|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
596-923 |
0e+00 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 534.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 596 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 674
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 675 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 751
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 752 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 831
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 832 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 911
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 568956226 912 LRFAERVRSVEL 923
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
604-921 |
3.21e-147 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 440.47 E-value: 3.21e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 604 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 680
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 681 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 760
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 761 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 837
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 838 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFA 915
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 568956226 916 ERVRSV 921
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
598-925 |
2.14e-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: 428.14 E-value: 2.14e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 673
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 674 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 753
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 754 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 831
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 832 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 909
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 568956226 910 YSLRFAERVRSVELGP 925
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
598-919 |
2.66e-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: 378.14 E-value: 2.66e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 674
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 675 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 752
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 753 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 830
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 831 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 909
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 568956226 910 YSLRFAERVR 919
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
598-921 |
1.35e-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: 332.12 E-value: 1.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 669
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 670 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 746
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 747 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 822
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 823 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 901
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 568956226 902 EKNTSETLYSLRFAERVRSV 921
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
599-922 |
1.10e-102 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 324.67 E-value: 1.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 599 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 676
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 677 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 750
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 751 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 820
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 821 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 897
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 568956226 898 VSPVEKNTSETLYSLRFAERVRSVE 922
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
598-921 |
5.69e-94 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 301.57 E-value: 5.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 660
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 661 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 739
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 740 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 818
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 819 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 893
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 568956226 894 MVVQVSPVEKNTSETLYSLRFAERVRSV 921
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
598-921 |
5.24e-91 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 292.70 E-value: 5.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 675
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 676 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 752
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 753 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 832
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 833 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 911
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 568956226 912 LRFAERVRSV 921
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
597-921 |
2.50e-89 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 289.64 E-value: 2.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 597 GNIRVIARVRPVTKEDGEGPeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQE 661
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 662 VQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDLL 739
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 740 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 814
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 815 TGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 884
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 568956226 885 SLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSV 921
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
598-921 |
1.43e-88 |
|
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: 286.15 E-value: 1.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 676
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 677 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 756
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 757 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 832
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 833 RVGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 910
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 568956226 911 SLRFAERVRSV 921
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
598-921 |
4.65e-86 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 280.75 E-value: 4.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 672
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 673 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 741
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 742 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 816
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 817 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 896
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 568956226 897 QVSPVEKNTSETLYSLRFAERVRSV 921
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
582-922 |
6.69e-81 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 273.92 E-value: 6.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 582 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 661
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 662 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 740
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 741 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 820
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 821 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 898
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 568956226 899 SPVEKNTSETLYSLRFAERVRSVE 922
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
599-916 |
4.49e-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: 256.17 E-value: 4.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 599 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 667
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 668 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 743
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 744 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 818
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 819 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 890
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 568956226 891 KTLMVVQVSPVEKNTSETLYSLRFAE 916
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
598-919 |
2.16e-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: 254.36 E-value: 2.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 676
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 677 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgkEP- 743
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 744 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 820
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 821 gKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 896
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 568956226 897 QVSPVEKNTSETLYSLRFAERVR 919
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
598-919 |
2.96e-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: 239.33 E-value: 2.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 674
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 675 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 754
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 755 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 833
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 834 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLR 913
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 568956226 914 FAERVR 919
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
599-919 |
1.31e-70 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 237.86 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 599 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 667
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 668 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 744
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 745 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 819
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 820 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 898
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 568956226 899 SPVEKNTSETLYSLRFAERVR 919
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
598-918 |
2.87e-66 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 225.64 E-value: 2.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 598 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 669
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 670 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 745
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 746 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 825
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 826 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 903
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 568956226 904 NTSETLYSLRFAERV 918
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
599-922 |
1.59e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 216.34 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 599 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 677
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 678 FAYGQTGAGKTYTMEGtPENP-----------GINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLgk 741
Cdd:PLN03188 170 FAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 742 EP-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLR 818
Cdd:PLN03188 247 DPsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 819 T--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSK 891
Cdd:PLN03188 325 SfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAK 404
|
330 340 350
....*....|....*....|....*....|.
gi 568956226 892 TLMVVQVSPVEKNTSETLYSLRFAERVRSVE 922
Cdd:PLN03188 405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
578-739 |
1.68e-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: 151.60 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 578 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 657
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 658 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 737
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 568956226 738 LL 739
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
646-865 |
7.41e-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: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 646 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 724
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 725 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 804
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956226 805 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 865
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-542 |
9.01e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 229 QLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELRRCEV 308
Cdd:TIGR02169 671 SEPAELQRLRERLE-----------GLKRELSSLQSELRRIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 309 ELQELRAQ--------PVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLS------------ELNLEVQQKTDRLAEV 368
Cdd:TIGR02169 738 RLEELEEDlssleqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 369 ELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV 445
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 446 LKEMEQQLQ---------NSHQLTVQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEEDKNRA 495
Cdd:TIGR02169 898 LRELERKIEeleaqiekkRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLA 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568956226 496 IE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 542
Cdd:TIGR02169 978 IQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-582 |
6.23e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 255 LQNQVENLKEKlISQAQEVSRLRSELggtdAEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLR 334
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAEL----RELELALLVLRLEELREELEELQEELKEAE-------------EELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 335 DKLSQLQLEVAENKGMLSELNLEVQQKTDRLaeveLRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTV 414
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 415 EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT--------------VQLRAQIAMYEAELER--AH 478
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 479 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 558
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330 340
....*....|....*....|....*.
gi 568956226 559 EIGQAIEEVNS--NNQELLRKYRREL 582
Cdd:TIGR02168 483 ELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
237-499 |
3.45e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 70.43 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 237 LRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQ 316
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 317 pvvpcegcehsqessqlrdkLSQLQLEVAENKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 394
Cdd:COG3206 242 --------------------LAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 395 ETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAe 473
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV- 362
|
250 260
....*....|....*....|....*.
gi 568956226 474 LERAHGQMLEEMQSLEEDKNRAIEEA 499
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-506 |
3.99e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELR 304
Cdd:COG1196 246 AELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 305 RCEVELQELRAQpvvpcegcehsqeSSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 384
Cdd:COG1196 320 ELEEELAELEEE-------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 385 RLSRRLRDSHETIASLRAQsppvKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 464
Cdd:COG1196 387 ELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568956226 465 AQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 506
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-584 |
1.96e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 252 TTQLQNQVENLKEKLiSQAQEVSRLRSELGGTDAE---KHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehsq 328
Cdd:COG1196 195 LGELERQLEPLERQA-EKAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAE------------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 329 essqlrdkLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvk 408
Cdd:COG1196 262 --------LAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEE----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 409 yvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSL 488
Cdd:COG1196 325 --LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 489 EEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEE 566
Cdd:COG1196 403 EELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAA 478
|
330
....*....|....*...
gi 568956226 567 VNSNNQELLRKYRRELQL 584
Cdd:COG1196 479 LAELLEELAEAAARLLLL 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-574 |
6.13e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTT---QLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHR--DRLM---VEN 296
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTerdQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlwDRDTgnsITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRCEVELQELRAQPVVPCEGCEHSQE--------SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEV 368
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMErqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 369 ELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQRQVLK 447
Cdd:pfam15921 495 ERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 448 EMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENL 514
Cdd:pfam15921 566 ILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERL 645
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 515 AGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 574
Cdd:pfam15921 646 RAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-504 |
2.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELR 304
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERLEELEEEL---------AELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 305 RCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 384
Cdd:COG1196 341 ELEEELEEAEEE----------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 385 RLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 464
Cdd:COG1196 411 ALLERLERLEEELEELEEA-------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568956226 465 AQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFARAQ 504
Cdd:COG1196 484 EELAEAAARLL-----LLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-403 |
3.36e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTTQL-QNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN------- 296
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARL--DALREELDELEAQIrgnggdr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 -EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC 375
Cdd:COG4913 340 lEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 568956226 376 LAEKAQEEERLSRRLRDSHETIASLRAQ 403
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
327-628 |
4.05e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 327 SQESSQL--RDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 404
Cdd:TIGR02168 667 KTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 405 PPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG----- 479
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanl 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 480 ----QMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRS 555
Cdd:TIGR02168 823 rerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRS 894
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956226 556 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI-RVIARVRPVTKEDGEGPEA-TNAVTFDPDD 628
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEAlENKIEDDEEE 969
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-604 |
1.22e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 236 VLRERLALHDSDR-----QATTTQLQNQVENLkEKLISQAQEVSRLRSELGGTDAEKHR--DRLMVENEQLRQELRRCEV 308
Cdd:PRK03918 150 VVRQILGLDDYENayknlGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 309 ELQELRAqpvvpcegcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEK 379
Cdd:PRK03918 229 EVKELEE-----------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 380 AQEEERLSR-------RLRDSHETIASLRAQSPPVKYVIKtvevESSKTKQALSESQTRNQHLQEQVAmqrqVLKEMEQQ 452
Cdd:PRK03918 292 AEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 453 LQNSHQLTVQ---LRAQIAMYEAE--------LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----- 506
Cdd:PRK03918 364 YEEAKAKKEElerLKKRLTGLTPEklekeleeLEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcg 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 507 -----------MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELL 575
Cdd:PRK03918 443 relteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEEL 520
|
410 420
....*....|....*....|....*....
gi 568956226 576 RKYRRELQLRKKchnELVRLKGNIRVIAR 604
Cdd:PRK03918 521 EKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
580-864 |
1.67e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 58.21 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 580 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 647
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 648 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 726
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 727 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 800
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956226 801 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 864
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-597 |
3.00e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 220 VHRTVEAMSQLQEELVVLRERLALHDSDR---QATTTQLQNQVENLKEKLISQAQEVSRLRsELGGtDAEKHRdRLMVEN 296
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELK-ELKE-KAEEYI-KLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRCEVEL----QELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNlEVQQKTDRLAEVELRL 372
Cdd:PRK03918 303 EEYLDELREIEKRLsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 373 KDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTV-----EVESSKTKQALSESQTRNQHLQEQVAMQRQVL 446
Cdd:PRK03918 382 TGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELkkaieELKKAKGKCPVCGRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 447 KEMEQQLQNSHQLTVQLRAQIAMYEAELER-----AHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNL 521
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956226 522 LTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKG 597
Cdd:PRK03918 542 KSLKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
221-585 |
4.02e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 221 HRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQN-----QVENLKEKLISQAQEVSRLRSELggtdaeKHRDRLMVE 295
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 296 NEQLRQELRRCEVELQELRAQPVVpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdc 375
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 376 laEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQTRNQHLQEQV 439
Cdd:COG4717 237 --EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 440 AMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVemkavhENLAGVR 518
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGV------EDEEELR 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956226 519 tNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 585
Cdd:COG4717 389 -AALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-477 |
4.32e-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: 56.31 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 254 QLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLmvenEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQL 333
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQL-----AALERRI----AALARRIRALEQELAALE-------------AELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 334 RDKLSQLQLEVAENKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLRAQSPP 406
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956226 407 VKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERA 477
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-501 |
5.43e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 220 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLqnqvENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQL 299
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELAEELAELEEKL---------EELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 300 RQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLaevelrlkdclaEK 379
Cdd:TIGR02168 357 EAELEELEAELEELESRLE------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR------------ER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 380 AQEEERLSRRLRDSHEtiaslraqsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQnshql 459
Cdd:TIGR02168 419 LQQEIEELLKKLEEAE---------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD----- 478
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568956226 460 tvQLRAQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFA 501
Cdd:TIGR02168 479 --AAERELAQLQARLD-----SLERLQENLEGFSEGVKALLK 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
264-566 |
5.80e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.11 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 264 EKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELR--------------RCEVELQELRAQpvvpceGCEHSQE 329
Cdd:pfam01576 359 EELTEQLEQAKRNKANL-----EKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQAR------LSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 330 SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSP 405
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 406 PVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQLTVQLRAQIAMYEaELERAHGQMLEE 484
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYD-KLEKTKNRLQQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 485 MQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRG 544
Cdd:pfam01576 582 LDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQ 661
|
330 340
....*....|....*....|..
gi 568956226 545 FPLLLqEALRSVKAEIGQAIEE 566
Cdd:pfam01576 662 LRAEM-EDLVSSKDDVGKNVHE 682
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
247-583 |
5.91e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 247 DRQATTtqLQNQVENLKEKLISQAQEVSRLRSELG---------GTDAEKHRDRLMVENEQLRQE--LRRCEVELQELRA 315
Cdd:PRK04863 285 LEEALE--LRRELYTSRRQLAAEQYRLVEMARELAelneaesdlEQDYQAASDHLNLVQTALRQQekIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 316 QPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKD 374
Cdd:PRK04863 363 RLEEQNEVVEEADEQqEENEARAEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 375 CLAE-KAQEEERLSRRLR-----DSHETIASLRAQSppVKYVIKTV-EVESSKTKQALSE--SQTRNQ-HLQEQVAMQRQ 444
Cdd:PRK04863 443 WLEEfQAKEQEATEELLSleqklSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 445 VLKEMEQQLQNsHQLTVQLRAQ-----IAMY--EAELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLA 515
Cdd:PRK04863 521 RLSELEQRLRQ-QQRAERLLAEfckrlGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956226 516 GVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 583
Cdd:PRK04863 600 ARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-479 |
1.25e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 221 HRTVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLR 300
Cdd:COG1196 291 YELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEEL---------EEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 301 QELRRCEVELQELRAQpvvpcegcEHSQESSQLRDKLSQLQLEVAEnkgmlSELNLEVQQKTDRLAEVELRLKDCLAEKA 380
Cdd:COG1196 358 AELAEAEEALLEAEAE--------LAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 381 QEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT 460
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEA------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250
....*....|....*....
gi 568956226 461 VQLRAQIAMYEAELERAHG 479
Cdd:COG1196 487 AEAAARLLLLLEAEADYEG 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-516 |
1.28e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 285 AEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDR 364
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 365 LAEVELRLKDCLAEKAQEEERLSRRLR-----DSHETIASLRAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQH 434
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 435 LQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENL 514
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERT 243
|
..
gi 568956226 515 AG 516
Cdd:COG4942 244 PA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
246-587 |
2.20e-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: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 246 SDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQ------------LRQELRRCEVELQEL 313
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeLEKQLNQLKSEISDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 314 RAQPVVPCEGCEHSQESSQlRDKLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDS 393
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 394 HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIamyeAE 473
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 474 LErahgqmlEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQ 550
Cdd:TIGR04523 445 LT-------NQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK----ELE 509
|
330 340 350
....*....|....*....|....*....|....*..
gi 568956226 551 EALRSVKAEIGQAIEEVNSNNQELLRKyrrELQLRKK 587
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEK---ESKISDL 543
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
291-567 |
2.42e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 291 RLMVENeqlRQELRRCEVELQELRAQpvvpcegCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVEL 370
Cdd:COG4913 228 DALVEH---FDDLERAHEALEDAREQ-------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 371 -RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQRQVLKE 448
Cdd:COG4913 298 eELRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 449 MEQQLQNSHQLTVQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPAL 528
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956226 529 RTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 567
Cdd:COG4913 422 RELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
258-404 |
2.54e-07 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 53.48 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 258 QVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvPCEGCEhSQESSQLRDKL 337
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLL-----MKELELLNSIKPKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956226 338 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 404
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
210-527 |
4.18e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 210 LSGAPGPDPVvhrtvEAMSQLQEELVVLRERLALHdsdrQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHR 289
Cdd:COG3096 826 LAVAFAPDPE-----AELAALRQRRSELERELAQH----RAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLA 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 290 DRLmvenEQLRQELRRCEVELQELRaqpvvpcegcEHSQESSQLRDKLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVE 369
Cdd:COG3096 893 DRL----EELREELDAAQEAQAFIQ----------QHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLK 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 370 LRLkDCLAEKAQEEERLS-----RRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTR-NQHLQEQVAMQ- 442
Cdd:COG3096 955 QQI-FALSEVVQRRPHFSyedavGLLGENSDLNEKLRAR-------LEQAEEARREAREQLRQAQAQySQYNQVLASLKs 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 443 -----RQVLKEMEQ--------------------------QLQNSHQLTVQLRAQIAMYEAELERAHGQMLEemqsLEED 491
Cdd:COG3096 1027 srdakQQTLQELEQeleelgvqadaeaeerarirrdelheELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK----AERD 1102
|
330 340 350
....*....|....*....|....*....|....*....
gi 568956226 492 ---KNRAIEEAFARAQVEMKAVHENlaGVRTNLLTLQPA 527
Cdd:COG3096 1103 ykqEREQVVQAKAGWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
205-552 |
9.96e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 205 GRCSSLSGAPGPDPVVHRTVEAMSQLQEELVVlrERLALHDSDRQAT--TTQLQN----------QVENLKEKLISQAQE 272
Cdd:pfam15921 455 GKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSdlTASLQEkeraieatnaEITKLRSRVDLKLQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 273 VSRLRSElggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQ--PVVPCEGcEHSQESSQLRDKLSQLQLEVAENKGM 350
Cdd:pfam15921 533 LQHLKNE------GDHLRNVQTECEALKLQMAEKDKVIEILRQQieNMTQLVG-QHGRTAGAMQVEKAQLEKEINDRRLE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 351 LSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLRAQSPPVKYVIKT 413
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 414 ----VEVESSKTKQALSESQTrnqhlqeQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELErahgQMLEEMQSLE 489
Cdd:pfam15921 686 kseeMETTTNKLKMQLKSAQS-------ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLE 754
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956226 490 EDKNRAIEEAFARAQvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEA 552
Cdd:pfam15921 755 EAMTNANKEKHFLKE-EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
364-596 |
1.86e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 364 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 443
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 444 QVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 521
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956226 522 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 596
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
263-458 |
2.01e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.91 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 263 KEKLISQAQEVSRLRSELGGT-------DAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegceHSQESSQLRD 335
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEAQ---------QQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 336 KLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 415
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568956226 416 VESSKTKQALSESQTRNQHLQEQVAMQRQV----LKEMEQQLQNSHQ 458
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQG 212
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
222-535 |
2.50e-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: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 222 RTVEAMSQLQEElvvlrERLALHDSDRQATTTQLQNQVENLKEKLISQAQ------EVSRLRSELGGTDAEKHRD--RLM 293
Cdd:pfam17380 310 REVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERELERIRqeerkrELERIRQEEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 294 VE----NEQLRQELRRC------EVELQELRAQPVVPCEGCEHSQESSQLRDkLSQLQLEVAENKGMLSELNLEVQQKTD 363
Cdd:pfam17380 385 MErqqkNERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 364 RL--AEVELRLKDCLAEKAQEEERLSRRLRDshetiaslraqsppvkyviKTVEVESSKTKQALSESQTRNQHLQEQVAM 441
Cdd:pfam17380 464 RLrqQEEERKRKKLELEKEKRDRKRAEEQRR-------------------KILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 442 QRQVLKEMEQQlqnshqltvqlraqiamYEAELERAHGQMLEEMQSLEEDKNRAIEE-----AFARAQVEMKAVHENLAG 516
Cdd:pfam17380 525 RQKAIYEEERR-----------------REAEEERRKQQEMEERRRIQEQMRKATEErsrleAMEREREMMRQIVESEKA 587
|
330 340
....*....|....*....|....
gi 568956226 517 -----VRTNLLTLQPALRTLTNDY 535
Cdd:pfam17380 588 raeyeATTPITTIKPIYRPRISEY 611
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
225-513 |
5.07e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLmvenEQLRQELR 304
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ----QQRSQLEQAKEGL----SALNRLLPRLNLLADETLADRV----EEIREQLD 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 305 RCEVELQELRAQPVVpCEGCEhsQESSQLR---DKLSQLQLEVAENKGMLSElnleVQQKTDRLAEVELRL--------K 373
Cdd:PRK04863 905 EAEEAKRFVQQHGNA-LAQLE--PIVSVLQsdpEQFEQLKQDYQQAQQTQRD----AKQQAFALTEVVQRRahfsyedaA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 374 DCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEM---- 449
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQ-------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpa 1050
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956226 450 ---------------EQQLQNSHQLTVQLRAQIAMYEAELERAHGQmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHEN 513
Cdd:PRK04863 1051 dsgaeerararrdelHARLSANRSRRNQLEKQLTFCEAEMDNLTKK-LRKLERDYHEMREQVVNAKAGWCAVLRLVKDN 1128
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
222-406 |
5.30e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 222 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLIS--QAQEVSRLRSELGGTDAEKHRDRLMVE---N 296
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLkylA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 376
Cdd:COG4942 146 PARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|
gi 568956226 377 AEKAQEEERLSRRLRDSHETIASLRAQSPP 406
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-403 |
5.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQ 301
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 302 ELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQ 381
Cdd:TIGR02168 888 ALALLRSELEELSEELR------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
170 180
....*....|....*....|..
gi 568956226 382 EEERLSRRLRDShetIASLRAQ 403
Cdd:TIGR02168 962 KIEDDEEEARRR---LKRLENK 980
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
227-499 |
6.74e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.07 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 227 MSQLQEE-LVVLRERLALHDSDRQATTtqLQNQVENLKEklisQAQEV-SRLRSELGGTD---------------AEKHR 289
Cdd:pfam05622 154 VKLLEERnAEYMQRTLQLEEELKKANA--LRGQLETYKR----QVQELhGKLSEESKKADklefeykkleekleaLQKEK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 290 DRLMVENEQLRQ---ELRRCEVELQELRAQPVVPCEGCEHSQE------SSQLRDKLSQLQLEvaeNKgMLSELnlEVQQ 360
Cdd:pfam05622 228 ERLIIERDTLREtneELRCAQLQQAELSQADALLSPSSDPGDNlaaeimPAEIREKLIRLQHE---NK-MLRLG--QEGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 361 KTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVESSKT------KQALSESQTRNQH 434
Cdd:pfam05622 302 YRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956226 435 LQEQVAMQRQVLKEMEQQLQNSHQLTVqlraqiamyeAELERAHGQMLEEMQSLEEDKNRAIEEA 499
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-585 |
7.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 221 HRTVEAMSQLQEELVVLRERLALHDSDR--------QATTTQLQNQVENLKEKLISQAQEVSRLR---SELGGTDA---- 285
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKlekeleelEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 286 ------EKHRDRLM----VENEQLRQELRRCEVELQELRAQpVVPCEGcEHSQESSQLRDKLSQLQLEVAENKgmLSELN 355
Cdd:PRK03918 441 cgreltEEHRKELLeeytAELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESELIKLKELAEQLKELEEK--LKKYN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 356 LEVQQKTDRLAEvelRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppVKYVIKTVEVESSKTKQALSES-----QT 430
Cdd:PRK03918 517 LEELEKKAEEYE---KLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELgfesvEE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 431 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMK 508
Cdd:PRK03918 590 LEERLKELEPFYNEYleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 509 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAE---IGQAIEEVnSNNQELLRKYRRELQLR 585
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKElekLEKALERV-EELREKVKKYKALLKER 740
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
307-585 |
9.37e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 307 EVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQlEVAENkgmLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERL 386
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEE---LEQLREELEQAREELEQLEEELE----QARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 387 SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQ 466
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 467 IAMYEAELERAHGQMLEEMQsleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFP 546
Cdd:COG4372 159 LESLQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956226 547 LLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 585
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-585 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 377 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 456
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 457 HQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 522
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956226 523 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 585
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 ... |
232-489 |
1.18e-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: 49.58 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 232 EELVVLRERLALHDSDRQATTTQLQNQvENLKEKLISQAQEVSRLRSELggtdaekhrdrlmvenEQLRQELRRCEVELQ 311
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI----------------EEQRRLLQTLHSQEI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 312 ELRAQPVVPCEGCEHSQESSQLRDKLSQLQlevaENKGMLSELNLEVQQKTDRLAEvelrlkdclaEKAQEEERLSRRlR 391
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKELDILQR----------EQATIDTRTSAF-R 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 392 DSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQTRNQHLQEqvamQRQVLKEMEQQLQNSHQLTVQlraqiamyE 471
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE----SAQSLKEREQQLQTKEQIHLQ--------E 485
|
250
....*....|....*...
gi 568956226 472 AELERAHGQMLEEMQSLE 489
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEP 503
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
221-589 |
1.26e-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: 49.20 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 221 HRTVEAMSQLQEELVVLRERLALHDSDRQATTtQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQL- 299
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR--DLQGQLa 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 300 ----RQELRRCEVELQELRAQPVVPCEGCE--HSQESSQ-LRDKLSQLQ-----LEVAENKGMLSELNLEVQQKTDRLAE 367
Cdd:TIGR00618 428 hakkQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQsLKEREQQLQtkeqiHLQETRKKAVVLARLLELQEEPCPLC 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 368 VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyVIKTVEVE-SSKTKQA--LSESQTRNQHLQEQVAMQRQ 444
Cdd:TIGR00618 508 GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET-------SEEDVYHQlTSERKQRasLKEQMQEIQQSFSILTQCDN 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 445 VLKEMEQQLQNshqLTVQLRAQIAMyEAELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAgvrtnLLTL 524
Cdd:TIGR00618 581 RSKEDIPNLQN---ITVRLQDLTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK-----LTAL 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956226 525 QPALRTLTNDYNGLK-RQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCH 589
Cdd:TIGR00618 649 HALQLTLTQERVREHaLSIRVLPKELLAsrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-515 |
2.69e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVEN----LKEKLISQAQEVSRLRSELggtdAEKHRdrlmvENEQLR 300
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSI----AEKER-----ELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 301 QELRRCEVELQELRAQpvvpCEGCEHSQESSQLRdkLSQLQLEVAENKgmlSELNLEVQqktdRLAEVELRLKDCLAEKA 380
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAE----IEELEREIEEERKR--RDKLTEEYAELK---EELEDLRA----ELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 381 QEEERLS---RRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSH 457
Cdd:TIGR02169 389 DYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956226 458 QLTVQLRAQIAMYEAELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 515
Cdd:TIGR02169 469 QELYDLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
218-581 |
3.30e-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: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 218 PVVHRtvEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRdrlmvene 297
Cdd:pfam07111 233 PEVHS--QTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPK-------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 298 QLRQELRRCEVELQELRAQpvVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 377
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQ--LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQM 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 378 E--KAQEEERLSRRLRDS--------------------------HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQ 429
Cdd:pfam07111 381 ElsRAQEARRRQQQQTASaeeqlkfvvnamsstqiwlettmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 430 TRNQHLQEQVA---MQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQve 506
Cdd:pfam07111 461 LRQESCPPPPPappVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956226 507 mkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 581
Cdd:pfam07111 538 -----ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
210-589 |
4.04e-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: 47.66 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 210 LSGAPGPD-PVVHRTVEAMSQLQEELVVLRERLalhDSDRQaTTTQLQNQVENLKEKLISQAQEVSRLRSELGGT----- 283
Cdd:TIGR00618 519 DIDNPGPLtRRMQRGEQTYAQLETSEEDVYHQL---TSERK-QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnitv 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 284 DAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKtD 363
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK-E 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 364 RLAEVELRLkdclaekaQEEERLSRRLRDSHETIAslraQSPPVKYVIKTVEVESSKTKQALS------------ESQTR 431
Cdd:TIGR00618 674 LLASRQLAL--------QKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIEnassslgsdlaaREDAL 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 432 NQHLQEQVAMQRQVLKEME-QQLQNSHQLTV--QLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMK 508
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTeAHFNNNEEVTAalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE-IGQEIPSDEDILN 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 509 AVHENLAGVRTNLLTLqpaLRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIGQAIEEVNSNNQ-------ELLRKYR 579
Cdd:TIGR00618 821 LQCETLVQEEEQFLSR---LEEKSATLGEITHQLLKYEECSKqlAQLTQEQAKIIQLSDKLNGINQikiqfdgDALIKFL 897
|
410
....*....|
gi 568956226 580 RELQLRKKCH 589
Cdd:TIGR00618 898 HEITLYANVR 907
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
223-592 |
4.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 223 TVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSE---------LGGTDAE---KHRD 290
Cdd:PRK02224 242 VLEEHEERREELETLEAEIE----DLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagLDDADAEaveARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 291 RLMVENEQLRQELRRCEVELQELRAQPVVPCEGC-EHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 369
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDAdDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 370 LRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE--------------VESSKTKQALSESQTRN 432
Cdd:PRK02224 398 ERFGDApvdLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERV 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 433 QHLQEQVAMQRQVLKEMEQQLQNSHQLtVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIE--------EAFARAQ 504
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEElreraaelEAEAEEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 505 VE-MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRqvrgfplllQEALRSVKAEIGQAIEEVNSNNQEL--LRKYRRE 581
Cdd:PRK02224 557 REaAAEAEEEAEEAREEVAELNSKLAELKERIESLER---------IRTLLAAIADAEDEIERLREKREALaeLNDERRE 627
|
410
....*....|..
gi 568956226 582 -LQLRKKCHNEL 592
Cdd:PRK02224 628 rLAEKRERKREL 639
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
229-404 |
4.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 229 QLQEELVVLRERLALHDSDRQATTTQLQ--NQVENLKEKLI---SQAQEVSRLRSELggTDAEKHRDRLmvenEQLRQEL 303
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIdvaSAEREIAELEAEL--ERLDASSDDL----AALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 304 RRCEVELQELRAQpvvpCEGCEhsQESSQLRDKLSQLQLEVAENKGMLSElnLEVQQKTDRLAEVELRLKDCLAEKAqeE 383
Cdd:COG4913 695 EELEAELEELEEE----LDELK--GEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERFAAALGDAV--E 764
|
170 180
....*....|....*....|.
gi 568956226 384 ERLSRRLRDSHETIASLRAQS 404
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
328-504 |
5.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 328 QESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 400
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 401 RAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEA---ELE 475
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 568956226 476 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 504
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
167-504 |
5.17e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 167 KEDELPKRQAPAPRRDREAPEAGGTMNVENTGGRL---------FGIGRCSSLSGAPGPDPvvhrtvEAMSQLQEELVVL 237
Cdd:pfam15709 220 KSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVinsketedaSERGAFSSDSVVEDPWL------SSKYDAEESQVSI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 238 RERLAlhdSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSElggtdaeKHRDRLMVEneqlRQELRRCEVELQElraqp 317
Cdd:pfam15709 294 DGRSS---PTQTFVVTGNMESEEERSEEDPSKALLEKREQEK-------ASRDRLRAE----RAEMRRLEVERKR----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 318 vvpcegcehsQESSQLRdKLSQLQLEVAENkgMLSELNLEVQQKTDRLAEVELRLKDclAEKAQEEERLSRRLRdshETI 397
Cdd:pfam15709 355 ----------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQ---LQA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 398 ASLRAQSPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQVLKEMEQQlqnsHQLTVQLRAQiamyEAEl 474
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKRLMEMAEE----ERLEYQRQKQ----EAE- 487
|
330 340 350
....*....|....*....|....*....|
gi 568956226 475 ERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 504
Cdd:pfam15709 488 EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-591 |
5.85e-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: 47.35 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 229 QLQEELVVLRERLALHDSDRQATTTQ-----LQNQVENLKEKLISQAQEVSRL-RSELGGTDAEKHRDRLMVENEQLRQE 302
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKkevksLQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 303 LRRCEVELQELRA----QPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 378
Cdd:TIGR00606 555 KSRHSDELTSLLGyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 379 KAQEE--ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEM 449
Cdd:TIGR00606 635 QDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 450 EQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALR 529
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDL----KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEE 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 530 T---LTNDYNGLKRqvrgfpllLQEALRSVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 591
Cdd:TIGR00606 783 SakvCLTDVTIMER--------FQMELKDVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
225-593 |
6.76e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQLRQELR 304
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS--SELEEMTKFKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 305 RCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclAEKAQEEE 384
Cdd:pfam05483 402 NKEVELEELKKI----------LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 385 RLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 464
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 465 AQIAMYEAELERAHGQMLEEMQSLEEDKnRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 544
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568956226 545 fpllLQEALRSVKAEIGQAIEEVNSNNQ---ELLRKYRRELQLRKKCHNELV 593
Cdd:pfam05483 627 ----ENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
237-594 |
9.52e-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: 46.35 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 237 LRERLALHDSDRQATTTQLQ---NQ-------VENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRC 306
Cdd:pfam10174 294 LKQELSKKESELLALQTKLEtltNQnsdckqhIEVLKESLTAKEQRAAILQTEV---------DALRLRLEEKESFLNKK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 307 EVELQELRAQpvvpcEGCEhSQESSQLRD--------------KLSQLQLEVAENKGMLSELNLEVQQ-KTDR------L 365
Cdd:pfam10174 365 TKQLQDLTEE-----KSTL-AGEIRDLKDmldvkerkinvlqkKIENLQEQLRDKDKQLAGLKERVKSlQTDSsntdtaL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 366 AEVElrlkDCLAEKAQEEERL----SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAM 441
Cdd:pfam10174 439 TTLE----EALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 442 QRQVLKEMEQQLQNSHQLTVQLRAQI--AMYEAELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMkavhENLAGvrt 519
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEES-GKAQAEV----ERLLG--- 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956226 520 nlltlqpALRTLTNDYNGLKRQVRGFPLLlqeALRSVKaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 594
Cdd:pfam10174 587 -------ILREVENEKNDKDKKIAELESL---TLRQMK-EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
220-524 |
1.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 220 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQL---QNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN 296
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 376
Cdd:COG4372 111 EELQEELEELQKERQDLE-------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 377 AEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVamQRQVLKEMEQQLQN 455
Cdd:COG4372 178 EAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA--LELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956226 456 SHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTL 524
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
231-585 |
1.14e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 231 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEkLISQAQEVSRLRSELGgTDAEKHRDRLMVENEQLRQE--LRRCEV 308
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLE-QDYQAASDHLNLVQTALRQQekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 309 ELQELRAQPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENKGMLSELN--LEVQQK--------TDRLAEVELRL----- 372
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYQqaLDVQQTraiqyqqaVQALEKARALCglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 373 -----KDCLAE-KAQEEER------LSRRLRDSHETIASLRAQSPPVKYVIKTVEVES--SKTKQALSESQTRnQHLQEQ 438
Cdd:COG3096 435 tpenaEDYLAAfRAKEQQAteevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ-QALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 439 VAMQRQVLKEMEQQLQNSH-------QLTVQLRAQIAMYEaELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVH 511
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQL 587
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956226 512 ENLAGVRTNLLTLQPALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 585
Cdd:COG3096 588 EQLRARIKELAARAPAWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-400 |
1.16e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELGgtDAEKHRDRLMVENEQLRQELR 304
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAA----NLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 305 RCEVELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 384
Cdd:TIGR02168 870 ELESELEALLN------ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
170
....*....|....*.
gi 568956226 385 RLSRRLRDSHETIASL 400
Cdd:TIGR02168 944 RLSEEYSLTLEEAEAL 959
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-586 |
1.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 222 RTVEAMSQLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKL-ISQAQEVSRLRSELggtdaekhrDRLMVENEQLR 300
Cdd:COG4717 153 ERLEELRELEEELEELEAELA-----------ELQEELEELLEQLsLATEEELQDLAEEL---------EELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 301 QELRRCEVELQELRAQpvvpCEGCEHSQESSQLRDKLSQLQL----------------EVAENKGMLSELNLEVQQKTDR 364
Cdd:COG4717 213 EELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAGVLFLVLGLLAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 365 LAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ-----SPPVKYVIKTVEvESSKTKQALSESQTRNQHLQEQV 439
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppDLSPEELLELLD-RIEELQELLREAEELEEELQLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 440 AMQRQV----------LKEMEQQLQNSHQLtVQLRAQIAMYEAELERAHGQMLEEMQSLEEDknrAIEEAFARAQVEMKA 509
Cdd:COG4717 368 LEQEIAallaeagvedEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEE 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956226 510 VHENLAGVRTNLLTLQPALRTLTNDynGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNN--QELLRKYRRELQLRK 586
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED--GELAE-------LLQELEELKAELRELAEEWAALKlaLELLEEAREEYREER 513
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
225-392 |
1.35e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL-----GGTDAEKHRDRLMVENEQL 299
Cdd:PRK09039 53 SALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 300 RQELRRCEVELQELRAQpvvpcegcehsqeSSQLRDKLSQLQ--LEVAENKGmlselnlevQQKTDRLAEVELRLKDCLA 377
Cdd:PRK09039 129 KQVSARALAQVELLNQQ-------------IAALRRQLAALEaaLDASEKRD---------RESQAKIADLGRRLNVALA 186
|
170 180
....*....|....*....|..
gi 568956226 378 EKAQEeerLSR-------RLRD 392
Cdd:PRK09039 187 QRVQE---LNRyrseffgRLRE 205
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
231-603 |
1.55e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 231 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRCEVEL 310
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL---------EQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 311 QELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRL 390
Cdd:COG4372 83 EELNEQLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 391 RDSHETIASLRAQSPPVKYVIKtvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMY 470
Cdd:COG4372 157 EQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 471 EAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 550
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568956226 551 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIA 603
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
282-568 |
1.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 282 GTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQlEVAENKGMLSELNLEVQQK 361
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAE----------LDALQERREALQRLA-EYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 362 TDRLAEVEL------RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQT 430
Cdd:COG4913 674 EAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 431 RNQHLQEQV--AMQRQVLKEMEQQLQNSHQltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMK 508
Cdd:COG4913 747 LRALLEERFaaALGDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYL 818
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 509 AVHENLagVRTNLLTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 568
Cdd:COG4913 819 ALLDRL--EEDGLPEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-389 |
2.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 222 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENL---------KEKLISQAQEVSRLRSELGGTDAEKHRDRL 292
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleqAEEYQELKEELEELEEQLEELLGELEELLE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 293 MVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQL--QLEVAENKGMLSELNLEVQQKTDRLAEVE- 369
Cdd:COG4717 424 ALDEEELEEELEELEEELEELE-------------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAe 490
|
170 180
....*....|....*....|....
gi 568956226 370 ----LRLKDCLAEKAQEEERLSRR 389
Cdd:COG4717 491 ewaaLKLALELLEEAREEYREERL 514
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
222-386 |
2.38e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 222 RTVEAMSQLQEELVVLRERLALHDSDRQAtttqlqnqVENLKEKLisqaqevsrlrselggTDAEKHRDRLMVENEQLRQ 301
Cdd:pfam13851 58 RLTEPLQKAQEEVEELRKQLENYEKDKQS--------LKNLKARL----------------KVLEKELKDLKWEHEVLEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 302 ELRRCEVELQELRAQpvvpCEGCEHS-QESSQLRD-----KLSQLQlEVAENK-----GMLSELNLEvqqkTDRLAEVEL 370
Cdd:pfam13851 114 RFEKVERERDELYDK----FEAAIQDvQQKTGLKNlllekKLQALG-ETLEKKeaqlnEVLAAANLD----PDALQAVTE 184
|
170
....*....|....*.
gi 568956226 371 RLKDCLAEKAQEEERL 386
Cdd:pfam13851 185 KLEDVLESKNQLIKDL 200
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
260-524 |
2.53e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 260 ENLKEKLISQAQEVSRLRSELggtdaekhRDRLMVENEQLRQELRRcevELQELRAQpvvpcegcehSQESSQLRDKLSQ 339
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFSLLK--------KETIYLQSAQRVELAER---QLQELKID----------VKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 340 LQLEVAENKGML-SELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLRAQSPPVKYVIKTVEV 416
Cdd:COG5022 904 LESEIIELKKSLsSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTI 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 417 ESSKTKQALSESQTRNQHLQEQV----AMQRQV--LKEMEQQLQNSHQLTVQLRA-----QIAMYEAELERAHgqMLEEM 485
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQKLKGLL--LLENN 1060
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956226 486 QSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 524
Cdd:COG5022 1061 QLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
223-510 |
3.49e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 223 TVEAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSElggtdAEKHRDRlmveneqlRQE 302
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRD----ELNEELKELAEKRDELNAQVKELREE-----AQELREK--------RDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 303 LRRcevELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELN--------LEVQQKTDRL-AEVELRLK 373
Cdd:COG1340 69 LNE---KVKELKE------ERDELNEKLNELREELDELRKELAELNKAGGSIDklrkeierLEWRQQTEVLsPEEEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 374 DCLAEKAQEEERLsRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQL 453
Cdd:COG1340 140 EKIKELEKELEKA-KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956226 454 QNSHQLTVQLRAQIAMYEAELErahgQMLEEMQSLEE------DKNRAIEEAFARAQVEMKAV 510
Cdd:COG1340 212 DELHKEIVEAQEKADELHEEII----ELQKELRELRKelkklrKKQRALKREKEKEELEEKAE 270
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
330-492 |
3.83e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 43.06 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 330 SSQLRDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 403
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 404 SPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLE 483
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASE--------------LKKEFEEVSELIKS 175
|
....*....
gi 568956226 484 EMQSLEEDK 492
Cdd:cd07627 176 ELERFERER 184
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
225-579 |
4.26e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLMVENEQLRQE-- 302
Cdd:PRK04778 140 EEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTESGDYVEAREILDQLEEELAALEQIme 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 303 -----LRRCEVE----LQELRAqpvvpceGCEHSQESS------QLRDKLSQLQLEVAENKGMLSELNL--------EVQ 359
Cdd:PRK04778 216 eipelLKELQTElpdqLQELKA-------GYRELVEEGyhldhlDIEKEIQDLKEQIDENLALLEELDLdeaeekneEIQ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 360 QKTDRL-----AEVELRlKDCLAEKAQEEERLSRRLRDSHETIASLR--AQSppvkYVIKTVEVESSKTKQA-LSESQTR 431
Cdd:PRK04778 289 ERIDQLydileREVKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEIDrvKQS----YTLNESELESVRQLEKqLESLEKQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 432 NQHLQEQVAMQRQV-------LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHgQMLEEMQS-LEEDKnRAIE------ 497
Cdd:PRK04778 364 YDEITERIAEQEIAyselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR-EKLERYRNkLHEIK-RYLEksnlpg 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 498 ------EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQ 562
Cdd:PRK04778 442 lpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAE 521
|
410
....*....|....*..
gi 568956226 563 AIEEVnsnnQELLRKYR 579
Cdd:PRK04778 522 ALNEA----ERLFREYD 534
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
225-458 |
5.14e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL------------GGTDAEKHRDRL 292
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLidlkehasslasSGLKKDSKLKSL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 293 MVENEQLRQELRRCEVELQelRAQpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRl 372
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLK--KAH-----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 373 KDCLAEKAQE-EERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQ--RQVLKEM 449
Cdd:pfam10174 595 KNDKDKKIAElESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEktRQELDAT 674
|
....*....
gi 568956226 450 EQQLQNSHQ 458
Cdd:pfam10174 675 KARLSSTQQ 683
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
255-498 |
5.80e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 255 LQNQV-ENLKEKL-ISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcEGCEHSQESSQ 332
Cdd:pfam07888 32 LQNRLeECLQERAeLLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE---ELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 333 LRDKLSQ----LQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkDCLAEKAqeeERLSRRLRDSHETIASLRAQSPPVK 408
Cdd:pfam07888 109 SSEELSEekdaLLAQRAAHEARIRELEEDIKTLTQRVLERETEL-ERMKERA---KKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 409 YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAElERAHGQMLEEMQSL 488
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS-ERKVEGLGEELSSM 263
|
250
....*....|
gi 568956226 489 EEDKNRAIEE 498
Cdd:pfam07888 264 AAQRDRTQAE 273
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
239-459 |
7.50e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 239 ERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLR-QELRRCEVELQELRAQP 317
Cdd:pfam07888 160 KKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlTTAHRKEAENEALLEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 318 VVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHET 396
Cdd:pfam07888 240 RSLQERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDR 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956226 397 IASLRA---------QSPPVKYVIKTVEVESSKTKQALSESQTRNQhLQEQVAMQRQVLKEMEQQLQNSHQL 459
Cdd:pfam07888 320 IEKLSAelqrleerlQEERMEREKLEVELGREKDCNRVQLSESRRE-LQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
254-593 |
7.88e-04 |
|
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: 43.47 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 254 QLQNQVENLKEKLISQAQEVSRLRS-----ELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcegcEHSQ 328
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK------SKEK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 329 ESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVK 408
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN----------------LE 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 409 YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSL 488
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK----LSSIIKNI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 489 EEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQPALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIE 565
Cdd:TIGR04523 637 KSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKIKESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR 702
|
330 340 350
....*....|....*....|....*....|.
gi 568956226 566 evNSNNQELLRKYR---RELQLRKKCHNELV 593
Cdd:TIGR04523 703 --IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
227-574 |
8.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 227 MSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLK-------EKLISQAQ-EVSRL--RSELGGTDAEKHRDRLMVEN 296
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLqqhqdriEQLISEHEvEITGLteKASSARSQANSIQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRCEVELQELRAQPvvpcegcehSQESSQLR-------DKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 369
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTV---------SQLRSELReakrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 370 LRLKDCLAEKAQEEERLS------RRLRDSHE----TIASLRAQSPPvkyviKTVEVESSKTKQALSESQTRNQHLQEQV 439
Cdd:pfam15921 377 DQLQKLLADLHKREKELSlekeqnKRLWDRDTgnsiTIDHLRRELDD-----RNMEVQRLEALLKAMKSECQGQMERQMA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 440 AMQ-----RQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEdKNRAIEEAFA-----RAQVEMKA 509
Cdd:pfam15921 452 AIQgknesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAeitklRSRVDLKL 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956226 510 VH--------ENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKA---EIGQAIEEVNSNNQEL 574
Cdd:pfam15921 531 QElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqvEKAQLEKEINDRRLEL 606
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
297-611 |
9.19e-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: 43.19 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRCEVE----LQELRAQPVVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 371
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 372 LKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 451
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 452 ---QLQNSHQL--------------------------TVQLR-AQIAMYEAELERaHGQMLEEMQSLEEDKNRAIEEAFa 501
Cdd:pfam05557 154 lrqNLEKQQSSlaeaeqrikelefeiqsqeqdseivkNSKSElARIPELEKELER-LREHNKHLNENIENKLLLKEEVE- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 502 raqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL- 574
Cdd:pfam05557 232 ----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSAr 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568956226 575 -LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 611
Cdd:pfam05557 308 qLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
226-403 |
9.37e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 226 AMSQLQEELvvlrerLALHDSDRQATttQLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLmvenEQLRQELRR 305
Cdd:COG1579 1 AMPEDLRAL------LDLQELDSELD--RLEHRLKELPAELAELEDELAALEARL-----EAAKTEL----EDLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 306 CEVELQELRAQPVvpcegcEHSQESSQLRD--KLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE 383
Cdd:COG1579 64 LELEIEEVEARIK------KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
170 180
....*....|....*....|
gi 568956226 384 ERLSRRLRDSHETIASLRAQ 403
Cdd:COG1579 138 AELEEKKAELDEELAELEAE 157
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
258-641 |
9.92e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 258 QVENLKEKL--ISQAQEVSRLRSELGGTDAEKHRDRlmvENEQLRQELRRCEVELQelRAQPVVPCEGCEHSQESSQLRD 335
Cdd:PTZ00121 1458 KAEEAKKKAeeAKKADEAKKKAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 336 KLSQLQLEVAENKGMLSELnlevqQKTDRLAEVELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVE 415
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL-----KKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 416 VESS-KTKQALSESQTRNQhlQEQVAMQRQVLKEMEQ-------------QLQNSHQLTVQLRAQIAMYEAELERAhgqm 481
Cdd:PTZ00121 1603 EEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK---- 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 482 LEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIG 561
Cdd:PTZ00121 1677 AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEA 1735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 562 QAIEEVNSNNQELLRKYRRE----LQLRKKCHNELVRLKGNIRVIARvRPVTKEDGEGPEATNAVTFDPDDDS--IIHLL 635
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGG 1814
|
....*.
gi 568956226 636 HKGKPV 641
Cdd:PTZ00121 1815 KEGNLV 1820
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
355-583 |
1.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 355 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQ 423
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 424 ALSESQTRNQ--HLQEQVAMQRQVLKEMEQQLQnshqltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFA 501
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLA-------EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 502 RAQVEMKAvheNLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 578
Cdd:COG3206 270 AQLAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 568956226 579 RRELQ 583
Cdd:COG3206 340 EARLA 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
338-610 |
1.04e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 338 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDS-------HET 396
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKNltvepvkGSN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 397 IASLRAQSP-PVK-----------YVIKTVEVESSKTKQA--------------LSESQT-----RNQH----LQEQVAM 441
Cdd:COG3206 137 VIEISYTSPdPELaaavanalaeaYLEQNLELRREEARKAlefleeqlpelrkeLEEAEAaleefRQKNglvdLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 442 QRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQS--LEEDKNRAIEEAFARAQV---------EMKAV 510
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELsarytpnhpDVIAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 511 HENLAGVRTNLLT-LQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRkYRRELQLRKKCH 589
Cdd:COG3206 297 RAQIAALRAQLQQeAQRILASLEAELEALQARE--------ASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELY 367
|
330 340 350
....*....|....*....|....*....|..
gi 568956226 590 NELV-RLK----------GNIRVIARVRPVTK 610
Cdd:COG3206 368 ESLLqRLEearlaealtvGNVRVIDPAVVPLK 399
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
385-508 |
1.22e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 385 RLSRRLRDshETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 454
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956226 455 -------NSHQLtVQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 508
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-389 |
1.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 227 MSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDA--EKHRDRLM-VENEQLRQEL 303
Cdd:COG1579 19 LDRLEHRLKELPAELA----ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGnVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 304 RRcEVELQELRAqpvvpcegcehsqesSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE 383
Cdd:COG1579 95 QK-EIESLKRRI---------------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*.
gi 568956226 384 ERLSRR 389
Cdd:COG1579 159 EELEAE 164
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
257-518 |
2.08e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 257 NQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRqELRRcevELQELRAQpvVPcegcEHSQESSQLRDK 336
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEI-----EELKEKRDELNEELK-ELAE---KRDELNAQ--VK----ELREEAQELREK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 337 LSQLQLEVAENKGMLSELNLEVQQKTDRLAEVElRLKDCLAEKAQEEERLSR---RLRDSHET--------------IAS 399
Cdd:COG1340 66 RDELNEKVKELKEERDELNEKLNELREELDELR-KELAELNKAGGSIDKLRKeieRLEWRQQTevlspeeekelvekIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 400 LRAQsppvkyvIKTVEVESSKTKQaLSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG 479
Cdd:COG1340 145 LEKE-------LEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 568956226 480 QMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVR 518
Cdd:COG1340 217 EIVEAQEKADE-----LHEEIIELQKELRELRKELKKLR 250
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
389-596 |
2.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 389 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 455
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 456 SH-----QLTVQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 523
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956226 524 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 596
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
255-522 |
3.59e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 255 LQNQVENLKEKLISQAQEVSRLRsELGGTDAEKHRDRLmvenEQLRQELRrcevelqelraqpvvpcegcEHSQESSQLR 334
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK--------------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 335 DKLSQLQLEVAENKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrLRDSHETIAslraqsp 405
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK-IKDKLKELQ------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 406 pvkyviktvevessktkQALSESQTRNQHLQE---QVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQML 482
Cdd:PHA02562 313 -----------------HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568956226 483 EEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 522
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
224-596 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 224 VEAMSQLQEELVVLRERLALHDSDRQATT------TQLQNQVENLKEKL--ISQAQEVSRLRSElggtDAEKHRDRLMVE 295
Cdd:pfam05622 27 QEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLELQHR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 296 NEQLR---QELRRCEVELQELRaqpvvpcegcehsqESSqlrDKLSQLQLEVAENKGMLSELN-LEVQQKTdrlaevelr 371
Cdd:pfam05622 103 NEELTslaEEAQALKDEMDILR--------------ESS---DKVKKLEATVETYKKKLEDLGdLRRQVKL--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 372 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSE---SQTRNQHLQ---EQVAMQRQV 445
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQkekERLIIERDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 446 LKEMEQQLQNSHQLTVQLRAQIAMYEAELErAHGQMLEEMQSLEedknraIEEAFARAQVEMKAVHENLAGvrtNLLTLQ 525
Cdd:pfam05622 237 LRETNEELRCAQLQQAELSQADALLSPSSD-PGDNLAAEIMPAE------IREKLIRLQHENKMLRLGQEG---SYRERL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956226 526 PALRTLTNDYNGLKRQVRGFPLLLQEALRsvkaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 596
Cdd:pfam05622 307 TELQQLLEDANRRKNELETQNRLANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
334-507 |
4.07e-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: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 334 RDKLSQLQLEVAENKGMLSELNLEVQQktdRLAEVELRLKDCLAEKAQEEERLSRR--------LRDSHETIASLRAqsp 405
Cdd:cd07596 34 RRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAAEELSSLSEAQANQelvkllepLKEYLRYCQAVKE--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 406 pvkyVIKT-----VEVESSKtkQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAqiamyeaELERAHGQ 480
Cdd:cd07596 108 ----TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARK-------RYEEISER 174
|
170 180 190
....*....|....*....|....*....|
gi 568956226 481 MLEEMQSLEEDKNRAIEEA---FARAQVEM 507
Cdd:cd07596 175 LKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-600 |
4.60e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 231 QEELVVLR-ERLALHDSDRQATTTQLQNQ------VENLKEKLISQAQEVSRLRSELggTDAEKHRDRlmvENEQLRQEL 303
Cdd:pfam12128 438 EEYRLKSRlGELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSEL--RQARKRRDQ---ASEALRQAS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 304 RRCE---VELQELRAQPVVPCEGCEH--SQESSQLRDKLSQL-QLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 377
Cdd:pfam12128 513 RRLEerqSALDELELQLFPQAGTLLHflRKEAPDWEQSIGKViSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 378 -EKAQEEERLSRR-------LRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTR-----NQHLQEQVAMQRQ 444
Cdd:pfam12128 593 pEWAASEEELRERldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKA 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 445 V---LKEMEQQLQN-SHQLTVQLRAQIAMYEA---ELERAHGQMLEEMQSLEEDKNRA---IEEAFARAQVEMKA----- 509
Cdd:pfam12128 673 LaerKDSANERLNSlEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVVEGALDAQlalLKAAIAARRSGAKAelkal 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 510 ---VHENLAGV---RTNLLTLQPALRTLT---NDYNGLKRQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQE 573
Cdd:pfam12128 753 etwYKRDLASLgvdPDVIAKLKREIRTLErkiERIAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNIERAISELQQQLAR 832
|
410 420 430
....*....|....*....|....*....|.
gi 568956226 574 LLRKYRRELQL----RKKCHNELVRLKGNIR 600
Cdd:pfam12128 833 LIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| BAR_Bin3 |
cd07590 |
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ... |
431-515 |
5.57e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153274 Cd Length: 225 Bit Score: 39.66 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 431 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAqIAMYEAELERAHGQMLEEMQSLEEDKNRAIE---EAFARAQV 505
Cdd:cd07590 117 REQSLQEYERLQAKVekLAEKEKTGPNLAKLEQAEKA-LAAARADFEKQNIKLLEELPKFYNGRTDYFQpcfEALIKSQV 195
|
90
....*....|....
gi 568956226 506 ----EMKAVHENLA 515
Cdd:cd07590 196 lyysQSTKIFTQLA 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-534 |
6.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 333 LRDKLSQLQLEVAENKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyvi 411
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELRE--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 412 ktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqlTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 491
Cdd:COG4717 117 ---ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956226 492 KNRAIEEA---FARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 534
Cdd:COG4717 190 TEEELQDLaeeLEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-587 |
6.54e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 287 KHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEgcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLA 366
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACE----------IRDQITSKEAQLESSREIVKSYENELDPLKNRLK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 367 EVE------LRLKD---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQTRNQHLQE 437
Cdd:TIGR00606 256 EIEhnlskiMKLDNeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 438 QVAMQRQVLKEMEQQLQNsHQLTVQLRA---QIAMYEAELERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMK 508
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLV-EQGRLQLQAdrhQEHIRARDSLIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 509 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQ 583
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELS 488
|
....
gi 568956226 584 LRKK 587
Cdd:TIGR00606 489 KAEK 492
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
225-531 |
6.55e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 225 EAMSQLQEELVvLRERL-ALHdsdrqATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQL---- 299
Cdd:PRK10246 413 AALAQHAEQRP-LRQRLvALH-----GQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL-----NEMRQRYKEKTQQLadvk 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 300 ---RQELRRCEVELQELRAQPVVPCEGCEHSQESSqlrdkLSQLQ-LEVAENKGMLSELNLEVQQKTDRLAEVELRLkDC 375
Cdd:PRK10246 482 ticEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPA-----VEAYQaLEPGVNQSRLDALEKEVKKLGEEGAALRGQL-DA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 376 LAEKAQEEERLSRRLRDSHETIaslraqsppvkyviktvevesSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLqn 455
Cdd:PRK10246 556 LTKQLQRDESEAQSLRQEEQAL---------------------TQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-- 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 456 sHQLT--VQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR----------------AIEEAFARAQvemkAVHENLAGV 517
Cdd:PRK10246 613 -RLLSqrHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSWQ----QRQNELTAL 687
|
330
....*....|....
gi 568956226 518 RTNLLTLQPALRTL 531
Cdd:PRK10246 688 QNRIQQLTPLLETL 701
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
224-491 |
6.72e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.22 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 224 VEAMSqLQEELVVLRERLALHDSDRQATTTQLQNQVENLKE---KLISQAQEVSRLRSELGGTDaEKHRDRLMVEN---- 296
Cdd:PLN03229 479 VIAMG-LQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDefnKRLSRAPNYLSLKYKLDMLN-EFSRAKALSEKkska 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 297 EQLRQELRRcevELQELRAQPvvpcegcehsqessQLRDKLSQLQLEVAENK-GMLSELNLEVQQKTDRL-AEVELRLKD 374
Cdd:PLN03229 557 EKLKAEINK---KFKEVMDRP--------------EIKEKMEALKAEVASSGaSSGDELDDDLKEKVEKMkKEIELELAG 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 375 CLAEKAQEEERLSRRLRDSHETIAslraqSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEqvaMQRQVLKEMEQQLQ 454
Cdd:PLN03229 620 VLKSMGLEVIGVTKKNKDTAEQTP-----PPNLQEKIESLNEEINKKIERVIRSSDLKSKIEL---LKLEVAKASKTPDV 691
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568956226 455 NSHQLTVQLRAQI------AMYEAELERAHGQMLEEMQSLEED 491
Cdd:PLN03229 692 TEKEKIEALEQQIkqkiaeALNSSELKEKFEELEAELAAARET 734
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
227-451 |
7.36e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 227 MSQLQEELVVLRERLALHDSDRqattTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQEL--- 303
Cdd:pfam15905 96 LQALEEELEKVEAKLNAAVREK----TSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLeak 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 304 -RRCEVELQELRAQPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENK---GMLSELNLEVQQKTDRLAEVEL---RLKDC 375
Cdd:pfam15905 172 mKEVMAKQEGMEGKLQVTQKNLEHSKGKvAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVEKYKLdiaQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 376 LAEKAQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSK-TKQALSESQTRN---QHLQEQVAMQRQVLKEMEQ 451
Cdd:pfam15905 252 LKEKNDEIESLKQSLE---EKEQELSKQIKDLNEKCKLLESEKEElLREYEEKEQTLNaelEELKEKLTLEEQEHQKLQQ 328
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
351-475 |
7.82e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 351 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQT 430
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568956226 431 RNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE 475
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
270-391 |
8.26e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.83 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 270 AQEVSRLRSELGGTDAE-KHRDRLMVE-NEQLRQ---ELRRCEVELQELRAqpvvpcegcehsqESSQLRDKLSQLQLEV 344
Cdd:pfam06818 30 LNEIVALRAQLRELRAKlEEKEEQIQElEDSLRSktlELEVCENELQRKKN-------------EAELLREKVGKLEEEV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568956226 345 AENKGMLSELNLEVQQKTDRLAEVELRLK--DCLAEKAQEEERLSRRLR 391
Cdd:pfam06818 97 SGLREALSDVSPSGYESVYESDEAKEQRQeeADLGSLRREVERLRAELR 145
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
411-490 |
8.70e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.67 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 411 IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQMLEEMQS 487
Cdd:pfam12718 23 VKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNnenLTRKIQLLEEELEESDKRLKETTEK 102
|
...
gi 568956226 488 LEE 490
Cdd:pfam12718 103 LRE 105
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
217-343 |
9.25e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 217 DPVVHRTVEAMSQLQEELVVLRErlaLHDSDRQATTTQLQnqveNLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN 296
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELD----RAKEKLKKLLQEIMIKVKKL--EELEEELQELESKI 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568956226 297 EQLRQELRRCEVELQELRAQpVVPCEGCEHSqESSQLRDKLSQLQLE 343
Cdd:smart00787 242 EDLTNKKSELNTEIAEAEKK-LEQCRGFTFK-EIEKLKEQLKLLQSL 286
|
|
| Vps5 |
pfam09325 |
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
334-506 |
9.44e-03 |
|
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.
Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 38.80 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 334 RDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---QSPPV 407
Cdd:pfam09325 54 RKELASATGEFAKSLASLASLELStgLSRALSQLAEVEERIKELLERQALQDVLtLGETIDEYLRLIGSVKAvfnQRVKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956226 408 KYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLEEMQS 487
Cdd:pfam09325 134 WQSWQNAEQELSKKKEQLEKLLRANKSQNDKLQQAKKEVEELERRVQQ--------------AEKEFEDISELIKKELER 199
|
170 180
....*....|....*....|..
gi 568956226 488 LEEDKN---RAIEEAFARAQVE 506
Cdd:pfam09325 200 FELERVddfKNSVEIYLESAIE 221
|
|
| |
