|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-371 |
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: 597.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 7 CCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 87 GQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDSTRdpd 166
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPET--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 167 trHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVN 246
Cdd:cd01372 150 --DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 247 eavtglpdgtpPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSK 326
Cdd:cd01372 228 -----------ADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 355390331 327 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 371
Cdd:cd01372 297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
9-377 |
1.33e-138 |
|
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: 430.84 E-value: 1.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVL-------LGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNA 81
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 82 TVLAYGQTGAGKTYTMGTgfdmatSEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSAQFLELYNEEILDLFDS 161
Cdd:smart00129 82 TIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 162 trdpdtrhRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMrmctq 241
Cdd:smart00129 148 --------SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQK----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 242 pdlvneavtglpdGTPPSSEyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVvHVP 321
Cdd:smart00129 215 -------------IKNSSSG-SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR-HIP 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331 322 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 377
Cdd:smart00129 280 YRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
14-370 |
2.85e-137 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 426.99 E-value: 2.85e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 14 RIRPQLSKEKIEGCHICTSVTPGEPQVLL-------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAY 86
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 87 GQTGAGKTYTMGTgfdmatSEEEQGIIPRAIAHLFGGIAERKRRaqeqgvagPEFKVSAQFLELYNEEILDLFDSTRDPD 166
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPSNKNK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 167 TrhrrsNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRmctqpdlvn 246
Cdd:pfam00225 147 R-----KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRN--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 247 eavtglpdgTPPSSEYETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRDS 325
Cdd:pfam00225 213 ---------RSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK--HIPYRDS 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 355390331 326 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:pfam00225 282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
9-368 |
2.41e-124 |
|
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: 392.00 E-value: 2.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKiEGCHICTSVTPG------EPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:cd00106 2 VRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 83 VLAYGQTGAGKTYTMgtgfdMATSEEEQGIIPRAIAHLFggiaerkRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd00106 81 IFAYGQTGSGKTYTM-----LGPDPEQRGIIPRALEDIF-------ERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 163 RdpdtrhrRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMctqp 242
Cdd:cd00106 149 P-------KKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNR---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 243 DLVNEAVTGlpdgtppsseyetltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPY 322
Cdd:cd00106 218 EKSGESVTS---------------SKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPY 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 355390331 323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 368
Cdd:cd00106 281 RDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
8-370 |
5.58e-104 |
|
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: 335.58 E-value: 5.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 8 CVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKA--------FTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGY 79
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 80 NATVLAYGQTGAGKTYTMGtGFDmaTSEEEQGIIPRAIAHLFGGIAerkrRAQEQgvagPEFKVSAQFLELYNEEILDLF 159
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTME-GKR--EDPELRGIIPNSFAHIFGHIA----RSQNN----QQFLVRVSYLEIYNEEIRDLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 160 DStrdpDTRHRrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrMC 239
Cdd:cd01371 151 GK----DQTKR---LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----EC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 240 TQPDLVNEAVTGLpdgtppsseyetltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqsKKVVH 319
Cdd:cd01371 220 SEKGEDGENHIRV--------------GKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD--GKSTH 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 355390331 320 VPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01371 284 IPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
8-372 |
3.96e-103 |
|
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: 333.02 E-value: 3.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 8 CVKVAVRIRPQLSKEKIE-GCHICTSVTPGEPQVLLGKD---KAFTYDFVFDLDTWQEQIYSTcVSKLIEGCFEGYNATV 83
Cdd:cd01366 3 NIRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 84 LAYGQTGAGKTYTM-GTgfdmatsEEEQGIIPRAIAHLFGGIAERKrraqEQGVagpEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd01366 82 FAYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELK----EKGW---SYTIKASMLEIYNETIRDLLAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 163 RDPDTRHrrsNIKiHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrmctqp 242
Cdd:cd01366 148 NAPQKKL---EIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 243 dlvneavtglpDGTPPSSEyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdqSKKVVHVPY 322
Cdd:cd01366 215 -----------SGRNLQTG-EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPY 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 355390331 323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 372
Cdd:cd01366 280 RNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
9-370 |
4.00e-101 |
|
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: 328.15 E-value: 4.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGCHICTSVT--------PGEPQVLL--------------GKDKAFTYDFVFDLDTWQEQIYST 66
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 67 CVSKLIEGCFEGYNATVLAYGQTGAGKTYTM-GTgfdmatsEEEQGIIPRAIAHLFGGIAERKrraqeqgvAGPEFKVSA 145
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLK--------DEKEFEVSM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 146 QFLELYNEEILDLFDSTRDPdtrhrrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRS 225
Cdd:cd01370 147 SYLEIYNETIRDLLNPSSGP--------LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 226 HAIFTIHLCQMrmcTQPDLVNEAVTglpdgtppsseyetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGN 305
Cdd:cd01370 219 HAVLQITVRQQ---DKTASINQQVR---------------QGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGN 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355390331 306 VISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01370 281 CINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
9-377 |
1.96e-99 |
|
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: 323.92 E-value: 1.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGC--------HICTSVTPGEPQVLLGKDKAFTYDFVFDLDTW-----------QEQIYSTCVS 69
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSkcivqmsgKETTLKNPKQADKNNKATREVPKSFSFDYSYWshdsedpnyasQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 70 KLIEGCFEGYNATVLAYGQTGAGKTYTMgtgfdMATsEEEQGIIPRAIAHLFggiaERKRRAQEQGVagpEFKVSAQFLE 149
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTM-----MGT-QEQPGIIPRLCEDLF----SRIADTTNQNM---SYSVEVSYME 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 150 LYNEEILDLFDstrdPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIF 229
Cdd:cd01365 150 IYNEKVRDLLN----PKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 230 TIHLCQMRMctqpdlvnEAVTGLPdgtppsseyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 309
Cdd:cd01365 226 TIVLTQKRH--------DAETNLT---------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISA 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331 310 LGDQSKKV-----VHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVN 377
Cdd:cd01365 289 LADMSSGKskkksSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
9-379 |
4.95e-96 |
|
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: 313.68 E-value: 4.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGK-DKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYG 87
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 88 QTGAGKTYTM--GTGFDMATSEEEQGIIPRAIAHLFGGIaerkRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRdp 165
Cdd:cd01373 83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLI----QREKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPAS-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 166 dtrhrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqMRMCTQPDLV 245
Cdd:cd01373 157 ------RNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 246 NeavtglpdgtppsseyeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSK-KVVHVPYRD 324
Cdd:cd01373 229 N-----------------IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRD 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 355390331 325 SKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQD 379
Cdd:cd01373 292 SKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
6-370 |
6.51e-95 |
|
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: 309.65 E-value: 6.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 6 DCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKD--KAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATV 83
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 84 LAYGQTGAGKTYTM-GTGFDmatsEEEQGIIPRAIAHLFGGIaerkrraqEQGVAGPEFKVSAQFLELYNEEILDLFDST 162
Cdd:cd01369 81 FAYGQTSSGKTYTMeGKLGD----PESMGIIPRIVQDIFETI--------YSMDENLEFHVKVSYFEIYMEKIRDLLDVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 163 RDpdtrhrrsNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQp 242
Cdd:cd01369 149 KT--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETE- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 243 dlvneavtglpdgtppsseyETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqsKKVVHVPY 322
Cdd:cd01369 220 --------------------KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 355390331 323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01369 278 RDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
9-379 |
8.16e-94 |
|
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: 307.72 E-value: 8.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLL--------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYN 80
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 81 ATVLAYGQTGAGKTYTMgTGfDMATSE-------EEQGIIPRAIAHLFggiaerkrraQEQGVAGPEFKVSAQFLELYNE 153
Cdd:cd01364 84 CTIFAYGQTGTGKTYTM-EG-DRSPNEeytweldPLAGIIPRTLHQLF----------EKLEDNGTEYSVKVSYLEIYNE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 154 EILDLFDStrDPDTRHRrsnIKIHEDAN--GGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTI 231
Cdd:cd01364 152 ELFDLLSP--SSDVSER---LRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 232 HLcqmrmctqpdLVNEAvtglpdgtppSSEYETL--TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 309
Cdd:cd01364 227 TI----------HIKET----------TIDGEELvkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 310 LGDQSKkvvHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQD 379
Cdd:cd01364 287 LVERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
9-370 |
1.55e-89 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 294.24 E-value: 1.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQ 88
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 89 TGAGKTYTMgTGfdmatSEEEQGIIPRAIAHLFGGIAERKRRaqeqgvagpEFKVSAQFLELYNEEILDLFDSTRdpdtr 168
Cdd:cd01374 82 TSSGKTFTM-SG-----DEDEPGIIPLAIRDIFSKIQDTPDR---------EFLLRVSYLEIYNEKINDLLSPTS----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 169 hrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcQMRMCTQPDlvNEA 248
Cdd:cd01374 142 ---QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELE--EGT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 249 VTglpdgtppsseYETLTakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDqSKKVVHVPYRDSKLT 328
Cdd:cd01374 216 VR-----------VSTLN----LIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLT 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 355390331 329 RLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 370
Cdd:cd01374 280 RILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
43-507 |
6.99e-88 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 298.58 E-value: 6.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 43 GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGtgfdmaTSEEEQGIIPRAIAHLFG 122
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMS------GTEEEPGIIPLSLKELFS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 123 GIAERKRRAqeqgvagpEFKVSAQFLELYNEEILDLFDSTRDPdtrhrrsnIKIHEDANGGIYTTGVTSRLIHSQEELIQ 202
Cdd:COG5059 127 KLEDLSMTK--------DFAVSISYLEIYNEKIYDLLSPNEES--------LNIREDSLLGVKVAGLTEKHVSSKEEILD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 203 CLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmrmctqpdlvneavtglpDGTPPSSEYeTLTAKFHFVDLAGSERLKR 282
Cdd:COG5059 191 LLRKGEKNRTTASTEINDESSRSHSIFQIEL--------------------ASKNKVSGT-SETSKLSLVDLAGSERAAR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 283 TGATGERAKEGISINCGLLALGNVISALGDQsKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLK 362
Cdd:COG5059 250 TGNRGTRLKEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 363 YANRARNIKNKVVVNQDK-TSQQISALRAEIARLQMELMEYKAGKRVIGEDgaegySDLFRENAMLQKengaLRLRVKAM 441
Cdd:COG5059 329 FASRAKSIKNKIQVNSSSdSSREIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQS----LKKETETL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 442 QEAIDAINNRVTQLMSQEANLLLAKaGDGNEAIGALIQNYI----REIEELRTKLLESEAMNESLRRSLS 507
Cdd:COG5059 400 KSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIdrllLLREEELSKKKTKIHKLNKLRHDLS 468
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
9-368 |
3.20e-69 |
|
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: 235.86 E-value: 3.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEGCHICTSVTpGEPQVLL------GKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 83 VLAYGQTGAGKTYTMgtgfdmATSEEEQGIIPRAIAHLFggiaerkRRAQEQGVAGpefKVSAQFLELYNEEILDLFDSt 162
Cdd:cd01376 81 VFAYGSTGAGKTFTM------LGSPEQPGLMPLTVMDLL-------QMTRKEAWAL---SFTMSYLEIYQEKILDLLEP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 163 rdpdtrhRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQmrmctQP 242
Cdd:cd01376 144 -------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQ-----RE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 243 DLVNeavtglpdgtppsseYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdqSKKVVHVPY 322
Cdd:cd01376 212 RLAP---------------FRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 355390331 323 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 368
Cdd:cd01376 274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
45-368 |
9.77e-69 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 235.17 E-value: 9.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 45 DKAFTYDFVFDlDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGfdmATSEEEQGIIPRAIAHLFGGI 124
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGG---TENYKHRGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 125 AERKRRAqeqgvagpeFKVSAQFLELYNEEILDLFDSTrdPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCL 204
Cdd:cd01375 123 EERPTKA---------YTVHVSYLEIYNEQLYDLLSTL--PYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 205 KQGALSRTTASTQMNVQSSRSHAIFTIHLcQMRMCTqpdlvneavtglpdgtpPSSEyETLTAKFHFVDLAGSERLKRTG 284
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIHL-EAHSRT-----------------LSSE-KYITSKLNLVDLAGSERLSKTG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 285 ATGERAKEGISINCGLLALGNVISALGDQSKKvvHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 364
Cdd:cd01375 253 VEGQVLKEATYINKSLSFLEQAIIALSDKDRT--HVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330
|
....
gi 355390331 365 NRAR 368
Cdd:cd01375 331 SRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
9-366 |
2.73e-68 |
|
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: 233.73 E-value: 2.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKIEG-CHICTSVTPGEPQVLLGKDK----------AFTYDFVFDLDTWQEQIYSTCVSKLIEGCFE 77
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 78 GYNATVLAYGQTGAGKTYTMGTGFdmATSEEEQGIIPRAIAHLFGGIAERKRRAQeqgvagpeFKVSAQFLELYNEEILD 157
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDN--------LGVTVSFFEIYGGKVFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 158 LFdstrdpdtrHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLcqmr 237
Cdd:cd01367 152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 238 mctqpdlvneavtglpdgtpPSSEYETLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDQSkk 316
Cdd:cd01367 219 --------------------RDRGTNKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 355390331 317 vVHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 366
Cdd:cd01367 277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
9-364 |
1.40e-67 |
|
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: 232.28 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 9 VKVAVRIRPQLSKEKI---EGC-HI--CTSVTPGEPQVLLG---------KDKAFTYDFVFDLDTWQEQIYSTCVSKLIE 73
Cdd:cd01368 3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 74 GCFEGYNATVLAYGQTGAGKTYTMgTGfdmatSEEEQGIIPRAIAHLFGGIaerkrraqeqgvagPEFKVSAQFLELYNE 153
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTM-QG-----SPGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 154 EILDLFDSTRDPDTRHRRSnIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHL 233
Cdd:cd01368 143 YIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 234 CQmrmctqpdlvneavtgLPDGTPPSSEYET---LTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 310
Cdd:cd01368 222 VQ----------------APGDSDGDVDQDKdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVL 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331 311 GDQ--SKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 364
Cdd:cd01368 286 RENqlQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-404 |
3.75e-65 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 244.07 E-value: 3.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 3 GQGDCCVKVAVRIRPQLSKEKIEgchicTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNAT 82
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGEEGE-----MIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 83 VLAYGQTGAGKTYTM----GTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVagpEFKVSAQFLELYNEEILDL 158
Cdd:PLN03188 169 VFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQIKHADRQL---KYQCRCSFLEIYNEQITDL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 159 FDSTRdpdtrhrrSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTihlcqmrm 238
Cdd:PLN03188 246 LDPSQ--------KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT-------- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 239 CtqpdLVNEAVTGLPDGTppsSEYETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD--QSKK 316
Cdd:PLN03188 310 C----VVESRCKSVADGL---SSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisQTGK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 317 VVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDkTSQQISALRAEIARLQ 396
Cdd:PLN03188 381 QRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLR 459
|
....*...
gi 355390331 397 MELMEYKA 404
Cdd:PLN03188 460 DELQRVKA 467
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1292-1600 |
4.47e-65 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 222.98 E-value: 4.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1292 EGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVST-SYIKVWDIRDSaK 1368
Cdd:cd00200 6 KGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDLETG-E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1369 CIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-NAVRIWELSRFQPVGKLTGHIGPVMCLT 1447
Cdd:cd00200 85 CVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1448 VTQTasqHDLVVTGSKDHYVKMFELGecvtgTIGPTHNFEPpHYDGIECLAIQGD--ILFSGSRDNGIKKWDLDQQELIQ 1525
Cdd:cd00200 143 FSPD---GTFVASSSQDGTIKLWDLR-----TGKCVATLTG-HTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 1526 QIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:cd00200 214 TLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1189-1602 |
1.72e-48 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 178.95 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1189 RDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDK 1268
Cdd:COG2319 11 AASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1269 GIISPVGGAKGAR---TAPLQCVSMAEGHTKPILCLDATD--ELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKY 1343
Cdd:COG2319 91 RLLASASADGTVRlwdLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1344 cSHSG-LVFSVSTSY-IKVWDIrDSAKCIRTLTSSgqvisgdacaatstraitsaqgEHQINQIALSPSGTMLYAASG-N 1420
Cdd:COG2319 171 -SPDGkLLASGSDDGtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1421 AVRIWELSRFQPVGKLTGHIGPVMCLTVTqtasqHD--LVVTGSKDHYVKMFELGecvTGTIGPTHnfePPHYDGIECLA 1498
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHSGSVRSVAFS-----PDgrLLASGSADGTVRLWDLA---TGELLRTL---TGHSGGVNSVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1499 I--QGDILFSGSRDNGIKKWDLDQQELIQQIPnAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSP 1576
Cdd:COG2319 296 FspDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGA 374
|
410 420
....*....|....*....|....*...
gi 355390331 1577 INAICTNA--KHIFTASSDLTVKFWSVR 1602
Cdd:COG2319 375 VTSVAFSPdgRTLASGSADGTVRLWDLA 402
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
929-1010 |
4.06e-43 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.
Pssm-ID: 410203 [Multi-domain] Cd Length: 82 Bit Score: 151.88 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 355390331 1009 TK 1010
Cdd:cd22262 81 TK 82
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1399-1602 |
5.61e-36 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 139.01 E-value: 5.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1399 EHQINQIALSPSGTMLYAASGNA-VRIWELSRFQPVGKLTGHIGPVMCLTVTqtaSQHDLVVTGSKDHYVKMFEL--GEC 1475
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPVRDVAAS---ADGTYLASGSSDKTIRLWDLetGEC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1476 VtgtigptHNFEPpHYDGIECLAIQ--GDILFSGSRDNGIKKWDLDQQELIQQIpNAHKDWVCALAFIPGRPMLLSACRA 1553
Cdd:cd00200 86 V-------RTLTG-HTSYVSSVAFSpdGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 355390331 1554 GVIKVWNVDNFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWSVR 1602
Cdd:cd00200 157 GTIKLWDLRTGKCVATLTGHTGEVNSVAfsPDGEKLLSSSSDGTIKLWDLS 207
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
929-1010 |
2.63e-28 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 109.63 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 355390331 1009 TK 1010
Cdd:cd22263 81 AK 82
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
929-1010 |
6.17e-27 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 105.36 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 929 QRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKgLQELAEEIEVLAANIDYINDGITDCQATIVQLEE 1008
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKDESV-LRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 355390331 1009 TK 1010
Cdd:cd22248 80 SK 81
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
7-158 |
2.52e-17 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 80.34 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 7 CCVKVAVRIRPQLSKEkiegCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCvSKLIEGCFEGYNATVLAY 86
Cdd:pfam16796 20 GNIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAY 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355390331 87 GQTGAGKTYTMgtgfdmatseeeqgiIPRAIAHLFGGIAERKRraqeqgvaGPEFKVSAQFLELYNEEILDL 158
Cdd:pfam16796 95 GQTGSGSNDGM---------------IPRAREQIFRFISSLKK--------GWKYTIELQFVEIYNESSQDL 143
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
11-309 |
1.47e-14 |
|
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: 73.15 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 11 VAVRIRPQLSKEKIEGCHICTSvtpgepqvllgkdkaftyDFVFDLDTWQEQIYSTCvSKLIEGCFEGYN-ATVLAYGQT 89
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVF------------------YRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 90 GAGKTYTMgtgfdmatseeeQGIIPRAIAHLFGGIaerkrraqeqgvagpefkvsaqflelyneeildlfdstrdpdtrh 169
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAFNGI--------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 170 rrsnikiheDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRtTASTQMNVQSSRSHAIFTIhlcqmrmctqpdlvneav 249
Cdd:cd01363 85 ---------NKGETEGWVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 250 tglpdgtppsseyetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 309
Cdd:cd01363 137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
633-842 |
9.25e-14 |
|
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: 74.80 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRV---LQNLSTMECYTEEKANKIKAD 709
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 710 YEKRLR---------------------EMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE 768
Cdd:COG4942 106 LAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355390331 769 EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRlAKPMSERVAGRAGLKPP 842
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLPWP 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
642-1085 |
1.30e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.96 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 642 EIEIKQKLIDELENSQRRLQTL---KHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANkikadyEKRLREMN 718
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL------EAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 719 RDLQKLQAAQKEHARLlknqsryERELKKLQAEVAEMKKAKVALMKQMREEqQRRRLVETKRNRE-----IAQLKKEQRR 793
Cdd:COG4717 146 ERLEELEERLEELREL-------EEELEELEAELAELQEELEELLEQLSLA-TEEELQDLAEELEelqqrLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 794 QEFQIRALESQKRQ--QEMVLRRKTQEVSALRRLAKPMS----------------ERVAG----RAGLKPPMLDSGAEVS 851
Cdd:COG4717 218 AQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAallallglggsllsliLTIAGvlflVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 852 ASTTSSEAESGARSVSSIVRQwnRKINHFLGDHPAPTVNGTRPARKKFQ-----KKGASQSFSKAARLKWQSLERRIIDI 926
Cdd:COG4717 298 ASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDrieelQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 927 VmqRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQ-----ELAEEIEVLAANIDYINDGITDCQA 1001
Cdd:COG4717 376 L--AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1002 TIVQLEETKEELDSTDTsvvisscsLAEARllldnflkasidkgLQVAQKEAQIRLLEGRLRQTDMAGSsqnhlLLDALR 1081
Cdd:COG4717 454 ELAELEAELEQLEEDGE--------LAELL--------------QELEELKAELRELAEEWAALKLALE-----LLEEAR 506
|
....
gi 355390331 1082 EKAE 1085
Cdd:COG4717 507 EEYR 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
472-1064 |
9.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 472 EAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSpyslgaspaapafggspassmEDASEVIRRAKQDLERL 551
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL---------------------EEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 552 KKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKE-- 629
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEee 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 630 -VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteekankika 708
Cdd:COG1196 381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL---------------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 709 dyEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQMREEQQ-----RRRLVETKRNRE 783
Cdd:COG1196 445 --EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 784 IAQLKKEQRRQEF----QIRALESQKRQQemVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSASTTSSEA 859
Cdd:COG1196 522 LAGAVAVLIGVEAayeaALEAALAAALQN--IVVEDDEVAAAAIEYLK---AAKAGRATFLPLDKIRARAALAAALARGA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 860 ESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARkkfqkkgasqsfskaARLKWQSLERRIIDIVMQRMTIVNLEAD 939
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE---------------AALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 940 MERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDgitdcQATIVQLEETKEELDSTDTS 1019
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER-----LEEELEEEALEEQLEAEREE 736
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 355390331 1020 VVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1064
Cdd:COG1196 737 LLE---ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-1094 |
3.31e-10 |
|
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: 65.08 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 383 QQISALRAEIARLQMELMEYKAGKRVIGEDgaegYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANL 462
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 463 LlakagDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAApafggspASSMEDASEVIR 542
Cdd:TIGR02168 315 E-----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-------ESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 543 RAKQDLERLKKKE----VRQRRKSPEKEAFKKR-AKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEES 617
Cdd:TIGR02168 383 TLRSKVAQLELQIaslnNEIERLEARLERLEDRrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 618 LVDSDSDPEEKevnfQADLADLTCEIEIKQKLIDELENSQRRLQTLkhqYEEKLILLQNKIRDTQLeRDRVLQNLSTMEC 697
Cdd:TIGR02168 463 LEELREELEEA----EQALDAAERELAQLQARLDSLERLQENLEGF---SEGVKALLKNQSGLSGI-LGVLSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 698 Y------------------TEEKANK-IKADYEKRLREMN---RDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEM 755
Cdd:TIGR02168 535 YeaaieaalggrlqavvveNLNAAKKaIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 756 KKA----------------KVALMKQMREEQQ--------------------RRRLVETKRNREIAQLKKEQRRQEFQIR 799
Cdd:TIGR02168 615 RKAlsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIA 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 800 ALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVagraglkppmldSGAEVSASTTSSEAESGARSVSSIVRQWNRKINH 879
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQI------------SALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 880 FLGDHpaptvngtrparkkfQKKGASQSFSKAARLKWQSLERRIidivmQRMTIvNLEADMERLIKKREELFLLQEALRR 959
Cdd:TIGR02168 763 IEELE---------------ERLEEAEEELAEAEAEIEELEAQI-----EQLKE-ELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 960 KRER---LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQAtivQLEETKEELDSTDTSVVISSCSLAEARLLLDN 1036
Cdd:TIGR02168 822 LRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355390331 1037 FlkasiDKGLQVAQKEAQiRLLEGRLRQTDMAGSSQNHL---------LLDALREK----AEAHPELQALI 1094
Cdd:TIGR02168 899 L-----SEELRELESKRS-ELRRELEELREKLAQLELRLeglevridnLQERLSEEysltLEEAEALENKI 963
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
632-1230 |
4.57e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 64.75 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 632 FQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYE 711
Cdd:pfam15921 315 YMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----DQLQKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 712 KRLREMNrdLQKLQAaQKEHARLLKNQ---SRYERELKKLQAEVAEMKkakvALMKQMREEQQrrrlveTKRNREIAQLK 788
Cdd:pfam15921 388 KREKELS--LEKEQN-KRLWDRDTGNSitiDHLRRELDDRNMEVQRLE----ALLKAMKSECQ------GQMERQMAAIQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 789 KEQRRQEfQIRALESQKRQQEMVLRRKTQEVSAlRRLAKPMSERVAG-------------------------RAGLKPPM 843
Cdd:pfam15921 455 GKNESLE-KVSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVSdltaslqekeraieatnaeitklrsRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 844 L----DSGAEVSASTTSSEA----ESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFS-- 909
Cdd:pfam15921 533 LqhlkNEGDHLRNVQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKil 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 910 ---KAARLKwqSLERRIIDIVMQRMTIVNleADMERLIKKREelfllqeaLRRKRERLQAESPEEEKGLQELAEEIEVLA 986
Cdd:pfam15921 613 kdkKDAKIR--ELEARVSDLELEKVKLVN--AGSERLRAVKD--------IKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 987 ANIDYINDGI-TDCQATIVQLEETKEELDSTDTSVVISSCSLAEArllldnfLKASIDKGLQVAQKEAQIRLLEGRLRQT 1065
Cdd:pfam15921 681 RNFRNKSEEMeTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA-------MKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1066 DMAGSSQN---HLLLDalrEKAEAHPELQALiynVQQENGYASTDEEISefsegsfSQSFTMKGSTSHDDFKFKsepKLS 1142
Cdd:pfam15921 754 EEAMTNANkekHFLKE---EKNKLSQELSTV---ATEKNKMAGELEVLR-------SQERRLKEKVANMEVALD---KAS 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1143 AQMkavsAECLGPPLDISTKNITKSLASLVEIKE-DGVGFSvRDPYYRDRVSRTVSLPTRGSTFPR-QSRATETSPLTRR 1220
Cdd:pfam15921 818 LQF----AECQDIIQRQEQESVRLKLQHTLDVKElQGPGYT-SNSSMKPRLLQPASFTRTHSNVPSsQSTASFLSHHSRK 892
|
650
....*....|
gi 355390331 1221 KSYDRGQPIR 1230
Cdd:pfam15921 893 TNALKEDPTR 902
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
701-1092 |
1.69e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 701 EKANKIKADYEKR--------LREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKAKVALMKQMREEQQR 772
Cdd:COG1196 213 ERYRELKEELKELeaellllkLRELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 773 RRLVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKpmsERVAGRAGLKPPMLDSGAEVSA 852
Cdd:COG1196 290 EYELL----AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 853 STTSSEAESGARsvSSIVRQWNRKinhflgdhpaptvngtrpARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMT 932
Cdd:COG1196 363 AEEALLEAEAEL--AEAEEELEEL------------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 933 IVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEE 1012
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1013 LDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQA 1092
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-1015 |
2.29e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 702 KANKIKAdyEKRLREMNRDLQKLQAAQKEHARLLKN---QSRYERELKKLQAEVAEMKKAKVAL-MKQMREEQQRRRLVE 777
Cdd:TIGR02168 171 KERRKET--ERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELALLVLrLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 778 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA-GRAGLKPpmlDSGAEVSASTTS 856
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQiLRERLAN---LERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 857 SEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQsfskAARLKWQSLERRIIDIVMQ----RMT 932
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLELQiaslNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 933 IVNLEADMERLIKKREELFLLQEALRRK-----RERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLE 1007
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
....*...
gi 355390331 1008 ETKEELDS 1015
Cdd:TIGR02168 482 RELAQLQA 489
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
642-818 |
3.76e-09 |
|
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: 61.68 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 642 EIEIKQKLIDELEnsqrRLQTLKHQYEEKL---ILLQNKIRDTQLERDR-VLQNLSTMECYTEEKAN----KIKADYEKR 713
Cdd:pfam17380 369 EIAMEISRMRELE----RLQMERQQKNERVrqeLEAARKVKILEEERQRkIQQQKVEMEQIRAEQEEarqrEVRRLEEER 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 714 LREMNRDLQKLQAAQKEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQ----RRRLVETKRNREIAQLKK 789
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERL--RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKLLEKEM 522
|
170 180 190
....*....|....*....|....*....|....
gi 355390331 790 EQRR----QEFQIRALESQKR-QQEMVLRRKTQE 818
Cdd:pfam17380 523 EERQkaiyEEERRREAEEERRkQQEMEERRRIQE 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
633-1014 |
5.61e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 633 QADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcYTEEKANKIKADYEK 712
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 713 RLREMNRDLQKLQAAQKEHarllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQR----RRLVETKRNReIAQLK 788
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEA----------EAEIEELEAQIEQLKEELKALREALDELRAEltllNEEAANLRER-LESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 789 KEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPpmldsgaevSASTTSSEAESGARSVSS 868
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA---------SLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 869 IVRQWNRKInhflgdhpaptvngtRPARKKFQKKGASQSfskAARLKWQSLERRIIDIVMQRMTIVNLEADMerLIKKRE 948
Cdd:TIGR02168 902 ELRELESKR---------------SELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEE--AEALEN 961
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331 949 ELFLLQEALRRKRERLQAEspeeekgLQELA-------EEIEVLAANIDYINDGITDCQATIVQLEETKEELD 1014
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENK-------IKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-1084 |
7.93e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 626 EEKEVNFQADLADLTCEIEIKQKLIDELEnsqRRLQTLKHQYEE----KLILLQNKIRDTQLERDRVLQNLSTME--CYT 699
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALR---EELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEalLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 700 -EEKANKIKADYEKRLREMNRDLQKLQ----AAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRR 774
Cdd:COG4913 371 lGLPLPASAEEFAALRAEAAALLEALEeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 775 LVETKRNREIA--------QLKKEQRRQEFQI-RALESQK-------RQQEMVLRrktqevsALRRLakPMSERVAGRaG 838
Cdd:COG4913 449 LAEALGLDEAElpfvgeliEVRPEEERWRGAIeRVLGGFAltllvppEHYAAALR-------WVNRL--HLRGRLVYE-R 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 839 LKPpmldsgAEVSASTTSSEAESGARSVS---SIVRQW-NRKINHF-----------LGDHP-APTVNG------TRpAR 896
Cdd:COG4913 519 VRT------GLPDPERPRLDPDSLAGKLDfkpHPFRAWlEAELGRRfdyvcvdspeeLRRHPrAITRAGqvkgngTR-HE 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 897 KKFQKKGASQS---FSKAARLKWqsLERRIidivmqrmtiVNLEADMERLIKKREELFLLQEALRRKRERLQ--AESPEE 971
Cdd:COG4913 592 KDDRRRIRSRYvlgFDNRAKLAA--LEAEL----------AELEEELAEAEERLEALEAELDALQERREALQrlAEYSWD 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 972 EKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDstdtsvvisscslaEARLLLDNFLKASIDKGLQVAQK 1051
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE--------------ELEEELDELKGEIGRLEKELEQA 725
|
490 500 510
....*....|....*....|....*....|...
gi 355390331 1052 EAQIRLLEGRLRQTDMAGSSQNHLLLDALREKA 1084
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
623-896 |
9.36e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 623 SDPEEKEVnfQADLADLTCEIeikQKLIDELENSQRRLQTLKHQYEEklilLQNKIRDTQLERDRVLQNLSTmecyTEEK 702
Cdd:COG3883 14 ADPQIQAK--QKELSELQAEL---EAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAE----AEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 703 ANKIKADYEKRLREMNRD----------------------LQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKV 760
Cdd:COG3883 81 IEERREELGERARALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 761 ALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLK 840
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331 841 PPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPAR 896
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
484-822 |
1.65e-08 |
|
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: 59.70 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 484 EIEELRTKLLESEAMNESLRRSLSRASARSpyslgaspaapafgGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSP 563
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRL--------------DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 564 EKEAFKKraKLQQEnseetdeneaeeeeeerdesgceeeegrededeDSGSEESLVDSDSDPEEKE---VNFQADLADLt 640
Cdd:TIGR02169 741 ELEEDLS--SLEQE---------------------------------IENVKSELKELEARIEELEedlHKLEEALNDL- 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 641 cEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLER---DRVLQNLSTMECYTEEKANKIKADYE---KRL 714
Cdd:TIGR02169 785 -EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKK 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 715 REMNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKkakvalmKQMREEQQRRRLVETKRNRE---IAQLKKEQ 791
Cdd:TIGR02169 864 EELEEELEELEAALRD----------LESRLGDLKKERDELE-------AQLRELERKIEELEAQIEKKrkrLSELKAKL 926
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 355390331 792 RRQEFQIRALESQKRQQE-------------MVLRRKTQEVSAL 822
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEeipeeelsledvqAELQRVEEEIRAL 970
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
670-1062 |
4.62e-08 |
|
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: 57.60 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 670 KLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKAD---YEKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELK 746
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRVAELK---EELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 747 KLQAEVAEMKKAKVALMKQMREEQQRRRLVE----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKT 816
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 817 QEvsaLRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTS------SEAESGA-----RSVSSIVRQWNRKINhFLGDHP 885
Cdd:pfam07888 185 EE---LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEAlleelRSLQERLNASERKVE-GLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 886 APTVNgtrparkkfqKKGASQSFSKAARLKWQSLERRIIDIVMQ-----------RMTIV-NLEADMERLIKkreelflL 953
Cdd:pfam07888 261 SSMAA----------QRDRTQAELHQARLQAAQLTLQLADASLAlregrarwaqeRETLQqSAEADKDRIEK-------L 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 954 QEALRRKRERLQAESPEEEKGLQELAEEievlaanidyindgiTDCqaTIVQLEETKEELDStdtsvvisscslaearll 1033
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEVELGRE---------------KDC--NRVQLSESRRELQE------------------ 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 355390331 1034 ldnfLKASidkgLQVAQKEAQ------------IRLLEGRL 1062
Cdd:pfam07888 369 ----LKAS----LRVAQKEKEqlqaekqelleyIRQLEQRL 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
633-838 |
9.07e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 633 QADLADLTCEIEIKQKLIDELENsqrRLQTLKHQYEEKLILLQNKIRDTQLE----RDRVLQNLSTMECYteekaNKIKA 708
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRA---ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYL-----KYLAP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 709 DYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLK 788
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-------AELAELQ 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 355390331 789 KEQRRQEFQIRALESQKRQQEmvLRRKTQEVSALR-RLAKPMSERVAGRAG 838
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAA--ERTPAAGFAALKgKLPWPVSGRVVRRFG 268
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-1105 |
1.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 702 KANKIKAdyEKRLREMNRDLQKLQAAQKEharlLKNQsryereLKKL--QAEVA--------EMKKAKVALM-KQMREEQ 770
Cdd:COG1196 171 KERKEEA--ERKLEATEENLERLEDILGE----LERQ------LEPLerQAEKAeryrelkeELKELEAELLlLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 771 QRRRLVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRrlakpmservagraglkppmldsGAEV 850
Cdd:COG1196 239 AELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-----------------------AEEY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 851 SASTTSSEAEsgarsvssivrqwnrkinhflgdhpaptvngtrpARKKFQKKGASQSFSKAARLKWQ--SLERRIIDIVM 928
Cdd:COG1196 292 ELLAELARLE----------------------------------QDIARLEERRRELEERLEELEEElaELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 929 QRMT----IVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIV 1004
Cdd:COG1196 338 ELEEleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1005 QLEETKEELDStdtsvvisscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKA 1084
Cdd:COG1196 418 RLEEELEELEE----------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
410 420
....*....|....*....|.
gi 355390331 1085 EAHPELQALIYNVQQENGYAS 1105
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
626-834 |
1.47e-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: 56.61 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 626 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDtqLERDRVLQNLSTMECYTEeKANK 705
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELS-KLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 706 IKADYEKRLREMNRDLQKL----QAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRn 781
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL- 884
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 355390331 782 reiAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 834
Cdd:TIGR02169 885 ---GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
665-841 |
2.22e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 55.63 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 665 HQYEEKLILLQNKI-RDTQLE--RDRVLQNLS----------TMECYTEEKANKIKADYEKRLREMNRDLQKLQ---AAQ 728
Cdd:COG2433 346 DAYKNKFERVEKKVpPDVDRDevKARVIRGLSieealeelieKELPEEEPEAEREKEHEERELTEEEEEIRRLEeqvERL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 729 KEHARLLKNQSR-YERELKKLQAEVAEMKKakvalmkQMREEQQRRRLVeTKRNREIAQLKKEQRRQEFQIRALESQ--- 804
Cdd:COG2433 426 EAEVEELEAELEeKDERIERLERELSEARS-------EERREIRKDREI-SRLDREIERLERELEEERERIEELKRKler 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 355390331 805 -KRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKP 841
Cdd:COG2433 498 lKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
362-982 |
2.32e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 362 KYANRARNIKNKVVVNQDK---TSQQISALRAEIARLQMELMEYKAGKRVIgEDGAEGYSDLFRENAMLQKENGALRLRV 438
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 439 KAMQEAIDAINNRVTQLMSQEANLL-LAKAGDGNEAIGALIQNY---IREIEELRTKLleseamnESLRRSLSRasarsp 514
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKeLKEKAEEYIKLSEFYEEYldeLREIEKRLSRL-------EEEINGIEE------ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 515 yslgaspaapafggspasSMEDASEVIRRakqdLERLKKKEVRQRRkspEKEAFKKRAKLQQENSEETDENEAEEEEEER 594
Cdd:PRK03918 329 ------------------RIKELEEKEER----LEELKKKLKELEK---RLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 595 DESGCEEEEGredededsgseESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKlill 674
Cdd:PRK03918 384 LTPEKLEKEL-----------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE---- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 675 qnkirdtqlERDRVlqnlstMECYTEEKAN--KIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRY------ERELK 746
Cdd:PRK03918 449 ---------HRKEL------LEEYTAELKRieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkelEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 747 KLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRK----TQEV-SA 821
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELeER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 822 LRRLAKPMSERVAgraglkppMLDSGAEV--------SASTTSSEAESGARSVSSIVRQWNRKINHFLGDHpapTVNGTR 893
Cdd:PRK03918 594 LKELEPFYNEYLE--------LKDAEKELereekelkKLEEELDKAFEELAETEKRLEELRKELEELEKKY---SEEEYE 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 894 PARKKFQKKgASQSFSKAARLKwqSLERRIIDIvmqRMTIVNLEADMERLIKKREELFLLQ------EALRRKRERLQAE 967
Cdd:PRK03918 663 ELREEYLEL-SRELAGLRAELE--ELEKRREEI---KKTLEKLKEELEEREKAKKELEKLEkalervEELREKVKKYKAL 736
|
650
....*....|....*...
gi 355390331 968 spEEEKGL---QELAEEI 982
Cdd:PRK03918 737 --LKERALskvGEIASEI 752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
642-824 |
3.83e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 642 EIEIKQKLIDELENSQRRLQTLKHQYEEKLILL-------QNKIRDTQLERDRVLQNLSTMECYTE-------------E 701
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeklniQKNIDKIKNKLLKLELLLSNLKKKIQknkslesqiselkK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 702 KANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKR 780
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKE 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 355390331 781 NREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRR 824
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
482-1017 |
3.86e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 482 IREIEELR-----TKLLESEAMNESLRRSlsrASARSPYSLGASPAAPAFGGSPASSMEDASEV-----IRRA--KQDLE 549
Cdd:PTZ00121 1229 VKKAEEAKkdaeeAKKAEEERNNEEIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKkkadeAKKAeeKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 550 RLKKKEVRQRRKSPEK---EAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPE 626
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 627 EKEVNFQADLADLTCEiEIKQKlIDEL---ENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTmECYTEEKA 703
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAE-EDKKK-ADELkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 704 NKiKADYEKRLREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVAlmKQMREEQQRRRLVET 778
Cdd:PTZ00121 1463 KK-KAEEAKKADEAKKKAEEAKKADEakkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 779 KRNREIA---QLKK-EQRRQEFQIRALESQKRQQE---MVLRR----KTQEVSALRRLAKPMSERVAGRAGLKPPMLDSG 847
Cdd:PTZ00121 1540 KKAEEKKkadELKKaEELKKAEEKKKAEEAKKAEEdknMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 848 AEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKA---ARLKWQSLERRii 924
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEALKKE-- 1697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 925 diVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEiEVLAANIDYINDGITDCQATIV 1004
Cdd:PTZ00121 1698 --AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIR 1774
|
570
....*....|....*
gi 355390331 1005 QLEET--KEELDSTD 1017
Cdd:PTZ00121 1775 KEKEAviEEELDEED 1789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
626-855 |
5.18e-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: 54.69 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 626 EEKEVNFQADLADLTCEIEIKQKLIDELEN-SQRRLQTL-------KHQYEEKLILLQNKIRDTQLERdrvlqnlstmec 697
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKrLEEIEQLLeelnkkiKDLGEEEQLRVKEKIGELEAEI------------ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 698 yteEKANKIKADYEKRLREMNRDLQKLQAaqkEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVE 777
Cdd:TIGR02169 304 ---ASLERSIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 355390331 778 TKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTT 855
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
724-1024 |
1.13e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 724 LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreEQQRRRLVETkrNREIAQLKKEQRRQEFQIRALES 803
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAAL--ARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 804 QKRQQEMVLRRKTQEVSalRRLakpmseRVAGRAGLKPPMLdsgaevsasttsseaesgarsvssivrqwnrkinhFLgd 883
Cdd:COG4942 91 EIAELRAELEAQKEELA--ELL------RALYRLGRQPPLA-----------------------------------LL-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 884 hpaptvngtrparkkFQKKGASQSFSKAARLKwQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRER 963
Cdd:COG4942 126 ---------------LSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 355390331 964 LQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISS 1024
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
649-827 |
1.25e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 649 LIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKLQAAQ 728
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL--------EQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 729 KEHARLLKnqsRYERELKKLQAEVAEMKKAKVALM---KQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALEsqK 805
Cdd:COG4372 97 AQAQEELE---SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE--Q 171
|
170 180
....*....|....*....|..
gi 355390331 806 RQQEMVLRRKTQEVSALRRLAK 827
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEAN 193
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
673-818 |
1.28e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 673 LLQNKIRDTQLERDRVLQNLST-MECYTEEK-------ANKIKADYEKRLREMNRDLQKLQAaqkehaRLLKNQSRYERE 744
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKeAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEK------RLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 745 LKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR------EIAQLKKEQRRQEfQIRALESQKRQQEMVLRRKTQE 818
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqeleRISGLTAEEAKEI-LLEKVEEEARHEAAVLIKEIEE 180
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
644-810 |
1.30e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 50.92 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 644 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnkirdTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQK 723
Cdd:pfam14988 22 KLWNQYVQECEEIERRRQELASRYTQQTAELQ-----TQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 724 LQAA-----QKEHARLLKNQSRYERELKKLQA-EVAEMKKAKVALMKQMREEQQRRRLVETKRN--REIAQLKKEQRRQE 795
Cdd:pfam14988 97 VRAEtaekdREAHLQFLKEKALLEKQLQELRIlELGERATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQLI 176
|
170
....*....|....*
gi 355390331 796 FQIRALESQKRQQEM 810
Cdd:pfam14988 177 QETQALEAIKSKLEN 191
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
643-831 |
1.51e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 52.37 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 643 IEIKQ---KLIDELENSQRRLQTLKHQyeeklillQNKIRDTQLERDRVLQNLSTMECYTE----EKANKIKADyEKRLr 715
Cdd:pfam15742 62 AELKQaqqKLLDSTKMCSSLTAEWKHC--------QQKIRELELEVLKQAQSIKSQNSLQEklaqEKSRVADAE-EKIL- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 716 emnrDLQKlqaaQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETK-----------RNREi 784
Cdd:pfam15742 132 ----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNvnelqqqvrslQDKE- 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 355390331 785 AQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSE 831
Cdd:pfam15742 203 AQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSS 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
650-804 |
1.61e-06 |
|
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: 51.08 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 650 IDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKaDYEKRLrEMNRDLQKLQAAQK 729
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQL-GNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355390331 730 EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQ 804
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
364-1029 |
2.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 364 ANRARNIKNKVVVNQDKTSQQI-SALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRvKAMQ 442
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 443 EAIDAINNRVTQLMSQEANLL--LAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNES------LRRSLSRASARSP 514
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 515 YSLGASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEK---EAFKKRA----KLQQENSEETDENEA 587
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDEAKKKAeedkKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 588 EEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQY 667
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 668 EEKLILLQNKIRDTQL---ERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERE 744
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAkkaEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 745 LKKLQAEVA-EMKKAKVALMKQMREEQQRRRLVETKRNREiAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALR 823
Cdd:PTZ00121 1578 MALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 824 RLAKPMSERVAGRAglkppmldSGAEVSASTTSSEAESGARSVSSIVRQwnrkinhflgdhpaptvngTRPARKKFQ-KK 902
Cdd:PTZ00121 1657 EENKIKAAEEAKKA--------EEDKKKAEEAKKAEEDEKKAAEALKKE-------------------AEEAKKAEElKK 1709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 903 GASQSFSKAARLKWQSLERRIidivmqrmTIVNLEADMERLIKKREELFLLQE-----ALRRKRERLQAESPEEEKGL-- 975
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKI--------KAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAEEIRKEKEAvi 1781
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 355390331 976 -QELAEEIEVLAANIDYINDGITDCQATIVQ--------LEETKEELDSTDTSVVISSCSLAE 1029
Cdd:PTZ00121 1782 eEELDEEDEKRRMEVDKKIKDIFDNFANIIEggkegnlvINDSKEMEDSAIKEVADSKNMQLE 1844
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
646-834 |
2.09e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 646 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLsTMECYTEEKANKIKADYEKRlREMNRDLQKLQ 725
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL-YQEEQERKERQKEREEAEKK-ARQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 726 AAQKEHARLLKnqsryerelkklQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQefqiraLESQK 805
Cdd:pfam13868 242 EEQIELKERRL------------AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ------IEERE 303
|
170 180
....*....|....*....|....*....
gi 355390331 806 RQQEMVLRRKTQEVSALRRLAKPMSERVA 834
Cdd:pfam13868 304 EQRAAEREEELEEGERLREEEAERRERIE 332
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
652-832 |
2.18e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 652 ELENSQRRLQTLKhqyEEKLILLQNKIRDT---QLER----DRVLQNLstmecyteEKANKIKADYEKRLREMNRDLQKL 724
Cdd:pfam17380 354 RQEERKRELERIR---QEEIAMEISRMRELerlQMERqqknERVRQEL--------EAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 725 QA--AQKEHAR---LLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKEQRRqefQIR 799
Cdd:pfam17380 423 EQirAEQEEARqreVRRLEEERAREMERVRLEEQE-RQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQRR---KIL 497
|
170 180 190
....*....|....*....|....*....|...
gi 355390331 800 ALESQKRQQEMVlrrktQEVSALRRLAKPMSER 832
Cdd:pfam17380 498 EKELEERKQAMI-----EEERKRKLLEKEMEER 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
741-1062 |
2.72e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 741 YERELKKLQAEVAEM--------KKAKVALMKQMREEQQRRRLVETKR--NREIAQLKKEQRRQEFQIRALESQKRQQEM 810
Cdd:TIGR02168 675 RRREIEELEEKIEELeekiaeleKALAELRKELEELEEELEQLRKELEelSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 811 VLRRKT-QEVSALRRLAKPMSERVAG---RAGLKPPMLDSGAEVSASttsseaESGARSVSSIVRQWNRKINhflgdhpa 886
Cdd:TIGR02168 755 ELTELEaEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKAL------REALDELRAELTLLNEEAA-------- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 887 ptvngtrparkkfqkkgasqsfskAARLKWQSLERRIID----IVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRE 962
Cdd:TIGR02168 821 ------------------------NLRERLESLERRIAAterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 963 RLQAESPEEE-------KGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSvvISSCSLAEARLLLD 1035
Cdd:TIGR02168 877 ALLNERASLEealallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN--LQERLSEEYSLTLE 954
|
330 340
....*....|....*....|....*..
gi 355390331 1036 NFLKASIDKGLQVAQKEAQIRLLEGRL 1062
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
656-837 |
3.14e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 656 SQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQK--EHAR 733
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERkrELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 734 LLKNQSRYE----RELKKLQ-----------AEVAEMKKAKV-------------ALMKQMREEQqrrrlvETKRNREIA 785
Cdd:pfam17380 365 IRQEEIAMEisrmRELERLQmerqqknervrQELEAARKVKIleeerqrkiqqqkVEMEQIRAEQ------EEARQREVR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 355390331 786 QLKKEQRRQEFQIRaLESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRA 837
Cdd:pfam17380 439 RLEEERAREMERVR-LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
714-830 |
3.33e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 714 LREMNRDLQKLQAAQkehARLLKNQSRYERELKKLQAEVAEMKK-------------AKVALMKQMREEQQRRRLvetkr 780
Cdd:COG1842 32 IRDMEEDLVEARQAL---AQVIANQKRLERQLEELEAEAEKWEEkarlalekgredlAREALERKAELEAQAEAL----- 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 355390331 781 NREIAQLKKEQRRQEFQIRALESQ----KRQQEMVL-RRKTQEvsALRRLAKPMS 830
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKleelKAKKDTLKaRAKAAK--AQEKVNEALS 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
911-1112 |
4.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 911 AARLKWQSLERRIIDivmQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANID 990
Cdd:COG1196 229 LLLLKLRELEAELEE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 991 YINDGITDCQATIVQLEETKEELDSTDTSVVIsscSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGS 1070
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 355390331 1071 SQNHLLLDALREKAEAHPELQALIynvQQENGYASTDEEISE 1112
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEE 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
650-833 |
4.20e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 650 IDELENSQRRLQTLKHQY-----EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKL 724
Cdd:COG4913 264 YAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 725 QA----AQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQrrrlvetkrnrEIAQLKKEQRRQEFQIRA 800
Cdd:COG4913 344 EReierLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE-----------ALEEELEALEEALAEAEA 412
|
170 180 190
....*....|....*....|....*....|...
gi 355390331 801 LESQKRQQemvLRRKTQEVSALRRLAKPMSERV 833
Cdd:COG4913 413 ALRDLRRE---LRELEAEIASLERRKSNIPARL 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
712-832 |
5.84e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 712 KRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK--AKVALMKQMREEQQRRRLVETKRNREIAQLKK 789
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 355390331 790 EQRRQEfQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 832
Cdd:COG4717 151 LEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
626-818 |
7.05e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 626 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLstMECYTEEKANK 705
Cdd:pfam13868 41 EERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV--ERIQEEDQAEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 706 IKADYEKR-----LREMNRDLQKLQAAQK-----EHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRl 775
Cdd:pfam13868 119 EEKLEKQRqlreeIDEFNEEQAEWKELEKeeereEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ- 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 355390331 776 vETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQE 818
Cdd:pfam13868 198 -DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQ 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
719-1084 |
2.04e-05 |
|
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: 49.45 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 719 RDLQKLQAAQKEHARLLKNQSRYErELKKLQAEVAEMKKAKVALMKQMREEQQRRrlvetkrnreiaqlKKEQRRQEFQI 798
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFN-TLESAELRLSHLHFGYKSDETLIASRQEER--------------QETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 799 RALESQKRQqemVLRRKTQEVSALR-RLAKPMSERVAGRAGLKPpMLDSGAEvsasTTSSEAESgARSVSSIVRQWNRKI 877
Cdd:pfam12128 293 RTLDDQWKE---KRDELNGELSAADaAVAKDRSELEALEDQHGA-FLDADIE----TAAADQEQ-LPSWQSELENLEERL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 878 NHFLGDHpaptvngtRPARKKFQK---KGASQSFSKAARLKwQSLERriidivmQRMTIVNLEADMERLIKKreelflLQ 954
Cdd:pfam12128 364 KALTGKH--------QDVTAKYNRrrsKIKEQNNRDIAGIK-DKLAK-------IREARDRQLAVAEDDLQA------LE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 955 EALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLL 1034
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRR 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 355390331 1035 DNFLkasidkglqVAQKEAQIRLLE--GRLRQTDMAGSSQNHLLLDALREKA 1084
Cdd:pfam12128 502 DQAS---------EALRQASRRLEErqSALDELELQLFPQAGTLLHFLRKEA 544
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
631-836 |
2.60e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 631 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNK---IRDTQLErdrvLQNLSTMECYTEEKANKIK 707
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeIHDLEIQ----LTAIKTSEEHYLKEVEDLK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 708 ADYEK-RLR--EMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvETKRNREI 784
Cdd:pfam05483 478 TELEKeKLKniELTAHCDKLLLENKE---LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----EMNLRDEL 550
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331 785 AQLKKE--QRRQEFQIRALESQK--RQQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:pfam05483 551 ESVREEfiQKGDEVKCKLDKSEEnaRSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
631-805 |
2.74e-05 |
|
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: 48.86 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 631 NFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEE-KANKIKAD 709
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 710 YEKRLREMNRDLQKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMreeqqrrrlveTKRNREIAQLKK 789
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----------SSLEKELEKAKK 624
|
170
....*....|....*.
gi 355390331 790 EQRRQEFQIRALESQK 805
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKK 640
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
717-827 |
3.62e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 45.26 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 717 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRlvetkrnREIAQLKKE-QRRQE 795
Cdd:pfam03938 7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKE-------QELQKKEQElQQLQQ 79
|
90 100 110
....*....|....*....|....*....|..
gi 355390331 796 FQIRALesQKRQQEMVLRRKTQEVSALRRLAK 827
Cdd:pfam03938 80 KAQQEL--QKKQQELLQPIQDKINKAIKEVAK 109
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
671-823 |
3.86e-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: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 671 LILLQNKIRDTQLERDRVLQNLstmecytEEKANKIKADYE---KRLREMNRDLQKLQaaQKEHARLLKNQSRYERELKK 747
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDresDRNQELQKRIRLLE--KREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355390331 748 LQAEVAEMKKAKvalmKQMREEQQRRRLVETKRNrEIAQLKKEQRRQEFQIRALESQK---RQQEMVLRRKTQEVSALR 823
Cdd:pfam05557 82 KKYLEALNKKLN----EKESQLADAREVISCLKN-ELSELRRQIQRAELELQSTNSELeelQERLDLLKAKASEAEQLR 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
654-818 |
4.12e-05 |
|
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: 46.84 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 654 ENSQRRLQTLkHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyTE-EKANKIKADYEKRLREMNRDLQKLQAAQKEHA 732
Cdd:COG1579 3 PEDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALE--ARlEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 733 RLLkNQSRYERELKKLQAEVAEMKKAKVALMKQMRE-----EQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQ 807
Cdd:COG1579 80 EQL-GNVRNNKEYEALQKEIESLKRRISDLEDEILElmeriEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 355390331 808 QEMVLRRKTQE 818
Cdd:COG1579 159 EELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-827 |
4.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 378 QDKTSQQISALRAEIARLQMELMEYKAgkrvigedgAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMS 457
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEK---------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 458 QEANlllakagdgneaigalIQNYIREIEELRTKLLESEAMN-ESLRRSLSRASARspyslgaspaapafggspassMED 536
Cdd:COG4717 168 LEAE----------------LAELQEELEELLEQLSLATEEElQDLAEELEELQQR---------------------LAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 537 ASEVIRRAKQDLERLKKKEvrqRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEE 616
Cdd:COG4717 211 LEEELEEAQEELEELEEEL---EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 617 SLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTME 696
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 697 CYTEEKA--NKIKADYEKRLREMNRDLQKLQAAQKEHARLlknQSRYERELKKLQAEVAEMKKAkvALMKQMREEQQRRR 774
Cdd:COG4717 368 LEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEEL---EEQLEELLGELEELLEALDEE--ELEEELEELEEELE 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 355390331 775 LVEtkrnREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEvSALRRLAK 827
Cdd:COG4717 443 ELE----EELEELREELAELEAELEQLEEDGELAELLQELEELK-AELRELAE 490
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
701-823 |
4.55e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 44.52 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 701 EKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKnqsRYERELKKLQAEVAEMKKakvalmKQMREEQQRRRLVETKR 780
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE---ELEEERRQAEEEAERLEQ------KRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 355390331 781 NREiaqlkKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALR 823
Cdd:pfam20492 73 MEA-----EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
369-1060 |
5.41e-05 |
|
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: 48.04 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 369 NIKNKVVVNQDKTSQQIsALRAEIARLQMElmEYKAGKRVIgEDGAEGYSDLFRENAMLQKENGALRLrvkamqeaidaI 448
Cdd:pfam02463 131 SPEAYNFLVQGGKIEII-AMMKPERRLEIE--EEAAGSRLK-RKKKEALKKLIEETENLAELIIDLEE-----------L 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 449 NNRVTQLMSQEANLL-----LAKAGDGNEAIGALIQNYIRE--IEELRTKLLESEAMNESLRRSLSRA---SARSPYSLG 518
Cdd:pfam02463 196 KLQELKLKEQAKKALeyyqlKEKLELEEEYLLYLDYLKLNEerIDLLQELLRDEQEEIESSKQEIEKEeekLAQVLKENK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 519 ASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESG 598
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 599 CEEEEGREDEDEDSGSEESLVDSDSdpeEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKI 678
Cdd:pfam02463 356 EEEEELEKLQEKLEQLEEELLAKKK---LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-EI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 679 RDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKA 758
Cdd:pfam02463 432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 759 KVALMKQMR------EEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 832
Cdd:pfam02463 512 LLALIKDGVggriisAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 833 VAGRAGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINH-FLGDHPAPTVNGTRPARKKFQKKGASQSFSKA 911
Cdd:pfam02463 592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKeSAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 912 ARLKWQSLErRIIDIVMQRMTIVNLEADME----RLIKKREELFLLQEALRRK---RERLQAESPEEEKGLQELAEEIEV 984
Cdd:pfam02463 672 TKELLEIQE-LQEKAESELAKEEILRRQLEikkkEQREKEELKKLKLEAEELLadrVQEAQDKINEELKLLKQKIDEEEE 750
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 355390331 985 LAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEG 1060
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
700-989 |
5.84e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 700 EEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKK---AKVALMKQMREEQQRRRLV 776
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEqlqAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 777 ETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTS 856
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 857 SEAESGArsVSSIVRQWNRKINHFLGDHPAptvnGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNL 936
Cdd:COG4372 190 KEANRNA--EKEEELAEAEKLIESLPRELA----EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 355390331 937 EADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANI 989
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
715-819 |
6.21e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 715 REMNRDL-QKLQAAQKEHARLLKNQSRYER-ELKKLQAEVAEMKKakvalmkQMREE----QQRR----RLVETKRNREI 784
Cdd:pfam15709 328 REQEKASrDRLRAERAEMRRLEVERKRREQeEQRRLQQEQLERAE-------KMREEleleQQRRfeeiRLRKQRLEEER 400
|
90 100 110
....*....|....*....|....*....|....*
gi 355390331 785 AQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEV 819
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQEL 435
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
646-826 |
7.25e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 646 KQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNlstmecyTEEKANKIKADYEK---------RLR- 715
Cdd:pfam15709 321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQE-------QLERAEKMREELELeqqrrfeeiRLRk 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 716 -------------EMNRDLQkLQAAQkEHARLlkNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR 782
Cdd:pfam15709 394 qrleeerqrqeeeERKQRLQ-LQAAQ-ERARQ--QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLM 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 355390331 783 EIAqlkkEQRRQEFQIRALESQ-KRQQEMVLRRKTQEVSAlrRLA 826
Cdd:pfam15709 470 EMA----EEERLEYQRQKQEAEeKARLEAEERRQKEEEAA--RLA 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
651-825 |
7.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 651 DELENSQRRLQTLKhqyeeklilLQNKIRDTQLERDRVLQNLSTMEcyteEKANKIKADYEKRLREMNRDLQKLQAAQKE 730
Cdd:COG3206 189 KELEEAEAALEEFR---------QKNGLVDLSEEAKLLLQQLSELE----SQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 731 HARLLKNQ--SRYERELKKLQAEVAEMK-------------KAKVA-LMKQMREEQQrRRLVETKRNREIAQLKK---EQ 791
Cdd:COG3206 256 LPELLQSPviQQLRAQLAELEAELAELSarytpnhpdvialRAQIAaLRAQLQQEAQ-RILASLEAELEALQAREaslQA 334
|
170 180 190
....*....|....*....|....*....|....
gi 355390331 792 RRQEFQIRALESQKRQQEmvLRRKTQEVSALRRL 825
Cdd:COG3206 335 QLAQLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1563-1600 |
1.08e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.14 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 355390331 1563 NFTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
651-798 |
1.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 651 DELENSQRRLQTLKHQYEEKLILLQNKIRDTqlerDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK-LQAAQK 729
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEA----EKLKEEL-------EEKKEKLQEEEDKLLEEAEKEAQQaIKEAKK 584
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 355390331 730 EHARLLknqsryeRELKKLQAEVAEMKKAKVAlmkqmreEQQRRRLVETKRNREIAQLKKEQRRQEFQI 798
Cdd:PRK00409 585 EADEII-------KELRQLQKGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1286-1321 |
1.33e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.79 E-value: 1.33e-04
10 20 30
....*....|....*....|....*....|....*...
gi 355390331 1286 QCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1321
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
645-788 |
1.52e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 645 IKQKLIDELENSQRRLQTLKhQYEEKLILLQNKIRDTQ--LERD-RVLQNLstmecytEEKANKIKADYEKRLREmnrdl 721
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLM-KELELLNSIKPKLRDRKdaLEEElRQLKQL-------EDELEDCDPTELDRAKE----- 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 722 qKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLK 788
Cdd:smart00787 212 -KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLK 277
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
483-901 |
1.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 483 REIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDASEVIRRA--KQDLERLKKKEvrQRR 560
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAeeAKKADEAKKAE--EAK 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 561 KSPE-KEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADL 639
Cdd:PTZ00121 1535 KADEaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 640 TCEIEIKQKLIDELENSQRRLQTLKHQYEEKlillqnKIRDTQLERdrvlqnlstmecytEEKANKIKADYEKRLREmnR 719
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEE------KKKAEELKK--------------AEEENKIKAAEEAKKAE--E 1672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 720 DLQKLQAAQKEHarllKNQSRYERELKKLQAEvaemkKAKVALMKQMREEQQRR----RLVETKRNREIAQLKKEQrrqe 795
Cdd:PTZ00121 1673 DKKKAEEAKKAE----EDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKaeelKKAEEENKIKAEEAKKEA---- 1739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 796 fqiralESQKRQQEMvLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAESGARSV---SSIVRQ 872
Cdd:PTZ00121 1740 ------EEDKKKAEE-AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFANIIE 1812
|
410 420 430
....*....|....*....|....*....|....*....
gi 355390331 873 WNRKINHFLGDHP----------APTVNGTRPARKKFQK 901
Cdd:PTZ00121 1813 GGKEGNLVINDSKemedsaikevADSKNMQLEEADAFEK 1851
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1529-1560 |
1.73e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 40.37 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|..
gi 355390331 1529 NAHKDWVCALAFIPGRPMLLSACRAGVIKVWN 1560
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
277-796 |
1.84e-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: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 277 SERLKRTGATGERAKEGISINCGLLALGNVISALGDQSK-KVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRdfm 355
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN--- 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 356 eTLNTLKYANRARNIKNKVVVNQDKTSQQISALRAE-IARLQMELMEYKAGKRVIGEDGAEGYSDL--------FRENAM 426
Cdd:pfam02463 605 -LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKSEVKASLSeltkelleIQELQE 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 427 LQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSL 506
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 507 SRASARSPYSLGASpaapafggspassmEDASEVIRRAKQDLERLKKKEV---RQRRKSPEKEAFKKRAKLQQENSEETD 583
Cdd:pfam02463 764 EEKSELSLKEKELA--------------EEREKTEKLKVEEEKEEKLKAQeeeLRALEEELKEEAELLEEEQLLIEQEEK 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 584 ENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDpEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTL 663
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ-ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 664 KHQYEEKLILLQNKIrdtQLERDRVLQNLStmECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYER 743
Cdd:pfam02463 909 LNLLEEKENEIEERI---KEEAEILLKYEE--EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 355390331 744 ELKKLQAEVAEMKKAKvalMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEF 796
Cdd:pfam02463 984 EEKEERYNKDELEKER---LEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
543-1110 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 543 RAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEE--EEEERDESGCEEEEGREDEDedsgSEESLVD 620
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKklQEEELKLLAKEEEELKSELL----KLERRKV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 621 SDSDPEEKEVNfqadladltcEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTE 700
Cdd:pfam02463 311 DDEEKLKESEK----------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 701 EKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKR 780
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 781 NREIAQLKKEqRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSAST--TSSE 858
Cdd:pfam02463 461 LKDELELKKS-EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlgVAVE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 859 AESGARSVSSIVRQWNRKINHFLGDHpapTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQrmtiVNLEA 938
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQK---LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ----LDKAT 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 939 DMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDT 1018
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1019 SVVISSCSLAEARL---LLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSsqnhLLLDALREKAEAHPELQALIY 1095
Cdd:pfam02463 693 EILRRQLEIKKKEQrekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE----EEEEEEKSRLKKEEKEEEKSE 768
|
570
....*....|....*
gi 355390331 1096 NVQQENGYASTDEEI 1110
Cdd:pfam02463 769 LSLKEKELAEEREKT 783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-836 |
2.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 626 EEKEVNFQADLAdltceieikQKLIDELENSQRRLQTLKHQYEeklILLQnkIRDTQLERDRVLQNLSTmecyteekank 705
Cdd:COG4913 219 EEPDTFEAADAL---------VEHFDDLERAHEALEDAREQIE---LLEP--IRELAERYAAARERLAE----------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 706 ikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRR--RLvetkrNRE 783
Cdd:COG4913 274 --LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleQL-----ERE 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 355390331 784 IAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
708-963 |
2.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 708 ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSR------YERELKKLQAEVAEMKKAKVALMK-QMREEQQRRRLVETKr 780
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDDLAAlEEQLEELEAELEELE- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 781 nREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVS-ALRRLAKPMSERVAGRAglkppmldSGAEVSASTTSSEA 859
Cdd:COG4913 706 -EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAALGDA--------VERELRENLEERID 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 860 ESGARsVSSIVRQWNRKINHFLGDHPAPTVNGTRparkkfqkkgasqsfSKAARLKWQSLERRIIDIVmqrmtIVNLEAD 939
Cdd:COG4913 777 ALRAR-LNRAEEELERAMRAFNREWPAETADLDA---------------DLESLPEYLALLDRLEEDG-----LPEYEER 835
|
250 260
....*....|....*....|....*.
gi 355390331 940 MERLIKKREELFL--LQEALRRKRER 963
Cdd:COG4913 836 FKELLNENSIEFVadLLSKLRRAIRE 861
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
717-827 |
2.67e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 43.29 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 717 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRrrlvetKRNREIAQLKKE--QRRQ 794
Cdd:COG2825 31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQ------KKERELQKKQQElqRKQQ 104
|
90 100 110
....*....|....*....|....*....|....*
gi 355390331 795 EFQiRALesQKRQQEMV--LRRKTQEvsALRRLAK 827
Cdd:COG2825 105 EAQ-QDL--QKRQQELLqpILEKIQK--AIKEVAK 134
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1284-1321 |
2.72e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.99 E-value: 2.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 355390331 1284 PLQCVSMAEGHTKPILCLD--ATDELLFTGSKDRSCKMWN 1321
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
676-832 |
2.84e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 676 NKIRDTQLERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRyERELKKLQAEVAEM 755
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEE--ERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 756 KKakvalmKQMREEQQRRRLVETKRNREiaqlKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSER 832
Cdd:pfam13868 98 QE------REQMDEIVERIQEEDQAEAE----EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
642-1110 |
3.28e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 642 EIEIKQKLIDELENSQRRLQTLKHQYEEKLIL----LQNKIRdtqLERDRV-LQNLSTMECYTEEKANKIKADY------ 710
Cdd:pfam07111 54 ELEGSQALSQQAELISRQLQELRRLEEEVRLLretsLQQKMR---LEAQAMeLDALAVAEKAGQAEAEGLRAALagaemv 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 711 EKRLREMN-RDLQKLQAAQKEHARLLKNQsrYERELKKLQAEVAEMKKAKVALmkQMREEQQRRRLVETKRNREI--AQL 787
Cdd:pfam07111 131 RKNLEEGSqRELEEIQRLHQEQLSSLTQA--HEEALSSLTSKAEGLEKSLNSL--ETKRAGEAKQLAEAQKEAELlrKQL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 788 KKEQRRQEFQIRALES-QKRQQEMVLRRKTQEVSALRR--LAKPMSERVAGRAGLKPPMLDSGAEVSAST--TSSEAESG 862
Cdd:pfam07111 207 SKTQEELEAQVTLVESlRKYVGEQVPPEVHSQTWELERqeLLDTMQHLQEDRADLQATVELLQVRVQSLThmLALQEEEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 863 ARSVS--------------SIVRQWNRKINHFLGDHPAP------TVNGTRPARKKFQKKGASQSFSKAarLKWQSLERR 922
Cdd:pfam07111 287 TRKIQpsdslepefpkkcrSLLNRWREKVFALMVQLKAQdlehrdSVKQLRGQVAELQEQVTSQSQEQA--ILQRALQDK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 923 IIDIVMQRMTIVNLEADMERLikkreelfllQEAlrRKRERLQAESPEEEkglqelaeeievLAANIDYINDGITDCQAT 1002
Cdd:pfam07111 365 AAEVEVERMSAKGLQMELSRA----------QEA--RRRQQQQTASAEEQ------------LKFVVNAMSSTQIWLETT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1003 IVQLEETKEELDStdtsvvisscslaearllLDNFLKASIDK-----GLqVAQKE--AQIRLLEGRLRQTDMAGSSQNHL 1075
Cdd:pfam07111 421 MTRVEQAVARIPS------------------LSNRLSYAVRKvhtikGL-MARKValAQLRQESCPPPPPAPPVDADLSL 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 355390331 1076 LLDALR-EKAEAHPELQALIYNVQQENGYASTDEEI 1110
Cdd:pfam07111 482 ELEQLReERNRLDAELQLSAHLIQQEVGRAREQGEA 517
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
643-814 |
3.29e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 42.59 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 643 IEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMEcyteekankikadyekRLREMNRDLQ 722
Cdd:COG2882 11 LDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAA----------------QLRNYQQFIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 723 KLQAAQKEHARLLKN-QSRYERELKKLQaevaemkkakvalmkqmrEEQQRRRLVETKRNREIAQLKKEQRRQEfqiral 801
Cdd:COG2882 75 RLDEAIEQQQQQVAQaEQQVEQARQAWL------------------EARQERKALEKLKERRREEERQEENRRE------ 130
|
170
....*....|...
gi 355390331 802 esQKRQQEMVLRR 814
Cdd:COG2882 131 --QKELDELASRR 141
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
642-813 |
3.65e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 642 EIEIKQKLIDELENSQRR----LQTLKHQYEEKlillqnKIRDTQLERDRVLQnlstmECYTEEKANKIKADYEKRLREM 717
Cdd:pfam15709 367 QLERAEKMREELELEQQRrfeeIRLRKQRLEEE------RQRQEEEERKQRLQ-----LQAAQERARQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 718 NRDLQKlQAAQKEHARllknqsryERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnreiAQLKKEQRRQ--E 795
Cdd:pfam15709 436 QRKKQQ-EEAERAEAE--------KQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK----ARLEAEERRQkeE 502
|
170
....*....|....*....
gi 355390331 796 FQIR-ALESQKRQQEMVLR 813
Cdd:pfam15709 503 EAARlALEEAMKQAQEQAR 521
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
644-809 |
4.09e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 44.83 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 644 EIKQKLIDELENSQRRLQTL--KHQY-EEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKI--KADYEKRLRemn 718
Cdd:pfam15066 318 EVLQKLKHTNRKQQMQIQDLqcSNLYlEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVIleKNDINKTLQ--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 719 rDLQKLQAAQKEHARllknQSRYERELkkLQAEVAEMKKAKVALMKQ-MREEQQRRRLVE---------TKRNREIAQLK 788
Cdd:pfam15066 395 -NLQEILANTQKHLQ----ESRKEKET--LQLELKKIKVNYVHLQERyITEMQQKNKSVSqclemdktlSKKEEEVERLQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 355390331 789 --------------------KEQRRQEFQIRALESQKRQQE 809
Cdd:pfam15066 468 qlkgelekattsaldllkreKETREQEFLSLQEEFQKHEKE 508
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
633-802 |
4.70e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 633 QADLADLTCEIEIKQKLIDELENSQ---RRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIkAD 709
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLeelRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL-AD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 710 YEKRLREMNRDLQK-----LQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQ-----MREEQQRRRLVETK 779
Cdd:pfam07888 291 ASLALREGRARWAQeretlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELK 370
|
170 180
....*....|....*....|....*...
gi 355390331 780 RNREIAQLKKEQRRQEFQ-----IRALE 802
Cdd:pfam07888 371 ASLRVAQKEKEQLQAEKQelleyIRQLE 398
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
708-836 |
4.72e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.51 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 708 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEVAEM-KKAKVALMKQmrEEQQRRRLVETKRNRE-- 783
Cdd:pfam04012 21 EDPEKMLEQAIRDMQSeLVKARQALAQTIARQKQLERRLEQQTEQAKKLeEKAQAALTKG--NEELAREALAEKKSLEkq 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 355390331 784 --------------IAQLKKEQRRQEFQIRALESQKR-----------QQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:pfam04012 99 aealetqlaqqrsaVEQLRKQLAALETKIQQLKAKKNllkarlkaakaQEAVQTSLGSLSTSSATDSFERIEEKIEER 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
636-809 |
5.93e-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: 44.63 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 636 LADLTCEIEIKQKLIDELENS----QRRLQTLKHQYEEKLILL--------QNKIRDTQLERDRVLQNLSTMEcyteEKA 703
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQlnqlKSEISDLNNQKEQDWNKElkselknqEKKLEEIQNQISQNNKIISQLN----EQI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 704 NKIK-------ADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLV 776
Cdd:TIGR04523 345 SQLKkeltnseSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 355390331 777 E----------TKRNREIAQLKKEQRRQEFQIRALESQKRQQE 809
Cdd:TIGR04523 425 EkeierlketiIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
700-822 |
6.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 700 EEKANKIKADYEKRLREMNRDlqKLQAAQKEharLLKNQSRYERELKKLQAEVAEMKKaKValmkQMREEQQRRRLVE-T 778
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKE--ALLEAKEE---IHKLRNEFEKELRERRNELQKLEK-RL----LQKEENLDRKLELlE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 355390331 779 KRNREIAQLKK--EQRRQEFQIRALESQKRQQEMvlRRKTQEVSAL 822
Cdd:PRK12704 107 KREEELEKKEKelEQKQQELEKKEEELEELIEEQ--LQELERISGL 150
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
767-1116 |
6.41e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 767 REEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKppMLDS 846
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER--QLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 847 GAEVSASTTSSEAESGARSVS--SIVRQWNRKINHfLGDHPAPTVngtrparkkfQKKGASQSfSKAARLkwqsleRRII 924
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEieQLLEELNKKIKD-LGEEEQLRV----------KEKIGELE-AEIASL------ERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 925 DIVMQRM-----TIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDC 999
Cdd:TIGR02169 311 AEKERELedaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 1000 QATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQ----KEAQIRLLEGRLRQT--DMAGSSQN 1073
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEekedKALEIKKQEWKLEQLaaDLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 355390331 1074 HL------------LLDALREKAEAHPELQALiynVQQENGYASTDEEISEFSEG 1116
Cdd:TIGR02169 471 LYdlkeeydrvekeLSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQG 522
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
379-819 |
6.81e-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: 44.33 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 379 DKTSQQISALRAEIARLQMEL-----------MEYKAGKRVIGEDgaegySDLFRENAMLQKENGALRlrvKAMQEAIDA 447
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELeemtkfknnkeVELEELKKILAED-----EKLLDEKKQFEKIAEELK---GKEQELIFL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 448 INNRVTQLMSQEANLLLAKAGDgneaigaliQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPyslgaspaapafg 527
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSE---------EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK------------- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 528 gSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEafKKRAKLQQEnseetdeneaeeeeeERDESGCEEEEGRED 607
Cdd:pfam05483 503 -ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE--EKEMNLRDE---------------LESVREEFIQKGDEV 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 608 EDEDSGSEESLVDSDSDPEEKEVN---FQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLE 684
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQmkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 685 RDRVLQNLSTMeCYTEEKANKIKADYEKRLREmnrDLQKLQAAQKEHARLLKNQSryerelKKLQAEVAEMkkakVALMK 764
Cdd:pfam05483 645 LASAKQKFEEI-IDNYQKEIEDKKISEEKLLE---EVEKAKAIADEAVKLQKEID------KRCQHKIAEM----VALME 710
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 765 qmREEQQRRRLVEtKRNREIAQLKKEQRRQEFQIRALESQ--KRQQEMVLRRKTQEV 819
Cdd:pfam05483 711 --KHKHQYDKIIE-ERDSELGLYKNKEQEQSSAKAALEIElsNIKAELLSLKKQLEI 764
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
682-947 |
7.01e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 682 QLERDRVLQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVA 761
Cdd:COG3064 38 EAEEERLAELEAKRQ--AEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 762 LMKQMREEQQRRRLVETKRN-----REIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGR 836
Cdd:COG3064 116 AAEKEKAEEAKRKAEEEAKRkaeeeRKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 837 AGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKW 916
Cdd:COG3064 196 AAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275
|
250 260 270
....*....|....*....|....*....|.
gi 355390331 917 QSLERRIIDIVMQRMTIVNLEADMERLIKKR 947
Cdd:COG3064 276 SGLVVVAAALAGLAAAAAGLVLDDSAALAAE 306
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
624-827 |
8.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 624 DPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEeklillqnKIRDTQLERDRVLQnlstmecyTEEKA 703
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVAS--------AEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 704 nkikADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAkvalMKQMREEQQR-RRLVETKRNR 782
Cdd:COG4913 671 ----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDElQDRLEAAEDL 742
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 355390331 783 EIAQLKK--EQRRQEFQIRALESQKRQQemVLRRKTQEVSALRRLAK 827
Cdd:COG4913 743 ARLELRAllEERFAAALGDAVERELREN--LEERIDALRARLNRAEE 787
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
626-1016 |
8.88e-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: 44.01 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 626 EEKEVNFQADLADLTCEIEIKQKLIDELENSQRRlqtlkhqyeeklilLQNKIRDTQLERDRVLQNLSTME--------C 697
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR--------------LQQELDDLLVDLDHQRQLVSNLEkkqkkfdqM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 698 YTEEKA-------NKIKADYEKRLRE-----MNRDLQKLQAAQKEharllknqsrYERELKKLQAEVAEMKKAKVALMKQ 765
Cdd:pfam01576 610 LAEEKAisaryaeERDRAEAEAREKEtralsLARALEEALEAKEE----------LERTNKQLRAEMEDLVSSKDDVGKN 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 766 MREEQQRRRLVETkrnrEIAQLKKEQRRQEFQIRALESQKRQQEMVLRR-KTQEVSALRRLAKPMSERvaGRAGLKppml 844
Cdd:pfam01576 680 VHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRLEVNMQAlKAQFERDLQARDEQGEEK--RRQLVK---- 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 845 dsgaEVSASTTSSEAESGARSVSSIVRqwnRKINHFLGDHPAPTvngtrparkKFQKKGASQSFSKAARLKWQ--SLERR 922
Cdd:pfam01576 750 ----QVRELEAELEDERKQRAQAVAAK---KKLELDLKELEAQI---------DAANKGREEAVKQLKKLQAQmkDLQRE 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 923 IIDIVMQRMTIVNLEADMERLIKKRE-ELFLLQEALR-RKRERLQAESPEEekglqELAEEIEVLAANIDYINDGITDCQ 1000
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEaELLQLQEDLAaSERARRQAQQERD-----ELADEIASGASGKSALQDEKRRLE 888
|
410
....*....|....*.
gi 355390331 1001 ATIVQLEETKEELDST 1016
Cdd:pfam01576 889 ARIAQLEEELEEEQSN 904
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
711-834 |
8.97e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 711 EKRLREMNRDLQKLQaaqKEHARLLKNQSRYERELKKLQAEVAEmKKAKVALMKQmREEQQRRRLVETKRNREIAQLKKE 790
Cdd:COG1579 23 EHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEA-RIKKYEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 355390331 791 QRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVA 834
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
701-872 |
1.39e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 701 EKANKIKADYEKRLREMNRDLQKLQAAQK--EHARLLKNQSRYERELK-------KLQAEVAEMKKAKVALMKQMREEQQ 771
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKakqaaeaKAKAEAEAERKAKEEAAKQAEEEAK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 772 RRRLVETKRNREIAQLKKEQ------------RRQEFQIRALESQKRQQEMVLRRKTQEVSALRRL---AKPMSERVAGR 836
Cdd:TIGR02794 158 AKAAAEAKKKAEEAKKKAEAeakakaeaeakaKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAeaeRKADEAELGDI 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 355390331 837 AGLkppMLDSGAEVSASTTSSEAESGARSVSSIVRQ 872
Cdd:TIGR02794 238 FGL---ASGSNAEKQGGARGAAAGSEVDKYAAIIQQ 270
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1564-1600 |
1.51e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....*....
gi 355390331 1564 FTPIGEIKGHDSPINAIC--TNAKHIFTASSDLTVKFWS 1600
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVWD 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
644-832 |
1.63e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 644 EIKQKLIDELENSQRRLQTLKHQYEEKLILLQnKIRDTQLERDRVLQNLstmecytEEKANKIKADYEKRLREMNRDLQK 723
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR-ELETHIEEYDREFNEI-------ENASSSLGSDLAAREDALNQSLKE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 724 LQAAQKEHARLLKNqsryERELKKLQAEVAEMKKAKVALMKQmrEEQQRRRLVETkRNREIAQLKKE---QRRQEFQIRA 800
Cdd:TIGR00618 748 LMHQARTVLKARTE----AHFNNNEEVTAALQTGAELSHLAA--EIQFFNRLREE-DTHLLKTLEAEigqEIPSDEDILN 820
|
170 180 190
....*....|....*....|....*....|....*..
gi 355390331 801 LESQKRQQEM-----VLRRKTQEVSALRRLAKPMSER 832
Cdd:TIGR00618 821 LQCETLVQEEeqflsRLEEKSATLGEITHQLLKYEEC 857
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
535-847 |
1.71e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 535 EDASEVIRRAKQDLERLKKKE-----VRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDED 609
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEepsgqVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 610 EDSGSEESLVDSDSDPEEKEVNFQADLADLT---------CEIEIKQKLIDELENSQRRLQTLKHQYEEKLillqNKIRD 680
Cdd:pfam02029 86 QKEFDPTIADEKESVAERKENNEEEENSSWEkeekrdsrlGRYKEEETEIREKEYQENKWSTEVRQAEEEG----EEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 681 TQLERDRVLQNLSTMECYTEEKANKIKADYEKRL----REMNRDLQKLQAAQ--------KEHARLLKNQSRYERELKKL 748
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKvfldQKRGHPEVKSQNGEeevtklkvTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 749 QAEVAEMKKAKVALMKQMREEQQRRRLVETKRNR--EIAQLKK--EQRRqefQIRALESQKRQQEMvLRRKTQEVSALRR 824
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAelELEELKKkrEERR---KLLEEEEQRRKQEE-AERKLREEEEKRR 317
|
330 340
....*....|....*....|...
gi 355390331 825 LAKPMSERVAGRAGLKPPMLDSG 847
Cdd:pfam02029 318 MKEEIERRRAEAAEKRQKLPEDS 340
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1529-1560 |
1.73e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.73e-03
10 20 30
....*....|....*....|....*....|..
gi 355390331 1529 NAHKDWVCALAFIPGRPMLLSACRAGVIKVWN 1560
Cdd:pfam00400 8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
379-539 |
1.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 379 DKTSQQISALRAEIARLQMELME-----YKAGKRVIGED---GAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINN 450
Cdd:COG3883 68 DKLQAEIAEAEAEIEERREELGEraralYRSGGSVSYLDvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 451 RVTQLMSQEANL--LLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGG 528
Cdd:COG3883 148 KKAELEAKLAELeaLKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
170
....*....|.
gi 355390331 529 SPASSMEDASE 539
Cdd:COG3883 228 AAAAAAAAAAA 238
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
714-842 |
2.49e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 714 LREMNRDLQKLQAaQKEHARLLKNQSRYEReLKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnREIAQLKKEQRR 793
Cdd:COG0542 413 LDELERRLEQLEI-EKEALKKEQDEASFER-LAELRDELAELEEELEALKARWEAEKELIEEIQELK-EELEQRYGKIPE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 794 QEFQIRALESQKRQQEMVLR-------------RKT---------QEVSALRRLAKPMSERVAG---------------R 836
Cdd:COG0542 490 LEKELAELEEELAELAPLLReevteediaevvsRWTgipvgklleGEREKLLNLEEELHERVIGqdeaveavadairrsR 569
|
....*.
gi 355390331 837 AGLKPP 842
Cdd:COG0542 570 AGLKDP 575
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
708-994 |
2.49e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 708 ADYEKRLREMNRDLQK-LQAAQKEHARLLKNQSRYERELKKLQAEvaeMKKAKVALmKQMREEQqrRRLVETKRNreiaq 786
Cdd:pfam12128 596 AASEEELRERLDKAEEaLQSAREKQAAAEEQLVQANGELEKASRE---ETFARTAL-KNARLDL--RRLFDEKQS----- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 787 lkkEQRRQEfqiRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRA-GLKPPMLDSGAEVSASTTSSEA------ 859
Cdd:pfam12128 665 ---EKDKKN---KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKrEARTEKQAYWQVVEGALDAQLAllkaai 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 860 ---ESGARSVSSIVRQWNRKinhflgDHPAPTVNGTRPARKKFQKKGASQSFSKAAR-----LKWQSLERRIIDIVMQRM 931
Cdd:pfam12128 739 aarRSGAKAELKALETWYKR------DLASLGVDPDVIAKLKREIRTLERKIERIAVrrqevLRYFDWYQETWLQRRPRL 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 355390331 932 --TIVNLEADMERLikkREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYIND 994
Cdd:pfam12128 813 atQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
616-1012 |
2.49e-03 |
|
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: 42.85 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 616 ESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQT----LKHQYEEklilLQNKIRDTQLERDRVLQN 691
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQqveeMKTQLEE----LEDELQATEDAKLRLEVN 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 692 LSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAA----QKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMR 767
Cdd:pfam01576 722 MQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAEledeRKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLK 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 768 EEQqrrrlvetkrnreiAQLKKEQR--------RQEFQIRALESQKRQQ--EMVLRRKTQEVSALRRLAK-------PMS 830
Cdd:pfam01576 802 KLQ--------------AQMKDLQReleearasRDEILAQSKESEKKLKnlEAELLQLQEDLAASERARRqaqqerdELA 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 831 ERVAGRAGLKPPMLDSGAEVSASTTSSEAE-SGARSVSSIVRQWNRKINhflgdHPAPTVNGTRPARKKFQKK--GASQS 907
Cdd:pfam01576 868 DEIASGASGKSALQDEKRRLEARIAQLEEElEEEQSNTELLNDRLRKST-----LQVEQLTTELAAERSTSQKseSARQQ 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 908 F---SKAARLKWQSLERRIIDivMQRMTIVNLEADMERLikkreELFLLQEAlrrkRERLQAES--PEEEKGLQELAEEI 982
Cdd:pfam01576 943 LerqNKELKAKLQEMEGTVKS--KFKSSIAALEAKIAQL-----EEQLEQES----RERQAANKlvRRTEKKLKEVLLQV 1011
|
410 420 430
....*....|....*....|....*....|....
gi 355390331 983 EVLAANIDYINDGITDCQATIV----QLEETKEE 1012
Cdd:pfam01576 1012 EDERRHADQYKDQAEKGNSRMKqlkrQLEEAEEE 1045
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
717-834 |
2.62e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 717 MNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQqrrrlvETKRNREIAQLKKEQRRQef 796
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA------REKKEKELQKKVQEFQRK-- 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 355390331 797 qiraleSQKRQQEMVlRRKTQEVSALRRLAKPMSERVA 834
Cdd:smart00935 78 ------QQKLQQDLQ-KRQQEELQKILDKINKAIKEVA 108
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
644-773 |
2.75e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 644 EIKQKLIDELENSQRRLQTLKH-QYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA---NKIKADYEKRLRE-MN 718
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghlTNLRAERRKQLEEiLE 708
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 355390331 719 RDLQKLQAAQKEH----ARLLKNQSRYerelKKLQAEVAEMKKAKVALMKQMREEQQRR 773
Cdd:pfam10174 709 MKQEALLAAISEKdaniALLELSSSKK----KKTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
625-817 |
3.08e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 625 PEEKEVNFQADLADLTCEIEIKQKL-IDELENSQRRLQTLKhQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKA 703
Cdd:PRK11281 36 PTEADVQAQLDALNKQKLLEAEDKLvQQDLEQTLALLDKID-RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 704 NKIKADY-----EKRLREMNRDLQKLQAAQKE-HARLLKNQSRYERelkkLQAEVAEMkkakvalmkQMREEQQRRRLVE 777
Cdd:PRK11281 115 RETLSTLslrqlESRLAQTLDQLQNAQNDLAEyNSQLVSLQTQPER----AQAALYAN---------SQRLQQIRNLLKG 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 355390331 778 TKRNREiaQLKKEQRRQ-EFQIRALESQKRQQEMVLRRKTQ 817
Cdd:PRK11281 182 GKVGGK--ALRPSQRVLlQAEQALLNAQNDLQRKSLEGNTQ 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
378-577 |
3.20e-03 |
|
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: 41.67 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 378 QDKTSQQISALRAEIARLQMELMEYKAGKRvigedgaegysDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLms 457
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEK-----------ALLKQLAALERRIAALARRIRALEQELAALEAELAEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 458 qeanlllakagdgneaigaliqnyIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDA 537
Cdd:COG4942 89 ------------------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 355390331 538 SEVIRRA----KQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQE 577
Cdd:COG4942 145 APARREQaeelRADLAELAALRAELEAERAELEALLAELEEERA 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
918-1100 |
3.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 918 SLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEAL--------RRKRERLQAESPEEEKGLQELAEEIEVLAANI 989
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 990 DYINDGITDCQATI-----VQLEETKEELDSTDTSvvisscsLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQ 1064
Cdd:COG4913 319 DALREELDELEAQIrgnggDRLEQLEREIERLERE-------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*.
gi 355390331 1065 TDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQE 1100
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
615-824 |
3.32e-03 |
|
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: 42.08 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 615 EESLVDSDSDPEEKE---VNFQADLADLTCEIEIKQKLIDELENSQRRLQTLK-------HQYEEKLILLQNKIRDTQLE 684
Cdd:pfam01576 74 EEILHELESRLEEEEersQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteakiKKLEEDILLLEDQNSKLSKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 685 RDRVLQNLSTMECY---TEEKA---NKIK-------ADYEKRLREMNRDLQKLQAA-----------QKEHARL------ 734
Cdd:pfam01576 154 RKLLEERISEFTSNlaeEEEKAkslSKLKnkheamiSDLEERLKKEEKGRQELEKAkrklegestdlQEQIAELqaqiae 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 735 LKNQ-SRYERELKKLQAEVAEMKKAKVALMKQMRE-EQQRRRLVETKRNREIAQLKKEQRRQEF--QIRAL--------E 802
Cdd:pfam01576 234 LRAQlAKKEEELQAALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAEKQRRDLgeELEALkteledtlD 313
|
250 260
....*....|....*....|..
gi 355390331 803 SQKRQQEMVLRRKtQEVSALRR 824
Cdd:pfam01576 314 TTAAQQELRSKRE-QEVTELKK 334
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
651-822 |
3.46e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 651 DELENSQRRLQ-TLKHQYEEklILLQNKirDTQLER-DRVLQNLS-TME---------------CYTEEKaNKIKADYEK 712
Cdd:cd16269 86 DEDQKFQKKLMeQLEEKKEE--FCKQNE--EASSKRcQALLQELSaPLEekisqgsysvpggyqLYLEDR-EKLVEKYRQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 713 RLR---EMNRDLQK-LQAAQKEHARLLK-NQSRYERELKKLqaevAEMKKAKVALMKQMREEQQRRRLVETKRNRE---- 783
Cdd:cd16269 161 VPRkgvKAEEVLQEfLQSKEAEAEAILQaDQALTEKEKEIE----AERAKAEAAEQERKLLEEQQRELEQKLEDQErsye 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 355390331 784 --IAQLKKE-----QRRQEFQIRALESQKRQQEMVLRRKTQEVSAL 822
Cdd:cd16269 237 ehLRQLKEKmeeerENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
712-842 |
3.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 712 KRLREMNRDLQKLQAAQKEHARL--LKNQSRY---ERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVEtkrnREIAQ 786
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELeyLRAALRLwfaQRRLELLEAELEELRAELARLEAELERLEARLDALR----EELDE 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 355390331 787 LKKEQRRQEFQ-IRALESQKRQQEMVLRRKTQEVSALRRLAKpmservagRAGLKPP 842
Cdd:COG4913 328 LEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLA--------ALGLPLP 376
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
722-808 |
3.79e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 40.30 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 722 QKLQAAQKEHARL-LKN---QSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRR--------------------LVE 777
Cdd:pfam06391 68 KKIEQYEKENKDLiLKNkmkLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKekakqelidelmtsnkdaeeIIA 147
|
90 100 110
....*....|....*....|....*....|.
gi 355390331 778 TKRNReIAQLKKEQRRQEFQIRALESQKRQQ 808
Cdd:pfam06391 148 QHKKT-AKKRKSERRRKLEELNRVLEQKPTQ 177
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
919-1021 |
4.14e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 919 LERRIIDIVMQRMTIVNL--EADMERLIKKREELFLLQEALRRKRERLQAEspeeekglQELAEEIEVLAANIDYINDGI 996
Cdd:COG0542 416 LERRLEQLEIEKEALKKEqdEASFERLAELRDELAELEEELEALKARWEAE--------KELIEEIQELKEELEQRYGKI 487
|
90 100
....*....|....*....|....*
gi 355390331 997 TDCQATIVQLEETKEELDSTDTSVV 1021
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREEV 512
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
664-824 |
4.75e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 664 KHQYEEKLI-LLQNK----IRDTQLERDR----VLQNLST-ME---------------CYTEEKaNKIKADYEKRLREMN 718
Cdd:pfam02841 94 NQEFQKELVeLLEAKkddfLKQNEEASSKycsaLLQDLSEpLEekisqgtfskpggykLFLEER-DKLEAKYNQVPRKGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 719 RDLQKLQaaqkehaRLLKNQSRYERELkkLQAEvaemkKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQI 798
Cdd:pfam02841 173 KAEEVLQ-------EFLQSKEAVEEAI--LQTD-----QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 355390331 799 RALESQKRQ---------------QEMVLRRKTQEVSALRR 824
Cdd:pfam02841 239 RSYQEHVKQliekmeaereqllaeQERMLEHKLQEQEELLK 279
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
633-837 |
5.75e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 633 QADLADLTCEIEIKQKLIdeLENSQRR---LQTLKHQyEEKLILLQNKIRDTQlerdrvlQNLSTMEcyteekankikad 709
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSV--RQQQQQRaslLAQLKKQ-EEAISQASRKLRETQ-------NTLNQLN------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 710 yeKRLREMNRDLQKLQAAQKEHARLLKNQ----------------------SRYER-----------------ELKKLQA 750
Cdd:PRK11637 103 --KQIDELNASIAKLEQQQAAQERLLAAQldaafrqgehtglqlilsgeesQRGERilayfgylnqarqetiaELKQTRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 751 EVAEMKKAKVAlmKQmreEQQRRRLVETKRnreiAQLKKEQRRQEFQ--IRALES--QKRQQEMVLRRktQEVSALR--- 823
Cdd:PRK11637 181 ELAAQKAELEE--KQ---SQQKTLLYEQQA----QQQKLEQARNERKktLTGLESslQKDQQQLSELR--ANESRLRdsi 249
|
250
....*....|....*...
gi 355390331 824 ----RLAKPMSERVAGRA 837
Cdd:PRK11637 250 araeREAKARAEREAREA 267
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1430-1471 |
6.62e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 6.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 355390331 1430 FQPVGKLTGHIGPVMCLTVTQTasqHDLVVTGSKDHYVKMFE 1471
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPD---GKLLASGSDDGTVKVWD 39
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
673-841 |
7.37e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 673 LLQNKIRDTQLERDRV-LQNLSTMEcyTEEKANKIKADYEKRLREMNRDLQKLQAAQKeHARLLKNQSRYERELKKLQAE 751
Cdd:pfam05262 186 LREDNEKGVNFRRDMTdLKERESQE--DAKRAQQLKEELDKKQIDADKAQQKADFAQD-NADKQRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 752 VAEMKKAKVAlmKQMREEQQR---RRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVL--RRKTQEVSA-LRRL 825
Cdd:pfam05262 263 PADTSSPKED--KQVAENQKReieKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELeaQKKREPVAEdLQKT 340
|
170 180
....*....|....*....|.
gi 355390331 826 -----AKPMSERVAGRAGLKP 841
Cdd:pfam05262 341 kpqveAQPTSLNEDAIDSSNP 361
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
632-797 |
7.68e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 632 FQADLADLTCEIE----IKQKLIDEL----ENSQRRLQTLKHQYEEKLILLQNkiRDTQLERDRVLQNLST----MECYT 699
Cdd:cd00176 45 LEAELAAHEERVEalneLGEQLIEEGhpdaEEIQERLEELNQRWEELRELAEE--RRQRLEEALDLQQFFRdaddLEQWL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 700 EEKANKIKADyekrlrEMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALmkqmREEQQRRRLVETK 779
Cdd:cd00176 123 EEKEAALASE------DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD----ADEEIEEKLEELN 192
|
170
....*....|....*...
gi 355390331 780 RNREIAQLKKEQRRQEFQ 797
Cdd:cd00176 193 ERWEELLELAEERQKKLE 210
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
710-815 |
8.61e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 39.69 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 710 YEKRLREMNRDLQKLQAAQKEharllknQSRYERELKKLQAEVAEMK-----------KAKVALMKQMREEQQRRRLVET 778
Cdd:pfam13904 57 YENWLAAKQRQRQKELQAQKE-------EREKEEQEAELRKRLAKEKyqewlqrkarqQTKKREESHKQKAAESASKSLA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 355390331 779 KRNREIAQ-----------LKKEQRRQEFQIRALESQKRQQEMVLRRK 815
Cdd:pfam13904 130 KPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
646-915 |
9.29e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 646 KQKLIDELENSQRRLQT----LKHQYEEKLILlqNKIRDTQLERDRVLQNLSTMECYTEEKANKIKA------------- 708
Cdd:PTZ00108 997 KEYLLGKLERELARLSNkvrfIKHVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAeeeegaeeddead 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 709 ------------DYEKRLR--------EMNRDLQK-LQAAQKEHARLLKN--QSRYERELKKLQAEVAEMKKAKVALMKQ 765
Cdd:PTZ00108 1075 deddeeelgaavSYDYLLSmpiwsltkEKVEKLNAeLEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAK 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 766 MREEQQRRRLVETKRNREIAQLKKEQRRQefqirALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLD 845
Cdd:PTZ00108 1155 EQRLKSKTKGKASKLRKPKLKKKEKKKKK-----SSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDE 1229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355390331 846 SGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHP----APTVNGTRPARKKFQKKGASQSFSKAARLK 915
Cdd:PTZ00108 1230 EQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGkpknAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
658-857 |
9.58e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 658 RRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQnlstmecyteEKANKIKADYEKRLREMNRDLQKLQaaqKEHARLLKN 737
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALL----------EAKELLLRERNQQRQEARREREELQ---REEERLVQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355390331 738 QSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRnREIAQLKKEQRRQEFqIRALESQKRQQemvlrrKTQ 817
Cdd:PRK12705 90 EEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNEL-YRVAGLTPEQARKLL-LKLLDAELEEE------KAQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 355390331 818 EVSALRRLAKPMSERVAgRAGLKPPMLDSGAEVSASTTSS 857
Cdd:PRK12705 162 RVKKIEEEADLEAERKA-QNILAQAMQRIASETASDLSVS 200
|
|
| |
