 664 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 742
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 743 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 822
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 823 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 900
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 1958746508 901 SPVEKNTSETLYSLKFAERVRSVE 924
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
601-918 |
3.22e-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: 256.55 E-value: 3.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 601 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 669
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 670 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 745
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 746 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 820
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 821 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 892
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 1958746508 893 KTLMVVQVSPVEKNTSETLYSLKFAE 918
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
600-921 |
1.61e-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: 254.74 E-value: 1.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 678
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 679 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgkEP- 745
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 746 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 822
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 823 gKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 898
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 1958746508 899 QVSPVEKNTSETLYSLKFAERVR 921
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
600-921 |
1.72e-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: 239.71 E-value: 1.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 676
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 677 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 756
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 757 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 835
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 836 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLK 915
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 1958746508 916 FAERVR 921
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
601-921 |
6.88e-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: 235.94 E-value: 6.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 601 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 669
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 670 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 746
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 747 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 821
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 822 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 900
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 1958746508 901 SPVEKNTSETLYSLKFAERVR 921
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
600-920 |
6.34e-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: 224.87 E-value: 6.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 600 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 671
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 672 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 747
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 748 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 827
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 828 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 905
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 1958746508 906 NTSETLYSLKFAERV 920
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
601-924 |
8.03e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 214.41 E-value: 8.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 601 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 679
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 680 FAYGQTGAGKTYTMEGtPENP-----------GINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLgk 743
Cdd:PLN03188 170 FAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 744 EP-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLR 820
Cdd:PLN03188 247 DPsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 821 T--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSK 893
Cdd:PLN03188 325 SfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAK 404
|
330 340 350
....*....|....*....|....*....|.
gi 1958746508 894 TLMVVQVSPVEKNTSETLYSLKFAERVRSVE 924
Cdd:PLN03188 405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
580-741 |
1.42e-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: 151.99 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 580 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 659
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 660 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 739
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 1958746508 740 LL 741
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
648-867 |
7.37e-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: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 648 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 726
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 727 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 806
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746508 807 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 867
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-595 |
5.86e-15 |
|
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: 79.72 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 286 DVEKHRDRLMVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTD 365
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELE-------------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 366 RLAevelRLKDCLAEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 445
Cdd:TIGR02168 748 RIA----QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 446 QVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVRTNLLT 525
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 526 LQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELV 595
Cdd:TIGR02168 899 LSEELRELESKRSELRRELE----ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-544 |
3.79e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.95 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 231 QLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCEA 310
Cdd:TIGR02169 671 SEPAELQRLRERLE-----------GLKRELSSLQSELRRIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 311 ELQELRAQPVVPCQGCEHS-QESTQLRDRLSQLQLEVAENK-------------------GMLSELNLEVQQKTDRLAEV 370
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVkSELKELEARIEELEEDLHKLEealndlearlshsripeiqAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 371 ELRLKDCLAEKAQEEER---LSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV 447
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 448 LKEMEQQLQ---------NSHQLTIQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEEDKNRA 497
Cdd:TIGR02169 898 LRELERKIEeleaqiekkRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLA 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958746508 498 IE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 544
Cdd:TIGR02169 978 IQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-584 |
5.78e-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: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 257 LQNQVENLKEKlISQAQEVSRLRSELGgtdvEKHRDRLMVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLR 336
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAELR----ELELALLVLRLEELREELEELQEELKEAE-------------EELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 337 DRLSQLQLEVAENKGMLSELNLEVQQKTDRLaeveLRLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvIKTV 416
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 417 EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT--------------IQLRAQIAMYEAELER--AH 480
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 481 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 560
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330 340
....*....|....*....|....*.
gi 1958746508 561 EIGQAIEEVNS--NNQELLRKYRREL 584
Cdd:TIGR02168 483 ELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
239-501 |
1.40e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.59 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 239 LRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRLMVENEQLRQELRRCEAELQELRAq 318
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 319 pvvpcqgcehsqestqlrdRLSQLQLEVAENKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 396
Cdd:COG3206 241 -------------------RLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 397 ETIASLKAQsppvkyvIKTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAe 475
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV- 362
|
250 260
....*....|....*....|....*.
gi 1958746508 476 LERAHGQMLEEMQSLEEDKNRAIEEA 501
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-508 |
1.57e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELR 306
Cdd:COG1196 246 AELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 307 RCEAELQELRAQpvvpcqgcehsqeSTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 386
Cdd:COG1196 320 ELEEELAELEEE-------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 387 RLSRRLRDSHETIASLKAQsppvKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLR 466
Cdd:COG1196 387 ELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958746508 467 AQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 508
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-586 |
7.07e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 254 TTQLQNQVENLKEKLiSQAQEVSRLRSELGGTDVE---KHRDRLMVENEQLRQELRRCEAELQELRAQpvvpcqgcehsq 330
Cdd:COG1196 195 LGELERQLEPLERQA-EKAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAE------------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 331 estqlrdrLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkdcLAEKAQEEERLSRRLRDSHETIASLKAQsppvk 410
Cdd:COG1196 262 --------LAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEE----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 411 yvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSL 490
Cdd:COG1196 325 --LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 491 EEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEE 568
Cdd:COG1196 403 EELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAA 478
|
330
....*....|....*...
gi 1958746508 569 VNSNNQELLRKYRRELQL 586
Cdd:COG1196 479 LAELLEELAEAAARLLLL 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-584 |
7.42e-11 |
|
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: 66.63 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 270 SQAQEVSRLRSELGGTDVEKhrdrlmvenEQLRQELRRCEAELQELRAQPvvpcqgCEHSQESTQLRDRLSQLQLEVAEN 349
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKREL---------SSLQSELRRIENRLDELSQEL------SDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 350 KGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSrRLRDSHETIASLKAQSPpvkyvIKTVEVESSKtkqalse 429
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEARLSHSR-----IPEIQAELSK------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 430 sqtrnqhLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQV 507
Cdd:TIGR02169 803 -------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeELEEELEELEA 875
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746508 508 EMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRKYRREL 584
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI--------EKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-506 |
9.76e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQLRQELR 306
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERLEELEEEL---------AELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 307 RCEAELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 386
Cdd:COG1196 341 ELEEELEEAEEE----------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 387 RLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLR 466
Cdd:COG1196 411 ALLERLERLEEELEELEEA-------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958746508 467 AQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFARAQ 506
Cdd:COG1196 484 EELAEAAARLL-----LLLEAEADYEGFLEGVKAALLLAG 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
227-576 |
1.67e-09 |
|
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: 62.06 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVS-------RLRSELGGTDVEKhrDRLMV 296
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKELSlekeqnkRLWDRDTGNSITI--DHLRR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 297 ENEQLRQELRRCEAELQELRAQpvvpCQG-CEHSQESTQLR----DRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 371
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSE----CQGqMERQMAAIQGKneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 372 LRLKDcLAEKAQEEERlsrRLRDSHETIASLKAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQRQVLKE 450
Cdd:pfam15921 496 RTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIEI 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 451 MEQQLQNSHQLTIQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENLA 517
Cdd:pfam15921 567 LRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERLR 646
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746508 518 GV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 576
Cdd:pfam15921 647 AVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-405 |
5.65e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQL-QNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVEN------- 298
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARL--DALREELDELEAQIrgnggdr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 299 -EQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC 377
Cdd:COG4913 340 lEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 1958746508 378 LAEKAQEEERLSRRLRDSHETIASLKAQ 405
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-606 |
1.00e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 238 VLRERLALHDSDR-----QATTTQLQNQVENLkEKLISQAQEVSRLRSELGG--TDVEKHRDRLMVENEQLRQELRRCEA 310
Cdd:PRK03918 150 VVRQILGLDDYENayknlGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKelEEVLREINEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 311 ELQELRAqpvvpcqgcehsqestqLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEK 381
Cdd:PRK03918 229 EVKELEE-----------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 382 AQEEERLSR-------RLRDSHETIASLKAQSPPVKYVIKTVEVESSK---TKQALSESQTRNQHLQEQV---AMQRQVL 448
Cdd:PRK03918 292 AEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEERHelyEEAKAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 449 KEMEQQLQNSHQLTIQ------LRAQIAMYEAELERAH-GQMLEEMQSLEEDKNRAIEEaFARAQVE------------- 508
Cdd:PRK03918 372 EELERLKKRLTGLTPEklekelEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcgrelteehr 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 509 ---MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELLRKYRRELQ 585
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420
....*....|....*....|.
gi 1958746508 586 LRKKchnELVRLKGNIRVIAR 606
Cdd:PRK03918 529 KLKE---KLIKLKGEIKSLKK 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
222-503 |
1.21e-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: 59.30 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 222 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLqnqvENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQL 301
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELAEELAELEEKL---------EELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 302 RQELRRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLaevelrlkdclaEK 381
Cdd:TIGR02168 357 EAELEELEAELEELESRLE------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR------------ER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 382 AQEEERLSRRLRDSHEtiaslkaqsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQnshql 461
Cdd:TIGR02168 419 LQQEIEELLKKLEEAE---------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD----- 478
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958746508 462 tiQLRAQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFA 503
Cdd:TIGR02168 479 --AAERELAQLQARLD-----SLERLQENLEGFSEGVKALLK 513
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
582-866 |
1.43e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 58.60 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 582 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 649
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 650 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 728
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 729 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 802
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746508 803 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 866
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
223-481 |
3.03e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 223 HRTVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQLR 302
Cdd:COG1196 291 YELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEEL---------EEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 303 QELRRCEAELQELRAQpvvpcqgcEHSQESTQLRDRLSQLQLEVAEnkgmlSELNLEVQQKTDRLAEVELRLKDCLAEKA 382
Cdd:COG1196 358 AELAEAEEALLEAEAE--------LAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 383 QEEERLSRRLRDSHETIASLKAQsppvkyviktvevessktKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT 462
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEA------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250
....*....|....*....
gi 1958746508 463 IQLRAQIAMYEAELERAHG 481
Cdd:COG1196 487 AEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-630 |
3.08e-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: 57.76 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 336 RDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKT 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 416 VEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHG---------QMLEE 486
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlrerlESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 487 MQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAI 566
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRSELEELSEEL 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746508 567 EEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI-RVIARVRPVTKEDGEGPEA-TNAVTFDPDD 630
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEAlENKIEDDEEE 969
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-479 |
3.90e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 256 QLQNQVENLKEKLISQAQEVSRLRSELggtdvEKHRDRLmvenEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQL 335
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQL-----AALERRI----AALARRIRALEQELAALE-------------AELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 336 RDRLSQLQLEVAENKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLKAQSPP 408
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746508 409 VKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERA 479
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-585 |
4.47e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 249 DRQATTtqLQNQVENLKEKLISQAQEVSRLRSELG---------GTDVEKHRDRLMVENEQLRQE--LRRCEAELQELRA 317
Cdd:PRK04863 285 LEEALE--LRRELYTSRRQLAAEQYRLVEMARELAelneaesdlEQDYQAASDHLNLVQTALRQQekIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 318 QPVVPCQGCEHSQES-TQLRDRLSQLQLEVAENKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKD 376
Cdd:PRK04863 363 RLEEQNEVVEEADEQqEENEARAEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 377 CLAE-KAQEEERLSRRLR-----DSHETIASLKAQSppVKYVIKTV-EVESSKTKQALSE--SQTRNQ-HLQEQVAMQRQ 446
Cdd:PRK04863 443 WLEEfQAKEQEATEELLSleqklSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 447 VLKEMEQQLQNsHQLTIQLRAQ-----IAMY--EAELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLA 517
Cdd:PRK04863 521 RLSELEQRLRQ-QQRAERLLAEfckrlGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746508 518 GVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 585
Cdd:PRK04863 600 ARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-587 |
5.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 223 HRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQN-----QVENLKEKLISQAQEVSRLRSELggtdveKHRDRLMVE 297
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 298 NEQLRQELRRCEAELQELRAQPVVpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdc 377
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 378 laEKAQEEERLSRRLRD--SHETIASLKAQSPPVKYVIKTV--------------EVESSKTKQALSESQTRNQHLQEQV 441
Cdd:COG4717 237 --EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 442 AMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVEmkavheNLAGVR 520
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGVE------DEEELR 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746508 521 tNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 587
Cdd:COG4717 389 -AALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
293-569 |
5.22e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 293 RLMVENeqlRQELRRCEAELQELRAQ-----PVVpcqgcEHSQESTQLRDRLSQLQLevaenkgMLSELNLEVQQKTDRL 367
Cdd:COG4913 228 DALVEH---FDDLERAHEALEDAREQiellePIR-----ELAERYAAARERLAELEY-------LRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 368 AEVEL-RLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQR 445
Cdd:COG4913 293 LEAELeELRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 446 QVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLT 525
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958746508 526 LQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 569
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-518 |
7.95e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 297 ENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKD 376
Cdd:COG4942 28 ELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 377 CLAEKAQEEERLSRRLR-----DSHETIASLKAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQ 446
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746508 447 VLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENLAG 518
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERTPA 245
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
260-406 |
1.28e-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: 54.64 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 260 QVENLKEKLisqAQEVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCEAELQELRAQPVvPCQGCEhSQESTQLRDRL 339
Cdd:smart00787 141 LLEGLKEGL---DENLEGLKEDY--KLLMKELELLNSIKPKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746508 340 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLKAQS 406
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-589 |
1.83e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 248 SDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRLMVENEQ------------LRQELRRCEAELQEL 315
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeLEKQLNQLKSEISDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 316 RAQPVVPCQGCEHSQESTQlRDRLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDS 395
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 396 HETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIamyeAE 475
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 476 LErahgqmlEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQ 552
Cdd:TIGR04523 445 LT-------NQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK----ELE 509
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958746508 553 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKK 589
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
227-582 |
2.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQL---QNQVENLKEKLISQAQEVSRLRSELGgtDVEKHRDRLMVENEQLRQ 303
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDLG--NAEDFLEELREERDELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 304 ELRRCEAELQELR------------------AQPVvpcQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTD 365
Cdd:PRK02224 427 REAELEATLRTARerveeaealleagkcpecGQPV---EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 366 rLAEVELRLKDcLAEKAqeeERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 445
Cdd:PRK02224 504 -LVEAEDRIER-LEERR---EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 446 QVLKEMEQQLQNSHQLTIQLrAQIAMYEAELERAHGQmLEEMQSLEE----------DKNRAIEEAFARAQVEmkAVHEN 515
Cdd:PRK02224 579 SKLAELKERIESLERIRTLL-AAIADAEDEIERLREK-REALAELNDerrerlaekrERKRELEAEFDEARIE--EARED 654
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746508 516 LAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIG---QAIEEVNSNNQELLRKYRR 582
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEnrvEALEALYDEAEELESMYGD 726
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
266-568 |
2.15e-07 |
|
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: 55.18 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 266 EKLISQAQEVSRLRSELggtdvEKHRDRLMVENEQLRQELR--------------RCEAELQELRAQpvvpcqGCEHSQE 331
Cdd:pfam01576 359 EELTEQLEQAKRNKANL-----EKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQAR------LSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 332 STQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLKAQSP 407
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 408 PVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQLTIQLRAQIAMYEaELERAHGQMLEE 486
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYD-KLEKTKNRLQQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 487 MQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRG 546
Cdd:pfam01576 582 LDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQ 661
|
330 340
....*....|....*....|..
gi 1958746508 547 FPLLLqEALRSVKAEIGQAIEE 568
Cdd:pfam01576 662 LRAEM-EDLVSSKDDVGKNVHE 682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-470 |
3.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 128 SLAQCRALSVDWPGPRSPHRLYLTVQQALQDKGCESKSQGTK----EDRLPKRQApapRRDREAPEAGGTMNvekpggRL 203
Cdd:COG4913 115 TLAQVFWLKGDASSLGDVKRFFVIADGPLDLEDFEEFAHGFDiralKARLKKQGV---EFFDSFSAYLARLR------RR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 204 LGIGRCSSLSgspgpdpVVHRTVeAMSQLQ--EELV---VLRERLA-------------LHDSDRQATTTQLQ----NQV 261
Cdd:COG4913 186 LGIGSEKALR-------LLHKTQ-SFKPIGdlDDFVreyMLEEPDTfeaadalvehfddLERAHEALEDAREQiellEPI 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 262 ENLKEKLISQAQEVSRLRSELGGTDVEKHRDRLmvenEQLRQELRRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQ 341
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRL----ELLEAELEELRAELARLEAELE------RLEARLDALREELDE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 342 LQLEVAENKG-MLSELNLEVQQKTDRLAEVELRLKDcLAEKAQeeeRLSRRLRDSHETIASLKAQsppVKYVIKTVEVES 420
Cdd:COG4913 328 LEAQIRGNGGdRLEQLEREIERLERELEERERRRAR-LEALLA---ALGLPLPASAEEFAALRAE---AAALLEALEEEL 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958746508 421 SKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIA 470
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
227-529 |
5.54e-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: 53.80 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHdsdrQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDVEKHRDRLMVENEQL----- 301
Cdd:COG3096 836 AELAALRQRRSELERELAQH----RAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLADRLEELREELdaaqe 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 302 -RQELRRCEAELQELRAQPVV----PCQGCEHSQESTQLRDRLSQLQL------EVAENK---------GML---SELNL 358
Cdd:COG3096 908 aQAFIQQHGKALAQLEPLVAVlqsdPEQFEQLQADYLQAKEQQRRLKQqifalsEVVQRRphfsyedavGLLgenSDLNE 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 359 EVQQKTDRlAEVELRLKDCLAEKAQEeerlsrRLRDSHETIASLKAqsppvkyviktveveSSKTK-QALSESQTRNQHL 437
Cdd:COG3096 988 KLRARLEQ-AEEARREAREQLRQAQA------QYSQYNQVLASLKS---------------SRDAKqQTLQELEQELEEL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 438 -----QEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEemqsLEED---KNRAIEEAFARAQVEM 509
Cdd:COG3096 1046 gvqadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK----AERDykqEREQVVQAKAGWCAVL 1121
|
330 340
....*....|....*....|
gi 1958746508 510 KAVHENlaGVRTNLLTLQPA 529
Cdd:COG3096 1122 RLARDN--DVERRLHRRELA 1139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
366-598 |
8.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 366 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 445
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 446 QVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 523
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746508 524 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 598
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
234-491 |
1.25e-06 |
|
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: 52.66 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 234 EELVVLRERLALHDSDRQATTTQLQNQvENLKEKLISQAQEVSRLRSELggtdvekhrdrlmvenEQLRQELRRCEAELQ 313
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI----------------EEQRRLLQTLHSQEI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 314 ELRAQPVVPCQGCEHSQESTQLRDRLSQLQlevaENKGMLSELNLEVQQKTDRLAEvelrlkdclaEKAQEEERLSRRlR 393
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKELDILQR----------EQATIDTRTSAF-R 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 394 DSHETIASLKAQSPPVKYVIKTVEVESSKTKQalsESQTRNQHLQEqvamQRQVLKEMEQQLQNSHQLTIQlraqiamyE 473
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE----SAQSLKEREQQLQTKEQIHLQ--------E 485
|
250
....*....|....*...
gi 1958746508 474 AELERAHGQMLEEMQSLE 491
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEP 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-554 |
1.53e-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: 52.43 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 225 TVEAMSQLQEELVVlrERLALHDSDRQAT--TTQLQN----------QVENLKEKLISQAQEVSRLRSElggtdvEKHRD 292
Cdd:pfam15921 473 TKEMLRKVVEELTA--KKMTLESSERTVSdlTASLQEkeraieatnaEITKLRSRVDLKLQELQHLKNE------GDHLR 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 293 RLMVENEQLRQELRRCEAELQELRAQPVVPCQGC-EHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 371
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 372 LRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLKAQSPPVKYVIKT----VEVESSKTKQALSES 430
Cdd:pfam15921 625 ARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMETTTNKLKMQLKSA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 431 QTrnqhlqeQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELErahgQMLEEMQSLEEDKNRAIEEAFARAQvEMK 510
Cdd:pfam15921 705 QS-------ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNANKEKHFLKE-EKN 772
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958746508 511 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEA 554
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
224-537 |
2.38e-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: 51.66 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 224 RTVEAMSQLQEElvvlrERLALHDSDRQATTTQLQNQVENLKEKLISQAQ------EVSRLRSELGGTDVEKHRD--RLM 295
Cdd:pfam17380 310 REVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERELERIRqeerkrELERIRQEEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 296 VE----NEQLRQELRRC------EAELQELRAQPVVPCQGCEHSQESTQLRDrLSQLQLEVAENKGMLSELNLEVQQKTD 365
Cdd:pfam17380 385 MErqqkNERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 366 RL--AEVELRLKDCLAEKAQEEERLSRRLRDshetiaslkaqsppvkyviKTVEVESSKTKQALSESQTRNQHLQEQVAM 443
Cdd:pfam17380 464 RLrqQEEERKRKKLELEKEKRDRKRAEEQRR-------------------KILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 444 QRQVLKEMEQQlqnshqltiqlraqiamYEAELERAHGQMLEEMQSLEEDKNRAIEE-----AFARAQVEMKAVHENLAG 518
Cdd:pfam17380 525 RQKAIYEEERR-----------------REAEEERRKQQEMEERRRIQEQMRKATEErsrleAMEREREMMRQIVESEKA 587
|
330 340
....*....|....*....|....
gi 1958746508 519 -----VRTNLLTLQPALRTLTNDY 537
Cdd:pfam17380 588 raeyeATTPITTIKPIYRPRISEY 611
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
229-501 |
3.49e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.84 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 229 MSQLQEE-LVVLRERLALHDSDRQATTtqLQNQVENLKEklisQAQEV-SRLRSELGGTD---------------VEKHR 291
Cdd:pfam05622 154 VKLLEERnAEYMQRTLQLEEELKKANA--LRGQLETYKR----QVQELhGKLSEESKKADklefeykkleekleaLQKEK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 292 DRLMVENEQLRQ---ELRRCEAELQELRAQPVVPCQGCEHSQE------STQLRDRLSQLQLEvaeNKgMLSELnlEVQQ 362
Cdd:pfam05622 228 ERLIIERDTLREtneELRCAQLQQAELSQADALLSPSSDPGDNlaaeimPAEIREKLIRLQHE---NK-MLRLG--QEGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 363 KTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLKAQsppVKYVIKTVEVESSKT------KQALSESQTRNQH 436
Cdd:pfam05622 302 YRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746508 437 LQEQVAMQRQVLKEMEQQLQNSHQLTIqlraqiamyeAELERAHGQMLEEMQSLEEDKNRAIEEA 501
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
224-408 |
3.53e-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: 50.53 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 224 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLIS--QAQEVSRLRSELGGTDVEKHRDRLMVE---N 298
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLkylA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 299 EQLRQELRRCEAELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 378
Cdd:COG4942 146 PARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|
gi 1958746508 379 AEKAQEEERLSRRLRDSHETIASLKAQSPP 408
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
277-602 |
4.32e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 277 RLRSELGGTDVEKHRDRLMVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSEL 356
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 357 NLEVQQKTDRLAEVElrlkdclaekaQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQH 436
Cdd:COG4372 86 NEQLQAAQAELAQAQ-----------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 437 LQEQVAMQRQVLKEMEQQLQNshQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENL 516
Cdd:COG4372 155 LEEQLESLQEELAALEQELQA--LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 517 AGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 596
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
....*.
gi 1958746508 597 LKGNIR 602
Cdd:COG4372 313 LEDALL 318
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-602 |
5.78e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 223 HRTVEAMSQLQEELVVLRERLALHDSDR--------QATTTQLQNQVENLKEKLISQAQEVSRLR---SELGGTD----- 286
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKlekeleelEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKgkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 287 -----VEKHRDRLMvenEQLRQELRRCEAELQELRAQpvvpcqgcehsqeSTQLRDRLSQLQLEVAENKGMLSELNLevq 361
Cdd:PRK03918 441 cgrelTEEHRKELL---EEYTAELKRIEKELKEIEEK-------------ERKLRKELRELEKVLKKESELIKLKEL--- 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 362 qkTDRLAEVELRLKDCLAEKAQEEERLSRRLRdshETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQV 441
Cdd:PRK03918 502 --AEQLKELEEKLKKYNLEELEKKAEEYEKLK---EKLIKLKGE-------IKSLKKELEKLEELKKKLAELEKKLDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 442 AMQRQVLKEMEQQLQNS-HQLTIQLRaqiamyeaELERAHGQMLEEMQSleEDKNRAIEEAFARAQVEMKAVHENLAGVR 520
Cdd:PRK03918 570 EELAELLKELEELGFESvEELEERLK--------ELEPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEELAETE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 521 TNLLTLQPALRTLTNDYNGLK-RQVRGFPLLLQEALRSVKAEIGQA---IEEVNSNNQEL------LRKYRRELQLRKKC 590
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELekrREEIKKTLEKLkeeleeREKAKKELEKLEKA 719
|
410
....*....|..
gi 1958746508 591 HNELVRLKGNIR 602
Cdd:PRK03918 720 LERVEELREKVK 731
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
265-460 |
5.86e-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: 49.37 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 265 KEKLISQAQEVSRLRSELGGT-------DVEKHRDRLMVENEQLRQELRRCEAELQELRAQpvvpcqgceHSQESTQLRD 337
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEAQ---------QQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 338 RLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLKAQSpPVKYVIKTVE 417
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958746508 418 VESSKTKQALSESQTRNQHLQEQVAMQRQV----LKEMEQQLQNSHQ 460
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQG 212
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
296-544 |
6.61e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 296 VENEQLRQELRRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQlevaenkGMLSELN-LEVQQKTDRLAEVELRL 374
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ------QQRSQLEQAKEGLSALN-------RLLPRLNlLADETLADRVEEIREQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 375 KDCLAEKA-----------------------QEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVE-------VESSKTK 424
Cdd:PRK04863 904 DEAEEAKRfvqqhgnalaqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaAEMLAKN 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 425 QALSES-QTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIamyeaeleRAHGQMLEE-MQSLEEDKNRAIEEAF 502
Cdd:PRK04863 984 SDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY--------DAKRQMLQElKQELQDLGVPADSGAE 1055
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746508 503 ARAQVEMKAVHENLAGVRT--------------NLLTLQPALRTLTNDYNGLKRQV 544
Cdd:PRK04863 1056 ERARARRDELHARLSANRSrrnqlekqltfceaEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
242-501 |
8.91e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 242 RLALHD--SDRQATTTQLQNQVE-----NLKEKLISQAQEVSRLRSELGGTDVEKHR--------DRLMVENEQLRQELR 306
Cdd:PRK02224 175 RLGVERvlSDQRGSLDQLKAQIEekeekDLHERLNGLESELAELDEEIERYEEQREQaretrdeaDEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 307 RCEAELQELRAQpvvpCQGCEHSQE--STQLRDRLSQLQLEVAENKGMLSELNLE------VQQKTDRLAEVELRLKDCL 378
Cdd:PRK02224 255 TLEAEIEDLRET----IAETEREREelAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 379 AEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNs 458
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN- 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958746508 459 hqltiqLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEA 501
Cdd:PRK02224 410 ------AEDFLEELREERDELREREAELEATLRTARER-VEEA 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
227-405 |
1.24e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVENEQLRQ 303
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 304 ELRRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQ 383
Cdd:TIGR02168 888 ALALLRSELEELSEELR------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
170 180
....*....|....*....|..
gi 1958746508 384 EEERLSRRLRDShetIASLKAQ 405
Cdd:TIGR02168 962 KIEDDEEEARRR---LKRLENK 980
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
251-509 |
1.61e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 251 QATTTQLQNQVENLKEKL----ISQ-----AQEVSRLRSELggtdVEKHRDRLMVENEQLRQEL---RRCEAELqelraq 318
Cdd:PRK10929 172 QAQLTALQAESAALKALVdeleLAQlsannRQELARLRSEL----AKKRSQQLDAYLQALRNQLnsqRQREAER------ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 319 pvvpcqgcehSQESTQLrdrlsqlqleVAENKGMLSELNLEvQQKTDRlaevelRLKDCLAEKAQEEERLSRRLRdsheT 398
Cdd:PRK10929 242 ----------ALESTEL----------LAEQSGDLPKSIVA-QFKINR------ELSQALNQQAQRMDLIASQQR----Q 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 399 IASlkaQSPPVKYVIKTVEVESsktkQALSESQTRNQHLQEQVAMqrqvLKEME--QQLQNShqlTIQLRAQIAMYEAEL 476
Cdd:PRK10929 291 AAS---QTLQVRQALNTLREQS----QWLGVSNALGEALRAQVAR----LPEMPkpQQLDTE---MAQLRVQRLRYEDLL 356
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958746508 477 ERAHGQM---LEEMQSLEEDKNRaIEEAFARAQVEM 509
Cdd:PRK10929 357 NKQPQLRqirQADGQPLTAEQNR-ILDAQLRTQREL 391
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
231-593 |
1.75e-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: 48.89 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 231 QLQEELVVLRERLALHDSDRQATTTQ-----LQNQVENLKEKLISQAQEVSRL-RSELGGTDVEKHRDRLMVENEQLRQE 304
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKkevksLQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 305 LRRCEAELQELRA----QPVVPCQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 380
Cdd:TIGR00606 555 KSRHSDELTSLLGyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 381 KAQEE--ERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEM 451
Cdd:TIGR00606 635 QDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 452 EQQLQNSHQLTIQLRAQIAMYEAELERahgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALR 531
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDL----KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEE 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 532 T---LTNDYNGLKRqvrgfpllLQEALRSVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 593
Cdd:TIGR00606 783 SakvCLTDVTIMER--------FQMELKDVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
303-596 |
1.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 303 QELRRCEAELQELRAQPvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTD--RLAEVELRLKDCLAE 380
Cdd:COG4717 71 KELKELEEELKEAEEKE----------EEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 381 KAQEEERLsRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTR-NQHLQEQVAMQRQVLKEMEQQLQNSH 459
Cdd:COG4717 141 LAELPERL-EELEERLEELRELEEE-------LEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 460 QLTIQLRAQIAMYEAELERAhgqmleEMQSLEEDKNRAIEEAFARAQVemkavhenlAGVRTNLLTLQPALRTLTNDYNG 539
Cdd:COG4717 213 EELEEAQEELEELEEELEQL------ENELEAAALEERLKEARLLLLI---------AAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746508 540 LKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNN------QELLRKYRRELQLRKKCHNELVR 596
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleEEELEELLAALGLPPDLSPEELL 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
231-406 |
2.00e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 231 QLQEELVVLRERLALHDSDRQATTTQLQ--NQVENLKEKLI---SQAQEVSRLRSELggTDVEKHRDRLmvenEQLRQEL 305
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIdvaSAEREIAELEAEL--ERLDASSDDL----AALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 306 RRCEAELQELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSElnLEVQQKTDRLAEVELRLKDCLAEKAqeE 385
Cdd:COG4913 695 EELEAELEELEEELD------ELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERFAAALGDAV--E 764
|
170 180
....*....|....*....|.
gi 1958746508 386 ERLSRRLRDSHETIASLKAQS 406
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
229-388 |
2.39e-05 |
|
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: 46.44 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 229 MSQLQEELVVLRERLalhdsdrqattTQLQNQVENLKEKLISQAQEVSRL-RSELGGTDVEKHRDRLMVENEQLRQELRR 307
Cdd:pfam13851 49 MSEIQQENKRLTEPL-----------QKAQEEVEELRKQLENYEKDKQSLkNLKARLKVLEKELKDLKWEHEVLEQRFEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 308 CEAELQELRAQpvvpcqgCEHS----QESTQLRDRLSQLQL----EVAENK-----GMLSELNLEvqqkTDRLAEVELRL 374
Cdd:pfam13851 118 VERERDELYDK-------FEAAiqdvQQKTGLKNLLLEKKLqalgETLEKKeaqlnEVLAAANLD----PDALQAVTEKL 186
|
170
....*....|....
gi 1958746508 375 KDCLAEKAQEEERL 388
Cdd:pfam13851 187 EDVLESKNQLIKDL 200
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
233-587 |
3.20e-05 |
|
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: 48.02 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 233 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEkLISQAQEVSRLRSELGgTDVEKHRDRLMVENEQLRQE--LRRCEA 310
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLE-QDYQAASDHLNLVQTALRQQekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 311 ELQELRAQPVVPCQGCEHSQES-TQLRDRLSQLQLEVAENKGMLSELN--LEVQQK--------TDRLAEVELRL----- 374
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYQqaLDVQQTraiqyqqaVQALEKARALCglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 375 -----KDCLAE-KAQEEER------LSRRLRDSHETIASLKAQSPPVKYVIKTVEVES--SKTKQALSESQTRnQHLQEQ 440
Cdd:COG3096 435 tpenaEDYLAAfRAKEQQAteevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ-QALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 441 VAMQRQVLKEMEQQLQNSHQLTIQLraqiamyeAELERAHGQMLEEMQSLEEDKNRAiEEAFARAQVEMKAVHENLAGVR 520
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLL--------EEFCQRIGQQLDAAEELEELLAEL-EAQLEELEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746508 521 TNLLTLQPALRTLTndynglKRQvrgfP--LLLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 587
Cdd:COG3096 585 QQLEQLRARIKELA------ARA----PawLAAQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
299-570 |
3.28e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 299 EQLRQELRRCEAELQELRAQpvvpCQGCEhsQESTQLRDRLSQLQ--LEVAENKGMLSELNLEVQQKTDRLAEVEL---- 372
Cdd:COG4913 613 AALEAELAELEEELAEAEER----LEALE--AELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 373 --RLKDCLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSE-----SQTRNQHLQEQV--AM 443
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLELRALLEERFaaAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 444 QRQVLKEMEQQLQNSHQltiQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMKAVHENLagVRTNL 523
Cdd:COG4913 760 GDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYLALLDRL--EEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958746508 524 LTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 570
Cdd:COG4913 830 PEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
220-583 |
3.31e-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: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 220 PVVHRtvEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRdrlmvene 299
Cdd:pfam07111 233 PEVHS--QTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPK-------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 300 QLRQELRRCEAELQELRAQpvVPCQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 379
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQ--LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQM 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 380 E--KAQEEERLSRRLRDS--------------------------HETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQ 431
Cdd:pfam07111 381 ElsRAQEARRRQQQQTASaeeqlkfvvnamsstqiwlettmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 432 TRNQHLQEQVA---MQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQve 508
Cdd:pfam07111 461 LRQESCPPPPPappVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746508 509 mkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 583
Cdd:pfam07111 538 -----ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
379-587 |
3.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 379 AEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 458
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 459 HQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 524
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746508 525 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 587
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRD----LRRELRELEAEI-ASLERRKSNipaRLLALRDAlAEALGLD 456
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
223-591 |
5.69e-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: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 223 HRTVEAMSQLQEELVVLRERLALHDSDRQATTtQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRlmVENEQL- 301
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR--DLQGQLa 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 302 ----RQELRRCEAELQELRAQPVVPCQGCE--HSQESTQ-LRDRLSQLQ-----LEVAENKGMLSELNLEVQQKTDRLAE 369
Cdd:TIGR00618 428 hakkQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQsLKEREQQLQtkeqiHLQETRKKAVVLARLLELQEEPCPLC 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 370 VELRLKDCLAEKAQEEERLSRRLRDSHETIASLKAqsppvkyVIKTVEVE-SSKTKQA--LSESQTRNQHLQEQVAMQRQ 446
Cdd:TIGR00618 508 GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET-------SEEDVYHQlTSERKQRasLKEQMQEIQQSFSILTQCDN 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 447 VLKEMEQQLQNshqLTIQLRAQIAMyEAELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAgvrtnLLTL 526
Cdd:TIGR00618 581 RSKEDIPNLQN---ITVRLQDLTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK-----LTAL 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746508 527 QPALRTLTNDYNGLK-RQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCH 591
Cdd:TIGR00618 649 HALQLTLTQERVREHaLSIRVLPKELLAsrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
227-460 |
6.90e-05 |
|
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: 46.74 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL------------GGTDVEKHRDRL 294
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLidlkehasslasSGLKKDSKLKSL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 295 MVENEQLRQELRRCEAELQelRAQpvvpcQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRl 374
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLK--KAH-----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 375 KDCLAEKAQE-EERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQ--RQVLKEM 451
Cdd:pfam10174 595 KNDKDKKIAElESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEktRQELDAT 674
|
....*....
gi 1958746508 452 EQQLQNSHQ 460
Cdd:pfam10174 675 KARLSSTQQ 683
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
233-605 |
8.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 233 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdvekhrDRLMVENEQLRQELRRCEAEL 312
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL---------EQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 313 QELRAQPVvpcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRL 392
Cdd:COG4372 83 EELNEQLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 393 RDSHETIASLKAQSPPVKYVIKtvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMY 472
Cdd:COG4372 157 EQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 473 EAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 552
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958746508 553 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIA 605
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
224-391 |
8.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 224 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENL---------KEKLISQAQEVSRLRSELGGTDVEKHRDRL 294
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleqAEEYQELKEELEELEEQLEELLGELEELLE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 295 MVENEQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQL--QLEVAENKGMLSELNLEVQQKTDRLAEVE- 371
Cdd:COG4717 424 ALDEEELEEELEELEEELEELE-------------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAe 490
|
170 180
....*....|....*....|....
gi 1958746508 372 ----LRLKDCLAEKAQEEERLSRR 391
Cdd:COG4717 491 ewaaLKLALELLEEAREEYREERL 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-610 |
9.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 335 LRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAevelrlkdcLAEKAQEEERLSRRLRDSHETIASLKAQsppvkyvik 414
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRE---------ALQRLAEYSWDEIDVASAEREIAELEAE--------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 415 tvevessktKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDK 494
Cdd:COG4913 677 ---------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 495 NRAIEEAFARAQVE------MKAVHENLAGVRTNLLTLQPALRTLTNDYNglkrqvRGFPLLLQEALRSVkAEIGQAIEE 568
Cdd:COG4913 748 RALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFN------REWPAETADLDADL-ESLPEYLAL 820
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958746508 569 VNS-NNQELLRKYRRELQLRKKCHNELV-----RLKGNIRVI-ARVRPV 610
Cdd:COG4913 821 LDRlEEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIkERIDPL 869
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-506 |
1.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 330 QESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 402
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 403 KAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEA---ELE 477
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 1958746508 478 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 506
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
227-595 |
1.05e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDVEKHRDRlmVENEQLRQELR 306
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS--SELEEMTKFKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 307 RCEAELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclAEKAQEEE 386
Cdd:pfam05483 402 NKEVELEELKKI----------LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 387 RLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLR 466
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 467 AQIAMYEAELERAHGQMLEEMQSLEEDKnRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 546
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958746508 547 fpllLQEALRSVKAEIGQAIEEVNSNNQ---ELLRKYRRELQLRKKCHNELV 595
Cdd:pfam05483 627 ----ENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-517 |
1.11e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 222 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEklisqaQEVSRLRSELGGT--DVEKHRDRLMVENE 299
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------EEQLRVKEKIGELeaEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 300 QLRQ---ELRRCEAELQELRAqpvvpcqgcehsqESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKD 376
Cdd:TIGR02169 316 ELEDaeeRLAKLEAEIDKLLA-------------EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 377 CLAEKAQEEERLS---RRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 453
Cdd:TIGR02169 383 TRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746508 454 QLQNSHQLTIQLRAQIAMYEAELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 517
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
334-500 |
1.36e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 334 QLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLsRRLRDSHETIASLKAqsppvkYVI 413
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNKE------YEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 414 KTVEVESSKTKQALSESQTRNqhLQEQVAMQRQVLKEMEQQLQnshqltiQLRAQIAMYEAELERAHGQMLEEMQSLEED 493
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 1958746508 494 KNRAIEE 500
Cdd:COG1579 165 REELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
224-588 |
1.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 224 RTVEAMSQLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKL-ISQAQEVSRLRSELggtdvekhrDRLMVENEQLR 302
Cdd:COG4717 153 ERLEELRELEEELEELEAELA-----------ELQEELEELLEQLsLATEEELQDLAEEL---------EELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 303 QELRRCEAELQELRAQpvvpCQGCEHSQESTQLRDRLSQLQL----------------EVAENKGMLSELNLEVQQKTDR 366
Cdd:COG4717 213 EELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAGVLFLVLGLLAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 367 LAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLKAQ-----SPPVKYVIKTVEvESSKTKQALSESQTRNQHLQEQV 441
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppDLSPEELLELLD-RIEELQELLREAEELEEELQLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 442 AMQRQV----------LKEMEQQLQNSHQLtIQLRAQIAMYEAELERAHGQMLEEMQSLEEDknrAIEEAFARAQVEMKA 511
Cdd:COG4717 368 LEQEIAallaeagvedEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEE 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746508 512 VHENLAGVRTNLLTLQPALRTLTNDYNGLKrqvrgfpllLQEALRSVKAEIGQAIEEVNSNN--QELLRKYRRELQLRK 588
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAE---------LLQELEELKAELRELAEEWAALKlaLELLEEAREEYREER 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
300-477 |
1.44e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 300 QLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 379
Cdd:COG1579 21 RLEHRLKELPAELAELE-------------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 380 EK-----AQEEERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVamqRQVLKEMEQQ 454
Cdd:COG1579 88 NKeyealQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAE 157
|
170 180
....*....|....*....|...
gi 1958746508 455 LQnshqltiQLRAQIAMYEAELE 477
Cdd:COG1579 158 LE-------ELEAEREELAAKIP 173
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
230-466 |
2.42e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 230 SQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSE---LGGT--DVEKHRDRLMVENEQLRQE 304
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERakkAGAQrkEEEAERKQLQAKLQQTEEE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 305 LRRCEAELQELR-AQPVVPCQGCEHSQESTQLRDRLSQLQLEVAENKGMLSELN-------------------------- 357
Cdd:pfam07888 187 LRSLSKEFQELRnSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaserkveglgeelssmaaq 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 358 ------------LEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLKA---------QSPPVKYVIKTV 416
Cdd:pfam07888 267 rdrtqaelhqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAelqrleerlQEERMEREKLEV 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958746508 417 EVESSKTKQALSESQTRNQhLQEQVAMQRQVLKEMEQQLQNSHQLTIQLR 466
Cdd:pfam07888 347 ELGREKDCNRVQLSESRRE-LQELKASLRVAQKEKEQLQAEKQELLEYIR 395
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
299-613 |
2.52e-04 |
|
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: 45.12 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 299 EQLRQELRRCEAE----LQELRAQPVVPCQGCEH-SQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 373
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDReSDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 374 LKdclaEKAQEEErlsrrlrDSHETIASLKAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 453
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 454 QLQN---------SHQLTIQ-LRAQIAMYE----------------AELERAHGQMLEE---MQSLEEDKNRAIEEAFar 504
Cdd:pfam05557 154 LRQNlekqqsslaEAEQRIKeLEFEIQSQEqdseivknskselariPELEKELERLREHnkhLNENIENKLLLKEEVE-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 505 aqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL-- 576
Cdd:pfam05557 232 ---DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSArq 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958746508 577 LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 613
Cdd:pfam05557 309 LEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
222-526 |
2.53e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 222 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQL---QNQVENLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVEN 298
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 299 EQLRQELRRCEAELQELRaqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 378
Cdd:COG4372 111 EELQEELEELQKERQDLE-------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 379 AEKAQEE-ERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVamQRQVLKEMEQQLQN 457
Cdd:COG4372 178 EAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA--LELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746508 458 SHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTL 526
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
294-581 |
3.70e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 294 LMVENEQLRQELRRCEAELQELRAQPVvpcqgcehSQESTQLRDRL----SQLQLEVAENKgmlselnlEVQQKTDRLAE 369
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEA--------EEKNEEIQERIdqlyDILEREVKARK--------YVEKNSDTLPD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 370 VELRLKDCLAEKAQEEERLSRRLRDSH---ETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQ 446
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVKQSYTLNEselESVRQLEKQ-------LESLEKQYDEITERIAEQEIAYSELQEELEEILK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 447 VLKEMEQQlqnshQLTIQLRAQiAMYEAELErAHgQMLEEMQS-LEEDKnRAIE------------EAFARAQVEMKAVH 513
Cdd:PRK04778 391 QLEEIEKE-----QEKLSEMLQ-GLRKDELE-AR-EKLERYRNkLHEIK-RYLEksnlpglpedylEMFFEVSDEIEALA 461
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746508 514 ENLAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQAIEEVnsnnQELLRKYR 581
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAEALNEA----ERLFREYD 534
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
227-394 |
4.94e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL-----GGTDVEKHRDRLMVENEQL 301
Cdd:PRK09039 53 SALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 302 RQELRRCEAELQELRAQpvvpcqgcehsqeSTQLRDRLSQLQ--LEVAENKGmlselnlevQQKTDRLAEVELRLKDCLA 379
Cdd:PRK09039 129 KQVSARALAQVELLNQQ-------------IAALRRQLAALEaaLDASEKRD---------RESQAKIADLGRRLNVALA 186
|
170 180
....*....|....*....|..
gi 1958746508 380 EKAQEeerLSR-------RLRD 394
Cdd:PRK09039 187 QRVQE---LNRyrseffgRLRE 205
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
227-570 |
5.57e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 227 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLisqaQEVSRLRSElgGTDVEKHR--DRLMVENEQLRQE 304
Cdd:PRK04778 140 EEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTES--GDYVEAREilDQLEEELAALEQI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 305 LRRCEAELQELraQPVVPcqgcehsQESTQLRDRLSQLQLE--VAENKGMLSELnlevQQKTDRLAEVELRLKDC-LAEK 381
Cdd:PRK04778 214 MEEIPELLKEL--QTELP-------DQLQELKAGYRELVEEgyHLDHLDIEKEI----QDLKEQIDENLALLEELdLDEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 382 AQEEERLSRRLRDSHETI-ASLKAQsppvkyviKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQ 460
Cdd:PRK04778 281 EEKNEEIQERIDQLYDILeREVKAR--------KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 461 LTIQLRAQIAMYEAELERAHGQ-----MLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTltn 535
Cdd:PRK04778 353 LEKQLESLEKQYDEITERIAEQeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHE--- 429
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958746508 536 dyngLKRQVR-----GFPLLLQEALRSVKAEIGQAIEEVN 570
Cdd:PRK04778 430 ----IKRYLEksnlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
219-345 |
8.30e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 219 DPVVHRTVEAMSQLQEELVVLRErlaLHDSDRQATTTQLQNqvenLKEKLISQAQEVSRLRSELggTDVEKHRDRLMVEN 298
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELDR----AKEKLKKLLQEIMIKVKKL--EELEEELQELESKI 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958746508 299 EQLRQELRRCEAELQELRAQpVVPCQGCEHSQEStQLRDRLSQLQLE 345
Cdd:smart00787 242 EDLTNKKSELNTEIAEAEKK-LEQCRGFTFKEIE-KLKEQLKLLQSL 286
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
224-602 |
8.65e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 224 RTVEAMSQLQE----------ELVVLRERLALHDSDRQ--ATTTQLQNQVEnLKEKLISQ--------AQEVSRLRSE-- 281
Cdd:pfam10174 186 RIAEAEMQLGHlevlldqkekENIHLREELHRRNQLQPdpAKTKALQTVIE-MKDTKISSlernirdlEDEVQMLKTNgl 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 282 LGGTD----------VEKHRDRLMVENEQLRQELRRCEAELQELRA-------QPVVPCQGCEHSQESTQLRD-RLSQLQ 343
Cdd:pfam10174 265 LHTEDreeeikqmevYKSHSKFMKNKIDQLKQELSKKESELLALQTkletltnQNSDCKQHIEVLKESLTAKEqRAAILQ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 344 LEVAENKGMLSELNLEVQQKTDRLAEV---------ELR-LKDCLAEKAQEE-------ERLSRRLRDSHETIASLKAQs 406
Cdd:pfam10174 345 TEVDALRLRLEEKESFLNKKTKQLQDLteekstlagEIRdLKDMLDVKERKInvlqkkiENLQEQLRDKDKQLAGLKER- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 407 ppvkyvIKTVEVESSKT-------KQALSESQTRNQHLQEQVAMQ-RQVLKEMEQQLQNSHQLTIQLRAQiamyeaeler 478
Cdd:pfam10174 424 ------VKSLQTDSSNTdtalttlEEALSEKERIIERLKEQREREdRERLEELESLKKENKDLKEKVSAL---------- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 479 aHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKavhenlagvrtnLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSv 558
Cdd:pfam10174 488 -QPELTEKESSLIDLKEHASSLASSGLKKDSK------------LKSLEIAVEQKKEECSKLENQ-------LKKAHNA- 546
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958746508 559 kAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIR 602
Cdd:pfam10174 547 -EEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILR 589
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
225-499 |
1.01e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 225 TVEAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELGgtDVEKHRDRLMVENEQLRQE 304
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRD----ELNEELKELAEKRDELNAQVKELREEAQ--ELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 305 LRRCEAELQELRAQpvVPCQGCEHSQEST------QLRDRLSQLQLEVaENKGMLSELNLEVQQKTDRL------AEVEL 372
Cdd:COG1340 80 RDELNEKLNELREE--LDELRKELAELNKaggsidKLRKEIERLEWRQ-QTEVLSPEEEKELVEKIKELekelekAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 373 RLKDCLAEKAQEEERLSRRLRDSHETIASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEME 452
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958746508 453 QQLQnshqltiQLRAQIAMYEAELERAhgQMLEEMQSLEEDKNRAIE 499
Cdd:COG1340 237 KELR-------ELRKELKKLRKKQRAL--KREKEKEELEEKAEEIFE 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
228-405 |
1.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 228 AMSQLQEELVVLRERLALHDSDRQATTtQLQNQVENLKEKLISQAQEVSRlRSELGGTDVEKHRDRLMVENEQLRQELRR 307
Cdd:PRK04863 919 ALAQLEPIVSVLQSDPEQFEQLKQDYQ-QAQQTQRDAKQQAFALTEVVQR-RAHFSYEDAAEMLAKNSDLNEKLRQRLEQ 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 308 CEaelqelraqpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC-------LAE 380
Cdd:PRK04863 997 AE--------------------QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgAEE 1056
|
170 180
....*....|....*....|....*.
gi 1958746508 381 KAQE-EERLSRRLRDSHETIASLKAQ 405
Cdd:PRK04863 1057 RARArRDELHARLSANRSRRNQLEKQ 1082
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
357-585 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 357 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLKAQsppvkyvIKTVEVESSKTKQ 425
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 426 ALSESQTRNQ--HLQEQVAMQRQVLKEMEQQLQnshqltiQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFA 503
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLA-------EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 504 RAQVEMKAvheNLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 580
Cdd:COG3206 270 AQLAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 1958746508 581 RRELQ 585
Cdd:COG3206 340 EARLA 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
340-612 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 340 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDS-------HET 398
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKNltvepvkGSN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 399 IASLKAQSP-PVK-----------YVIKTVEVESSKTKQA--------------LSESQT-----RNQH----LQEQVAM 443
Cdd:COG3206 137 VIEISYTSPdPELaaavanalaeaYLEQNLELRREEARKAlefleeqlpelrkeLEEAEAaleefRQKNglvdLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 444 QRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQS--LEEDKNRAIEEAFARAQV---------EMKAV 512
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELsarytpnhpDVIAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 513 HENLAGVRTNLLT-LQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRkYRRELQLRKKCH 591
Cdd:COG3206 297 RAQIAALRAQLQQeAQRILASLEAELEALQARE--------ASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELY 367
|
330 340 350
....*....|....*....|....*....|..
gi 1958746508 592 NELV-RLK----------GNIRVIARVRPVTK 612
Cdd:COG3206 368 ESLLqRLEearlaealtvGNVRVIDPAVVPLK 399
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
262-526 |
1.20e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 262 ENLKEKLISQAQEVSRLRSELggtdvekhRDRLMVENEQLRQELRRceaELQELRAQpvvpcqgcehSQESTQLRDRLSQ 341
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFSLLK--------KETIYLQSAQRVELAER---QLQELKID----------VKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 342 LQLEVAENKGML-SELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLKAQSPPVKYVIKTVEV 418
Cdd:COG5022 904 LESEIIELKKSLsSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTI 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 419 ESSKTKQALSESQTRNQHLQEQV----AMQRQV--LKEMEQQLQNSHQLTIQLRA-----QIAMYEAELERAHgqMLEEM 487
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQKLKGLL--LLENN 1060
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958746508 488 QSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 526
Cdd:COG5022 1061 QLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
391-598 |
1.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 391 RLRDSHETIASLKAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 457
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 458 SH-----QLTIQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 525
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746508 526 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 598
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
257-524 |
1.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 257 LQNQVENLKEKLISQAQEVSRLRsELGGTDVEKHRDrlMVENEqlrqelrRCEAElqelraqpvvpcqgcEHSQESTQLR 336
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQN--KYDEL-------VEEAK---------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 337 DRLSQLQLEVAENKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrLRDSHETIAslkaqsp 407
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK-IKDKLKELQ------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 408 pvkyviktvevessktkQALSESQTRNQHLQE---QVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQML 484
Cdd:PHA02562 313 -----------------HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958746508 485 EEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 524
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
336-494 |
1.94e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 40.75 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 336 RDRLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLKA---QSPPV 409
Cdd:cd07627 34 RKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQRQKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 410 KYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltiqlraqiamYEAELERAHGQMLEEMQS 489
Cdd:cd07627 114 WQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASE--------------LKKEFEEVSELIKSELER 179
|
....*
gi 1958746508 490 LEEDK 494
Cdd:cd07627 180 FERER 184
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
331-590 |
2.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 331 ESTQLRDRLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLKAQSppvk 410
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAEIEDLRETIAETERER---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 411 yviKTVEVESSKTKQALSESQTRNQHL----------QEQVAMQRQVLKEMEQQLQNSHQltiQLRAQIAMYEAELERAh 480
Cdd:PRK02224 275 ---EELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLE---ECRVAAQAHNEEAESL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 481 gqmLEEMQSLEEDKNRAIEEAfARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqEALRSVKA 560
Cdd:PRK02224 348 ---REDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERD 422
|
250 260 270
....*....|....*....|....*....|..
gi 1958746508 561 EIGQAIEEVNSNNQELLRKYR--RELQLRKKC 590
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaEALLEAGKC 454
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
387-510 |
2.16e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 387 RLSRRLRDshETIASLKAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 456
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746508 457 -------NSHQLtIQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 510
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
169-506 |
2.46e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 169 KEDRLPKRQAPAPRRDREAPEAGGTMNVEKPGGRLLGIGRCSSLS--GSPGPDPVVHRT-VEAMSQLQEELVVLRERLAl 245
Cdd:pfam15709 220 KSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETEDASerGAFSSDSVVEDPwLSSKYDAEESQVSIDGRSS- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 246 hdSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSElggtdveKHRDRLMVEneqlRQELRRCEAELQElraqpvvpcqg 325
Cdd:pfam15709 299 --PTQTFVVTGNMESEEERSEEDPSKALLEKREQEK-------ASRDRLRAE----RAEMRRLEVERKR----------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 326 cehsQESTQLRdRLSQLQLEVAENkgMLSELNLEVQQKTDRLAEVELRLKDclAEKAQEEERLSRRLRdshETIASLKAQ 405
Cdd:pfam15709 355 ----REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQ---LQAAQERAR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 406 SPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQVLKEMEQQlqnsHQLTIQLRAQiamyEAElERAHGQ 482
Cdd:pfam15709 423 QQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKRLMEMAEE----ERLEYQRQKQ----EAE-EKARLE 493
|
330 340
....*....|....*....|....
gi 1958746508 483 MLEEMQSLEEDKNRAIEEAFARAQ 506
Cdd:pfam15709 494 AEERRQKEEEAARLALEEAMKQAQ 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
212-591 |
2.48e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 212 LSGSPGPD-PVVHRTVEAMSQLQEELVVLRERLalhdsdrqattTQLQNQVENLKEKLISQAQEVSRLRSElggtdvekh 290
Cdd:TIGR00618 519 DIDNPGPLtRRMQRGEQTYAQLETSEEDVYHQL-----------TSERKQRASLKEQMQEIQQSFSILTQC--------- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 291 RDRLMVENEQLRQELRRCEAELQELraqpvvpcqgcehSQESTQLRDrLSQLQLEVAENKGMLSELNLEVQQKTDRLAEV 370
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKL-------------SEAEDMLAC-EQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 371 ELRLKDCLAEKAQEEERLSRRL-----------RDSHETIA-SLKAQSPPVK----------YVIKTVEVESSKTKQALS 428
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSirvlpkellasRQLALQKMqSEKEQLTYWKemlaqcqtllRELETHIEEYDREFNEIE 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 429 E-SQTRNQHLQEQVAMQRQVLKEMEqqlqnsHQLTIQLRAQIAMYEAELERA-----HGQMLEEMQSLEEDKNRAIEEAF 502
Cdd:TIGR00618 725 NaSSSLGSDLAAREDALNQSLKELM------HQARTVLKARTEAHFNNNEEVtaalqTGAELSHLAAEIQFFNRLREEDT 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 503 A-----RAQVEMKAVH---------ENLAGVRTNLLTLqpaLRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIGQAI 566
Cdd:TIGR00618 799 HllktlEAEIGQEIPSdedilnlqcETLVQEEEQFLSR---LEEKSATLGEITHQLLKYEECSKqlAQLTQEQAKIIQLS 875
|
410 420 430
....*....|....*....|....*....|..
gi 1958746508 567 EEVNSNNQ-------ELLRKYRRELQLRKKCH 591
Cdd:TIGR00618 876 DKLNGINQikiqfdgDALIKFLHEITLYANVR 907
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
226-505 |
4.00e-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: 40.83 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 226 VEAMSQLQEELVVLRERLALHDSDRQATT------TQLQNQVENLKEKL--ISQAQEVSRLRSELGGTDVEKHRDR---- 293
Cdd:pfam05622 27 QEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCEELEKEVLELQHRneel 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 294 --LMVENEQLRQE---LR-------RCEA----------ELQELRAQ--------PVVPCQGCEHSQES---TQLRDRLS 340
Cdd:pfam05622 107 tsLAEEAQALKDEmdiLRessdkvkKLEAtvetykkkleDLGDLRRQvklleernAEYMQRTLQLEEELkkaNALRGQLE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 341 QLQLEVAENKGMLSELNLevqqKTDRLAEVELRLKDCLAEKAQEEERL-SRR--LRDSHE--------------TIASLK 403
Cdd:pfam05622 187 TYKRQVQELHGKLSEESK----KADKLEFEYKKLEEKLEALQKEKERLiIERdtLRETNEelrcaqlqqaelsqADALLS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 404 AQSPPVKYVIKtvEVESSKTKQALSESQTRNQHLQE-QVAMQRQVLKEMEQQLQNSHQLTIQLRAQiamyeaelERAHGQ 482
Cdd:pfam05622 263 PSSDPGDNLAA--EIMPAEIREKLIRLQHENKMLRLgQEGSYRERLTELQQLLEDANRRKNELETQ--------NRLANQ 332
|
330 340
....*....|....*....|...
gi 1958746508 483 MLEEMQSLEEDKNRAIEEAFARA 505
Cdd:pfam05622 333 RILELQQQVEELQKALQEQGSKA 355
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
299-509 |
4.19e-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: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 299 EQLRQELRRCEAELQELRAQpvvpcqgcehSQESTQLRDRLSQLQLEVAENKGMLSELNLEVQQktdRLAEVELRLKDCL 378
Cdd:cd07596 7 EEAKDYILKLEEQLKKLSKQ----------AQRLVKRRRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 379 AEKAQEEERLSRR--------LRDSHETIASLKAqsppvkyVIKT-----VEVESSKtkQALSESQTRNQHLQEQVAMQR 445
Cdd:cd07596 74 EELSSLSEAQANQelvkllepLKEYLRYCQAVKE-------TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746508 446 QVLKEMEQQLQNSHQLTIQLRAqiamyeaELERAHGQMLEEMQSLEEDKNRAIEEA---FARAQVEM 509
Cdd:cd07596 145 AKVEELEEELEEAESALEEARK-------RYEEISERLKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
286-520 |
4.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 286 DVEKHRDRLMVENEQLRQELRRCEAELQELRAQPV-----VPcqgcEHSQESTQLRDRLSQLQLEVAENKGMLSELNLEV 360
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDelnaqVK----ELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 361 QQKTDRLAEVElRLKDCLAEKAQEEERLSR---RLRDSHET--------------IASLKAQsppvkyvIKTVEVESSKT 423
Cdd:COG1340 88 NELREELDELR-KELAELNKAGGSIDKLRKeieRLEWRQQTevlspeeekelvekIKELEKE-------LEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 424 KQaLSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQSLEEdknraIEEAFA 503
Cdd:COG1340 160 EK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE-----LHEEII 233
|
250
....*....|....*..
gi 1958746508 504 RAQVEMKAVHENLAGVR 520
Cdd:COG1340 234 ELQKELRELRKELKKLR 250
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
231-466 |
5.26e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 231 QLQEELVVLRERLALHDSDRqatttqlqNQVENLKEKLISQAQEVSRlrSELGGTDVE---KHRD-RLMVEN-EQLRQEL 305
Cdd:COG3096 452 QATEEVLELEQKLSVADAAR--------RQFEKAYELVCKIAGEVER--SQAWQTAREllrRYRSqQALAQRlQQLRAQL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 306 RRCEaelQELRAQpvvpcqgcehsQESTQLRDRLSQLQLEVAENKGMLSELnlevqqktdrLAEVELRLKDCLAEKAQEE 385
Cdd:COG3096 522 AELE---QRLRQQ-----------QNAERLLEEFCQRIGQQLDAAEELEEL----------LAELEAQLEELEEQAAEAV 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 386 ERLS--RRLRDSHET-IASLKAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT 462
Cdd:COG3096 578 EQRSelRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALE 657
|
....
gi 1958746508 463 IQLR 466
Cdd:COG3096 658 SQIE 661
|
|
| Vps5 |
pfam09325 |
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
336-508 |
7.57e-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: 39.19 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 336 RDRLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLKA---QSPPV 409
Cdd:pfam09325 54 RKELASATGEFAKSLASLASLELStgLSRALSQLAEVEERIKELLERQALQDVLtLGETIDEYLRLIGSVKAvfnQRVKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 410 KYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltiqlraqiamYEAELERAHGQMLEEMQS 489
Cdd:pfam09325 134 WQSWQNAEQELSKKKEQLEKLLRANKSQNDKLQQAKKEVEELERRVQQ--------------AEKEFEDISELIKKELER 199
|
170 180
....*....|....*....|..
gi 1958746508 490 LEEDKN---RAIEEAFARAQVE 508
Cdd:pfam09325 200 FELERVddfKNSVEIYLESAIE 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
288-610 |
7.61e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 288 EKHRDRLMVENEQLRQELRRCEAELQElraqpvvpcqgcehSQEstqlrdRLSQLQLEVAENKGMLSELNLEVQQKTDRL 367
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAA--------------EQY------RLVEMARELAELNEAESDLEQDYQAASDHL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 368 A--------------------EVELRLKDCLA--EKAQEE-ERLSRRLRDSHETIASLKAQSPPVkyviktvevessktK 424
Cdd:PRK04863 338 NlvqtalrqqekieryqadleELEERLEEQNEvvEEADEQqEENEARAEAAEEEVDELKSQLADY--------------Q 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 425 QALSESQTRNqhLQEQVAMQRqvLKEMEQQLQNSHQLTIQLRAQIAMYEAELERAHGQMLEEMQ--SLEEDKNRAIEEAF 502
Cdd:PRK04863 404 QALDVQQTRA--IQYQQAVQA--LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQklSVAQAAHSQFEQAY 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 503 A----------------------RAQVEMKAVHENLAGVRTNLLTLQPALRT------LTNDYNglkrQVRGFPLLLQEA 554
Cdd:PRK04863 480 QlvrkiagevsrseawdvarellRRLREQRHLAEQLQQLRMRLSELEQRLRQqqraerLLAEFC----KRLGKNLDDEDE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746508 555 LRSVKAEIGQAIEEVNSnNQELLRKYRRELQlrkkchNELVRLKGNIRVIARVRPV 610
Cdd:PRK04863 556 LEQLQEELEARLESLSE-SVSEARERRMALR------QQLEQLQARIQRLAARAPA 604
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
274-455 |
8.22e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 38.73 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 274 EVSRLRSELggTDVEKHRDRLMVENEQLRQELRRCEAELQEL-RAQPVVPCQGCEHSQESTQLRDRLSQLQLEVAENKGM 352
Cdd:pfam15619 12 KIKELQNEL--AELQSKLEELRKENRLLKRLQKRQEKALGKYeGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746508 353 LSELNLEVQQKTDRLAEVELRLKD-CLAEKAQEEERLSR---RLRDSHETIASLKaqsppvkyviKTVEVESSKTKQAL- 427
Cdd:pfam15619 90 LKEKEAELLRLRDQLKRLEKLSEDkNLAEREELQKKLEQleaKLEDKDEKIQDLE----------RKLELENKSFRRQLa 159
|
170 180 190
....*....|....*....|....*....|....
gi 1958746508 428 ------SESQTRNQHLQEQVAMQRQVLKEMEQQL 455
Cdd:pfam15619 160 aekkkhKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| |
