|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
4-342 |
0e+00 |
|
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: 582.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 4 IPIKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 84 GQTGSGKTYTIGGGHVASVVEGQKGIIPRAIQEIFQSISENPS-IDFKIKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 162 EKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAENGEWYSHRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 755545674 322 SSDFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
9.65e-145 |
|
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: 443.94 E-value: 9.65e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 5 PIKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 78 ATVFAYGQTGSGKTYTIGGghvasvVEGQKGIIPRAIQEIFQSISEN-PSIDFKIKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 157 HIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEaaengewySHRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 755545674 317 CVSPSSSDFDESLNSLKYANRARNIRNKPALN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
2.28e-139 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 429.30 E-value: 2.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 11 RIRPLLCKEVLHNHQVCVRDIPNTQQIII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 84 GQTGSGKTYTIGGghvasvVEGQKGIIPRAIQEIFQSISENPS-IDFKIKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 162 EKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAENgewyshrHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEES-------VKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 755545674 321 SSSDFDESLNSLKYANRARNI 341
Cdd:pfam00225 306 SSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
5-339 |
6.66e-132 |
|
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: 409.34 E-value: 6.66e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 5 PIKVAVRIRPLlcKEVLHNHQVCVRDIPNTQQIIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPL--NGREARSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 78 ATVFAYGQTGSGKTYTIGGGHvasvvEGQKGIIPRAIQEIFQSISENPSID--FKIKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 156 LHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAengewyshRH 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE--------SV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 755545674 316 TCVSPSSSDFDESLNSLKYANRAR 339
Cdd:cd00106 303 ACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
6-341 |
3.54e-113 |
|
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: 358.57 E-value: 3.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEVLHNHQVCVRDIPNTqqiIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 83 YGQTGSGKTYTIGGGhvasvvEGQKGIIPRAIQEIFQSISENPSIDFKIKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 163 KGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVcqveknaEAAENGEWYSHRHIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-------ESSERGELEEGTVRVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 755545674 323 SDFDESLNSLKYANRARNI 341
Cdd:cd01374 303 SHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
6-343 |
6.60e-113 |
|
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: 358.06 E-value: 6.60e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVF 81
Cdd:cd01366 4 IRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 82 AYGQTGSGKTYTIGGghvasvVEGQKGIIPRAIQEIFQSISE--NPSIDFKIKVSYIEVYKEDLRDLL-ELETSMKDLHI 158
Cdd:cd01366 83 AYGQTGSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 159 RED-EKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVcqvekNAEAAENGEwyshrHIV 237
Cdd:cd01366 157 RHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-----SGRNLQTGE-----ISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 238 SKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITC 317
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 755545674 318 VSPSSSDFDESLNSLKYANRARNIRN 343
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
6-341 |
9.72e-113 |
|
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: 358.58 E-value: 9.72e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEVLHNHQVCVRDI----------------------PNTQQIIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhvasvvEGQKGIIPRAIQEIFQSISE-NPSIDFKIKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 143 LRDLleLETSMKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNA 222
Cdd:cd01370 156 IRDL--LNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 223 EAAENgewyshrHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 755545674 303 KDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRARNI 341
Cdd:cd01370 307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
6-341 |
3.68e-107 |
|
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: 342.90 E-value: 3.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 78 ATVFAYGQTGSGKTYTIGGghvASVVEGQKGIIPRAIQEIFQSISENPS-IDFKIKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 157 HIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVcqveKNAEAAENGEwyshRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 755545674 316 TCVSPSSSDFDESLNSLKYANRARNI 341
Cdd:cd01371 309 ANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
6-341 |
1.45e-101 |
|
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: 326.98 E-value: 1.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEVLHNHQVCVRdIPNTQQIIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 83 YGQTGSGKTYT-IGGGHvasvVEGQKGIIPRAIQEIFQSISENPS-IDFKIKVSYIEVYKEDLRDLleLETSMKDLHIRE 160
Cdd:cd01369 83 YGQTSSGKTYTmEGKLG----DPESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 161 DEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQveKNAEaaengewySHRHIVSKF 240
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENVE--------TEKKKSGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 241 HFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:cd01369 227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSP 304
|
330 340
....*....|....*....|.
gi 755545674 321 SSSDFDESLNSLKYANRARNI 341
Cdd:cd01369 305 SSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
6-348 |
2.89e-100 |
|
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: 325.08 E-value: 2.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEV---------LHNHQVCVRDIPNTQQIIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghvasvVEGQKGIIPRAIQEIFQSI--SENPSIDFKIKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNA 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 223 EAAENGEwyshrhIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 237 ETNLTTE------KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 755545674 298 ITRLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRARNIRNKPALN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-348 |
3.94e-97 |
|
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: 315.80 E-value: 3.94e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 78 ATVFAYGQTGSGKTYTIGGGHvaSVVEGQK-------GIIPRAIQEIFQSISENpSIDFKIKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 151 TS-MKDLHIRED--EKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAEN 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 228 GEwyshrhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 241 VK-------IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755545674 308 GSAKTVMITCVSPSSSDFDESLNSLKYANRARNIRNKPALN 348
Cdd:cd01364 311 GRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-337 |
6.96e-85 |
|
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: 280.72 E-value: 6.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 5 PIKVAVRIRPLLCKEVLHNhQVCVRDIPNTQQIII--GRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSL 72
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKK-EIDVVSVPSKLTLIVhePKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 73 IEGYNATVFAYGQTGSGKTYTIGGGHvaSVVEGQKGIIPRAIQEIFQSISENPSID-FKIKVSYIEVYKEDLRDLLElet 151
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 152 SMKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAeaaengewy 231
Cdd:cd01367 155 RKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNK--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 232 shrhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGS 309
Cdd:cd01367 226 ----LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGEN 298
|
330 340
....*....|....*....|....*...
gi 755545674 310 AKTVMITCVSPSSSDFDESLNSLKYANR 337
Cdd:cd01367 299 SKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
5-348 |
1.54e-84 |
|
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: 280.55 E-value: 1.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 5 PIKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 84 GQTGSGKTYTIgGGHVASVVE---GQKGIIPRAIQEIFQSI-----SENPSIDFKIKVSYIEVYKEDLRDLleLETSMKD 155
Cdd:cd01373 82 GQTGSGKTYTM-WGPSESDNEsphGLRGVIPRIFEYLFSLIqrekeKAGEGKSFLCKCSFLEIYNEQIYDL--LDPASRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 156 LHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAengewyshRH 235
Cdd:cd01373 159 LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFV--------NI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVM 314
Cdd:cd01373 231 RTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAI 310
|
330 340 350
....*....|....*....|....*....|....
gi 755545674 315 ITCVSPSSSDFDESLNSLKYANRARNIRNKPALN 348
Cdd:cd01373 311 IANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-373 |
2.98e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 287.41 E-value: 2.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhvasvvEGQKGIIPRAIQEIFQSISEN 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 125 PSI-DFKIKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 204 SSRSHAIFTISVCQVEKNaeaaengewySHRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKV----------SGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRARNIRNKPALNISPQADR-MDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330
....*....|.
gi 755545674 363 IKLLREALQSH 373
Cdd:COG5059 359 LSEDRSEIEIL 369
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
5-335 |
4.97e-83 |
|
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: 276.20 E-value: 4.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 5 PIKVAVRIRPLLCKEVLHNHQVCVRdIPNTQQI----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIE-VINSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhvasvvEGQKGIIPRAIQEIFQSISenpsiDFKIKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 149 LETS-----MKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQveknAE 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ----AP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 224 AAENGEWYSHRHI--VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKIT 299
Cdd:cd01368 226 GDSDGDVDQDKDQitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLT 305
|
330 340 350
....*....|....*....|....*....|....*.
gi 755545674 300 RLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYA 335
Cdd:cd01368 306 HLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
5-339 |
2.57e-80 |
|
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: 267.45 E-value: 2.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 5 PIKVAVRIRPLLCKEVLHNHQVCVRDIpNTQQIIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 79 TVFAYGQTGSGKTYTIGGghvasvVEGQKGIIPRAIQEIFQsISENPSIDFKIKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 159 REDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAeaaengewySHRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---------PFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 755545674 317 CVSPSSSDFDESLNSLKYANRAR 339
Cdd:cd01376 297 NIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
33-339 |
5.63e-74 |
|
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: 249.80 E-value: 5.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 33 NTQQiiigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHVASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 113 AIQEIFQSISENPSIDFKIKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQV 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 189 GNAARHTGTTQMNEHSSRSHAIFTISVcqveknaeAAENGEWYSHRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTIHL--------EAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545674 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-371 |
3.80e-60 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 227.51 E-value: 3.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLCKEvlhNHQVCVRDIPNTQQIIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 86 TGSGKTYTIGGGHVASVVEG----QKGIIPRAIQEIFQSISE------NPSIDFKIKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEeqikhaDRQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 156 LHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTisvCQVEKNAEAAENGewySHRH 235
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADG---LSSF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKTV 313
Cdd:PLN03188 327 KTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLA 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 755545674 314 MITCVSPSSSDFDESLNSLKYANRARNIRNKPALNispqadrmDEMEFEIKLLREALQ 371
Cdd:PLN03188 407 MVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN--------EVMQDDVNFLREVIR 456
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
8-280 |
2.40e-23 |
|
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: 98.19 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 8 VAVRIRPLLCKEVlhnhqvcvrdipNTQQIIIgrdrvfTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQT 86
Cdd:cd01363 1 VLVRVNPFKELPI------------YRDSKII------VFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 87 GSGKTYTIggghvasvvegqKGIIPRAIQEIFqsisenpsidfkikvSYIEVYKEDLRDLLEletsmkdlhiredekgnt 166
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 167 vivgakECQVESVEDVMSLLQVGNAARhTGTTQMNEHSSRSHAIFTIsvcqveknaeaaengewyshrhivskfhFVDLA 246
Cdd:cd01363 97 ------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIA 141
|
250 260 270
....*....|....*....|....*....|....
gi 755545674 247 GSERvtktgntgerfkesiqINSGLLALGNVISA 280
Cdd:cd01363 142 GFEI----------------INESLNTLMNVLRA 159
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
6-147 |
1.97e-22 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 94.59 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 6 IKVAVRIRPLLckevLHNHQVCVRDIPNTQQIIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPEL----LSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755545674 86 TGSGKTytiggghvasvvegqKGIIPRAIQEIFQSISEN-PSIDFKIKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSLkKGWKYTIELQFVEIYNESSQDLL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
763-1090 |
2.03e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 763 KLEHEAEQAKVELTETRKQLQELESK---DLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQdskklaslsiQNEKRAS 839
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVE----------QLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 840 ELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEgLNPKAEDQDGFNLNRRkspfrsgdqfq 919
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEE----------- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 920 kLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELS 999
Cdd:TIGR02168 819 -AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1000 EKSLQLEsspteekmKISEQVQALQRERDQLQRQRNSVDERLKHGRVlspKEEHLLFQL-------EEGIEALEAAIEFK 1072
Cdd:TIGR02168 898 ELSEELR--------ELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLseeysltLEEAEALENKIEDD 966
|
330
....*....|....*...
gi 755545674 1073 NESIQSRQNSLKASFQNL 1090
Cdd:TIGR02168 967 EEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
755-1042 |
2.71e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 755 RQYSLKVTKLEHEAEQAKVELTETRKQLQELESKDLSDVALKVKLQKEFrkkmDAAKMRVQVL-QKKQQDSKKLASLSIQ 833
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLeQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 834 NEKRASELEhnvdhlkyqkvQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAgqgeglnpKAEDQDGFNLNRrkspfR 913
Cdd:TIGR02168 318 LEELEAQLE-----------ELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELEAELEELES-----R 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 914 SGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLkkrEAIVSKKEALLQEKSLLEnkklrsSQALSTDGLKISARLNL 993
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELL------KKLEEAELKELQAELEE 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 755545674 994 LDQELSEKSLQLESSPTEEKmKISEQVQALQRERDQLQRQRNSVDERLK 1042
Cdd:TIGR02168 445 LEEELEELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLD 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
721-1278 |
1.83e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 721 KAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELESKdlsdvALKVKLQ 800
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-----AEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 801 KEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASelehnvDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKI 880
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA------DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 881 KELQLKAgqgeglnpKAEDQDgfnlnrrkspfRSGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKE 960
Cdd:PTZ00121 1392 KADEAKK--------KAEEDK-----------KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 961 AllQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSlqlessptEEKMKISEQVQALQRERDQLQRQRNSvdER 1040
Cdd:PTZ00121 1453 A--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA--------EEAKKKADEAKKAAEAKKKADEAKKA--EE 1520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1041 LKHGRVLSPKEEhllfqlEEGIEALEAAIEFKNESIQSRQNSLKASFQNLSQSEANVLEKlvclniteirailfkyfNKV 1120
Cdd:PTZ00121 1521 AKKADEAKKAEE------AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE-----------------DKN 1577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1121 INLRETERKQQLQNK--EMKMKVLERdnvvhELESALEHLRLQCDRRLTLQQ--KEHEQKMQLLLQHFKDQDGDSIIETL 1196
Cdd:PTZ00121 1578 MALRKAEEAKKAEEAriEEVMKLYEE-----EKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1197 KNYED----KIQQLEKDLYFYKKTSRDLKKRLKDPAQGAAQWQRTLTEHHDAGDGVLNPEETTVLSEELKWASRTENTKL 1272
Cdd:PTZ00121 1653 KKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
....*.
gi 755545674 1273 NGSERE 1278
Cdd:PTZ00121 1733 EEAKKE 1738
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
697-1108 |
1.27e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 697 KMESLQESQEINLQKLRTSeliLNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELT 776
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 777 ETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQ 856
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 857 RRLREEGEKKKQLDAEIKRDQQKIKELQlkagqgeglnpkaedqdgfnlnrrkspfrsgDQFQKLDEQRKWLDEEVEkvl 936
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELE-------------------------------SELEALLNERASLEEALA--- 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 937 SQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKI 1016
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1017 SEQVQALQRERDQLQR-------QRNSVDERLKHgrVLSPKEEhllfqLEEGIEALEAAIEFKNESIQSRqnsLKASFQN 1089
Cdd:TIGR02168 971 RRRLKRLENKIKELGPvnlaaieEYEELKERYDF--LTAQKED-----LTEAKETLEEAIEEIDREARER---FKDTFDQ 1040
|
410 420
....*....|....*....|....
gi 755545674 1090 LSQSEANVLEKLVC-----LNITE 1108
Cdd:TIGR02168 1041 VNENFQRVFPKLFGggeaeLRLTD 1064
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
731-1226 |
8.67e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 731 INIRMKEdlIKELIKTGNNAKSVSRQYsLKVTKLEHEAEQAKVELTETRKQLQELEsKDLSDVALKVKLQKEFRKKMDAA 810
Cdd:PRK03918 130 IYIRQGE--IDAILESDESREKVVRQI-LGLDDYENAYKNLGEVIKEIKRRIERLE-KFIKRTENIEELIKEKEKELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 811 KMRVQVLQKKQQD-SKKLASLSiQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQ 889
Cdd:PRK03918 206 LREINEISSELPElREELEKLE-KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 890 GEGLNPKAEDQDgfNLNRRKSPFRsgDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKreaIVSKKEALLQEKSLL 969
Cdd:PRK03918 285 LKELKEKAEEYI--KLSEFYEEYL--DELREIEKRLSRLEEEINGIEERIKELEEKEERLEE---LKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 970 EN--KKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVL 1047
Cdd:PRK03918 358 EErhELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1048 SP------KEEHLLFQLEEGIEALEaAIEFKNESIQSRQNSLKASFQNL-----SQSEANVLEKLVclniTEIRAILFKY 1116
Cdd:PRK03918 438 CPvcgrelTEEHRKELLEEYTAELK-RIEKELKEIEEKERKLRKELRELekvlkKESELIKLKELA----EQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1117 fnKVINLRETERKQQLQNKeMKMKVLERDNVVHELESALEHLRLQCDRRLTLQQKEHEQKMQllLQHFKDQDGDSIIETL 1196
Cdd:PRK03918 513 --KKYNLEELEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE--LAELLKELEELGFESV 587
|
490 500 510
....*....|....*....|....*....|..
gi 755545674 1197 KNYEDKIQQLEKdlyFYKK--TSRDLKKRLKD 1226
Cdd:PRK03918 588 EELEERLKELEP---FYNEylELKDAEKELER 616
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
812-1226 |
1.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 812 MRVQVLQKKQQD-SKKLASLSIQNEKRASELEHNVDHLKYQkvqlQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQg 890
Cdd:COG4717 46 MLLERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEK- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 891 eglnpkaedqdgfnLNRRKSPFRSGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREA-IVSKKEALLQEKSLL 969
Cdd:COG4717 121 --------------LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAeLAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 970 ENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESspTEEKMKISEQVQALQRERDQLQRQRNS--------VDERL 1041
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLlliaaallALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1042 KHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESI---QSRQNSLKASFQNLSQSEANVLEKLVCLNITEIRAILFKYFN 1118
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASlgkEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1119 KVINLRETERKQQLQNKEMKMKVL--ERDNVVHEL----ESALEHLRLQCDRRLTLQQKEHEQKMQL------LLQHFKD 1186
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELeqEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLeellgeLEELLEA 424
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 755545674 1187 QDGDSIIETLKNYEDKIQQLEKDLYFYKKTSRDLKKRLKD 1226
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
779-1161 |
1.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 779 RKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQK------ 852
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 853 ---VQLQRRLREEGEKKKQLDAEIKRDQQKIKEL-QLKAGQGEGLNPKAEDQDGFNLNRRKSPFRSGDQFQKLDEQRKWL 928
Cdd:COG4717 132 qelEALEAELAELPERLEELEERLEELRELEEELeELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 929 DEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLL--------------------------------------- 969
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllallfl 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 970 -ENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQrERDQLQRQRNSVDERLKHGRVLS 1048
Cdd:COG4717 292 lLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1049 PKEEHLLFQLEEGIEALEAAIEFKNE--SIQSRQNSLKasfQNLSQSEANVLEKLVCLNITEIRAILFKYFNKVINLRE- 1125
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELE---EQLEELLGELEELLEALDEEELEEELEELEEELEELEEe 447
|
410 420 430
....*....|....*....|....*....|....*..
gi 755545674 1126 -TERKQQLQNKEMKMKVLERDNVVHELESALEHLRLQ 1161
Cdd:COG4717 448 lEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1184 |
1.82e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 839 SELEHNVDHL--------KYQKVQLQRRLREEGE---KKKQLDAEIKRDQQKIKELQLKAgqgeglnpkaedqdgfnlnr 907
Cdd:COG1196 196 GELERQLEPLerqaekaeRYRELKEELKELEAELlllKLRELEAELEELEAELEELEAEL-------------------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 908 rkspfrsgdqfQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLrssQALSTDGLKI 987
Cdd:COG1196 256 -----------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR---RELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 988 SARLNLLDQELSEKSLQLESSpTEEKMKISEQVQALQRERDQLQRQRNSVDERLKhgrvlspKEEHLLFQLEEGIEALEA 1067
Cdd:COG1196 322 EEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELA-------EAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1068 AIEFKNESIQSRQNSLKASFQNLSQSEANVLEKLvcLNITEIRAILFKYFNKVINLRETERKQQLQNKEMKMKVLERDNV 1147
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330 340 350
....*....|....*....|....*....|....*..
gi 755545674 1148 VHELESALEHLRLQCDRRltLQQKEHEQKMQLLLQHF 1184
Cdd:COG1196 472 AALLEAALAELLEELAEA--AARLLLLLEAEADYEGF 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
697-1078 |
1.95e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 697 KMESLQESQEI-NLQKLRTSELILNKAKQKMRELTiniRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVEl 775
Cdd:PTZ00121 1553 KAEELKKAEEKkKAEEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA- 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 776 TETRKQLQELESKDlsdvALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKklaslsiqneKRASELEhnvdhlkyqkvql 855
Cdd:PTZ00121 1629 EEEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDK----------KKAEEAK------------- 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 856 qrrlREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQDGFNLNRRKSpfrsgDQFQKLDEQRKWLDEEVEKV 935
Cdd:PTZ00121 1682 ----KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-----EEAKKEAEEDKKKAEEAKKD 1752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 936 LSQRQELEML-EEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARL----NLLDQELSEKSLQLESSPT 1010
Cdd:PTZ00121 1753 EEEKKKIAHLkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiiegGKEGNLVINDSKEMEDSAI 1832
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755545674 1011 EEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESIQS 1078
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
696-1207 |
2.23e-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: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 696 LKMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHE-------A 768
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 769 EQAKVELTETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQdsKKLASLSIQNEKRASELEHNVDHL 848
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--ALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 849 KYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQdgfnlnrrkspfrsgdqfQKLDEQRKWL 928
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------------------EALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 929 DEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESS 1008
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1009 PTEEKMK-----ISEQVQALQRERDQLQRQRNSVDERLKHGRV-------LSPKEEHLLFQLEEGIEALEAAIEFKNESI 1076
Cdd:COG1196 532 VEAAYEAaleaaLAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpldkIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1077 QSRQNSLKASFQNLSQSEANVLEKLVCLNITEIRAILFKYFNKVINLR------ETERKQQLQNKEMKMKVLERDNVVHE 1150
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGgsltggSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 755545674 1151 LESALEHLRLQCDRRLTLQQKEHEQKMQLLLQHFKDQDGDSIIETLKNYEDKIQQLE 1207
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
761-1092 |
2.28e-07 |
|
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: 55.84 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 761 VTKLEHEAEQAKVELTETRKQLQELESKdLSDVALKV-KLQKEFRKKMdaakmRVQVLQKKQQD--------SKKLASLS 831
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLI-IDEKRQQLeRLRREREKAE-----RYQALLKEKREyegyellkEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 832 IQN-EKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKR-DQQKIKELQLKAGQGEGLNPKAEDQDGFNLnrrk 909
Cdd:TIGR02169 239 KEAiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKE---- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 910 spfrsgDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKReaivskKEALLQEkslLENKKlrssqalstdglkisA 989
Cdd:TIGR02169 315 ------RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEE---YAELK---------------E 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 990 RLNLLDQELSEKSLQLESSpTEEKMKISEQVQALQRERDQLQRQRNSVDERLKhgrvlspKEEHLLFQLEEGIEALEAAI 1069
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAET-RDELKDYREKLEKLKREINELKRELDRLQEELQ-------RLSEELADLNAAIAGIEAKI 436
|
330 340
....*....|....*....|...
gi 755545674 1070 EFKNESIQSRQNSLKASFQNLSQ 1092
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQ 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
697-1090 |
3.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 697 KMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELT 776
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 777 ETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQK---- 852
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLllll 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 853 -VQLQRRLREEGEKKKQLDAEIKRDQQKIKEL--------------------------------------QLKAGQGEGL 893
Cdd:COG1196 498 eAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigveaayeaaleaalaaalqnivveddevaaaaieylkAAKAGRATFL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 894 nPKAEDQDGFNLNRRKSPFRSGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSL---LE 970
Cdd:COG1196 578 -PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeGG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 971 NKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKhgRVLSPK 1050
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE--QLEAER 734
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 755545674 1051 EEHLLFQLEEGIEALEAAIEFKN-----ESIQSRQNSLKASFQNL 1090
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPeppdlEELERELERLEREIEAL 779
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
643-982 |
6.76e-07 |
|
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: 53.97 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 643 SDNSDDEDSEGQEKPRVRSRSHSWAKKpgsvcslVELSDTQAESQRSYLGNGDLKMESLQESQEINLQKLRTSELIlnKA 722
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKARE-------VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 723 KQKMRELtinirmkedlikELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVEltetrkqlQELESkdlsdvALKVKLQKE 802
Cdd:pfam17380 356 EERKREL------------ERIRQEEIAMEISRMRELERLQMERQQKNERVR--------QELEA------ARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 803 FRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELE----------HNVDHLKYQKVQlQRRLREEGEKKKQLDAE 872
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMErvrleeqerqQQVERLRQQEEE-RKRKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 873 IKRDQQKIKELQLKAGQGEGLNPKaedqdgfnlNRRKSPFRSGDQFQK--LDEQRKWLDEEVEKVLSQRQELEMLEEDLK 950
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEE---------RKRKLLEKEMEERQKaiYEEERRREAEEERRKQQEMEERRRIQEQMR 559
|
330 340 350
....*....|....*....|....*....|....*.
gi 755545674 951 KREAIVSKKEALLQEKSLL----ENKKLRSSQALST 982
Cdd:pfam17380 560 KATEERSRLEAMEREREMMrqivESEKARAEYEATT 595
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
775-1101 |
1.03e-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: 53.52 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 775 LTETRKQLQELESKdlsdvALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLAslsIQNEKRASELEHNvdhlkyqkvQ 854
Cdd:TIGR02168 195 LNELERQLKSLERQ-----AEKAERYKELKAELRELELALLVLRLEELREELEE---LQEELKEAEEELE---------E 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 855 LQRRLREEGEKKKQLDAEIKRDQQKIKELQlkagqGEGLNPKAEDQDgfnLNRRKspfrsgdqfQKLDEQRKWLDEEVEK 934
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQ-----KELYALANEISR---LEQQK---------QILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 935 VLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLEssptEEKM 1014
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE----LQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1015 KISEQVQALqreRDQLQ----RQRNSVDERLKHGRVLSPKE-----------EHLLFQLEEGIEALEAAIEFKNESIQSR 1079
Cdd:TIGR02168 397 SLNNEIERL---EARLErledRRERLQQEIEELLKKLEEAElkelqaeleelEEELEELQEELERLEEALEELREELEEA 473
|
330 340
....*....|....*....|....
gi 755545674 1080 QNSLKASFQNLSQ--SEANVLEKL 1101
Cdd:TIGR02168 474 EQALDAAERELAQlqARLDSLERL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
830-1101 |
1.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 830 LSIQNEKRASELE---HNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQ-GEGLNPKAEDQdgFNL 905
Cdd:COG1196 216 RELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElELELEEAQAEE--YEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 906 NRRKSPFRSGDQFQKLDEQRkwLDEEVEKVLSQRQELE-MLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDG 984
Cdd:COG1196 294 LAELARLEQDIARLEERRRE--LEERLEELEEELAELEeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 985 LKISARLNLLDQELSEKsLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIEA 1064
Cdd:COG1196 372 AELAEAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270
....*....|....*....|....*....|....*..
gi 755545674 1065 LEAAIEfKNESIQSRQNSLKASFQNLSQSEANVLEKL 1101
Cdd:COG1196 451 EAELEE-EEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
732-1226 |
2.03e-06 |
|
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: 52.33 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 732 NIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELESKDLSDVALKVKLQKEF---RKKMD 808
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkiKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 809 AAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAG 888
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 889 QGEGLNPKAEDQdgfnLNRRKSpfrsgdQFQKLDEQRK--WLDEEVEKVLSQRQELEMLEEDLKKREAIVSKK----EAL 962
Cdd:TIGR04523 278 QNNKKIKELEKQ----LNQLKS------EISDLNNQKEqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLneqiSQL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 963 LQEKSLLENKKLRSSQALSTDGLKISaRLNLLDQELSEKSLQLESSPTEEKMKISEQ---VQALQRERDQLQRQRNSVDE 1039
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLESKIQNQeklNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1040 RLKHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESIQSRQNSLKAsFQNLSQSEANVLEKLVcLNITEIRAILFKYFNK 1119
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV-LSRSINKIKQNLEQKQ-KELKSKEKELKKLNEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1120 VINLRE-----TERKQQLQNKEMKM--KVLERDNVVHELESALEHLRLQCDRRLTLQQKEHEQKMQLLLQHFKD---QDG 1189
Cdd:TIGR04523 505 KKELEEkvkdlTKKISSLKEKIEKLesEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKslkKKQ 584
|
490 500 510
....*....|....*....|....*....|....*..
gi 755545674 1190 DSIIETLKNYEDKIQQLEKDLYFYKKTSRDLKKRLKD 1226
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
715-1063 |
2.80e-06 |
|
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: 51.82 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 715 SELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELESKDLSDVA 794
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 795 LKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLAslsiqneKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIk 874
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLT-------QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 875 rdQQKIKELQLKAGQGEGLNPKAEDQDGFNLNRRKSPFRSGdqfQKLDE-QRKWLDEEV---------EKVLSQRQELEM 944
Cdd:pfam07888 181 --QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT---QKLTTaHRKEAENEAlleelrslqERLNASERKVEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 945 LEEDLKKREAIVSKKEALLQEKSL-------------LENKKLRSSQALSTDGLKISARLNLLD-QELSEKSLQLESSPT 1010
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELHQARLqaaqltlqladasLALREGRARWAQERETLQQSAEADKDRiEKLSAELQRLEERLQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 755545674 1011 EEKMKISEQVQALQRERD----QLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIE 1063
Cdd:pfam07888 336 EERMEREKLEVELGREKDcnrvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
697-1222 |
2.98e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 697 KMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSR--------------------Q 756
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelkekaeeyiklsefyeE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 757 YSLKVTKLEHEAEQAKVELTETRKQLQELESKDLSDVALKvKLQKEFRKKMDAAKMRVQVLQK-------KQQDSKKLAS 829
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK-KKLKELEKRLEELEERHELYEEakakkeeLERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 830 LSIQnekrasELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQlKAgqgeglnpkaedqdgfnlnRRK 909
Cdd:PRK03918 384 LTPE------KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK-KA-------------------KGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 910 SPF--RSGDQFQKLDEQRKWLdEEVEKVLSQRQELEMLEEDLKKREAIVSKKeaLLQEKSLLENKKLrssqalsTDGLK- 986
Cdd:PRK03918 438 CPVcgRELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKELRELEKV--LKKESELIKLKEL-------AEQLKe 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 987 ISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEE----GI 1062
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfeSV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1063 EALEAAIEfKNESIQSRQNSLKASFQNLsQSEANVLEKLVcLNITEIRAILFKYFNKVINLR-ETERKQQLQNKEMKMKV 1141
Cdd:PRK03918 588 EELEERLK-ELEPFYNEYLELKDAEKEL-EREEKELKKLE-EELDKAFEELAETEKRLEELRkELEELEKKYSEEEYEEL 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1142 LERdnvVHELESALEHLRLQCDrrltlQQKEHEQKMQLLLQHFKDQdgdsiIETLKNYEDKIQQLEKDLYFYKKTSRDLK 1221
Cdd:PRK03918 665 REE---YLELSRELAGLRAELE-----ELEKRREEIKKTLEKLKEE-----LEEREKAKKELEKLEKALERVEELREKVK 731
|
.
gi 755545674 1222 K 1222
Cdd:PRK03918 732 K 732
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
697-1228 |
4.06e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 697 KMESLQESQEINLQ-KLRTSELILNKAKQKMRELTINIRMKE--DLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKV 773
Cdd:COG5022 770 RIKKIQVIQHGFRLrRLVDYELKWRLFIKLQPLLSLLGSRKEyrSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQ 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 774 ELTETRKQLQELESKDLSDVALKVKlqkefrKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELehnvdhlkyqKV 853
Cdd:COG5022 850 KFGRSLKAKKRFSLLKKETIYLQSA------QRVELAERQLQELKIDVKSISSLKLVNLELESEIIEL----------KK 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 854 QLQRRLREEGEKKKQLDAEIKRdqqkikelqlkagqgegLNPKAEDQDGFNLNRRKSPfrsgdQFQKLDEQRKWLDEEVE 933
Cdd:COG5022 914 SLSSDLIENLEFKTELIARLKK-----------------LLNNIDLEEGPSIEYVKLP-----ELNKLHEVESKLKETSE 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 934 KVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSllenkKLRSSQALSTDGLKISARLNlldQELSEKSLQLESSPTEEK 1013
Cdd:COG5022 972 EYEDLLKKSTILVREGNKANSELKNFKKELAELS-----KQYGALQESTKQLKELPVEV---AELQSASKIISSESTELS 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1014 --MKISEQVQALQRERDQLQRQrnsvDERLKHGRVLSPKEEHLLFQLEEgIEALEAAIEFKNESIQSRQNSLKASFqnls 1091
Cdd:COG5022 1044 ilKPLQKLKGLLLLENNQLQAR----YKALKLRRENSLLDDKQLYQLES-TENLLKTINVKDLEVTNRNLVKPANV---- 1114
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1092 qSEANVLEKLVCLNITEIRAILfkyfNKVINLreterkqqLQNKEMKMKVLERDNVVHELESALEHLrLQCDRRLTLQQK 1171
Cdd:COG5022 1115 -LQFIVAQMIKLNLLQEISKFL----SQLVNT--------LEPVFQKLSVLQLELDGLFWEANLEAL-PSPPPFAALSEK 1180
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 755545674 1172 EheqKMQLLLQHFKDQDGDSIIETLKNYEDKIQQLEKDLYFYKKTSRDLKKRLKDPA 1228
Cdd:COG5022 1181 R---LYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPT 1234
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
719-1225 |
5.52e-06 |
|
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: 50.88 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 719 LNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKvTKLEHEAEQakvELTETRKQLqeleSKDLSDVALKVK 798
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEK-TKLQDENLK---ELIEKKDHL----TKELEDIKMSLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 799 LQKEFRKKMD-----AAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEI 873
Cdd:pfam05483 307 RSMSTQKALEedlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 874 KRDQQKIKEL-QLKAGQGEGLNP----KAEDQDGFNLNRrkspfrsgdQFQKLDEQRKWLDEEVEKVLSQRQ-ELEMLEE 947
Cdd:pfam05483 387 QKKSSELEEMtKFKNNKEVELEElkkiLAEDEKLLDEKK---------QFEKIAEELKGKEQELIFLLQAREkEIHDLEI 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 948 DLKkreAIVSKKEALLQE----KSLLENKKLRSSQaLSTDGLKISARLNLLDQELSEKSLQLESSPTE------EKMKIS 1017
Cdd:pfam05483 458 QLT---AIKTSEEHYLKEvedlKTELEKEKLKNIE-LTAHCDKLLLENKELTQEASDMTLELKKHQEDiinckkQEERML 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1018 EQVQALQRERDQLQRQRNSVDERLKHGR-----VLSPKEEHllfqlEEGIEALEAAIEFKNESIQSRQNSLKASFQNLS- 1091
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFIQKGdevkcKLDKSEEN-----ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNk 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1092 -----QSEANVLEKLVCLNITEIRAILFKYFNKVINLRETERK-QQLQN---KEMKMKVLERDNVVHELESAL----EHL 1158
Cdd:pfam05483 609 nieelHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfEEIIDnyqKEIEDKKISEEKLLEEVEKAKaiadEAV 688
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755545674 1159 RLQCDRRLTLQQKEHEqkMQLLLQHFKDQdGDSIIE----TLKNYEDKIQQ-------LEKDLYFYKKTSRDLKKRLK 1225
Cdd:pfam05483 689 KLQKEIDKRCQHKIAE--MVALMEKHKHQ-YDKIIEerdsELGLYKNKEQEqssakaaLEIELSNIKAELLSLKKQLE 763
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
716-1179 |
6.28e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 716 ELILNKAKQKMRELTINIRMKEDliKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELT----------ETRKQLQEL 785
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDeadevleeheERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 786 ESkDLSDvaLKVKLQKEFRKKmDAAKMRVQVLQKKqqdskkLASLSIQNEKRASE----------LEHNVDHLKYQKVQL 855
Cdd:PRK02224 257 EA-EIED--LRETIAETERER-EELAEEVRDLRER------LEELEEERDDLLAEaglddadaeaVEARREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 856 QRRLREEGEKKKQLDAEIKRDQQKIKELQLKAgqgEGLNPKAEDQDGFNLNRRKSPFRSGDQFQKLDEQRKWLDEEVEKV 935
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERA---EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 936 LSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGlkisarlnlldqELSEKSLQLESSP----TE 1011
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAG------------KCPECGQPVEGSPhvetIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1012 EKmkiSEQVQALQRERDQLQRQRNSVDERLKHGRVLSpKEEHLLFQLEEGIEALEAAIEFKNESIQSRQNSLKASFQNLS 1091
Cdd:PRK02224 472 ED---RERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1092 QSEANVLEKLVCLNITEIRAILFKYFNKVINLRETERKQQLQNKEmkmKVLERDNVVHELESALEHLRlqcDRRLTLQQK 1171
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE---RIRTLLAAIADAEDEIERLR---EKREALAEL 621
|
....*...
gi 755545674 1172 EHEQKMQL 1179
Cdd:PRK02224 622 NDERRERL 629
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
706-1070 |
1.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 706 EINLQKLRTSELILNKAKQKMRELTINIRMKEDL---IKELIKTGNNAKSVSRQYS--LKVTKLEHEAEQAKVELTETRK 780
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 781 QLQELESKdlsdvalkvklQKEFRKKMDAAKMRVQVLQKKQQD-SKKLASLSIQNEKRASELEHNVDHLKYQKVQLQRRL 859
Cdd:COG4717 147 RLEELEER-----------LEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 860 REEGEKKKQLDAEIKR---------DQQKIKELQLK----------AGQGEGLNPKAEDQDG--------------FNLN 906
Cdd:COG4717 216 EEAQEELEELEEELEQleneleaaaLEERLKEARLLlliaaallalLGLGGSLLSLILTIAGvlflvlgllallflLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 907 RRKSPFRSGDQFQKLDEQRKWLDEEVEKVLSQ-------------------------RQELEMLEEDLkKREAIVSKKEA 961
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeellelldrieelqelLREAEELEEEL-QLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 962 LLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEK---SLQLESSPTEEKMK-----ISEQVQALQRERDQLQRQ 1033
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEeeleeLEEELEELEEELEELREE 454
|
410 420 430
....*....|....*....|....*....|....*..
gi 755545674 1034 RNSVDERLKHgrvlsPKEEHLLFQLEEGIEALEAAIE 1070
Cdd:COG4717 455 LAELEAELEQ-----LEEDGELAELLQELEELKAELR 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1060 |
1.74e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 685 ESQRSYLGNGDLKMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDlIKELIKTGNNAKSVSRQYSLKVTKL 764
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 765 EHEAEQAKVELTETRKQLQELESKDLSDVALKvKLQKEFRKKMDAAKMRVQVLQK-------KQQDSKKLASLSIQN--- 834
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELK-KKLKELEKRLEELEERHELYEEakakkeeLERLKKRLTGLTPEKlek 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 835 -----EKRASELEHNVDHLKYQKVQLQRRLRE--------------------------EGEKKKQLDAEIKRDQQKIKEL 883
Cdd:PRK03918 392 eleelEKAKEEIEEEISKITARIGELKKEIKElkkaieelkkakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEI 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 884 QLKagQGEGLNPKAEDQDGFNLNRRKSPFRS-GDQFQKLDEQRKWLD--------EEVEKVLSQ----RQELEMLEEDLK 950
Cdd:PRK03918 472 EEK--ERKLRKELRELEKVLKKESELIKLKElAEQLKELEEKLKKYNleelekkaEEYEKLKEKliklKGEIKSLKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 951 KREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISarlnlldQELSEKSLQLESsPTEEKMKISEQVQALQRERDQL 1030
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESV-------EELEERLKELEP-FYNEYLELKDAEKELEREEKEL 621
|
410 420 430
....*....|....*....|....*....|
gi 755545674 1031 QRQRNSVDERLKHGRVLSPKEEHLLFQLEE 1060
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
719-1077 |
2.09e-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: 49.30 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 719 LNKAKQKMRELTINIRMKEDLIKELIKTGNNA----KSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELEsKDLSDva 794
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLE-EELEK-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 795 LKVKLQkEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQneKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIK 874
Cdd:TIGR02169 256 LTEEIS-ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 875 RDQQKIKELQLKAGQGEGLNPKAEDQdgfnLNRRKSPFRsgDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEdlkKREA 954
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEE----YAELKEELE--DLRAELEEVDKEFAETRDELKDYREKLEKLKR---EINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 955 IVSKKEALLQEKSLLENKKLRSSQALStdglKISARLNLLDQELSEKSLQLESSpTEEKMKISEQVQALQRERDQLQRQR 1034
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIA----GIEAKINELEEEKEDKALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 755545674 1035 NSVDERLKHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESIQ 1077
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-893 |
2.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 697 KMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELT 776
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 777 ETRKQLQE-----------------LESKDLSDVALKVKLQKEFrkkmdaAKMRVQVLQKKQQDSKKLASLSIQNEKRAS 839
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755545674 840 ELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGL 893
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
716-1247 |
2.93e-05 |
|
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: 48.96 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 716 ELILNKAKQKMRELtinIRMKEDLIKELIKTGNNAKSvsrQYSLKVTKLEHEAEQAKVELTETRKQLQELESKdlsdval 795
Cdd:pfam15921 259 ELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQNSMYMRQLSDLEST------- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 796 kvklqkefrkkmdAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHnvdhlkyQKVQLQRRLREEGEKKKQLDAEIKR 875
Cdd:pfam15921 326 -------------VSQLRSELREAKRMYEDKIEELEKQLVLANSELTE-------ARTERDQFSQESGNLDDQLQKLLAD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 876 DQQKIKELQLKAGQgeglNPKAEDQDgfnlnrrkspfrSGDQFqKLDEQRKWLDEEVEKVlsqrQELEMLEEDLKKR-EA 954
Cdd:pfam15921 386 LHKREKELSLEKEQ----NKRLWDRD------------TGNSI-TIDHLRRELDDRNMEV----QRLEALLKAMKSEcQG 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 955 IVSKKEALLQEKslleNKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSP---TEEKMKISEQVQALQRERDQLQ 1031
Cdd:pfam15921 445 QMERQMAAIQGK----NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSErtvSDLTASLQEKERAIEATNAEIT 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1032 RQRNSVDERLKHGRVLSPKEEHLLfQLEEGIEALEAAIEFKNESIQsrqnSLKASFQNLSQseanvlekLVCLNITEIRA 1111
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIE----ILRQQIENMTQ--------LVGQHGRTAGA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1112 ILFK--YFNKVINLReterkqQLQNKEMKMKVLERDNVVHELESALEHLRLQcdrRLTLQQKEHEQkmqllLQHFKD--Q 1187
Cdd:pfam15921 588 MQVEkaQLEKEINDR------RLELQEFKILKDKKDAKIRELEARVSDLELE---KVKLVNAGSER-----LRAVKDikQ 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545674 1188 DGDSIIETLKNYEDKIQQLEKDLYFYKK-----------TSRDLKKRLKDpAQGAAQWQRTLTEHHDAGDG 1247
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnkseemetTTNKLKMQLKS-AQSELEQTRNTLKSMEGSDG 723
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
699-1070 |
3.08e-05 |
|
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: 48.58 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 699 ESLQESQEINLQKLRTSELILNKAKQKMReltinirmKEDLIKELIKTGNNaksvsrqyslKVTKLEHEAEQAKVELTET 778
Cdd:pfam05557 69 EALREQAELNRLKKKYLEALNKKLNEKES--------QLADAREVISCLKN----------ELSELRRQIQRAELELQST 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 779 RKQLQELEskdlsdvalkvKLQKEFRKKMDAAKMRVQVLQKKQQDSK----KLASLSIQNEK----------------RA 838
Cdd:pfam05557 131 NSELEELQ-----------ERLDLLKAKASEAEQLRQNLEKQQSSLAeaeqRIKELEFEIQSqeqdseivknskselaRI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 839 SELEHNVDHLKY-----------------QKVQLQRRL-REEGEKKKQLDAEIKRD--QQKIKELQlKAGQGEGLN-PKA 897
Cdd:pfam05557 200 PELEKELERLREhnkhlnenienklllkeEVEDLKRKLeREEKYREEAATLELEKEklEQELQSWV-KLAQDTGLNlRSP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 898 ED---------QDGFNLNRRKSPFRSgdQFQKLDEQRKWLDEEVEKVLSQRQELEM-------LEEDLKKREAIVSKKEA 961
Cdd:pfam05557 279 EDlsrrieqlqQREIVLKEENSSLTS--SARQLEKARRELEQELAQYLKKIEDLNKklkrhkaLVRRLQRRVLLLTKERD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 962 LLqeKSLLENkkLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPT------EEKMKISEQVQALQRERDQLQRQRN 1035
Cdd:pfam05557 357 GY--RAILES--YDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAqlsvaeEELGGYKQQAQTLERELQALRQQES 432
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 755545674 1036 SVDERLKHGRV--LSPKEEHLLFQ---LEEGIEALEAAIE 1070
Cdd:pfam05557 433 LADPSYSKEEVdsLRRKLETLELErqrLREQKNELEMELE 472
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-1100 |
6.55e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 856 QRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQdgfnLNRRKspfrsgDQFQKLDEQRKWLDEEVEKV 935
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALA------RRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 936 lsqRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLEssptEEKMK 1015
Cdd:COG4942 89 ---EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR----ADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1016 ISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIEALEAAIefknESIQSRQNSLKASFQNLSQSEA 1095
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIARLEAEAA 237
|
....*
gi 755545674 1096 NVLEK 1100
Cdd:COG4942 238 AAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
698-976 |
7.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 698 MESLQES-QEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELiktgnnaksvsRQYSLKVTKLEHEAEQAKVELT 776
Cdd:PRK03918 505 LKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKKLDELEEELA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 777 ETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQ 856
Cdd:PRK03918 574 ELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 857 RRLREEGEKKKQldaeiKRDQQKIKELQLKAGQGEGLNpkaedqdgfnlNRRKSPFRSGDQfqkldeqrkwLDEEVEKVL 936
Cdd:PRK03918 654 KKYSEEEYEELR-----EEYLELSRELAGLRAELEELE-----------KRREEIKKTLEK----------LKEELEERE 707
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755545674 937 SQRQELEMLEEDLKKREAI---VSKKEALLQEKSLLENKKLRS 976
Cdd:PRK03918 708 KAKKELEKLEKALERVEELrekVKKYKALLKERALSKVGEIAS 750
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
761-1159 |
7.53e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 761 VTKLEHEAEQAKVELTETRKQLQELESKdlsdvalkvklqkefrkkMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASE 840
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQ------------------MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 841 LEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLK--AGQGEGLNPKAEDQDGFNLNRRKSPFRSGDQF 918
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 919 QKLdeqrkwLDEEVEKVLSQRQELEMLEE-DLKKREaivskkeallQEKSLLENKKLRS--SQALSTDGLKISARLNLLD 995
Cdd:TIGR00618 679 QLA------LQKMQSEKEQLTYWKEMLAQcQTLLRE----------LETHIEEYDREFNeiENASSSLGSDLAAREDALN 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 996 QELSEKSLQlesSPTEEKMKISEQVQALQRERDQLQR--QRNSVDERLKHGRVLSPKEEHLLFQLEEGIEaleaaiefkn 1073
Cdd:TIGR00618 743 QSLKELMHQ---ARTVLKARTEAHFNNNEEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIG---------- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1074 ESIQSRQNSLKASFQNLSQSEANVLEKLVCLNIT--EIRAILFKYfnkvinlreTERKQQLQNKEMKMKVLerdnvvHEL 1151
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATlgEITHQLLKY---------EECSKQLAQLTQEQAKI------IQL 874
|
....*...
gi 755545674 1152 ESALEHLR 1159
Cdd:TIGR00618 875 SDKLNGIN 882
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
785-1070 |
8.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 785 LESKDLSDVALKVKLQ----KEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQ---NEKRASELEHNVDHLKYQkvQLQR 857
Cdd:COG4913 218 LEEPDTFEAADALVEHfddlERAHEALEDAREQIELLEPIRELAERYAAARERlaeLEYLRAALRLWFAQRRLE--LLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 858 RLREEGEKKKQLDAEIKRDQQKIKELQlkagqgeglnpkaEDQDGFNLNRRKSpfrSGDQFQKLDEQRKWLDEEVEKVLS 937
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALR-------------EELDELEAQIRGN---GGDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 938 QRQELEMLEEDLKkreaivskkEALLQEKSLLENKKLRSSQALSTdglkISARLNLLDQELSEKSLQLEsspteekmKIS 1017
Cdd:COG4913 360 RRARLEALLAALG---------LPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALR--------DLR 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755545674 1018 EQVQALQRERDQLQRQRNSVDERLKHGR-----VLSPKEEHLLF-----QLEEGIEALEAAIE 1070
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLALRdalaeALGLDEAELPFvgeliEVRPEEERWRGAIE 481
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
683-1226 |
8.22e-05 |
|
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: 47.42 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 683 QAESQRSylgngdlKMESLQESQEINLQKLRtselilNKAKQKMRELTinirmkeDLIKELIKTGNNAKSVSRQYSLKVT 762
Cdd:pfam15921 286 KASSARS-------QANSIQSQLEIIQEQAR------NQNSMYMRQLS-------DLESTVSQLRSELREAKRMYEDKIE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 763 KLEHEAEQAKVELTETRKQLQEL--ESKDLSDvalkvklqkEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKrase 840
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFsqESGNLDD---------QLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI---- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 841 lehNVDHLKyqkvqlqRRLREEGEKKKQLDA---EIKRDQQKIKELQLKAGQGEGlnpkaedqdgfnlnrrkspfRSGDQ 917
Cdd:pfam15921 413 ---TIDHLR-------RELDDRNMEVQRLEAllkAMKSECQGQMERQMAAIQGKN--------------------ESLEK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 918 FQKLDEQRKWLDEEVEKVLsqrQELEMLEEDLKKREAIVSKKEALLQEKSllenkklRSSQALSTDGLKISARLNLLDQE 997
Cdd:pfam15921 463 VSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSDLTASLQEKE-------RAIEATNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 998 LSE---------------KSLQLESSPTEEKMKISEQ---------------VQALQRERDQLQRQRNSVDERLKHGRVL 1047
Cdd:pfam15921 533 LQHlknegdhlrnvqtecEALKLQMAEKDKVIEILRQqienmtqlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1048 SPKEEHLLFQLEEGIEALEAAiefKNESIQSRQNSLKAsFQNLSQSEANVLEKLVCL-----NITEIRAILFKYF-NKVI 1121
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELE---KVKLVNAGSERLRA-VKDIKQERDQLLNEVKTSrnelnSLSEDYEVLKRNFrNKSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1122 NLRETERKQQLQNKEMKMKVLERDNVVHELESALEH---LRLQCDRRLTLQQKE---HEQKMQLLLQ---------HFKD 1186
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkVAMGMQKQITAKRGQidaLQSKIQFLEEamtnankekHFLK 768
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 755545674 1187 QDGDSIIETLKNYEDKIQQLEKDLYFYKKTSRDLKKRLKD 1226
Cdd:pfam15921 769 EEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
760-883 |
9.36e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 760 KVTKLEHEA----EQAKVELtETRKQLQELESKDLSDvALKVKLQKEFR-KKMDAAKMRVQVLQKKQQDSKKLASLsiqn 834
Cdd:PRK12704 32 KIKEAEEEAkrilEEAKKEA-EAIKKEALLEAKEEIH-KLRNEFEKELReRRNELQKLEKRLLQKEENLDRKLELL---- 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 755545674 835 EKRASELEHnvdhlkyQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKEL 883
Cdd:PRK12704 106 EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
916-1100 |
1.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 916 DQFQKLDEQRkwldEEVEKVLSQRQELEMLEEDLKKREAIVSKKEAL------------LQEKSLLENK--KLRSSQALS 981
Cdd:COG4913 232 EHFDDLERAH----EALEDAREQIELLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAEleELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 982 TDGLKI-SARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEE 1060
Cdd:COG4913 308 EAELERlEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755545674 1061 GIEALEAAIEFKNESIQSRQNSLKASFQNLsQSEANVLEK 1100
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDL-RRELRELEA 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
802-1211 |
1.10e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 802 EFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVdhLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIK 881
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELK--LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 882 ELQLKAGQGEGLNPKAEDQDGFNLnrrKSPFRSGDQFQKLDEQRKWLDEEvekvLSQRQELEMLEEDLKKREAIVSKKEA 961
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIE---SSKQEIEKEEEKLAQVLKENKEE----EKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 962 LLQEKSLLENKKLrssQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERL 1041
Cdd:pfam02463 304 KLERRKVDDEEKL---KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1042 KHGRvlspkeehllfQLEEGIEALEAAIEFKNESIQSRQNSLKASFQNLSQSEANVLEKLVCLNITEIRA-ILFKYFNKV 1120
Cdd:pfam02463 381 LESE-----------RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIeLKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1121 INLRETERKQQLQNKEMKMKV---LERDNVVHELESALEHLRLQCDRRLTLQQKEHEQKMQLLLQHFKDQDGDSIIETLK 1197
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSedlLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
410
....*....|....
gi 755545674 1198 NYEDKIQQLEKDLY 1211
Cdd:pfam02463 530 RLGDLGVAVENYKV 543
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
674-992 |
1.64e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 674 CSLVELSDTQAESQRSYLG---NGDLKMESLQESQEINLQKLRTSELILNKA-KQKMRELTINIRMKEDLIKELIKTGNN 749
Cdd:pfam02463 183 ENLAELIIDLEELKLQELKlkeQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 750 AKSVSRQYSLK-------VTKLEHEAEQAKVELTETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQ 822
Cdd:pfam02463 263 EEEKLAQVLKEnkeeekeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 823 DSKKLASLSIQNEKRASELEHNVDHLkyqKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQDG 902
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEKLQEKL---EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 903 FNLNRRKSpfrsgdQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALST 982
Cdd:pfam02463 420 LLKEEKKE------ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330
....*....|
gi 755545674 983 DGLKISARLN 992
Cdd:pfam02463 494 KLEERSQKES 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
741-1067 |
1.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 741 KELIKTGNNAKSVSRQYSLKVTKLEHEAEQAK-VELTETRKQLQELESKDLSDVALKVKLQKEFRKKMDAakMRVQVLQK 819
Cdd:PTZ00121 1118 EEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV--RKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 820 KQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQ-QKIKELQLKAGQGEGLNPKAE 898
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 899 DQDGFNLNRRKSPFRSGDQFQKLDEQRKwldeeVEKVLSQRQELEMLEEDLKKREAIVSKKEALlqEKSLLENKKLRSSQ 978
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKKADAA--KKKAEEAKKAAEAA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 979 ALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDErLKHGRVLSPKEEHLLFQL 1058
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKA 1427
|
....*....
gi 755545674 1059 EEGIEALEA 1067
Cdd:PTZ00121 1428 EEKKKADEA 1436
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
760-1187 |
2.15e-04 |
|
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: 45.98 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 760 KVTKLEHEAEQAKVELTEtrkqLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRA- 838
Cdd:pfam12128 242 EFTKLQQEFNTLESAELR----LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAv 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 839 SELEHNVDHLKYQKvqlqRRLREEGEKKKQLDAEikRDQQKIKELQLKAGQGEGLNPKAED-QDGFNLNRRKSPFRSGDQ 917
Cdd:pfam12128 318 AKDRSELEALEDQH----GAFLDADIETAAADQE--QLPSWQSELENLEERLKALTGKHQDvTAKYNRRRSKIKEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 918 FQKLDEQRKWLDEEVEKVLSQ-RQELEMLEEDLKKR--EAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKIS-----A 989
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVaEDDLQALESELREQleAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQlenfdE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 990 RLNLLDQELSEKSLQLESSPTEE---KMKISEQVQALQRERDQLQRQRNSVDErLKH----------------------- 1043
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELrqaRKRRDQASEALRQASRRLEERQSALDE-LELqlfpqagtllhflrkeapdweqs 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1044 -GRVLSP-----------------KEEHLLFQLEEGIEALEA-AIEFKNESIQSRQNSLKASFQNLSQSEANVLEKLVCL 1104
Cdd:pfam12128 551 iGKVISPellhrtdldpevwdgsvGGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1105 NItEIRAIlfkyfnkviNLRETERKQQLQNKEMKmkvLERDNVVHELE------SALEHLRLQCDRRLTL--QQKEHEQK 1176
Cdd:pfam12128 631 NG-ELEKA---------SREETFARTALKNARLD---LRRLFDEKQSEkdkknkALAERKDSANERLNSLeaQLKQLDKK 697
|
490
....*....|.
gi 755545674 1177 MQLLLQHFKDQ 1187
Cdd:pfam12128 698 HQAWLEEQKEQ 708
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
672-1136 |
2.79e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 672 SVCSLVELSDTQAESQRSYLGNGDLKMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAk 751
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 752 svsrqyslkvtklEHEAEQAKVELTETRKQLQELESKDlsdvalkvKLQKEFRKKMDAAKMRVQVLQKKQQDskklasLS 831
Cdd:pfam05483 404 -------------EVELEELKKILAEDEKLLDEKKQFE--------KIAEELKGKEQELIFLLQAREKEIHD------LE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 832 IQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKE-----LQLKAGQGEGLNPKAEDQDGF--- 903
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtLELKKHQEDIINCKKQEERMLkqi 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 904 -NLNRRKSPFRSGDQF------QKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRS 976
Cdd:pfam05483 537 eNLEEKEMNLRDELESvreefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 977 SQALSTDGLKISARLNLLDQELSEKSLQLESSpteeKMKISEQVQALQRERD-----------QLQRQRNSVDERLKHGR 1045
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASA----KQKFEEIIDNYQKEIEdkkiseeklleEVEKAKAIADEAVKLQK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1046 VLSPKEEHllfQLEEGIEALEAAIEFKNESIQSRQNSLkASFQNLSQSEANVLEKLVcLNITEIRAILFKYFNKVINLRE 1125
Cdd:pfam05483 693 EIDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSEL-GLYKNKEQEQSSAKAALE-IELSNIKAELLSLKKQLEIEKE 767
|
490
....*....|.
gi 755545674 1126 TERKQQLQNKE 1136
Cdd:pfam05483 768 EKEKLKMEAKE 778
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
676-862 |
3.52e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 676 LVELSDTQAESQRSYLGN-----GDLKMESLQESQEINLQKLRTSELILNKAKQ--KMRELTINI--------------- 733
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQhgrtaGAMQVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVsdlelekvklvnags 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 734 ----------RMKEDLIKELIKTGNNAKSVSRQYSL--------------KVTKLEHEAEQAKVELTETRKQLQELESKD 789
Cdd:pfam15921 643 erlravkdikQERDQLLNEVKTSRNELNSLSEDYEVlkrnfrnkseemetTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 790 LSDVALKVKLQKEF---RKKMDAAKMRVQVL---------------QKKQQDSKKLASLSIQNEKRASELEhnvdHLKYQ 851
Cdd:pfam15921 723 GHAMKVAMGMQKQItakRGQIDALQSKIQFLeeamtnankekhflkEEKNKLSQELSTVATEKNKMAGELE----VLRSQ 798
|
250
....*....|.
gi 755545674 852 kvqlQRRLREE 862
Cdd:pfam15921 799 ----ERRLKEK 805
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
765-1070 |
5.08e-04 |
|
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: 44.78 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 765 EHEAEQAKVELTETRKQLQELESK--DLSD--VALKVKLQKEFRKKMDAAKMRVQVLQKKQqdskklaslsiqnekrasE 840
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKhqQLCEekNALQEQLQAETELCAEAEEMRARLAARKQ------------------E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 841 LEHNVDhlkyqkvQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQ----DGFNLNRRKSPFRSGD 916
Cdd:pfam01576 73 LEEILH-------ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvttEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 917 QFQKLDEQRKWLDEEVEKVLSQRQELE----MLEEDLKKREAIVSKKEALL--QEKSLLENKKL-RSSQALSTDG----L 985
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEekakSLSKLKNKHEAMISDLEERLkkEEKGRQELEKAkRKLEGESTDLqeqiA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 986 KISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERdQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIEAL 1065
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR-ELEAQISELQEDLESERAARNKAEKQRRDLGEELEAL 304
|
....*
gi 755545674 1066 EAAIE 1070
Cdd:pfam01576 305 KTELE 309
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
819-1225 |
5.92e-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: 44.24 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 819 KKQQDSKKLASlsIQNEKRASELEhnvdhLKyqkvQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLK-AGQGEGLNPKA 897
Cdd:TIGR04523 34 EEKQLEKKLKT--IKNELKNKEKE-----LK----NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKlKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 898 EDQDGFNL---NRRKSPFRSGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDL-KKREAIVSKKEALLQEKSLLENKK 973
Cdd:TIGR04523 103 SDLSKINSeikNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 974 LRSSQALSTDGLKISARLNLLD--QELSEKSLQLESSPTEEKMK---ISEQVQALQRERDQLQRQRNSVDERLKhgrVLS 1048
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQTQLN---QLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1049 PKEEHLLFQLEEGIEALEAAiEFKNESIQSRQNSLKASFQNLSQSEANVLEKLVCLNITEIRailfkyfnkvinlretER 1128
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE----------------KK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1129 KQQLQNK--EMKMKVLERDNVVHELESALEHLRLQcDRRLTLQQKEHEQKMQLLLqhfkdQDGDSIIETLKNYEDKIQQL 1206
Cdd:TIGR04523 323 LEEIQNQisQNNKIISQLNEQISQLKKELTNSESE-NSEKQRELEEKQNEIEKLK-----KENQSYKQEIKNLESQINDL 396
|
410
....*....|....*....
gi 755545674 1207 EKDLYFYKKTSRDLKKRLK 1225
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIK 415
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
763-971 |
6.69e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.07 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 763 KLEHEAEQAKVELTETRKQLQELESKDLS----DVALKVKLQkEFRKKMDAAKMRVQ-VLQKKQQDSKKLaslsiqnekr 837
Cdd:pfam09726 399 RLEQDIKKLKAELQASRQTEQELRSQISSltslERSLKSELG-QLRQENDLLQTKLHnAVSAKQKDKQTV---------- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 838 aselehnvdhlkyqkVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQDGFNLNRRKSPFRSgdQ 917
Cdd:pfam09726 468 ---------------QQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQRKRELES--E 530
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755545674 918 FQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEAlLQEKSL-LEN 971
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSA-MQDKNQhLEN 584
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
852-983 |
8.24e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 852 KVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAE-DQDgfnLNRRKSPFRsgDQFQKLDEQRKWLDE 930
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEfEKE---LRERRNELQ--KLEKRLLQKEENLDR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755545674 931 EVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTD 983
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
759-959 |
1.76e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 759 LKVTKLEHEAEQAKVELTETRKQLQELEsKDLSDVALKVKlqkEFRKKMDAAKMRVQVLQKKQQDSKKLaSLSIQNEKRA 838
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALE-ARLEAAKTELE---DLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 839 SELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKagqgeglnpkaedqdgfnLNRRKspfrsgdqf 918
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE------------------LEEKK--------- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 755545674 919 QKLDEQRKWLDEEVEKVLSQRQEL-EMLEEDLKKR-EAIVSKK 959
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELaAKIPPELLALyERIRKRK 187
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
719-1203 |
2.91e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 719 LNKAKQKMRELTINIRMKEDLIKELIKtgnNAKSVSRQYSLKVTKLEheAEQAKVELTETRKQLQELESKDLSDVALKVK 798
Cdd:TIGR01612 1417 IDECIKKIKELKNHILSEESNIDTYFK---NADENNENVLLLFKNIE--MADNKSQHILKIKKDNATNDHDFNINELKEH 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 799 LQKEFRKKMDAAKMRVQVLQKK---QQDSKKLASLsiQNEKRASELEHNVDHLKYQKVQLqrrLREEGEKKKQLDAEIKR 875
Cdd:TIGR01612 1492 IDKSKGCKDEADKNAKAIEKNKelfEQYKKDVTEL--LNKYSALAIKNKFAKTKKDSEII---IKEIKDAHKKFILEAEK 1566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 876 DQQKIKELqlkagqgeglnpkaedqdgfnlnrRKSPFRSGDQFQKLDEQRKwldeeveKVLSQRQELEMLEEDLKKREAI 955
Cdd:TIGR01612 1567 SEQKIKEI------------------------KKEKFRIEDDAAKNDKSNK-------AAIDIQLSLENFENKFLKISDI 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 956 VSKKEALLQEKSLLENKKlrSSQALSTDGLKISARLNLLDqelsekSLQ--LESSPTEEKmKISEQVQALQRERDQLQRQ 1033
Cdd:TIGR01612 1616 KKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLN------SLQefLESLKDQKK-NIEDKKKELDELDSEIEKI 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1034 RNSVDERLKHgrvlspKEEHLLFQLEEGIEALEAAIEFKNESIQSRQNSLKASFQNLSQSEANVLEKLVCLNiTEIRAI- 1112
Cdd:TIGR01612 1687 EIDVDQHKKN------YEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYN-TEIGDIy 1759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1113 --LFKYFNKVINLRETERKQQLQNKEMKMKvleRDNVVHELesalehlrlqcdrrltLQQKEHEQKMQLLLQHFKDQDGD 1190
Cdd:TIGR01612 1760 eeFIELYNIIAGCLETVSKEPITYDEIKNT---RINAQNEF----------------LKIIEIEKKSKSYLDDIEAKEFD 1820
|
490
....*....|...
gi 755545674 1191 SIIETLKNYEDKI 1203
Cdd:TIGR01612 1821 RIINHFKKKLDHV 1833
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
710-889 |
3.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 710 QKLRTSELILNKAKQKMRELTINIrmkEDLIKELIktgNNAKSVsRQYSLKVTKLEHEAEQAKVELTETRKQLQELESKd 789
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLE---ELEREL-EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 790 lsdvaLKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIqNEKRASElehnvdhlkyqkvqLQRRLREEGEKKkql 869
Cdd:PRK00409 567 -----LLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV-KAHELIE--------------ARKRLNKANEKK--- 623
|
170 180
....*....|....*....|
gi 755545674 870 daEIKRDQQKIKELQLKAGQ 889
Cdd:PRK00409 624 --EKKKKKQKEKQEELKVGD 641
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-884 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 707 INLQKLRTSeliLNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELE 786
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 787 S-KDLSDvalkvkLQKEfrkkMDAAKMRVQVLQKKQqdskklaslsIQNEKRASELEHNVDHLKYQKVQLQRRLReegEK 865
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISDLEDEI----------LELMERIEELEEELAELEAELAELEAELE---EK 143
|
170
....*....|....*....
gi 755545674 866 KKQLDAEIKRDQQKIKELQ 884
Cdd:COG1579 144 KAELDEELAELEAELEELE 162
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
934-1140 |
4.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 934 KVLSQRQELE-MLEEdlKKREAIVSKKEALLQEKSllENKKLRSSqalstdglkisarlnlLDQELSEKslqlessptee 1012
Cdd:PRK12704 32 KIKEAEEEAKrILEE--AKKEAEAIKKEALLEAKE--EIHKLRNE----------------FEKELRER----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 1013 KMKISEQVQALQRERDQLQRQRNSVDERlkhgrvlspkeehllfqlEEGIEALEAAIEFKNESIQSRQNSLkasfQNLSQ 1092
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKR------------------EEELEKKEKELEQKQQELEKKEEEL----EELIE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755545674 1093 SEANVLEKLVCLNITEIRAILFKyfnKVINLRETERKQQLQNKEMKMK 1140
Cdd:PRK12704 139 EQLQELERISGLTAEEAKEILLE---KVEEEARHEAAVLIKEIEEEAK 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
678-970 |
4.11e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 678 ELSDTQAESQRSyLGNGDLKMESLQESQEINLQKLRTSElilNKAKQKMRELTINIRMKEDLIKEL-----------IKT 746
Cdd:TIGR02169 706 ELSQELSDASRK-IGEIEKEIEQLEQEEEKLKERLEELE---EDLSSLEQEIENVKSELKELEARIeeleedlhkleEAL 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 747 GNNAKSVSRQyslKVTKLEHEAEQAKVELTETRKQLQELESKdLSDVALKVKLQKEFRK----KMDAAKMRVQVLQKKQQ 822
Cdd:TIGR02169 782 NDLEARLSHS---RIPEIQAELSKLEEEVSRIEARLREIEQK-LNRLTLEKEYLEKEIQelqeQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 823 DSK----KLASLSIQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAE 898
Cdd:TIGR02169 858 NLNgkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755545674 899 DqdgfNLNRRKSPFRSGDQFQKLDEQRKWLDEEVEKVlsqrQELEML-----EEDLKKREAIVSKKEALLQEKSLLE 970
Cdd:TIGR02169 938 D----PKGEDEEIPEEELSLEDVQAELQRVEEEIRAL----EPVNMLaiqeyEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
710-971 |
6.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 710 QKLRTSELILNKAKQKMRELTINIRMKEDLIK---ELIKTGNNAKSVSRQYSLKVTKLEHEAEQAkvelTETRKQLQELE 786
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDLVEaedRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 787 SkdlsDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKK----------LASLSIQNEKRASELEHNVDHLKYQKVQLQ 856
Cdd:PRK02224 551 A----EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerirtLLAAIADAEDEIERLREKREALAELNDERR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545674 857 RRLREEGEKKKQLDAEIkrDQQKIKELQLKAGQGEGLNPKAEDQdgfnlnrrkspfrsgdqFQKLDEQRKWLDEEVEKVL 936
Cdd:PRK02224 627 ERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQVEEK-----------------LDELREERDDLQAEIGAVE 687
|
250 260 270
....*....|....*....|....*....|....*
gi 755545674 937 SQRQELEMLEEDLKKREAIVSKKEALLQEKSLLEN 971
Cdd:PRK02224 688 NELEELEELRERREALENRVEALEALYDEAEELES 722
|
|
| |
