|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
597-924 |
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 1732428643 597 KGNIRVIARVRPVTKedGEGPEATNAVTFDPDDDSIIHLLHKG-KPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFN 675
Cdd:cd01366 1 KGNIRVFCRVRPLLP--SEENEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 676 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLL--GKEPQEKLEIRL 752
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 753 CPDgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGS 832
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 833 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 912
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 1732428643 913 LRFAERVRSVEL 924
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
605-922 |
3.26e-147 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 440.47 E-value: 3.26e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 605 RVRPVTKEDGEGPEATNAVTFDPDDDSI--IHLLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVCIFAY 681
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 682 GQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLY 761
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 762 VPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG---LRTTGKLNLVDLAGSERVGKS 838
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 839 G-AEGNRLREAQHINRSLSALGDVIAALRS-RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFA 916
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADkKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 1732428643 917 ERVRSV 922
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
599-926 |
2.12e-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: 2.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVTKEDGEGPEAtNAVTFDPDDDSIIHLLHKGKPV---SFELDKVFSPWASQQDVFQEVQA-LITSCIDGF 674
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSP-SVVPFPDKVGKTLTVRSPKNRQgekKFTFDKVFDATASQEDVFEETAApLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 675 NVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQeKLEIRlcP 754
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIR--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 755 DGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAGS 832
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 833 ERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 910
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*.
gi 1732428643 911 YSLRFAERVRSVELGP 926
Cdd:smart00129 317 STLRFASRAKEIKNKP 332
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
599-920 |
2.69e-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: 2.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPvtKEDGEGPEATNAVTFDPDDDSIIHL--LHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFN 675
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPpkNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 676 VCIFAYGQTGAGKTYTMEGT-PENPGINQRALQLLFSEVQE-KASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRlc 753
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 754 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRTTGKLNLVDLAG 831
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVkqRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 832 SERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ-GHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETL 910
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 1732428643 911 YSLRFAERVR 920
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
599-922 |
1.36e-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: 1.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVT-KEDGEGpeATNAVTFDPDDDSIIhlLHKGK------PVSFELDKVFSPWASQQDVFQE-VQALITSC 670
Cdd:cd01371 2 NVKVVVRCRPLNgKEKAAG--ALQIVDVDEKRGQVS--VRNPKatanepPKTFTFDAVFDPNSKQLDVYDEtARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 671 IDGFNVCIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEK 747
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 748 LEIRLCPDgSGqLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGK 823
Cdd:cd01371 158 LELKERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecseKGEDGENHIRV-GK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 824 LNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPV 902
Cdd:cd01371 235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 1732428643 903 EKNTSETLYSLRFAERVRSV 922
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
600-923 |
1.11e-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: 1.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 600 IRVIARVRPVT-KEDGEGPEatNAVTFDPDDDSIIhllhKGKPVSFELDKVFSPWASQQDVFQE-VQALITSCIDGFNVC 677
Cdd:cd01372 3 VRVAVRVRPLLpKEIIEGCR--ICVSFVPGEPQVT----VGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 678 IFAYGQTGAGKTYTMEGT------PENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIR 751
Cdd:cd01372 77 VLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 752 LCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLR--------TT 821
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqTKKNGPIAPMsaddknstFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 822 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQ---GHVPFRNSKLTYLLQDSLSGDSKTLMVVQ 898
Cdd:cd01372 237 SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 1732428643 899 VSPVEKNTSETLYSLRFAERVRSVE 923
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
599-922 |
5.66e-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: 5.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPV-TKEDGEGPEA------TNAVTFDPDDDSIIHLL----------HKGKPVSFELDKVFSPWASQQDVFQ 661
Cdd:cd01370 1 SLTVAVRVRPFsEKEKNEGFRRivkvmdNHMLVFDPKDEEDGFFHggsnnrdrrkRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 662 E-VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLL 740
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 741 GKEpQEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR- 819
Cdd:cd01370 161 NPS-SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 820 --TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG---HVPFRNSKLTYLLQDSLSGDSKTL 894
Cdd:cd01370 238 qvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 1732428643 895 MVVQVSPVEKNTSETLYSLRFAERVRSV 922
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
599-922 |
5.15e-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: 293.08 E-value: 5.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVT-KEDGEGPEATnaVTFDPDDDSIIHLLHKGKPVSFelDKVFSPWASQQDVFQE-VQALITSCIDGFNV 676
Cdd:cd01369 3 NIKVVCRFRPLNeLEVLQGSKSI--VKFDPEDTVVIATSETGKTFSF--DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 677 CIFAYGQTGAGKTYTMEGTPENP---GINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGkepQEKLEIRLC 753
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD---VSKTNLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 754 PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSE 833
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 834 RVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYS 912
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLST 315
|
330
....*....|
gi 1732428643 913 LRFAERVRSV 922
Cdd:cd01369 316 LRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
598-922 |
2.57e-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: 2.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 598 GNIRVIARVRPVTKEDGEGPeATNAVTFDPDDDSIIHL--------LHKGKPVSFELDKVF-------SPWASQQDVFQE 662
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERN-SKCIVQMSGKETTLKNPkqadknnkATREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 663 VQA-LITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASD-WQYNITVSAAEIYNEVLRDLL 740
Cdd:cd01365 80 LGEeLLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 741 GKEPQEK---LEIRLCPdgSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHAL--LIVTVRGVDCS 815
Cdd:cd01365 160 NPKPKKNkgnLKVREHP--VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 816 TGLRT--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL--------RSRQGHVPFRNSKLTYLLQD 885
Cdd:cd01365 238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKE 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1732428643 886 SLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSV 922
Cdd:cd01365 318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
599-922 |
1.37e-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: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVTKEDgegPEATNAVTFDPDDDSIIHllHKGKPVSFELDKVFSPWASQQDVFQEV-QALITSCIDGFNVC 677
Cdd:cd01374 1 KITVTVRVRPLNSRE---IGINEQVAWEIDNDTIYL--VEPPSTSFTFDHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 678 IFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkASDWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPDGS 757
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 758 GQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV----RGVDCSTGLRTtGKLNLVDLAGSE 833
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIesseRGELEEGTVRV-STLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 834 RVGKSGAEGNRLREAQHINRSLSALGDVIAALRS--RQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLY 911
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgkVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLN 310
|
330
....*....|.
gi 1732428643 912 SLRFAERVRSV 922
Cdd:cd01374 311 TLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
599-922 |
4.72e-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: 4.72e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVTKEDGEgPEATNAVTFDPDDDSII--HLLHKGKPV--SFELDKVFSPWASQQDVFQEVQA-LITSCIDG 673
Cdd:cd01364 3 NIQVVVRCRPFNLRERK-ASSHSVVEVDPVRKEVSvrTGGLADKSStkTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 674 FNVCIFAYGQTGAGKTYTMEG-----------TPENPGINQRALQLLFSEVQEKASDwqYNITVSAAEIYNEVLRDLLGK 742
Cdd:cd01364 82 YNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 743 EPQEKLEIRLC--PDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTG--- 817
Cdd:cd01364 160 SSDVSERLRMFddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDgee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 818 LRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 897
Cdd:cd01364 240 LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340
....*....|....*....|....*
gi 1732428643 898 QVSPVEKNTSETLYSLRFAERVRSV 922
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNI 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
583-923 |
6.79e-81 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 273.92 E-value: 6.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 583 LQLRKKCHNELVRLKGNIRVIARVRPvtkeDGEGPEATNAvtfdpdDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQE 662
Cdd:COG5059 7 SPLKSRLSSRNEKSVSDIKSTIRIIP----GELGERLINT------SKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 663 -VQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLG 741
Cdd:COG5059 77 tIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 742 KEPQEKLeirLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTT 821
Cdd:COG5059 157 PNEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 822 GKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALR--SRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 899
Cdd:COG5059 234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340
....*....|....*....|....
gi 1732428643 900 SPVEKNTSETLYSLRFAERVRSVE 923
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIK 337
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
600-917 |
5.03e-77 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 255.78 E-value: 5.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 600 IRVIARVRPVTKEDGEGPEA-------TNAVTFDPDDDSIIHLLHKG---KPVSFELDKVFSPWASQQDVFQEV-QALIT 668
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEgcievinSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 669 SCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEkasdwqYNITVSAAEIYNEVLRDLL----GKEP 744
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLepspSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 745 QEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVT-VRGVDCSTGLR---- 819
Cdd:cd01368 157 KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKlVQAPGDSDGDVdqdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 820 ---TTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQG-----HVPFRNSKLTYLLQDSLSGDS 891
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*.
gi 1732428643 892 KTLMVVQVSPVEKNTSETLYSLRFAE 917
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
599-920 |
2.20e-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: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVTKEDGEGpEATNAVTFDPDDDSIihlLHKGKPVSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVC 677
Cdd:cd01373 2 AVKVFVRIRPPAEREGDG-EYGQCLKKLSSDTLV---LHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 678 IFAYGQTGAGKTYTMEGTPENP--------GINQRALQLLFSEVQ---EKASD-WQYNITVSAAEIYNEVLRDLLgkEP- 744
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrekEKAGEgKSFLCKCSFLEIYNEQIYDLL--DPa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 745 QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGV---DCSTGLRTT 821
Cdd:cd01373 156 SRNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWekkACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 822 gKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL----RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVV 897
Cdd:cd01373 234 -RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340
....*....|....*....|...
gi 1732428643 898 QVSPVEKNTSETLYSLRFAERVR 920
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
599-920 |
2.99e-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: 2.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVtkEDGEGPEATNAVTFDPDDDSII--HLLHKGKPVSFELDKVFSPWASQQDVF-QEVQALITSCIDGFN 675
Cdd:cd01376 1 NVRVAVRVRPF--VDGTAGASDPSCVSGIDSCSVElaDPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 676 VCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKAsdWQYNITVSAAEIYNEVLRDLLgkEPQEKlEIRLCPD 755
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA--WALSFTMSYLEIYQEKILDLL--EPASK-ELVIRED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 756 GSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLR-TTGKLNLVDLAGSER 834
Cdd:cd01376 154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 835 VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLR 914
Cdd:cd01376 234 NRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313
|
....*.
gi 1732428643 915 FAERVR 920
Cdd:cd01376 314 FAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
600-920 |
1.41e-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: 1.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 600 IRVIARVRPVTKEDGEGpeatnaVTFDPDDDSI-IHLL---------HKGKPVSFELDKVFSPwASQQDVFQEV-QALIT 668
Cdd:cd01375 2 VQAFVRVRPTDDFAHEM------IKYGEDGKSIsIHLKkdlrrgvvnNQQEDWSFKFDGVLHN-ASQELVYETVaKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 669 SCIDGFNVCIFAYGQTGAGKTYTMEGTPEN---PGINQRALQLLFSEVQEKASDwQYNITVSAAEIYNEVLRDLLGKEPQ 745
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTK-AYTVHVSYLEIYNEQLYDLLSTLPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 746 ---EKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTV--RGVDCSTGLRT 820
Cdd:cd01375 154 vgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeaHSRTLSSEKYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 821 TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-RSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQV 899
Cdd:cd01375 234 TSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANI 313
|
330 340
....*....|....*....|.
gi 1732428643 900 SPVEKNTSETLYSLRFAERVR 920
Cdd:cd01375 314 YGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
599-919 |
2.90e-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: 2.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 599 NIRVIARVRPVTKEDgEGPEATNAVTFDPDDDSIIH-------LLHKGKPVSFELDKVFSPWASQQDVFQE-VQALITSC 670
Cdd:cd01367 1 KIKVCVRKRPLNKKE-VAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 671 IDGFNVCIFAYGQTGAGKTYTMEG----TPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLgkepQE 746
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 747 KLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGvdcSTGLRTTGKLNL 826
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRD---RGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 827 VDLAGSER-VGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGD-SKTLMVVQVSPVEK 904
Cdd:cd01367 233 VDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 1732428643 905 NTSETLYSLRFAERV 919
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
600-923 |
1.61e-57 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 216.34 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 600 IRVIARVRPVTKeDGEGPEATNAVTFDPdddsiihLLHKGKpvSFELDKVFSPWASQQDVFQEVQA-LITSCIDGFNVCI 678
Cdd:PLN03188 100 VKVIVRMKPLNK-GEEGEMIVQKMSNDS-------LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 679 FAYGQTGAGKTYTMEGtPENP-----------GINQRALQLLF---SEVQEKASDWQ--YNITVSAAEIYNEVLRDLLgk 742
Cdd:PLN03188 170 FAYGQTGSGKTYTMWG-PANGlleehlsgdqqGLTPRVFERLFariNEEQIKHADRQlkYQCRCSFLEIYNEQITDLL-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 743 EP-QEKLEIRlcPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALL--IVTVRGVDCSTGLR 819
Cdd:PLN03188 247 DPsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFtcVVESRCKSVADGLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 820 T--TGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAAL-----RSRQGHVPFRNSKLTYLLQDSLSGDSK 892
Cdd:PLN03188 325 SfkTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAK 404
|
330 340 350
....*....|....*....|....*....|.
gi 1732428643 893 TLMVVQVSPVEKNTSETLYSLRFAERVRSVE 923
Cdd:PLN03188 405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
579-740 |
1.79e-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: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 579 YRRELQLRKKCHNELVRLKGNIRVIARVRPVTkedgeGPEAtnAVTFDPDDDSIIHLLHKGKpvSFELDKVFSPWASQQD 658
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPEL-----LSEA--QIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 659 VFQEVQALITSCIDGFNVCIFAYGQTGAGktytmegtpENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRD 738
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 1732428643 739 LL 740
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
647-866 |
7.42e-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: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 647 DKVFSPWASQQDVFQEVQALITSCIDGFNV-CIFAYGQTGAGKTYTMEgtpenpGINQRALQLLFSEVQEKASDWQYNIT 725
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMK------GVIPYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 726 VSAAEIYNEVLrdllgkepqekleirlcpdgsgqlyvpgltefqvqsvdDINKVFEfgyNNRTTEfTNLNEHSSRSHALL 805
Cdd:cd01363 97 EITVTLEDQIL--------------------------------------QANPILE---AFGNAK-TTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732428643 806 IVtvrgvdcstglrttgklnLVDLAGSERvgksgaegnrlreaqhINRSLSALGDVIAALR 866
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-543 |
9.10e-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: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 230 QLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELRRCEV 309
Cdd:TIGR02169 671 SEPAELQRLRERLE-----------GLKRELSSLQSELRRIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 310 ELQELRAQ--------PVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLS------------ELNLEVQQKTDRLAEV 369
Cdd:TIGR02169 738 RLEELEEDlssleqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 370 ELRLKDCLAEKAQEEER---LSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQV 446
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 447 LKEMEQQLQ---------NSHQLTVQLRAQIAMYE-AELERAHGQMLE--------------------EMQSLEEDKNRA 496
Cdd:TIGR02169 898 LRELERKIEeleaqiekkRKRLSELKAKLEALEEElSEIEDPKGEDEEipeeelsledvqaelqrveeEIRALEPVNMLA 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1732428643 497 IE--EAFARAQVEMKAVHENLAGVRTnlltlqpALRTLTNDYNGLKRQV 543
Cdd:TIGR02169 978 IQeyEEVLKRLDELKEKRAKLEEERK-------AILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-583 |
6.73e-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: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 256 LQNQVENLKEKlISQAQEVSRLRSELggtdAEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLR 335
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERYKELKAEL----RELELALLVLRLEELREELEELQEELKEAE-------------EELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 336 DKLSQLQLEVAENKGMLSELNLEVQQKTDRLaeveLRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTV 415
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 416 EVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT--------------VQLRAQIAMYEAELER--AH 479
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERleAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 480 GQMLEEMQSLEEDKNRAIEEAFARAqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQEALRSVKA 559
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAER 482
|
330 340
....*....|....*....|....*.
gi 1732428643 560 EIGQAIEEVNS--NNQELLRKYRREL 583
Cdd:TIGR02168 483 ELAQLQARLDSleRLQENLEGFSEGV 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
238-500 |
3.73e-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: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 238 LRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQ 317
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 318 pvvpcegcehsqessqlrdkLSQLQLEVAENKGMLSEL--NLEVQQKTDRLAEVELRLkdclaekaqeeERLSRRLRDSH 395
Cdd:COG3206 242 --------------------LAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAEL-----------AELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 396 ETIASLRAQsppvkyvIKTVEVE-SSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAe 474
Cdd:COG3206 291 PDVIALRAQ-------IAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV- 362
|
250 260
....*....|....*....|....*.
gi 1732428643 475 LERAHGQMLEEMQSLEEDKNRAIEEA 500
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-507 |
4.10e-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: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQELR 305
Cdd:COG1196 246 AELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAEL--ARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 306 RCEVELQELRAQpvvpcegcehsqeSSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 385
Cdd:COG1196 320 ELEEELAELEEE-------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 386 RLSRRLRDSHETIASLRAQsppvKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 465
Cdd:COG1196 387 ELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1732428643 466 AQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVE 507
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-585 |
2.00e-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: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 253 TTQLQNQVENLKEKLiSQAQEVSRLRSELGGTDAE---KHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehsq 329
Cdd:COG1196 195 LGELERQLEPLERQA-EKAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAE------------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 330 essqlrdkLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRlkdcLAEKAQEEERLSRRLRDSHETIASLRAQsppvk 409
Cdd:COG1196 262 --------LAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEE----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 410 yvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSL 489
Cdd:COG1196 325 --LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 490 EEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEE 567
Cdd:COG1196 403 EELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAA 478
|
330
....*....|....*...
gi 1732428643 568 VNSNNQELLRKYRRELQL 585
Cdd:COG1196 479 LAELLEELAEAAARLLLL 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
226-575 |
7.65e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTT---QLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHR--DRLM---VEN 297
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTerdQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlwDRDTgnsITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRCEVELQELRAQPVVPCEGCEHSQE--------SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEV 369
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMErqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 370 ELRLKDcLAEKAQEEERlsrRLRDSHETIASLRAQSPpvkyvIKTVEVESSKTK-QALSESQTRNQHLQEQVAMQRQVLK 448
Cdd:pfam15921 495 ERTVSD-LTASLQEKER---AIEATNAEITKLRSRVD-----LKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKVIE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 449 EMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQM---LEEMQSLEEDKNRAIEEAFAR-AQVEMKAVH------ENL 515
Cdd:pfam15921 566 ILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRrleLQEFKILKDKKDAKIRELEARvSDLELEKVKlvnagsERL 645
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 516 AGV------RTNLL----TLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQEL 575
Cdd:pfam15921 646 RAVkdikqeRDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-505 |
2.24e-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: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELR 305
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERLEELEEEL---------AELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 306 RCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 385
Cdd:COG1196 341 ELEEELEEAEEE----------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 386 RLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 465
Cdd:COG1196 411 ALLERLERLEEELEELEEA-------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1732428643 466 AQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFARAQ 505
Cdd:COG1196 484 EELAEAAARLL-----LLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-404 |
3.42e-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: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTTQL-QNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN------- 297
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARL--DALREELDELEAQIrgnggdr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 -EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC 376
Cdd:COG4913 340 lEQLEREIERLERELEERE-------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 1732428643 377 LAEKAQEEERLSRRLRDSHETIASLRAQ 404
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-629 |
4.30e-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: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 328 SQESSQL--RDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEvelrLKDCLAEKAQEEERLSRRLRDSHETIASLRAQS 405
Cdd:TIGR02168 667 KTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 406 PPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG----- 480
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanl 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 481 ----QMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRS 556
Cdd:TIGR02168 823 rerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------ALLRS 894
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732428643 557 VKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNI-RVIARVRPVTKEDGEGPEA-TNAVTFDPDD 629
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEAlENKIEDDEEE 969
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-605 |
1.18e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 237 VLRERLALHDSDR-----QATTTQLQNQVENLkEKLISQAQEVSRLRSELGGTDAEKHR--DRLMVENEQLRQELRRCEV 309
Cdd:PRK03918 150 VVRQILGLDDYENayknlGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 310 ELQELRAqpvvpcegcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDC---------LAEK 380
Cdd:PRK03918 229 EVKELEE-----------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 381 AQEEERLSR-------RLRDSHETIASLRAQSPPVKYVIKtvevESSKTKQALSESQTRNQHLQEQVAmqrqVLKEMEQQ 453
Cdd:PRK03918 292 AEEYIKLSEfyeeyldELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLE----ELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 454 LQNSHQLTVQ---LRAQIAMYEAE--------LERAH----------GQMLEEMQSLEEDKNRAIEEaFARAQVE----- 507
Cdd:PRK03918 364 YEEAKAKKEElerLKKRLTGLTPEklekeleeLEKAKeeieeeiskiTARIGELKKEIKELKKAIEE-LKKAKGKcpvcg 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 508 -----------MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLqeALRSVKAEIGQAIEEVNSNNQELL 576
Cdd:PRK03918 443 relteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEEL 520
|
410 420
....*....|....*....|....*....
gi 1732428643 577 RKYRRELQLRKKchnELVRLKGNIRVIAR 605
Cdd:PRK03918 521 EKKAEEYEKLKE---KLIKLKGEIKSLKK 546
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
581-865 |
1.68e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 58.21 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 581 RELQLRKKCHNELVRLKgNIRVIARVRPvtkEDGEGPEATNAVTFDPDDDSIihllhKGKPV------------SFELDK 648
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISP---SSNSFEETINTLKFASRAKSI-----KNKIQvnsssdssreieEIKFDL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 649 VFSPWASQQDVFQEVQALITSCIDGfnvcIFAYGQTGAGKTYTMEgtPENPGINQRALQLLFSEVQ-EKASDWQYNITVS 727
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK--SRIDLIMKSIISGTFERKKlLKEEGWKYKSTLQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 728 AAEIY----NEVLRDLLGKEPQEKLEIRLCPDGSGQLY--VPGLTEFQVQSvdDINKvfefgyNNRTTEFTNLNEHSSRS 801
Cdd:COG5059 434 FLRIEidrlLLLREEELSKKKTKIHKLNKLRHDLSSLLssIPEETSDRVES--EKAS------KLRSSASTKLNLRSSRS 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732428643 802 HallivTVRGVDCSTGLRTTGK--LNLVDLAGSERvGKSGAEGNRLREAQHINRSLSALGDVIAAL 865
Cdd:COG5059 506 H-----SKFRDHLNGSNSSTKElsLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-598 |
2.91e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 221 VHRTVEAMSQLQEELVVLRERLALHDSDR---QATTTQLQNQVENLKEKLISQAQEVSRLRsELGGtDAEKHRdRLMVEN 297
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELK-ELKE-KAEEYI-KLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRCEVEL----QELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNlEVQQKTDRLAEVELRL 373
Cdd:PRK03918 303 EEYLDELREIEKRLsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 374 KDCLAEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTV-----EVESSKTKQALSESQTRNQHLQEQVAMQRQVL 447
Cdd:PRK03918 382 TGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELkkaieELKKAKGKCPVCGRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 448 KEMEQQLQNSHQLTVQLRAQIAMYEAELER-----AHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNL 522
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732428643 523 LTLQPALRTLtndyNGLKRQVRgfplLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKG 598
Cdd:PRK03918 542 KSLKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-586 |
4.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 222 HRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQN-----QVENLKEKLISQAQEVSRLRSELggtdaeKHRDRLMVE 296
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEELEERL------EELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 297 NEQLRQELRRCEVELQELRAQPVVpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdc 376
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 377 laEKAQEEERLSRRLRD--SHETIASLRAQSPPVKYVIKTV--------------EVESSKTKQALSESQTRNQHLQEQV 440
Cdd:COG4717 237 --EAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 441 AMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRA-IEEAFARAQVemkavhENLAGVR 519
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeIAALLAEAGV------EDEEELR 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732428643 520 tNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALR-----SVKAEIGQAIEEVNSNNQELLRKYRRELQLR 586
Cdd:COG4717 389 -AALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELE 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-478 |
4.81e-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: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 255 QLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLmvenEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQL 334
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQL-----AALERRI----AALARRIRALEQELAALE-------------AELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 335 RDKLSQLQLEVAENKGMLSELnLEVQQKTDRLAEVELRLKdclaekAQEEERLSRRL-------RDSHETIASLRAQSPP 407
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLS------PEDFLDAVRRLqylkylaPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732428643 408 VKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERA 478
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-502 |
5.49e-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: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 221 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQLqnqvENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQL 300
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELAEELAELEEKL---------EELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 301 RQELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLaevelrlkdclaEK 380
Cdd:TIGR02168 357 EAELEELEAELEELESRLE------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR------------ER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 381 AQEEERLSRRLRDSHEtiaslraqsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQnshql 460
Cdd:TIGR02168 419 LQQEIEELLKKLEEAE---------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD----- 478
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1732428643 461 tvQLRAQIAMYEAELErahgqMLEEMQSLEEDKNRAIEEAFA 502
Cdd:TIGR02168 479 --AAERELAQLQARLD-----SLERLQENLEGFSEGVKALLK 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
248-584 |
6.49e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 248 DRQATTtqLQNQVENLKEKLISQAQEVSRLRSELG---------GTDAEKHRDRLMVENEQLRQE--LRRCEVELQELRA 316
Cdd:PRK04863 285 LEEALE--LRRELYTSRRQLAAEQYRLVEMARELAelneaesdlEQDYQAASDHLNLVQTALRQQekIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 317 QPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENKGMLSELN--LEVQQKT-----------DR------LAEVELR-LKD 375
Cdd:PRK04863 363 RLEEQNEVVEEADEQqEENEARAEAAEEEVDELKSQLADYQqaLDVQQTRaiqyqqavqalERakqlcgLPDLTADnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 376 CLAE-KAQEEERLSRRLR-----DSHETIASLRAQSppVKYVIKTV-EVESSKTKQALSE--SQTRNQ-HLQEQVAMQRQ 445
Cdd:PRK04863 443 WLEEfQAKEQEATEELLSleqklSVAQAAHSQFEQA--YQLVRKIAgEVSRSEAWDVAREllRRLREQrHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 446 VLKEMEQQLQNsHQLTVQLRAQ-----IAMY--EAELERAHGQMLEEMQSLEEDKNRAIEEAFA--RAQVEMKAVHENLA 516
Cdd:PRK04863 521 RLSELEQRLRQ-QQRAERLLAEfckrlGKNLddEDELEQLQEELEARLESLSESVSEARERRMAlrQQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732428643 517 GVRTNLLTLQPA---LRTLTNDYNGLKRQVRGFPLLLQEALRSVKaeigQAIEEVNSNNQELLRKYRRELQ 584
Cdd:PRK04863 600 ARAPAWLAAQDAlarLREQSGEEFEDSQDVTEYMQQLLERERELT----VERDELAARKQALDEEIERLSQ 666
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
265-567 |
6.77e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.72 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 265 EKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELR--------------RCEVELQELRAQpvvpceGCEHSQE 330
Cdd:pfam01576 359 EELTEQLEQAKRNKANL-----EKAKQALESENAELQAELRtlqqakqdsehkrkKLEGQLQELQAR------LSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 331 SSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDClAEKAQEEER----LSRRLRDSHETIASLRAQSP 406
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-QELLQEETRqklnLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 407 PVKYVIKTVEVESSKTKQALSESQTRnqhlQEQVAMQRQVLKEMEQQLQ-NSHQLTVQLRAQIAMYEaELERAHGQMLEE 485
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKK----LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYD-KLEKTKNRLQQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 486 MQSL--EEDKNRAIEEAFARAQ-------VEMKAVHENLAGVR-----------TNLLTLQPALRTLTNDYNGLKRQVRG 545
Cdd:pfam01576 582 LDDLlvDLDHQRQLVSNLEKKQkkfdqmlAEEKAISARYAEERdraeaearekeTRALSLARALEEALEAKEELERTNKQ 661
|
330 340
....*....|....*....|..
gi 1732428643 546 FPLLLqEALRSVKAEIGQAIEE 567
Cdd:pfam01576 662 LRAEM-EDLVSSKDDVGKNVHE 682
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
222-480 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 222 HRTVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLR 301
Cdd:COG1196 291 YELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEEL---------EEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 302 QELRRCEVELQELRAQpvvpcegcEHSQESSQLRDKLSQLQLEVAEnkgmlSELNLEVQQKTDRLAEVELRLKDCLAEKA 381
Cdd:COG1196 358 AELAEAEEALLEAEAE--------LAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 382 QEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLT 461
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEA------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250
....*....|....*....
gi 1732428643 462 VQLRAQIAMYEAELERAHG 480
Cdd:COG1196 487 AEAAARLLLLLEAEADYEG 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-517 |
1.39e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 286 AEKHRDRLMVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDR 365
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 366 LAEVELRLKDCLAEKAQEEERLSRRLR-----DSHETIASLRAQSPPVK-----YVIKTVEVESSKTKQALSESQTRNQH 435
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRalyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 436 LQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMKAVHENL 515
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERT 243
|
..
gi 1732428643 516 AG 517
Cdd:COG4942 244 PA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-588 |
2.32e-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: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 247 SDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQ------------LRQELRRCEVELQEL 314
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeLEKQLNQLKSEISDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 315 RAQPVVPCEGCEHSQESSQlRDKLSQLQLEVAENKGMLSELNLEVQQktdrlaevelrLKDCLAEKAQEEERLSRRLRDS 394
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQ-EKKLEEIQNQISQNNKIISQLNEQISQ-----------LKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 395 HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIamyeAE 474
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 475 LErahgqmlEEMQSLE---EDKNRAIEEafarAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRgfplLLQ 551
Cdd:TIGR04523 445 LT-------NQDSVKEliiKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK----ELE 509
|
330 340 350
....*....|....*....|....*....|....*..
gi 1732428643 552 EALRSVKAEIGQAIEEVNSNNQELLRKyrrELQLRKK 588
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEK---ESKISDL 543
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-568 |
2.45e-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: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 292 RLMVENeqlRQELRRCEVELQELRAQpvvpcegCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVEL 371
Cdd:COG4913 228 DALVEH---FDDLERAHEALEDAREQ-------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 372 -RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyviktvevessktkqaLSESQTRN-QHLQEQVAMQRQVLKE 449
Cdd:COG4913 298 eELRAELARLEAELERLEARLDALREELDELEAQ---------------------IRGNGGDRlEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 450 MEQQLQNSHQLTVQLRAQIAMYEAELERAHgqmleemqsleedknRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPAL 529
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALR---------------AEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260 270
....*....|....*....|....*....|....*....
gi 1732428643 530 RTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEV 568
Cdd:COG4913 422 RELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
259-405 |
2.61e-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: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 259 QVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvPCEGCEhSQESSQLRDKL 338
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLL-----MKELELLNSIKPKLRDRKDALEEELRQLKQLED-ELEDCD-PTELDRAKEKL 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732428643 339 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE-RLSRRLRDSHEtIASLRAQS 405
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkLEQCRGFTFKE-IEKLKEQL 280
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
211-528 |
4.48e-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: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 211 LSGAPGPDPVvhrtvEAMSQLQEELVVLRERLALHdsdrQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHR 290
Cdd:COG3096 826 LAVAFAPDPE-----AELAALRQRRSELERELAQH----RAQEQQLRQQLDQLKEQL----QLLNKLLPQANLLADETLA 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 291 DRLmvenEQLRQELRRCEVELQELRaqpvvpcegcEHSQESSQLRDKLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVE 370
Cdd:COG3096 893 DRL----EELREELDAAQEAQAFIQ----------QHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLK 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 371 LRLkDCLAEKAQEEERLS-----RRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTR-NQHLQEQVAMQ- 443
Cdd:COG3096 955 QQI-FALSEVVQRRPHFSyedavGLLGENSDLNEKLRAR-------LEQAEEARREAREQLRQAQAQySQYNQVLASLKs 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 444 -----RQVLKEMEQ--------------------------QLQNSHQLTVQLRAQIAMYEAELERAHGQMLEemqsLEED 492
Cdd:COG3096 1027 srdakQQTLQELEQeleelgvqadaeaeerarirrdelheELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK----AERD 1102
|
330 340 350
....*....|....*....|....*....|....*....
gi 1732428643 493 ---KNRAIEEAFARAQVEMKAVHENlaGVRTNLLTLQPA 528
Cdd:COG3096 1103 ykqEREQVVQAKAGWCAVLRLARDN--DVERRLHRRELA 1139
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
206-553 |
1.18e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 206 GRCSSLSGAPGPDPVVHRTVEAMSQLQEELVVlrERLALHDSDRQAT--TTQLQN----------QVENLKEKLISQAQE 273
Cdd:pfam15921 455 GKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSdlTASLQEkeraieatnaEITKLRSRVDLKLQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 274 VSRLRSElggtdaEKHRDRLMVENEQLRQELRRCEVELQELRAQ--PVVPCEGcEHSQESSQLRDKLSQLQLEVAENKGM 351
Cdd:pfam15921 533 LQHLKNE------GDHLRNVQTECEALKLQMAEKDKVIEILRQQieNMTQLVG-QHGRTAGAMQVEKAQLEKEINDRRLE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 352 LSELNLEVQQKTDRLAEVELRLKDCLAEKA-----------------QEEERLSRRLRDSHETIASLRAQSPPVKYVIKT 414
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 415 ----VEVESSKTKQALSESQTrnqhlqeQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELErahgQMLEEMQSLE 490
Cdd:pfam15921 686 kseeMETTTNKLKMQLKSAQS-------ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLE 754
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732428643 491 EDKNRAIEEAFARAQvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEA 553
Cdd:pfam15921 755 EAMTNANKEKHFLKE-EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
365-597 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 365 RLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQR 444
Cdd:COG1196 223 KELEAELLLLK-LRELEAELEELEAELEELEAELEELEAE-------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 445 QVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVHENLAGVRTNL 522
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732428643 523 LTLQPALRTLTNDYNGLKRQVRGFpLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 597
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
264-459 |
2.20e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.53 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 264 KEKLISQAQEVSRLRSELGGT-------DAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegceHSQESSQLRD 336
Cdd:pfam09787 23 KEKLIASLKEGSGVEGLDSSTaltleleELRQERDLLREEIQKLRGQIQQLRTELQELEAQ---------QQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 337 KLSQLQLEVAENKgmlsELNLEVQQKTDRLAEVELRLKDclaEKAQEEERLSRRLRDSHETIASLRAQSpPVKYVIKTVE 416
Cdd:pfam09787 94 QLQELEEQLATER----SARREAEAELERLQEELRYLEE---ELRRSKATLQSRIKDREAEIEKLRNQL-TSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732428643 417 VESSKTKQALSESQTRNQHLQEQVAMQRQV----LKEMEQQLQNSHQ 459
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKNSlvlqLERMEQQIKELQG 212
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
223-536 |
2.75e-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: 51.28 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 223 RTVEAMSQLQEElvvlrERLALHDSDRQATTTQLQNQVENLKEKLISQAQ------EVSRLRSELGGTDAEKHRD--RLM 294
Cdd:pfam17380 310 REVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERELERIRqeerkrELERIRQEEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 295 VE----NEQLRQELRRC------EVELQELRAQPVVPCEGCEHSQESSQLRDkLSQLQLEVAENKGMLSELNLEVQQKTD 364
Cdd:pfam17380 385 MErqqkNERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 365 RL--AEVELRLKDCLAEKAQEEERLSRRLRDshetiaslraqsppvkyviKTVEVESSKTKQALSESQTRNQHLQEQVAM 442
Cdd:pfam17380 464 RLrqQEEERKRKKLELEKEKRDRKRAEEQRR-------------------KILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 443 QRQVLKEMEQQlqnshqltvqlraqiamYEAELERAHGQMLEEMQSLEEDKNRAIEE-----AFARAQVEMKAVHENLAG 517
Cdd:pfam17380 525 RQKAIYEEERR-----------------REAEEERRKQQEMEERRRIQEQMRKATEErsrleAMEREREMMRQIVESEKA 587
|
330 340
....*....|....*....|....
gi 1732428643 518 -----VRTNLLTLQPALRTLTNDY 536
Cdd:pfam17380 588 raeyeATTPITTIKPIYRPRISEY 611
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
226-514 |
5.35e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLmvenEQLRQELR 305
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQ----QQRSQLEQAKEGL----SALNRLLPRLNLLADETLADRV----EEIREQLD 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 306 RCEVELQELRAQPVVpCEGCEhsQESSQLR---DKLSQLQLEVAENKGMLSElnleVQQKTDRLAEVELRL--------K 374
Cdd:PRK04863 905 EAEEAKRFVQQHGNA-LAQLE--PIVSVLQsdpEQFEQLKQDYQQAQQTQRD----AKQQAFALTEVVQRRahfsyedaA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 375 DCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEM---- 450
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQ-------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpa 1050
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732428643 451 ---------------EQQLQNSHQLTVQLRAQIAMYEAELERAHGQmLEEMQSLEEDKNRAIEEAFARAQVEMKAVHEN 514
Cdd:PRK04863 1051 dsgaeerararrdelHARLSANRSRRNQLEKQLTFCEAEMDNLTKK-LRKLERDYHEMREQVVNAKAGWCAVLRLVKDN 1128
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
223-407 |
5.45e-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: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 223 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLIS--QAQEVSRLRSELGGTDAEKHRDRLMVE---N 297
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLkylA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 377
Cdd:COG4942 146 PARREQAEELRADLAELAAL----------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|
gi 1732428643 378 AEKAQEEERLSRRLRDSHETIASLRAQSPP 407
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-404 |
5.72e-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: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTTQ---LQNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVENEQLRQ 302
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 303 ELRRCEVELQELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQ 382
Cdd:TIGR02168 888 ALALLRSELEELSEELR------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
170 180
....*....|....*....|..
gi 1732428643 383 EEERLSRRLRDShetIASLRAQ 404
Cdd:TIGR02168 962 KIEDDEEEARRR---LKRLENK 980
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-586 |
7.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 222 HRTVEAMSQLQEELVVLRERLALHDSDR--------QATTTQLQNQVENLKEKLISQAQEVSRLR---SELGGTDA---- 286
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKlekeleelEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 287 ------EKHRDRLM----VENEQLRQELRRCEVELQELRAQpVVPCEGcEHSQESSQLRDKLSQLQLEVAENKgmLSELN 356
Cdd:PRK03918 441 cgreltEEHRKELLeeytAELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESELIKLKELAEQLKELEEK--LKKYN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 357 LEVQQKTDRLAEvelRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppVKYVIKTVEVESSKTKQALSES-----QT 431
Cdd:PRK03918 517 LEELEKKAEEYE---KLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELgfesvEE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 432 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMK 509
Cdd:PRK03918 590 LEERLKELEPFYNEYleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 510 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAE---IGQAIEEVnSNNQELLRKYRRELQLR 586
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKElekLEKALERV-EELREKVKKYKALLKER 740
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
228-500 |
7.36e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 228 MSQLQEE-LVVLRERLALHDSDRQATTtqLQNQVENLKEklisQAQEV-SRLRSELGGTD---------------AEKHR 290
Cdd:pfam05622 154 VKLLEERnAEYMQRTLQLEEELKKANA--LRGQLETYKR----QVQELhGKLSEESKKADklefeykkleekleaLQKEK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 291 DRLMVENEQLRQ---ELRRCEVELQELRAQPVVPCEGCEHSQE------SSQLRDKLSQLQLEvaeNKgMLSELnlEVQQ 361
Cdd:pfam05622 228 ERLIIERDTLREtneELRCAQLQQAELSQADALLSPSSDPGDNlaaeimPAEIREKLIRLQHE---NK-MLRLG--QEGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 362 KTDRLAEVELRLKDclAEKAQEEerLSRRLRDSHETIASLRAQsppVKYVIKTVEVESSKT------KQALSESQTRNQH 435
Cdd:pfam05622 302 YRERLTELQQLLED--ANRRKNE--LETQNRLANQRILELQQQ---VEELQKALQEQGSKAedssllKQKLEEHLEKLHE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732428643 436 LQEQVAMQRQVLKEMEQQLQNSHQLTVqlraqiamyeAELERAHGQMLEEMQSLEEDKNRAIEEA 500
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDSNLAQKI----------DELQEALRKKDEDMKAMEERYKKYVEKA 429
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
308-586 |
1.13e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 308 EVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQlEVAENkgmLSELNLEVQQKTDRLAEVELRLKdclaEKAQEEERL 387
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEE---LEQLREELEQAREELEQLEEELE----QARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 388 SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQ 467
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 468 IAMYEAELERAHGQMLEEMQsleEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFP 547
Cdd:COG4372 159 LESLQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 1732428643 548 LLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLR 586
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
378-586 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 378 AEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVEssktkqalsESQTRNQHLQEQVAMQRQVLKEMEQQLQNS 457
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 458 HQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQ--------------VEMKAVHENLAGVRTNLL 523
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732428643 524 TLQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIgQAIEEVNSN---NQELLRKY-RRELQLR 586
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 ... |
233-490 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 233 EELVVLRERLALHDSDRQATTTQLQNQvENLKEKLISQAQEVSRLRSELggtdaekhrdrlmvenEQLRQELRRCEVELQ 312
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI----------------EEQRRLLQTLHSQEI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 313 ELRAQPVVPCEGCEHSQESSQLRDKLSQLQlevaENKGMLSELNLEVQQKTDRLAEvelrlkdclaEKAQEEERLSRRlR 392
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKELDILQR----------EQATIDTRTSAF-R 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 393 DSHETIASLRAQSPPVKYVIKTVEVESSKTKQalsESQTRNQHLQEqvamQRQVLKEMEQQLQNSHQLTVQlraqiamyE 472
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQE----SAQSLKEREQQLQTKEQIHLQ--------E 485
|
250
....*....|....*...
gi 1732428643 473 AELERAHGQMLEEMQSLE 490
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEP 503
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
222-590 |
1.59e-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: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 222 HRTVEAMSQLQEELVVLRERLALHDSDRQATTtQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQL- 300
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR--DLQGQLa 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 301 ----RQELRRCEVELQELRAQPVVPCEGCE--HSQESSQ-LRDKLSQLQ-----LEVAENKGMLSELNLEVQQKTDRLAE 368
Cdd:TIGR00618 428 hakkQQELQQRYAELCAAAITCTAQCEKLEkiHLQESAQsLKEREQQLQtkeqiHLQETRKKAVVLARLLELQEEPCPLC 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 369 VELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyVIKTVEVE-SSKTKQA--LSESQTRNQHLQEQVAMQRQ 445
Cdd:TIGR00618 508 GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET-------SEEDVYHQlTSERKQRasLKEQMQEIQQSFSILTQCDN 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 446 VLKEMEQQLQNshqLTVQLRAQIAMyEAELERahgQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAgvrtnLLTL 525
Cdd:TIGR00618 581 RSKEDIPNLQN---ITVRLQDLTEK-LSEAED---MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK-----LTAL 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732428643 526 QPALRTLTNDYNGLK-RQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCH 590
Cdd:TIGR00618 649 HALQLTLTQERVREHaLSIRVLPKELLAsrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
226-516 |
2.81e-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: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVEN----LKEKLISQAQEVSRLRSELggtdAEKHRdrlmvENEQLR 301
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSI----AEKER-----ELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 302 QELRRCEVELQELRAQpvvpCEGCEHSQESSQLRdkLSQLQLEVAENKgmlSELNLEVQqktdRLAEVELRLKDCLAEKA 381
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAE----IEELEREIEEERKR--RDKLTEEYAELK---EELEDLRA----ELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 382 QEEERLS---RRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSH 458
Cdd:TIGR02169 389 DYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732428643 459 QLTVQLRAQIAMYEAELerahgqmleemqsleEDKNRAIEEAFARAQVEMKAVHENLA 516
Cdd:TIGR02169 469 QELYDLKEEYDRVEKEL---------------SKLQRELAEAEAQARASEERVRGGRA 511
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
219-582 |
3.63e-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: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 219 PVVHRtvEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRdrlmvene 298
Cdd:pfam07111 233 PEVHS--QTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPK-------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 299 QLRQELRRCEVELQELRAQpvVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 378
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQ--LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQM 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 379 E--KAQEEERLSRRLRDS--------------------------HETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQ 430
Cdd:pfam07111 381 ElsRAQEARRRQQQQTASaeeqlkfvvnamsstqiwlettmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 431 TRNQHLQEQVA---MQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQve 507
Cdd:pfam07111 461 LRQESCPPPPPappVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQ-LEQELQRAQ-- 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732428643 508 mkavhENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRE 582
Cdd:pfam07111 538 -----ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
224-593 |
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 1732428643 224 TVEAMSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSE---------LGGTDAE---KHRD 291
Cdd:PRK02224 242 VLEEHEERREELETLEAEIE----DLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagLDDADAEaveARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 292 RLMVENEQLRQELRRCEVELQELRAQPVVPCEGC-EHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 370
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDAdDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 371 LRLKDC---LAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVE--------------VESSKTKQALSESQTRN 433
Cdd:PRK02224 398 ERFGDApvdLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERV 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 434 QHLQEQVAMQRQVLKEMEQQLQNSHQLtVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIE--------EAFARAQ 505
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEElreraaelEAEAEEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 506 VE-MKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRqvrgfplllQEALRSVKAEIGQAIEEVNSNNQEL--LRKYRRE 582
Cdd:PRK02224 557 REaAAEAEEEAEEAREEVAELNSKLAELKERIESLER---------IRTLLAAIADAEDEIERLREKREALaeLNDERRE 627
|
410
....*....|..
gi 1732428643 583 -LQLRKKCHNEL 593
Cdd:PRK02224 628 rLAEKRERKREL 639
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
211-590 |
4.60e-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: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 211 LSGAPGPD-PVVHRTVEAMSQLQEELVVLRERLalhDSDRQaTTTQLQNQVENLKEKLISQAQEVSRLRSELGGT----- 284
Cdd:TIGR00618 519 DIDNPGPLtRRMQRGEQTYAQLETSEEDVYHQL---TSERK-QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnitv 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 285 DAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKtD 364
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK-E 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 365 RLAEVELRLkdclaekaQEEERLSRRLRDSHETIAslraQSPPVKYVIKTVEVESSKTKQALS------------ESQTR 432
Cdd:TIGR00618 674 LLASRQLAL--------QKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIEnassslgsdlaaREDAL 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 433 NQHLQEQVAMQRQVLKEME-QQLQNSHQLTV--QLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRaIEEAFARAQVEMK 509
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTeAHFNNNEEVTAalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE-IGQEIPSDEDILN 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 510 AVHENLAGVRTNLLTLqpaLRTLTNDYNGLKRQVRGFPLLLQ--EALRSVKAEIGQAIEEVNSNNQ-------ELLRKYR 580
Cdd:TIGR00618 821 LQCETLVQEEEQFLSR---LEEKSATLGEITHQLLKYEECSKqlAQLTQEQAKIIQLSDKLNGINQikiqfdgDALIKFL 897
|
410
....*....|
gi 1732428643 581 RELQLRKKCH 590
Cdd:TIGR00618 898 HEITLYANVR 907
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-405 |
4.71e-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: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 230 QLQEELVVLRERLALHDSDRQATTTQLQ--NQVENLKEKLI---SQAQEVSRLRSELggTDAEKHRDRLmvenEQLRQEL 304
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIdvaSAEREIAELEAEL--ERLDASSDDL----AALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 305 RRCEVELQELRAQpvvpCEGCEhsQESSQLRDKLSQLQLEVAENKGMLSElnLEVQQKTDRLAEVELRLKDCLAEKAqeE 384
Cdd:COG4913 695 EELEAELEELEEE----LDELK--GEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERFAAALGDAV--E 764
|
170 180
....*....|....*....|.
gi 1732428643 385 ERLSRRLRDSHETIASLRAQS 405
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
329-505 |
5.67e-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: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 329 QESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIAS-------L 401
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 402 RAQSpPVKYV--IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEA---ELE 476
Cdd:COG3883 110 GSES-FSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAllaQLS 188
|
170 180
....*....|....*....|....*....
gi 1732428643 477 RAHGQMLEEMQSLEEDKNRAIEEAFARAQ 505
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
168-505 |
5.88e-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: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 168 KEDELPKRQAPAPRRDREAPEAGGTMNVENTGGRL---------FGIGRCSSLSGAPGPDPvvhrtvEAMSQLQEELVVL 238
Cdd:pfam15709 220 KSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVinsketedaSERGAFSSDSVVEDPWL------SSKYDAEESQVSI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 239 RERLAlhdSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSElggtdaeKHRDRLMVEneqlRQELRRCEVELQElraqp 318
Cdd:pfam15709 294 DGRSS---PTQTFVVTGNMESEEERSEEDPSKALLEKREQEK-------ASRDRLRAE----RAEMRRLEVERKR----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 319 vvpcegcehsQESSQLRdKLSQLQLEVAENkgMLSELNLEVQQKTDRLAEVELRLKDclAEKAQEEERLSRRLRdshETI 398
Cdd:pfam15709 355 ----------REQEEQR-RLQQEQLERAEK--MREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQ---LQA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 399 ASLRAQSPPVKYVIKTVEVESSKTKQAL---SESQTRNQHLQEQVAMQRQVLKEMEQQlqnsHQLTVQLRAQiamyEAEl 475
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAeraEAEKQRQKELEMQLAEEQKRLMEMAEE----ERLEYQRQKQ----EAE- 487
|
330 340 350
....*....|....*....|....*....|
gi 1732428643 476 ERAHGQMLEEMQSLEEDKNRAIEEAFARAQ 505
Cdd:pfam15709 488 EKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-592 |
6.54e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 230 QLQEELVVLRERLALHDSDRQATTTQ-----LQNQVENLKEKLISQAQEVSRL-RSELGGTDAEKHRDRLMVENEQLRQE 303
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKkevksLQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 304 LRRCEVELQELRA----QPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAE 379
Cdd:TIGR00606 555 KSRHSDELTSLLGyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 380 KAQEE--ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESS-------KTKQALSESQTRNQHLQEQVAMQRQVLKEM 450
Cdd:TIGR00606 635 QDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 451 EQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSLEEdKNRAIEEafaraqvEMKAVHENLAGVRTNLLTLQPALR 530
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDL----KEKEIPELRN-KLQKVNR-------DIQRLKNDIEEQETLLGTIMPEEE 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 531 T---LTNDYNGLKRqvrgfpllLQEALRSVKAEIGQAIEEVNSNN---------------QELLRKYRRELQLRKKCHNE 592
Cdd:TIGR00606 783 SakvCLTDVTIMER--------FQMELKDVERKIAQQAAKLQGSDldrtvqqvnqekqekQHELDTVVSKIELNRKLIQD 854
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
226-594 |
7.00e-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: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRlmVENEQLRQELR 305
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS--SELEEMTKFKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 306 RCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkdclAEKAQEEE 385
Cdd:pfam05483 402 NKEVELEELKKI----------LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 386 RLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLR 465
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 466 AQIAMYEAELERAHGQMLEEMQSLEEDKnRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRG 545
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1732428643 546 fpllLQEALRSVKAEIGQAIEEVNSNNQ---ELLRKYRRELQLRKKCHNELV 594
Cdd:pfam05483 627 ----ENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-401 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSELGgtDAEKHRDRLMVENEQLRQELR 305
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAA----NLRERLESLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 306 RCEVELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEE 385
Cdd:TIGR02168 870 ELESELEALLN------ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
170
....*....|....*.
gi 1732428643 386 RLSRRLRDSHETIASL 401
Cdd:TIGR02168 944 RLSEEYSLTLEEAEAL 959
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
221-525 |
1.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 221 VHRTVEAMSQLQEELVVLRERLALHDSDRQATTTQL---QNQVENLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN 297
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCL 377
Cdd:COG4372 111 EELQEELEELQKERQDLE-------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 378 AEKAQEE-ERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVamQRQVLKEMEQQLQN 456
Cdd:COG4372 178 EAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA--LELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732428643 457 SHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTL 525
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-586 |
1.23e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 232 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEkLISQAQEVSRLRSELGgTDAEKHRDRLMVENEQLRQE--LRRCEV 309
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLE-QDYQAASDHLNLVQTALRQQekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 310 ELQELRAQPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENKGMLSELN--LEVQQK--------TDRLAEVELRL----- 373
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYQqaLDVQQTraiqyqqaVQALEKARALCglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 374 -----KDCLAE-KAQEEER------LSRRLRDSHETIASLRAQSPPVKYVIKTVEVES--SKTKQALSESQTRnQHLQEQ 439
Cdd:COG3096 435 tpenaEDYLAAfRAKEQQAteevleLEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ-QALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 440 VAMQRQVLKEMEQQLQNSH-------QLTVQLRAQIAMYEaELERAHGQMLEEMQSLEEDKNRAIEEafaraQVEMKAVH 512
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQnaerlleEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQ-----RSELRQQL 587
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732428643 513 ENLAGVRTNLLTLQPALRTltndynglkrqvrgfpllLQEALRSVKAEIGQAIE---EVNSNNQELLRKYRRELQLR 586
Cdd:COG3096 588 EQLRARIKELAARAPAWLA------------------AQDALERLREQSGEALAdsqEVTAAMQQLLEREREATVER 646
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
238-595 |
1.25e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 238 LRERLALHDSDRQATTTQLQ---NQ-------VENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRC 307
Cdd:pfam10174 294 LKQELSKKESELLALQTKLEtltNQnsdckqhIEVLKESLTAKEQRAAILQTEV---------DALRLRLEEKESFLNKK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 308 EVELQELRAQpvvpcEGCEhSQESSQLRD--------------KLSQLQLEVAENKGMLSELNLEVQQ-KTDR------L 366
Cdd:pfam10174 365 TKQLQDLTEE-----KSTL-AGEIRDLKDmldvkerkinvlqkKIENLQEQLRDKDKQLAGLKERVKSlQTDSsntdtaL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 367 AEVElrlkDCLAEKAQEEERL----SRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAM 442
Cdd:pfam10174 439 TTLE----EALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 443 QRQVLKEMEQQLQNSHQLTVQLRAQI--AMYEAELERAHGQMLEEMQSLEEDKNRAIEEAfARAQVEMkavhENLAGvrt 520
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEES-GKAQAEV----ERLLG--- 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732428643 521 nlltlqpALRTLTNDYNGLKRQVRGFPLLlqeALRSVKaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVR 595
Cdd:pfam10174 587 -------ILREVENEKNDKDKKIAELESL---TLRQMK-EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-587 |
1.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 223 RTVEAMSQLQEELVVLRERLAlhdsdrqatttQLQNQVENLKEKL-ISQAQEVSRLRSELggtdaekhrDRLMVENEQLR 301
Cdd:COG4717 153 ERLEELRELEEELEELEAELA-----------ELQEELEELLEQLsLATEEELQDLAEEL---------EELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 302 QELRRCEVELQELRAQpvvpCEGCEHSQESSQLRDKLSQLQL----------------EVAENKGMLSELNLEVQQKTDR 365
Cdd:COG4717 213 EELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAGVLFLVLGLLAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 366 LAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQ-----SPPVKYVIKTVEvESSKTKQALSESQTRNQHLQEQV 440
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppDLSPEELLELLD-RIEELQELLREAEELEEELQLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 441 AMQRQV----------LKEMEQQLQNSHQLtVQLRAQIAMYEAELERAHGQMLEEMQSLEEDknrAIEEAFARAQVEMKA 510
Cdd:COG4717 368 LEQEIAallaeagvedEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEE 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732428643 511 VHENLAGVRTNLLTLQPALRTLTNDynGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNN--QELLRKYRRELQLRK 587
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED--GELAE-------LLQELEELKAELRELAEEWAALKlaLELLEEAREEYREER 513
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
226-393 |
1.41e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALhdsdRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL-----GGTDAEKHRDRLMVENEQL 300
Cdd:PRK09039 53 SALDRLNSQIAELADLLSL----ERQGNQDLQDSVANLRASLSAAEAERSRLQALLaelagAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 301 RQELRRCEVELQELRAQpvvpcegcehsqeSSQLRDKLSQLQ--LEVAENKGmlselnlevQQKTDRLAEVELRLKDCLA 378
Cdd:PRK09039 129 KQVSARALAQVELLNQQ-------------IAALRRQLAALEaaLDASEKRD---------RESQAKIADLGRRLNVALA 186
|
170 180
....*....|....*....|..
gi 1732428643 379 EKAQEeerLSR-------RLRD 393
Cdd:PRK09039 187 QRVQE---LNRyrseffgRLRE 205
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
232-604 |
1.71e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 232 QEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaekhrDRLMVENEQLRQELRRCEVEL 311
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL---------EQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 312 QELRAQPVvpcegcEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRL 391
Cdd:COG4372 83 EELNEQLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 392 RDSHETIASLRAQSPPVKYVIKtvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMY 471
Cdd:COG4372 157 EQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 472 EAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQ 551
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1732428643 552 EALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIA 604
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-569 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 283 GTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQpvvpcegcehSQESSQLRDKLSQLQlEVAENKGMLSELNLEVQQK 362
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAE----------LDALQERREALQRLA-EYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 363 TDRLAEVEL------RLKDCLAEKAQEEERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSE-----SQT 431
Cdd:COG4913 674 EAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAaedlaRLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 432 RNQHLQEQV--AMQRQVLKEMEQQLQNSHQltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFaraqvEMK 509
Cdd:COG4913 747 LRALLEERFaaALGDAVERELRENLEERID---ALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP-----EYL 818
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 510 AVHENLagVRTNLLTLQPALRTLtndyngLKRQVRGFPLLLQEALRSVKAEIGQAIEEVN 569
Cdd:COG4913 819 ALLDRL--EEDGLPEYEERFKEL------LNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-390 |
2.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 223 RTVEAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENL---------KEKLISQAQEVSRLRSELGGTDAEKHRDRL 293
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleqAEEYQELKEELEELEEQLEELLGELEELLE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 294 MVENEQLRQELRRCEVELQELRaqpvvpcegcehsQESSQLRDKLSQL--QLEVAENKGMLSELNLEVQQKTDRLAEVE- 370
Cdd:COG4717 424 ALDEEELEEELEELEEELEELE-------------EELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAe 490
|
170 180
....*....|....*....|....
gi 1732428643 371 ----LRLKDCLAEKAQEEERLSRR 390
Cdd:COG4717 491 ewaaLKLALELLEEAREEYREERL 514
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
223-387 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 223 RTVEAMSQLQEELVVLRERLALHDSDRQAtttqlqnqVENLKEKLisqaqevsrlrselggTDAEKHRDRLMVENEQLRQ 302
Cdd:pfam13851 58 RLTEPLQKAQEEVEELRKQLENYEKDKQS--------LKNLKARL----------------KVLEKELKDLKWEHEVLEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 303 ELRRCEVELQELRAQpvvpCEGCEHS-QESSQLRD-----KLSQLQlEVAENK-----GMLSELNLEvqqkTDRLAEVEL 371
Cdd:pfam13851 114 RFEKVERERDELYDK----FEAAIQDvQQKTGLKNlllekKLQALG-ETLEKKeaqlnEVLAAANLD----PDALQAVTE 184
|
170
....*....|....*.
gi 1732428643 372 RLKDCLAEKAQEEERL 387
Cdd:pfam13851 185 KLEDVLESKNQLIKDL 200
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
261-525 |
2.51e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 261 ENLKEKLISQAQEVSRLRSELggtdaekhRDRLMVENEQLRQELRRcevELQELRAQpvvpcegcehSQESSQLRDKLSQ 340
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFSLLK--------KETIYLQSAQRVELAER---QLQELKID----------VKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 341 LQLEVAENKGML-SELNLEVQQKTDRLAEVE--LRLKDCLAEKAQEEERLSRRLRDsHETIASLRAQSPPVKYVIKTVEV 417
Cdd:COG5022 904 LESEIIELKKSLsSDLIENLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKSTI 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 418 ESSKTKQALSESQTRNQHLQEQV----AMQRQV--LKEMEQQLQNSHQLTVQLRA-----QIAMYEAELERAHgqMLEEM 486
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSkqygALQESTkqLKELPVEVAELQSASKIISSestelSILKPLQKLKGLL--LLENN 1060
|
250 260 270
....*....|....*....|....*....|....*....
gi 1732428643 487 QSLEEDKNRAIEEafaRAQVEMKAVHENLAGVRTNLLTL 525
Cdd:COG5022 1061 QLQARYKALKLRR---ENSLLDDKQLYQLESTENLLKTI 1096
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
224-511 |
3.68e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 224 TVEAMSQLQEELVVLRERLALHDSDRQatttQLQNQVENLKEKLISQAQEVSRLRSElggtdAEKHRDRlmveneqlRQE 303
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRD----ELNEELKELAEKRDELNAQVKELREE-----AQELREK--------RDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 304 LRRcevELQELRAqpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELN--------LEVQQKTDRL-AEVELRLK 374
Cdd:COG1340 69 LNE---KVKELKE------ERDELNEKLNELREELDELRKELAELNKAGGSIDklrkeierLEWRQQTEVLsPEEEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 375 DCLAEKAQEEERLsRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQL 454
Cdd:COG1340 140 EKIKELEKELEKA-KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732428643 455 QNSHQLTVQLRAQIAMYEAELErahgQMLEEMQSLEE------DKNRAIEEAFARAQVEMKAV 511
Cdd:COG1340 212 DELHKEIVEAQEKADELHEEII----ELQKELRELRKelkklrKKQRALKREKEKEELEEKAE 270
|
|
| BAR_Vps5p |
cd07627 |
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
331-493 |
4.01e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 42.68 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 331 SSQLRDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---Q 404
Cdd:cd07627 30 VSSQRKELASATEEFAETLEALSSLELSksLSDLLAALAEVQKRIKESLERQALQDVLtLGVTLDEYIRSIGSVRAafaQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 405 SPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLE 484
Cdd:cd07627 110 RQKLWQYWQSAESELSKKKAQLEKLKRQGKTQQEKLNSLLSELEEAERRASE--------------LKKEFEEVSELIKS 175
|
....*....
gi 1732428643 485 EMQSLEEDK 493
Cdd:cd07627 176 ELERFERER 184
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
226-580 |
4.81e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLisqaQEVSRLRSELGGTDAEKHRDRLMVENEQLRQE-- 303
Cdd:PRK04778 140 EEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEF----SQFVELTESGDYVEAREILDQLEEELAALEQIme 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 304 -----LRRCEVE----LQELRAqpvvpceGCEHSQESS------QLRDKLSQLQLEVAENKGMLSELNL--------EVQ 360
Cdd:PRK04778 216 eipelLKELQTElpdqLQELKA-------GYRELVEEGyhldhlDIEKEIQDLKEQIDENLALLEELDLdeaeekneEIQ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 361 QKTDRL-----AEVELRlKDCLAEKAQEEERLSRRLRDSHETIASLR--AQSppvkYVIKTVEVESSKTKQA-LSESQTR 432
Cdd:PRK04778 289 ERIDQLydileREVKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEIDrvKQS----YTLNESELESVRQLEKqLESLEKQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 433 NQHLQEQVAMQRQV-------LKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHgQMLEEMQS-LEEDKnRAIE------ 498
Cdd:PRK04778 364 YDEITERIAEQEIAyselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR-EKLERYRNkLHEIK-RYLEksnlpg 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 499 ------EAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR-------QVRGFPLLLQEALR--SVKAEIGQ 563
Cdd:PRK04778 442 lpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEeteelveNATLTEQLIQYANRyrSDNEEVAE 521
|
410
....*....|....*..
gi 1732428643 564 AIEEVnsnnQELLRKYR 580
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 ... |
226-459 |
5.50e-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: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSEL------------GGTDAEKHRDRL 293
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLidlkehasslasSGLKKDSKLKSL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 294 MVENEQLRQELRRCEVELQelRAQpvvpcEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRl 373
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLK--KAH-----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 374 KDCLAEKAQE-EERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQ--RQVLKEM 450
Cdd:pfam10174 595 KNDKDKKIAElESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEktRQELDAT 674
|
....*....
gi 1732428643 451 EQQLQNSHQ 459
Cdd:pfam10174 675 KARLSSTQQ 683
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
256-499 |
6.11e-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: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 256 LQNQV-ENLKEKL-ISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcEGCEHSQESSQ 333
Cdd:pfam07888 32 LQNRLeECLQERAeLLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE---ELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 334 LRDKLSQ----LQLEVAENKGMLSELNLEVQQKTDRLAEVELRLkDCLAEKAqeeERLSRRLRDSHETIASLRAQSPPVK 409
Cdd:pfam07888 109 SSEELSEekdaLLAQRAAHEARIRELEEDIKTLTQRVLERETEL-ERMKERA---KKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 410 YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAElERAHGQMLEEMQSL 489
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS-ERKVEGLGEELSSM 263
|
250
....*....|
gi 1732428643 490 EEDKNRAIEE 499
Cdd:pfam07888 264 AAQRDRTQAE 273
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
240-460 |
7.58e-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: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 240 ERLALHDSDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLR-QELRRCEVELQELRAQP 318
Cdd:pfam07888 160 KKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlTTAHRKEAENEALLEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 319 VVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHET 397
Cdd:pfam07888 240 RSLQERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDR 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732428643 398 IASLRA---------QSPPVKYVIKTVEVESSKTKQALSESQTRNQhLQEQVAMQRQVLKEMEQQLQNSHQL 460
Cdd:pfam07888 320 IEKLSAelqrleerlQEERMEREKLEVELGREKDCNRVQLSESRRE-LQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
255-594 |
8.59e-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: 43.09 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 255 QLQNQVENLKEKLISQAQEVSRLRS-----ELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVvpcegcEHSQ 329
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK------SKEK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 330 ESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLrdshetiaslraqsppVK 409
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN----------------LE 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 410 YVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERahgqMLEEMQSL 489
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK----LSSIIKNI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 490 EEDKNRAIEEAfaraqvemKAVHENLAGVR---TNLLTLQPALRTLTNDYNGLKRQvrgfplLLQEALRSVKAEIGQAIE 566
Cdd:TIGR04523 637 KSKKNKLKQEV--------KQIKETIKEIRnkwPEIIKKIKESKTKIDDIIELMKD------WLKELSLHYKKYITRMIR 702
|
330 340 350
....*....|....*....|....*....|.
gi 1732428643 567 evNSNNQELLRKYR---RELQLRKKCHNELV 594
Cdd:TIGR04523 703 --IKDLPKLEEKYKeieKELKKLDEFSKELE 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
228-575 |
8.96e-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: 43.18 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 228 MSQLQEELVVLRERLALHDSDRQATTTQLQNQVENLK-------EKLISQAQ-EVSRL--RSELGGTDAEKHRDRLMVEN 297
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLqqhqdriEQLISEHEvEITGLteKASSARSQANSIQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRCEVELQELRAQPvvpcegcehSQESSQLR-------DKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVE 370
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTV---------SQLRSELReakrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 371 LRLKDCLAEKAQEEERLS------RRLRDSHE----TIASLRAQSPPvkyviKTVEVESSKTKQALSESQTRNQHLQEQV 440
Cdd:pfam15921 377 DQLQKLLADLHKREKELSlekeqnKRLWDRDTgnsiTIDHLRRELDD-----RNMEVQRLEALLKAMKSECQGQMERQMA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 441 AMQ-----RQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEdKNRAIEEAFA-----RAQVEMKA 510
Cdd:pfam15921 452 AIQgknesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAeitklRSRVDLKL 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732428643 511 VH--------ENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKA---EIGQAIEEVNSNNQEL 575
Cdd:pfam15921 531 QElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqvEKAQLEKEINDRRLEL 606
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-404 |
9.99e-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: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 227 AMSQLQEELvvlrerLALHDSDRQATttQLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLmvenEQLRQELRR 306
Cdd:COG1579 1 AMPEDLRAL------LDLQELDSELD--RLEHRLKELPAELAELEDELAALEARL-----EAAKTEL----EDLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 307 CEVELQELRAQPVvpcegcEHSQESSQLRD--KLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE 384
Cdd:COG1579 64 LELEIEEVEARIK------KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
170 180
....*....|....*....|
gi 1732428643 385 ERLSRRLRDSHETIASLRAQ 404
Cdd:COG1579 138 AELEEKKAELDEELAELEAE 157
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
259-642 |
1.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 259 QVENLKEKL--ISQAQEVSRLRSELGGTDAEKHRDRlmvENEQLRQELRRCEVELQelRAQPVVPCEGCEHSQESSQLRD 336
Cdd:PTZ00121 1458 KAEEAKKKAeeAKKADEAKKKAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 337 KLSQLQLEVAENKGMLSELnlevqQKTDRLAEVELRLKdcLAEKAQEEERLSRRLRDSHEtiaSLRAQSPPVKYVIKTVE 416
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL-----KKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 417 VESS-KTKQALSESQTRNQhlQEQVAMQRQVLKEMEQ-------------QLQNSHQLTVQLRAQIAMYEAELERAhgqm 482
Cdd:PTZ00121 1603 EEKKmKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQlkkkeaeekkkaeELKKAEEENKIKAAEEAKKAEEDKKK---- 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 483 LEEMQSLEEDKNRAiEEAFARAQVEMKAVHEnlagvrtnlltlqpaLRTLTNDYNGLKRQVRGfplllQEALRSVKAEIG 562
Cdd:PTZ00121 1677 AEEAKKAEEDEKKA-AEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKK-----AEEENKIKAEEA 1735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 563 QAIEEVNSNNQELLRKYRRE----LQLRKKCHNELVRLKGNIRVIARvRPVTKEDGEGPEATNAVTFDPDDDS--IIHLL 636
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFanIIEGG 1814
|
....*.
gi 1732428643 637 HKGKPV 642
Cdd:PTZ00121 1815 KEGNLV 1820
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
298-612 |
1.05e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRCEVE----LQELRAQPVVPCEGCEHSQESSQ-LRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELR 372
Cdd:pfam05557 12 SQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQeLQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 373 LKdclaEKAQEEErlsrrlrDSHETIASLRAQSPPVKYVIKtvevessKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQ 452
Cdd:pfam05557 92 LN----EKESQLA-------DAREVISCLKNELSELRRQIQ-------RAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 453 ---QLQNSHQL--------------------------TVQLR-AQIAMYEAELERaHGQMLEEMQSLEEDKNRAIEEAFa 502
Cdd:pfam05557 154 lrqNLEKQQSSlaeaeqrikelefeiqsqeqdseivkNSKSElARIPELEKELER-LREHNKHLNENIENKLLLKEEVE- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 503 raqvEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKR--QVRGFPLLLQEALRSVKAEIGQA----IEEVNSNNQEL- 575
Cdd:pfam05557 232 ----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSPEDLSRRIEQLQQReivlKEENSSLTSSAr 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1732428643 576 -LRKYRREL-----QLRKKCHNELVRLKG----NIRVIARVRPVTKE 612
Cdd:pfam05557 308 qLEKARRELeqelaQYLKKIEDLNKKLKRhkalVRRLQRRVLLLTKE 354
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
356-584 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 356 NLEVQQKTD-RLAEVELRLKDclAEKAQE----------EERLSRRLRDSHETIASLRAQsppvkyvIKTVEVESSKTKQ 424
Cdd:COG3206 126 NLTVEPVKGsNVIEISYTSPD--PELAAAvanalaeaylEQNLELRREEARKALEFLEEQ-------LPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 425 ALSESQTRNQ--HLQEQVAMQRQVLKEMEQQLQnshqltvQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFA 502
Cdd:COG3206 197 ALEEFRQKNGlvDLSEEAKLLLQQLSELESQLA-------EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 503 RAQVEMKAvheNLAGVRTNLLTLQPALRTLTNDYNGLKRQvrgfpllLQEALRSVKAEIGQAIEEVNSNNQEL---LRKY 579
Cdd:COG3206 270 AQLAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREASLqaqLAQL 339
|
....*
gi 1732428643 580 RRELQ 584
Cdd:COG3206 340 EARLA 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
339-611 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 339 SQLQLEVAENKGMLSELNLEVQQKTDRLAEVE--------------LRLKDCLAEKAQEEERLSRRLRDS-------HET 397
Cdd:COG3206 57 ATLLVEPQSSDVLLSGLSSLSASDSPLETQIEilksrpvlervvdkLNLDEDPLGEEASREAAIERLRKNltvepvkGSN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 398 IASLRAQSP-PVK-----------YVIKTVEVESSKTKQA--------------LSESQT-----RNQH----LQEQVAM 442
Cdd:COG3206 137 VIEISYTSPdPELaaavanalaeaYLEQNLELRREEARKAlefleeqlpelrkeLEEAEAaleefRQKNglvdLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 443 QRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQS--LEEDKNRAIEEAFARAQV---------EMKAV 511
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELsarytpnhpDVIAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 512 HENLAGVRTNLLT-LQPALRTLTNDYNGLKRQVrgfplllqEALRSVKAEIGQAIEEVNSNNQELLRkYRRELQLRKKCH 590
Cdd:COG3206 297 RAQIAALRAQLQQeAQRILASLEAELEALQARE--------ASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELY 367
|
330 340 350
....*....|....*....|....*....|..
gi 1732428643 591 NELV-RLK----------GNIRVIARVRPVTK 611
Cdd:COG3206 368 ESLLqRLEearlaealtvGNVRVIDPAVVPLK 399
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
386-509 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 386 RLSRRLRDshETIASLRAQsppvkyvIKTVEVESSKTKQALSESQTRNQHL--QEQVAMQRQVLKEMEQQLQ-------- 455
Cdd:COG3524 169 QLSERARE--DAVRFAEEE-------VERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAeleaelaa 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732428643 456 -------NSHQLtVQLRAQIAMYEAELERAHGQMLEemQSLEEDKNRAIEEaFARAQVEMK 509
Cdd:COG3524 240 lrsylspNSPQV-RQLRRRIAALEKQIAAERARLTG--ASGGDSLASLLAE-YERLELERE 296
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
228-390 |
2.13e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 228 MSQLQEELVVLRERLAlhdsDRQATTTQLQNQVENLKEKLISQAQEVSRLRSELGGTDA--EKHRDRLM-VENEQLRQEL 304
Cdd:COG1579 19 LDRLEHRLKELPAELA----ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGnVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 305 RRcEVELQELRAqpvvpcegcehsqesSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEE 384
Cdd:COG1579 95 QK-EIESLKRRI---------------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*.
gi 1732428643 385 ERLSRR 390
Cdd:COG1579 159 EELEAE 164
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
258-519 |
2.39e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 258 NQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQLRqELRRcevELQELRAQpvVPcegcEHSQESSQLRDK 337
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEI-----EELKEKRDELNEELK-ELAE---KRDELNAQ--VK----ELREEAQELREK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 338 LSQLQLEVAENKGMLSELNLEVQQKTDRLAEVElRLKDCLAEKAQEEERLSR---RLRDSHET--------------IAS 400
Cdd:COG1340 66 RDELNEKVKELKEERDELNEKLNELREELDELR-KELAELNKAGGSIDKLRKeieRLEWRQQTevlspeeekelvekIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 401 LRAQsppvkyvIKTVEVESSKTKQaLSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHG 480
Cdd:COG1340 145 LEKE-------LEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 1732428643 481 QMLEEMQSLEEdknraIEEAFARAQVEMKAVHENLAGVR 519
Cdd:COG1340 217 EIVEAQEKADE-----LHEEIIELQKELRELRKELKKLR 250
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
390-597 |
2.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 390 RLRDSHETIASLRAQSPPVKYVIKT----VEVESSKTKQALSESQ--------TRNQHLQEQVAMQRQVLK-EMEQQLQN 456
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQnkydelveEAKTIKAEIEELTDELLNlVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 457 SH-----QLTVQLRAQIAMY--EAELERAHGQMLEEMQSLEEDKNR--AIEEAFARAQVEMKAVH---ENLAGVRTNLLT 524
Cdd:PHA02562 255 AAlnklnTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRitKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732428643 525 LQPALRTLTNDYNGLKRQVRGfpllLQEALRSVKAEIGQAIEEVNSNNQElLRKYRRELQLRKKCHNELVRLK 597
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLIT----LVDKAKKVKAAIEELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKEK 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
256-523 |
3.69e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 256 LQNQVENLKEKLISQAQEVSRLRsELGGTDAEKHRDRLmvenEQLRQELRrcevelqelraqpvvpcegcEHSQESSQLR 335
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQR-KKNGENIARKQNKY----DELVEEAK--------------------TIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 336 DKLSQLQLEVAENKGMLSELNLE---VQQKTDRLAEVELRLKD------CLAEKAQEEERLSRrLRDSHETIAslraqsp 406
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTAaakIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITK-IKDKLKELQ------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 407 pvkyviktvevessktkQALSESQTRNQHLQE---QVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQML 483
Cdd:PHA02562 313 -----------------HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1732428643 484 EEMQSLEEDKNRAIEEAFARAQVEMKAVHEnlaGVRTNLL 523
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHR---GIVTDLL 412
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
335-508 |
4.34e-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: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 335 RDKLSQLQLEVAENKGMLSELNLEVQQktdRLAEVELRLKDCLAEKAQEEERLSRR--------LRDSHETIASLRAqsp 406
Cdd:cd07596 34 RRELGSALGEFGKALIKLAKCEEEVGG---ELGEALSKLGKAAEELSSLSEAQANQelvkllepLKEYLRYCQAVKE--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 407 pvkyVIKT-----VEVESSKtkQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAqiamyeaELERAHGQ 481
Cdd:cd07596 108 ----TLDDradalLTLQSLK--KDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARK-------RYEEISER 174
|
170 180 190
....*....|....*....|....*....|
gi 1732428643 482 MLEEMQSLEEDKNRAIEEA---FARAQVEM 508
Cdd:cd07596 175 LKEELKRFHEERARDLKAAlkeFARLQVQY 204
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
225-597 |
4.35e-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: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 225 VEAMSQLQEELVVLRERLALHDSDRQATT------TQLQNQVENLKEKL--ISQAQEVSRLRSElggtDAEKHRDRLMVE 296
Cdd:pfam05622 27 QEEKNSLQQENKKLQERLDQLESGDDSGTpggkkyLLLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLELQHR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 297 NEQLR---QELRRCEVELQELRaqpvvpcegcehsqESSqlrDKLSQLQLEVAENKGMLSELN-LEVQQKTdrlaevelr 372
Cdd:pfam05622 103 NEELTslaEEAQALKDEMDILR--------------ESS---DKVKKLEATVETYKKKLEDLGdLRRQVKL--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 373 LKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSE---SQTRNQHLQ---EQVAMQRQV 446
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQkekERLIIERDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 447 LKEMEQQLQNSHQLTVQLRAQIAMYEAELErAHGQMLEEMQSLEedknraIEEAFARAQVEMKAVHENLAGvrtNLLTLQ 526
Cdd:pfam05622 237 LRETNEELRCAQLQQAELSQADALLSPSSD-PGDNLAAEIMPAE------IREKLIRLQHENKMLRLGQEG---SYRERL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732428643 527 PALRTLTNDYNGLKRQVRGFPLLLQEALRsvkaEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLK 597
Cdd:pfam05622 307 TELQQLLEDANRRKNELETQNRLANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-601 |
4.93e-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: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 232 QEELVVLR-ERLALHDSDRQATTTQLQNQ------VENLKEKLISQAQEVSRLRSELggTDAEKHRDRlmvENEQLRQEL 304
Cdd:pfam12128 438 EEYRLKSRlGELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSEL--RQARKRRDQ---ASEALRQAS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 305 RRCE---VELQELRAQPVVPCEGCEH--SQESSQLRDKLSQL-QLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLA 378
Cdd:pfam12128 513 RRLEerqSALDELELQLFPQAGTLLHflRKEAPDWEQSIGKViSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 379 -EKAQEEERLSRR-------LRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTR-----NQHLQEQVAMQRQ 445
Cdd:pfam12128 593 pEWAASEEELRERldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKA 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 446 V---LKEMEQQLQN-SHQLTVQLRAQIAMYEA---ELERAHGQMLEEMQSLEEDKNRA---IEEAFARAQVEMKA----- 510
Cdd:pfam12128 673 LaerKDSANERLNSlEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVVEGALDAQlalLKAAIAARRSGAKAelkal 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 511 ---VHENLAGV---RTNLLTLQPALRTLT---NDYNGLKRQVRGFPLLLQE-------ALRSVKAEIGQAIEEVNSNNQE 574
Cdd:pfam12128 753 etwYKRDLASLgvdPDVIAKLKREIRTLErkiERIAVRRQEVLRYFDWYQEtwlqrrpRLATQLSNIERAISELQQQLAR 832
|
410 420 430
....*....|....*....|....*....|.
gi 1732428643 575 LLRKYRRELQL----RKKCHNELVRLKGNIR 601
Cdd:pfam12128 833 LIADTKLRRAKlemeRKASEKQQVRLSENLR 863
|
|
| BAR_Bin3 |
cd07590 |
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ... |
432-516 |
5.73e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153274 Cd Length: 225 Bit Score: 39.27 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 432 RNQHLQEQVAMQRQV--LKEMEQQLQNSHQLTVQLRAqIAMYEAELERAHGQMLEEMQSLEEDKNRAIE---EAFARAQV 506
Cdd:cd07590 117 REQSLQEYERLQAKVekLAEKEKTGPNLAKLEQAEKA-LAAARADFEKQNIKLLEELPKFYNGRTDYFQpcfEALIKSQV 195
|
90
....*....|....
gi 1732428643 507 ----EMKAVHENLA 516
Cdd:cd07590 196 lyysQSTKIFTQLA 209
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
225-492 |
6.67e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.22 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 225 VEAMSqLQEELVVLRERLALHDSDRQATTTQLQNQVENLKE---KLISQAQEVSRLRSELGGTDaEKHRDRLMVEN---- 297
Cdd:PLN03229 479 VIAMG-LQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDefnKRLSRAPNYLSLKYKLDMLN-EFSRAKALSEKkska 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 298 EQLRQELRRcevELQELRAQPvvpcegcehsqessQLRDKLSQLQLEVAENK-GMLSELNLEVQQKTDRL-AEVELRLKD 375
Cdd:PLN03229 557 EKLKAEINK---KFKEVMDRP--------------EIKEKMEALKAEVASSGaSSGDELDDDLKEKVEKMkKEIELELAG 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 376 CLAEKAQEEERLSRRLRDSHETIAslraqSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEqvaMQRQVLKEMEQQLQ 455
Cdd:PLN03229 620 VLKSMGLEVIGVTKKNKDTAEQTP-----PPNLQEKIESLNEEINKKIERVIRSSDLKSKIEL---LKLEVAKASKTPDV 691
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1732428643 456 NSHQLTVQLRAQI------AMYEAELERAHGQMLEEMQSLEED 492
Cdd:PLN03229 692 TEKEKIEALEQQIkqkiaeALNSSELKEKFEELEAELAAARET 734
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
288-588 |
6.71e-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: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 288 KHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEgcehsqessqLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLA 367
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACE----------IRDQITSKEAQLESSREIVKSYENELDPLKNRLK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 368 EVE------LRLKD---CLAEKAQEEERLSRRLRDSHETIASLRAQSppvkyvIKTVEVESSKTKQALSESQTRNQHLQE 438
Cdd:TIGR00606 256 EIEhnlskiMKLDNeikALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 439 QVAMQRQVLKEMEQQLQNsHQLTVQLRA---QIAMYEAELERAHGQMLEEMQSLEEDK------NRAIEEAFARAQVEMK 509
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLV-EQGRLQLQAdrhQEHIRARDSLIQSLATRLELDGFERGPfserqiKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 510 AVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLL---QEALRSVKAEIGQAIEEVNS--NNQELLRKYRRELQ 584
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRilELDQELRKAERELS 488
|
....
gi 1732428643 585 LRKK 588
Cdd:TIGR00606 489 KAEK 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-535 |
6.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 334 LRDKLSQLQLEVAENKGMLSELNL-EVQQKTDRLAEVELRLKDcLAEKAQEEERLSRRLRDSHETIASLRAqsppvkyvi 412
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELRE--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 413 ktvEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqlTVQLRAQIAMYEAELERAHGQMLEEMQSLEED 492
Cdd:COG4717 117 ---ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732428643 493 KNRAIEEA---FARAQVEMKAVHENLAGVRTNLLTLQPALRTLTND 535
Cdd:COG4717 190 TEEELQDLaeeLEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
226-532 |
7.14e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 226 EAMSQLQEELVvLRERL-ALHdsdrqATTTQLQNQVENLKEKLISQAQEVSRLRSELggtdaEKHRDRLMVENEQL---- 300
Cdd:PRK10246 413 AALAQHAEQRP-LRQRLvALH-----GQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL-----NEMRQRYKEKTQQLadvk 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 301 ---RQELRRCEVELQELRAQPVVPCEGCEHSQESSqlrdkLSQLQ-LEVAENKGMLSELNLEVQQKTDRLAEVELRLkDC 376
Cdd:PRK10246 482 ticEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPA-----VEAYQaLEPGVNQSRLDALEKEVKKLGEEGAALRGQL-DA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 377 LAEKAQEEERLSRRLRDSHETIaslraqsppvkyviktvevesSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLqn 456
Cdd:PRK10246 556 LTKQLQRDESEAQSLRQEEQAL---------------------TQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-- 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 457 sHQLT--VQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNR----------------AIEEAFARAQvemkAVHENLAGV 518
Cdd:PRK10246 613 -RLLSqrHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSWQ----QRQNELTAL 687
|
330
....*....|....
gi 1732428643 519 RTNLLTLQPALRTL 532
Cdd:PRK10246 688 QNRIQQLTPLLETL 701
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
228-452 |
7.50e-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: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 228 MSQLQEELVVLRERLALHDSDRqattTQLQNQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQEL--- 304
Cdd:pfam15905 96 LQALEEELEKVEAKLNAAVREK----TSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLeak 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 305 -RRCEVELQELRAQPVVPCEGCEHSQES-SQLRDKLSQLQLEVAENK---GMLSELNLEVQQKTDRLAEVEL---RLKDC 376
Cdd:pfam15905 172 mKEVMAKQEGMEGKLQVTQKNLEHSKGKvAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVEKYKLdiaQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 377 LAEKAQEEERLSRRLRdshETIASLRAQSPPVKYVIKTVEVESSK-TKQALSESQTRN---QHLQEQVAMQRQVLKEMEQ 452
Cdd:pfam15905 252 LKEKNDEIESLKQSLE---EKEQELSKQIKDLNEKCKLLESEKEElLREYEEKEQTLNaelEELKEKLTLEEQEHQKLQQ 328
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
352-476 |
7.83e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 352 LSELNLEVQQKTDRLAEVELRlkdclaeKAQEEERLSRrLRDSHETIASLRAQsppvkyvIKTVEVESSktkQALSESQT 431
Cdd:PRK09039 55 LDRLNSQIAELADLLSLERQG-------NQDLQDSVAN-LRASLSAAEAERSR-------LQALLAELA---GAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1732428643 432 RNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE 476
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
271-392 |
8.90e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.44 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 271 AQEVSRLRSELGGTDAE-KHRDRLMVE-NEQLRQ---ELRRCEVELQELRAqpvvpcegcehsqESSQLRDKLSQLQLEV 345
Cdd:pfam06818 30 LNEIVALRAQLRELRAKlEEKEEQIQElEDSLRSktlELEVCENELQRKKN-------------EAELLREKVGKLEEEV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1732428643 346 AENKGMLSELNLEVQQKTDRLAEVELRLK--DCLAEKAQEEERLSRRLR 392
Cdd:pfam06818 97 SGLREALSDVSPSGYESVYESDEAKEQRQeeADLGSLRREVERLRAELR 145
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
412-491 |
8.96e-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: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 412 IKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQ---LRAQIAMYEAELERAHGQMLEEMQS 488
Cdd:pfam12718 23 VKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNnenLTRKIQLLEEELEESDKRLKETTEK 102
|
...
gi 1732428643 489 LEE 491
Cdd:pfam12718 103 LRE 105
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
218-344 |
9.51e-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: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 218 DPVVHRTVEAMSQLQEELVVLRErlaLHDSDRQATTTQLQnqveNLKEKLISQAQEVSRLRSELggTDAEKHRDRLMVEN 297
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQ---LEDELEDCDPTELD----RAKEKLKKLLQEIMIKVKKL--EELEEELQELESKI 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1732428643 298 EQLRQELRRCEVELQELRAQpVVPCEGCEHSqESSQLRDKLSQLQLE 344
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 ... |
335-507 |
9.71e-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: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 335 RDKLSQLQLEVAENKGMLSELNLE--VQQKTDRLAEVELRLKDCLAEKAQEEER-LSRRLRDSHETIASLRA---QSPPV 408
Cdd:pfam09325 54 RKELASATGEFAKSLASLASLELStgLSRALSQLAEVEERIKELLERQALQDVLtLGETIDEYLRLIGSVKAvfnQRVKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732428643 409 KYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNshqltvqlraqiamYEAELERAHGQMLEEMQS 488
Cdd:pfam09325 134 WQSWQNAEQELSKKKEQLEKLLRANKSQNDKLQQAKKEVEELERRVQQ--------------AEKEFEDISELIKKELER 199
|
170 180
....*....|....*....|..
gi 1732428643 489 LEEDKN---RAIEEAFARAQVE 507
Cdd:pfam09325 200 FELERVddfKNSVEIYLESAIE 221
|
|
| |
