|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
413-758 |
0e+00 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 544.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 413 KGNIRVFCRVRPLLPDDGGRqEASVIAYPtstESLGRGIDVVQSGNK-HPFTFDKVFDHGASQEEVFFEISQLVQSALDG 491
Cdd:cd01366 1 KGNIRVFCRVRPLLPSEENE-DTSHITFP---DEDGQTIELTSIGAKqKEFSFDKVFDPEASQEDVFEEVSPLVQSALDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 492 YKVCIFAYGQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSrtiaie 571
Cdd:cd01366 77 YNVCIFAYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPG------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 572 svradsSTSGRQYTITHD-VNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNEST 650
Cdd:cd01366 148 ------NAPQKKLEIRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 651 EQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMF 730
Cdd:cd01366 222 GEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMF 301
|
330 340
....*....|....*....|....*...
gi 1063721133 731 VNISPDPSSTGESLCSLRFAARVNACEI 758
Cdd:cd01366 302 VNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
421-756 |
2.45e-143 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 423.91 E-value: 2.45e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 421 RVRPLLPDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFE-ISQLVQSALDGYKVCIFAY 499
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 500 GQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSLSTQgWKYKMQVSMLEIYNESIRDLLSTSrtiaiesvradsST 579
Cdd:pfam00225 81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKER-SEFSVKVSYLEIYNEKIRDLLSPS------------NK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 580 SGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQ---G 656
Cdd:pfam00225 145 NKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvktG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 657 VLNLIDLAGSERLSRSG-ATGDRLKETQAINKSLSALSDVIFALA-KKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNIS 734
Cdd:pfam00225 225 KLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAdKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANIS 304
|
330 340
....*....|....*....|..
gi 1063721133 735 PDPSSTGESLCSLRFAARVNAC 756
Cdd:pfam00225 305 PSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
415-759 |
1.66e-142 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 422.37 E-value: 1.66e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLPDDGGRQEASVIAYPTSTeslGRGIDVVQSGNKHP---FTFDKVFDHGASQEEVFFEIS-QLVQSALD 490
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKV---GKTLTVRSPKNRQGekkFTFDKVFDATASQEDVFEETAaPLVDSVLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 491 GYKVCIFAYGQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSLsTQGWKYKMQVSMLEIYNESIRDLLSTSRtiai 570
Cdd:smart00129 78 GYNATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKR-EEGWQFSVKVSYLEIYNEKIRDLLNPSS---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 571 esvradsstsgRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRIS--GVNE 648
Cdd:smart00129 150 -----------KKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEqkIKNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 649 STEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAK--KEDHVPFRNSKLTYLLQPCLGGDSK 726
Cdd:smart00129 219 SSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSK 298
|
330 340 350
....*....|....*....|....*....|...
gi 1063721133 727 TLMFVNISPDPSSTGESLCSLRFAARVNACEIG 759
Cdd:smart00129 299 TLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
415-753 |
8.74e-119 |
|
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: 360.80 E-value: 8.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLpDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHpFTFDKVFDHGASQEEVFFEI-SQLVQSALDGYK 493
Cdd:cd00106 1 NVRVAVRVRPLN-GREARSAKSVISVDGGKSVVLDPPKNRVAPPKT-FAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 494 VCIFAYGQTGSGKTYTMMGRPetPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLStsrtiaiesv 573
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD--PEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLS---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 574 radsSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNEST--E 651
Cdd:cd00106 147 ----PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 652 QQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA-KKEDHVPFRNSKLTYLLQPCLGGDSKTLMF 730
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAdGQNKHIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|...
gi 1063721133 731 VNISPDPSSTGESLCSLRFAARV 753
Cdd:cd00106 303 ACISPSSENFEETLSTLRFASRA 325
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
416-758 |
8.64e-92 |
|
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: 291.16 E-value: 8.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 416 IRVFCRVRPLLPDDGGRQEASVIAYPTSTESlgrgidvVQSGNKHPFTFDKVFDHGASQEEVFFE-ISQLVQSALDGYKV 494
Cdd:cd01372 3 VRVAVRVRPLLPKEIIEGCRICVSFVPGEPQ-------VTVGTDKSFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 495 CIFAYGQTGSGKTYTMMG---RPETPEQKGLIPRSLEQIFKTSQSLStQGWKYKMQVSMLEIYNESIRDLLstsrtiaie 571
Cdd:cd01372 76 TVLAYGQTGSGKTYTMGTaytAEEDEEQVGIIPRAIQHIFKKIEKKK-DTFEFQLKVSFLEIYNEEIRDLL--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 572 svraDSSTSGR-QYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTL-----RISG 645
Cdd:cd01372 146 ----DPETDKKpTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTItleqtKKNG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 646 VNESTEQQVQGV-----LNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA---KKEDHVPFRNSKLTYLL 717
Cdd:cd01372 222 PIAPMSADDKNStftskFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGdesKKGAHVPYRDSKLTRLL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063721133 718 QPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARvnACEI 758
Cdd:cd01372 302 QDSLGGNSHTLMIACVSPADSNFEETLNTLKYANR--ARNI 340
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
414-753 |
4.50e-89 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 284.63 E-value: 4.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 414 GNIRVFCRVRPLLPDDGGRQEASVIAYPTSTESL--GRGIDVVQSGNK---HPFTFDKVFD-------HGASQEEVFFEI 481
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLknPKQADKNNKATRevpKSFSFDYSYWshdsedpNYASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 482 S-QLVQSALDGYKVCIFAYGQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRD 560
Cdd:cd01365 81 GeELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 561 LLSTSRTIAIESVRAdsstsgRQytitHDVNGnTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFT 640
Cdd:cd01365 158 LLNPKPKKNKGNLKV------RE----HPVLG-PYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 641 L-----RISGVNESTEQQVQGVlNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA--------KKEDHVP 707
Cdd:cd01365 227 IvltqkRHDAETNLTTEKVSKI-SLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALAdmssgkskKKSSFIP 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1063721133 708 FRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARV 753
Cdd:cd01365 306 YRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRA 351
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
415-752 |
6.93e-89 |
|
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: 283.20 E-value: 6.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLPDDGGRQEASVIaypTSTESLGRgIDVV---QSGNKHP--FTFDKVFDHGASQEEVFFEISQ-LVQSA 488
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIV---DVDEKRGQ-VSVRnpkATANEPPktFTFDAVFDPNSKQLDVYDETARpLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 489 LDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFkTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSRTI 568
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIF-GHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 569 AIEsVRADSSTSgrqytithdvngnTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRI--SGV 646
Cdd:cd01371 157 RLE-LKERPDTG-------------VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecSEK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 647 NESTEQQVQ-GVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAK-KEDHVPFRNSKLTYLLQPCLGGD 724
Cdd:cd01371 223 GEDGENHIRvGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDgKSTHIPYRDSKLTRLLQDSLGGN 302
|
330 340
....*....|....*....|....*...
gi 1063721133 725 SKTLMFVNISPDPSSTGESLCSLRFAAR 752
Cdd:cd01371 303 SKTVMCANIGPADYNYDETLSTLRYANR 330
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
415-752 |
4.18e-86 |
|
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: 275.75 E-value: 4.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPL--LPDDGGrQEASVIAYPTSTESLGrgidvvQSGNKHPFTFDKVFDHGASQEEVF-FEISQLVQSALDG 491
Cdd:cd01369 3 NIKVVCRFRPLneLEVLQG-SKSIVKFDPEDTVVIA------TSETGKTFSFDRVFDPNTTQEDVYnFAAKPIVDDVLNG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 492 YKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSlSTQGWKYKMQVSMLEIYNESIRDLLSTSRTiaie 571
Cdd:cd01369 76 YNGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYS-MDENLEFHVKVSYFEIYMEKIRDLLDVSKT---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 572 svradsstsgrQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTE 651
Cdd:cd01369 151 -----------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 652 QQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA-KKEDHVPFRNSKLTYLLQPCLGGDSKTLMF 730
Cdd:cd01369 220 KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTdGKKTHIPYRDSKLTRILQDSLGGNSRTTLI 299
|
330 340
....*....|....*....|..
gi 1063721133 731 VNISPDPSSTGESLCSLRFAAR 752
Cdd:cd01369 300 ICCSPSSYNESETLSTLRFGQR 321
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
415-758 |
6.69e-86 |
|
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: 274.98 E-value: 6.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLPDDGGRQEASviAYPTSTESLgrgIDVVQSGNkhPFTFDKVFDHGASQEEVFFEISQ-LVQSALDGYK 493
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQV--AWEIDNDTI---YLVEPPST--SFTFDHVFGGDSTNREVYELIAKpVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 494 VCIFAYGQTGSGKTYTMMGRPETPeqkGLIPRSLEQIFKTSQSLSTQgwKYKMQVSMLEIYNESIRDLLSTSrtiaiesv 573
Cdd:cd01374 74 GTIFAYGQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQDTPDR--EFLLRVSYLEIYNEKINDLLSPT-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 574 radsstsGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQ 653
Cdd:cd01374 141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 654 VQ---GVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA--KKEDHVPFRNSKLTYLLQPCLGGDSKTL 728
Cdd:cd01374 214 GTvrvSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSegKVGGHIPYRDSKLTRILQPSLGGNSRTA 293
|
330 340 350
....*....|....*....|....*....|
gi 1063721133 729 MFVNISPDPSSTGESLCSLRFAARvnACEI 758
Cdd:cd01374 294 IICTITPAESHVEETLNTLKFASR--AKKI 321
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
416-753 |
1.15e-76 |
|
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: 250.96 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 416 IRVFCRVRPllpddGGRQEASVIAYPTSTES--------LGRGIdVVQSGNKHPFTFDKVFdHGASQEEVFFEISQ-LVQ 486
Cdd:cd01375 2 VQAFVRVRP-----TDDFAHEMIKYGEDGKSisihlkkdLRRGV-VNNQQEDWSFKFDGVL-HNASQELVYETVAKdVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 487 SALDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSLSTQGwkYKMQVSMLEIYNESIRDLLSTsR 566
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKA--YTVHVSYLEIYNEQLYDLLST-L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 567 TIAIESVRAdsstsgrqYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGV 646
Cdd:cd01375 152 PYVGPSVTP--------MTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 647 NE--STEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA-KKEDHVPFRNSKLTYLLQPCLGG 723
Cdd:cd01375 224 SRtlSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSdKDRTHVPFRQSKLTHVLRDSLGG 303
|
330 340 350
....*....|....*....|....*....|
gi 1063721133 724 DSKTLMFVNISPDPSSTGESLCSLRFAARV 753
Cdd:cd01375 304 NCNTVMVANIYGEAAQLEETLSTLRFASRV 333
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
415-752 |
2.15e-76 |
|
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: 251.09 E-value: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLPDDGGRQEASVIAY-PTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFE-ISQLVQSALDGY 492
Cdd:cd01364 3 NIQVVVRCRPFNLRERKASSHSVVEVdPVRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSvVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 493 KVCIFAYGQTGSGKTYTMMG--------RPETPEQKGLIPRSLEQIFktsQSLSTQGWKYKMQVSMLEIYNESIRDLLST 564
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEGdrspneeyTWELDPLAGIIPRTLHQLF---EKLEDNGTEYSVKVSYLEIYNEELFDLLSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 565 SRTIAiESVRADSSTSGRqytithdvnGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRIS 644
Cdd:cd01364 160 SSDVS-ERLRMFDDPRNK---------RGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 645 gVNEST---EQQVQ-GVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPC 720
Cdd:cd01364 230 -IKETTidgEELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDS 308
|
330 340 350
....*....|....*....|....*....|..
gi 1063721133 721 LGGDSKTLMFVNISPDPSSTGESLCSLRFAAR 752
Cdd:cd01364 309 LGGRTKTSIIATISPASVNLEETLSTLEYAHR 340
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
415-755 |
2.74e-76 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 250.50 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPL--LPDDGGRQEASVIAYPTSTeslgrgidVVQSGNKHPFTFDKVFDHGASQEEVFFEISQ-LVQSALDG 491
Cdd:cd01373 2 AVKVFVRIRPPaeREGDGEYGQCLKKLSSDTL--------VLHSKPPKTFTFDHVADSNTNQESVFQSVGKpIVESCLSG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 492 YKVCIFAYGQTGSGKTYTMMGRPE-----TPEQKGLIPRSLEQIF---KTSQSLSTQGWKYKMQVSMLEIYNESIRDLLs 563
Cdd:cd01373 74 YNGTIFAYGQTGSGKTYTMWGPSEsdnesPHGLRGVIPRIFEYLFsliQREKEKAGEGKSFLCKCSFLEIYNEQIYDLL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 564 tsrtiaiesvraDSSTSGRQytITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRI 643
Cdd:cd01373 153 ------------DPASRNLK--LREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 644 SGVNESTEQQVQGV--LNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAK----KEDHVPFRNSKLTYLL 717
Cdd:cd01373 219 ESWEKKACFVNIRTsrLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahgKQRHVCYRDSKLTFLL 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 1063721133 718 QPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNA 755
Cdd:cd01373 299 RDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKL 336
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
411-754 |
4.21e-72 |
|
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: 239.17 E-value: 4.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 411 ELKGNIRVFCRV---RPLLPDDGGRQeasviayPTSTESLGRGIDVVQSGNKH-PFTFDKVFDHGASQEEVFFEISQ-LV 485
Cdd:cd01370 15 EKNEGFRRIVKVmdnHMLVFDPKDEE-------DGFFHGGSNNRDRRKRRNKElKYVFDRVFDETSTQEEVYEETTKpLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 486 QSALDGYKVCIFAYGQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSLSTQGwKYKMQVSMLEIYNESIRDLLSTS 565
Cdd:cd01370 88 DGVLNGYNATVFAYGATGAGKTHTMLG---TPQEPGLMVLTMKELFKRIESLKDEK-EFEVSMSYLEIYNETIRDLLNPS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 566 rtiaiesvradsstsGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVF--TLRI 643
Cdd:cd01370 164 ---------------SGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLqiTVRQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 644 SGVNESTEQQV-QGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALA---KKEDHVPFRNSKLTYLLQP 719
Cdd:cd01370 229 QDKTASINQQVrQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAdpgKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*
gi 1063721133 720 CLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVN 754
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAK 343
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
416-751 |
3.66e-69 |
|
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: 231.51 E-value: 3.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 416 IRVFCRVRPLLPDDGGRQEASVIAYPTSTE--------SLGRGIDVVQSGNKHPFTFDKVFDHGASQEEvFFE--ISQLV 485
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINSTTvvlhppkgSAANKSERNGGQKETKFSFSKVFGPNTTQKE-FFQgtALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 486 QSALDGYKVCIFAYGQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSlstqgwkYKMQVSMLEIYNESIRDLLSTS 565
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQG---SPGDGGILPRSLDVIFNSIGG-------YSVFVSYIEIYNEYIYDLLEPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 566 RTiaiesvradSSTSGRQ-YTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRI- 643
Cdd:cd01368 152 PS---------SPTKKRQsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLv 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 644 -------SGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFAL-----AKKEDHVPFRNS 711
Cdd:cd01368 223 qapgdsdGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqlQGTNKMVPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1063721133 712 KLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAA 751
Cdd:cd01368 303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSA 342
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
415-754 |
7.47e-68 |
|
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: 227.00 E-value: 7.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLPDDGGRqeasviayptSTESLGRGIDVVQ--------SGNKHPFTFDKVFDHGASQEEVFF-EISQLV 485
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGA----------SDPSCVSGIDSCSveladprnHGETLKYQFDAFYGEESTQEDIYArEVQPIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 486 QSALDGYKVCIFAYGQTGSGKTYTMMGRPETPeqkGLIPRSLEQIFKTSQslsTQGWKYKMQVSMLEIYNESIRDLLSTs 565
Cdd:cd01376 71 PHLLEGQNATVFAYGSTGAGKTFTMLGSPEQP---GLMPLTVMDLLQMTR---KEAWALSFTMSYLEIYQEKILDLLEP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 566 rtiaiesvrADSSTSGRQytithDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVftLRIsG 645
Cdd:cd01376 144 ---------ASKELVIRE-----DKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAV--LLI-K 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 646 VNESTE----QQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCL 721
Cdd:cd01376 207 VDQRERlapfRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSL 286
|
330 340 350
....*....|....*....|....*....|...
gi 1063721133 722 GGDSKTLMFVNISPDPSSTGESLCSLRFAARVN 754
Cdd:cd01376 287 GGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
462-752 |
1.96e-65 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 228.08 E-value: 1.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 462 FTFDKVFDHGASQEEVFFE-ISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGrpeTPEQKGLIPRSLEQIFKTSQSLStQ 540
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEEtIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLS-M 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 541 GWKYKMQVSMLEIYNESIRDLLSTSRtiaiESVRADSstsgrqytithDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQS 620
Cdd:COG5059 134 TKDFAVSISYLEIYNEKIYDLLSPNE----ESLNIRE-----------DSLLGVKVAGLTEKHVSSKEEILDLLRKGEKN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 621 RSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFAL- 699
Cdd:COG5059 199 RTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALg 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1063721133 700 -AKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAAR 752
Cdd:COG5059 279 dKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASR 332
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
415-753 |
6.33e-62 |
|
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: 211.39 E-value: 6.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 415 NIRVFCRVRPLLPDDGGRQEASVIAYPTSTE----SLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVF-FEISQLVQSAL 489
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTlivhEPKLKVDLTKYIENHTFRFDYVFDESSSNETVYrSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 490 DGYKVCIFAYGQTGSGKTYTMMGR-PETPEQKGLIPRSLEQIFKTSQSLSTQGwKYKMQVSMLEIYNESIRDLLSTSRTI 568
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDfSGQEESKGIYALAARDVFRLLNKLPYKD-NLGVTVSFFEIYGGKVFDLLNRKKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 569 AIesvRADSstsgrqytithdvNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISgvnE 648
Cdd:cd01367 160 RL---REDG-------------KGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR---D 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 649 STEQQVQGVLNLIDLAGSERLS-RSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCL-GGDSK 726
Cdd:cd01367 221 RGTNKLHGKLSFVDLAGSERGAdTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFiGENSK 300
|
330 340
....*....|....*....|....*..
gi 1063721133 727 TLMFVNISPDPSSTGESLCSLRFAARV 753
Cdd:cd01367 301 TCMIATISPGASSCEHTLNTLRYADRV 327
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
395-562 |
1.01e-55 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 187.81 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 395 LFEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDggrqeaSVIAYPTSTESLGRgidvvQSGNKHPFTFDKVFDHGASQ 474
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRPELLSE------AQIDYPDETSSDGK-----IGSKNKSFSFDRVFPPESEQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 475 EEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTytmmgrpetpeqKGLIPRSLEQIFKTSQSLStQGWKYKMQVSMLEIY 554
Cdd:pfam16796 70 EDVFQEISQLVQSCLDGYNVCIFAYGQTGSGSN------------DGMIPRAREQIFRFISSLK-KGWKYTIELQFVEIY 136
|
....*...
gi 1063721133 555 NESIRDLL 562
Cdd:pfam16796 137 NESSQDLL 144
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
416-755 |
2.23e-55 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 207.09 E-value: 2.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 416 IRVFCRVRPLLPDdggrQEASVIAYPTSTESLgrgidvvqSGNKHPFTFDKVFDHGASQEEVFFEI-SQLVQSALDGYKV 494
Cdd:PLN03188 100 VKVIVRMKPLNKG----EEGEMIVQKMSNDSL--------TINGQTFTFDSIADPESTQEDIFQLVgAPLVENCLAGFNS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 495 CIFAYGQTGSGKTYTMMGRPE-------TPEQKGLIPRSLEQIF---KTSQSLST-QGWKYKMQVSMLEIYNESIRDLLS 563
Cdd:PLN03188 168 SVFAYGQTGSGKTYTMWGPANglleehlSGDQQGLTPRVFERLFariNEEQIKHAdRQLKYQCRCSFLEIYNEQITDLLD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 564 TSRtiaiesvradsstsgRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRI 643
Cdd:PLN03188 248 PSQ---------------KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 644 SGVNESTEQQVQGV----LNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAK-----KEDHVPFRNSKLT 714
Cdd:PLN03188 313 ESRCKSVADGLSSFktsrINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtgKQRHIPYRDSRLT 392
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063721133 715 YLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNA 755
Cdd:PLN03188 393 FLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKA 433
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
463-735 |
6.17e-24 |
|
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: 99.34 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 463 TFDKVFDHGASQEEVFFEISQLVQSALDGYKV-CIFAYGQTGSGKTYTMmgrpetpeqKGLIPRSLEQIFKTSQSLSTQG 541
Cdd:cd01363 21 VFYRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETM---------KGVIPYLASVAFNGINKGETEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 542 WKYkmqvsmleiynesirdllstsrtiaiesvradsstsgrqytithdvngnthvsdLTIVDVCSIGQISSLLQQAAQSR 621
Cdd:cd01363 92 WVY------------------------------------------------------LTEITVTLEDQILQANPILEAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 622 sVGKTHMNEQSSRSHFVFTLrisgvnesteqqvqgvlnLIDLAGSERlsrsgatgdrlketqaINKSLSALSDVIFAlak 701
Cdd:cd01363 118 -NAKTTRNENSSRFGKFIEI------------------LLDIAGFEI----------------INESLNTLMNVLRA--- 159
|
250 260 270
....*....|....*....|....*....|....
gi 1063721133 702 kedhvpfrnskltyllqpclggdSKTLMFVNISP 735
Cdd:cd01363 160 -----------------------TRPHFVRCISP 170
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
393-702 |
1.11e-19 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 93.65 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 393 RQLFEGELLRKKLHNTILELKgNIRVFCRVRPLLPDDGG----RQEASVIAYPTSTESLGRGIDVVQSGNKhpFTFDKVF 468
Cdd:COG5059 285 HIPYRESKLTRLLQDSLGGNC-NTRVICTISPSSNSFEEtintLKFASRAKSIKNKIQVNSSSDSSREIEE--IKFDLSE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 469 DHGASQEEVFFEISQLVQSALDGykvcIFAYGQTGSGKTYTMMgrpetpEQKGLIPRSLEQ-IFKTSQSLSTQGWKYKMQ 547
Cdd:COG5059 362 DRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK------SRIDLIMKSIISgTFERKKLLKEEGWKYKST 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 548 VSMLEIYNESIRDLLStsrtiaiESVRADSSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLlqqaaqsRSVGKTH 627
Cdd:COG5059 432 LQFLRIEIDRLLLLRE-------EELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKASKL-------RSSASTK 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063721133 628 MNEQSSRSHFVFTLRISGVNESTEQQVqgvLNLIDLAGSERLsRSGATGDRLKETQAINKSLSALSDVIFALAKK 702
Cdd:COG5059 498 LNLRSSRSHSKFRDHLNGSNSSTKELS---LNQVDLAGSERK-VSQSVGELLRETQSLNKSLSSLGDVIHALGSK 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-361 |
3.28e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 71 DTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKEnLSSSLQSAEKRYSDKELDAKTKE-EELRATITEMKENIESLQEK 149
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALLVLRLEELREElEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 150 LsKEKLSKLDAIENHRREKDCRV-VAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLE 228
Cdd:TIGR02168 262 L-QELEEKLEELRLEVSELEEEIeELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 229 VAREAHTRAEKEKSSILENLTTLRG-------HSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHV 301
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAeleelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063721133 302 -----VQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLK 361
Cdd:TIGR02168 421 qeieeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-418 |
6.72e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 130 EELRATITEMKENIESLQEKLsKEKLSKLDAIENHRREKDCRVV-AEKLQVSLREELDKvkeekmaAKQKVTSLEDMYKR 208
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEeLSRQISALRKDLAR-------LEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 209 LQEYNTSLQQYNTKLQTDLEVAREAHTRAEkekssilENLTTLRGHSKSLQDQLASSRvsqdeavKQKDSLLMEVNNLQS 288
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAE-------AEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 289 ELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMS 368
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063721133 369 HTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRV 418
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-399 |
2.93e-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: 57.39 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 104 KENLSSSLQSAEKRYSDKELDAKTKEeelRATITEMKENIESLQEKLSKEklskLDAIENHRREKDCRVVA--EKLQVSL 181
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQ---LASLEEELEKLTEEISELEKR----LEEIEQLLEELNKKIKDlgEEEQLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 182 REELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQ 261
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 262 LASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKEsvgksshELDILIAKSGSLEETCSL 341
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-------AIAGIEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063721133 342 QKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEqkqcmheLQDRLADTERQLFEGE 399
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
111-416 |
6.58e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 111 LQSAEKRYSDKELDAKTKEEELRATITEMKENIEslqEKLSKEKLSKLDAIENHRREkdcrvvaeklqvsLREELDKVKE 190
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIE---EKEEKDLHERLNGLESELAE-------------LDEEIERYEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 191 EKMAAKQKVTSLEDMykrLQEYNTSLQQYNTkLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQD 270
Cdd:PRK02224 228 QREQARETRDEADEV---LEEHEERREELET-LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 271 EAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKssheldiliaksgsLEETCSLQKERIKMLE 350
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD--------------LEERAEELREEAAELE 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063721133 351 QELAFAKEKLKmvdlSMSHTMTEFEEQkqcMHELQDRLADTERQLFEGELLRKKLHNTILELKGNI 416
Cdd:PRK02224 370 SELEEAREAVE----DRREEIEELEEE---IEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-360 |
1.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 91 RWYQQVDETHVQDKENLSSSLQSAEKRYSDKEldakTKEEELRATITEMKENIESLQEKLS--KEKLSKLDAIENHRREK 168
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELE----AELEELRLELEELELELEEAQAEEYelLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 169 dcrvvaeklQVSLREELDKVKEEKMAAKQKVTSLEDmykRLQEYNTSLQQyntkLQTDLEVAREAHTRAEKEKSSILENL 248
Cdd:COG1196 311 ---------RRELEERLEELEEELAELEEELEELEE---ELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 249 TTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDIL 328
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|..
gi 1063721133 329 IAKSGSLEETCSLQKERIKMLEQELAFAKEKL 360
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-395 |
3.83e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 113 SAEKRYSDKELDAKtKEEELRATITEMKENIESLQEKLsKEKLSKLDAIENHRREkdcrvvAEKLQVSLREELDKVKEEK 192
Cdd:COG1196 219 KEELKELEAELLLL-KLRELEAELEELEAELEELEAEL-EELEAELAELEAELEE------LRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 193 MAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEA 272
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 273 VKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQE 352
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063721133 353 LAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQL 395
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-338 |
1.06e-06 |
|
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: 52.38 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 54 KDEVLALLNERAKAGKFDT----KGKIEQmTDIIKKLKVCVRWYQQVD---ETHVQDKENLSSSLQSAEKRYS------- 119
Cdd:TIGR02169 197 RQQLERLRREREKAERYQAllkeKREYEG-YELLKEKEALERQKEAIErqlASLEEELEKLTEEISELEKRLEeieqlle 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 120 --DKELDAKTKEE--ELRATITEMKENIESLQEKLsKEKLSKLDAIENHRREKDCRVVAEKLQV-SLREELDKVKEEKMA 194
Cdd:TIGR02169 276 elNKKIKDLGEEEqlRVKEKIGELEAEIASLERSI-AEKERELEDAEERLAKLEAEIDKLLAEIeELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 195 AKQKVTSLEDMYK----RLQEYNTSLQQYNTKL---QTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRV 267
Cdd:TIGR02169 355 LTEEYAELKEELEdlraELEEVDKEFAETRDELkdyREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063721133 268 SQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEET 338
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-413 |
2.00e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 72 TKGKIEQMTDIIKKLKVCVRWYQQVDETHVQ-----------DKENLSSSLQSAEKR---YSDKELDAKTKEEELRATIT 137
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkrltglTPEKLEKELEELEKAkeeIEEEISKITARIGELKKEIK 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 138 EMKENIESLQEKLSKEKLSKLDAIENHRRE-------------KDCRVVAEKLQvSLREELDKVkEEKMAAKQKVTSLED 204
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELTEEHRKElleeytaelkrieKELKEIEEKER-KLRKELREL-EKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 205 MYKRLQEYNTSLQQYNTKlqtDLEvareahtRAEKEKSSILENLTTLRGHSKSLQDQLASsrvsQDEAVKQKDSLLMEVN 284
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLE---ELE-------KKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLD 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 285 NLQSELQQVRDDRDRHVVQSQKLAGEIL-----MYKE--SVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAK 357
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLkelepFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063721133 358 EKLKmvDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELK 413
Cdd:PRK03918 647 KELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
94-412 |
2.72e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 94 QQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEE------ELRATITEMKENIESLQEKLSKEKLSKlDAIENHRRE 167
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADA-EAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 168 KDCRvvaeklQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILEN 247
Cdd:PRK02224 319 LEDR------DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 248 LTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDrdrhVVQSQKL--AGEILMYKESVGKSSHel 325
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER----VEEAEALleAGKCPECGQPVEGSPH-- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 326 diliakSGSLEEtcslQKERIKMLEQELAFAKEKLKMVD------LSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGE 399
Cdd:PRK02224 467 ------VETIEE----DRERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
330
....*....|...
gi 1063721133 400 LLRKKLHNTILEL 412
Cdd:PRK02224 537 ERAEELRERAAEL 549
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
5-275 |
5.26e-06 |
|
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: 50.21 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 5 KEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKI-EQMTDII 83
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnPEINDRI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 84 KKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIEN 163
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 164 HRREKD--CRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTK-LQTDLEVAREAHTRAEKE 240
Cdd:pfam10174 641 ARRREDnlADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKqLEEILEMKQEALLAAISE 720
|
250 260 270
....*....|....*....|....*....|....*
gi 1063721133 241 KSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQ 275
Cdd:pfam10174 721 KDANIALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
73-405 |
1.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 73 KGKIEQMTDIIKKLK-------VCVRwyqQVDETHvqdKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMkENIES 145
Cdd:PRK03918 418 KKEIKELKKAIEELKkakgkcpVCGR---ELTEEH---RKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLK 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 146 LQEKLSKEKlSKLDAIENhRREKDCRVVAEKLQVSlREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQT 225
Cdd:PRK03918 491 KESELIKLK-ELAEQLKE-LEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 226 DLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRvsqdEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQ 305
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 306 KLAGEILMYKESVGKSSHEldiliaksGSLEETCSLQKErIKMLEQELAFAKEKLKmvdlSMSHTMTEFEEQKQCMHELQ 385
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYE--------ELREEYLELSRE-LAGLRAELEELEKRRE----EIKKTLEKLKEELEEREKAK 710
|
330 340
....*....|....*....|
gi 1063721133 386 DRLADTERQLFEGELLRKKL 405
Cdd:PRK03918 711 KELEKLEKALERVEELREKV 730
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
144-398 |
1.88e-05 |
|
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: 47.97 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 144 ESLQEK---LSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLqqyn 220
Cdd:pfam07888 38 ECLQERaelLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 221 TKLQTDLEVAREAHTRAEKEkssILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRH 300
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRE---LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 301 VVQSQKLAG-------EILMYKESVGKSSHELDILIAKSGSLEETC----SLQkERIKMLEQELAFAKEKLKMVDLSMSH 369
Cdd:pfam07888 191 SKEFQELRNslaqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeelrSLQ-ERLNASERKVEGLGEELSSMAAQRDR 269
|
250 260
....*....|....*....|....*....
gi 1063721133 370 TMTEFEEQKQCMHELQDRLADTERQLFEG 398
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQLADASLALREG 298
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-394 |
2.89e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 103 DKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENI---ESLQEKLSKEKLsKLDAIENHRREkdcrvvaEKLQv 179
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariEELEEDLHKLEE-ALNDLEARLSH-------SRIP- 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 180 SLREELDKVKEEKmaaKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREahtrAEKEKSSILENLTTLRGHSKSLQ 259
Cdd:TIGR02169 795 EIQAELSKLEEEV---SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 260 DQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEE-- 337
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEip 947
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063721133 338 TCSLQKERIKMLEQELAFAKEKLKMVDLSmshTMTEFEEQKQCMHELQDRLADTERQ 394
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNML---AIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-361 |
3.19e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 94 QQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVV 173
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 174 AEKLQVSLREELDKVKEEKMAAKQKVTSLEdmyKRLQEYNTSLQQyntkLQTDLEVAREAHTRAEKEKSSILENLTTLRG 253
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAE----AEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 254 HSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSG 333
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250 260
....*....|....*....|....*...
gi 1063721133 334 SLEETCSLQKERIKMLEQELAFAKEKLK 361
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-299 |
3.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 174 AEKLQVsLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEV--AREAHTRAEKEKSSILENLTTL 251
Cdd:COG4913 609 RAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1063721133 252 RGhsksLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDR 299
Cdd:COG4913 688 AA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
98-412 |
5.04e-05 |
|
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: 47.09 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 98 ETHVQDKENLSSSLQSAEKRYSD--KELDAKTKEEE------------LRATITEMKENI---ESLQEKLSKEK------ 154
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQhiQDLEEQLDEEEaarqklqlekvtTEAKIKKLEEDIlllEDQNSKLSKERklleer 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 155 LSKLDAIENHRREK---------DCRVVAEKLQVSLREElDKVKEEKMAAKQKV----TSLEDMYKRLQEYNTSLQQYNT 221
Cdd:pfam01576 161 ISEFTSNLAEEEEKakslsklknKHEAMISDLEERLKKE-EKGRQELEKAKRKLegesTDLQEQIAELQAQIAELRAQLA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 222 KLQTDLEVAReahTRAEKE---KSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSEL-------- 290
Cdd:pfam01576 240 KKEEELQAAL---ARLEEEtaqKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELedtldtta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 291 --QQVRDDRDRHVVQSQK-LAGEILMYKESVG----KSSHELDILiakSGSLEET----CSLQKERiKMLEQELAFAKEK 359
Cdd:pfam01576 317 aqQELRSKREQEVTELKKaLEEETRSHEAQLQemrqKHTQALEEL---TEQLEQAkrnkANLEKAK-QALESENAELQAE 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1063721133 360 LKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEgelLRKKLHNTILEL 412
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE---LAEKLSKLQSEL 442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-325 |
6.81e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 124 DAKTKEEELRATITEMKENIESLQEKLSKeklskLDAIENHRREKdcRVVAEKLQVSLREELDKvkeekMAAKQKVTSLE 203
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA-----LEAELDALQER--REALQRLAEYSWDEIDV-----ASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 204 DMYKRLQEYNTSLQQyntkLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEv 283
Cdd:COG4913 675 AELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063721133 284 nNLQSELQQVRDDRDRHVVQsQKLAGEILMYKESVGKSSHEL 325
Cdd:COG4913 750 -LLEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEEL 789
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
104-425 |
6.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 104 KENLSSSLQSAEKRYSDKELDAKTKE-EELRATITEMKENIESLQEKLSKEKlSKLDAIENHRREKDCRVV-AEKLQVSL 181
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEElEQLREELEQAREELEQLEEELEQAR-SELEQLEEELEELNEQLQaAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 182 REELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQ 261
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 262 LASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSL 341
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 342 QKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRVFCR 421
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
....
gi 1063721133 422 VRPL 425
Cdd:COG4372 340 ADLL 343
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
63-278 |
1.18e-04 |
|
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: 45.14 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 63 ERAKAGKFDTKGKIEQMTDIIKKLKvcvrwyQQVDEThVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRAT---ITEM 139
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALK------KEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELekeIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 140 KENIESLQEKLSK-----EKLSKLDAIENHRREKDCRVVAEKLQV------SLREELDKVKEEKMAAKQKVTSLEDMYKR 208
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYlkylapARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 209 LQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDS 278
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
71-354 |
1.21e-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: 45.78 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 71 DTKGKIEQMTDIIKKLKvcvrwyQQVD--ETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESL-- 146
Cdd:TIGR04523 325 EIQNQISQNNKIISQLN------EQISqlKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLes 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 147 ----QEKLSKEKLSKLDAIENHRREKdcrvvaEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQ---- 218
Cdd:TIGR04523 399 kiqnQEKLNQQKDEQIKKLQQEKELL------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkv 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 219 ----YNtKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVR 294
Cdd:TIGR04523 473 lsrsIN-KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 295 DDRDRhvvqsQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELA 354
Cdd:TIGR04523 552 FELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-405 |
1.47e-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: 45.35 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 1 MFKKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDT-----KGK 75
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESelakeEIL 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 76 IEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKL 155
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 156 --SKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQyNTKLQTDLEVAREA 233
Cdd:pfam02463 776 laEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL-ELKEEQKLEKLAEE 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 234 HTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEvnNLQSELQQVRDDRDRHVVQSQKLAGEILM 313
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE--EESQKLNLLEEKENEIEERIKEEAEILLK 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 314 YKESVGKSSHELDILIAKSGSLEETcslQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQdrLADTER 393
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEE---EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE--EEKKKL 1007
|
410
....*....|..
gi 1063721133 394 QLFEGELLRKKL 405
Cdd:pfam02463 1008 IRAIIEETCQRL 1019
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
110-337 |
1.75e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 110 SLQSAEKRYSDKE-LDAKTKEEELRATITEMKENIESlQEKLSKEKLSklDAIENHRREKDCRVVAEKLQV-SLREELDK 187
Cdd:PLN02939 154 ALEDLEKILTEKEaLQGKINILEMRLSETDARIKLAA-QEKIHVEILE--EQLEKLRNELLIRGATEGLCVhSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 188 VKEEKMAAKQKVTSLEDMYKRLQEYNTSLqqyntklqtdlevareahTRAEKEKsSILENlttlrghskSLQDQLASSRV 267
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEVAETEERV------------------FKLEKER-SLLDA---------SLRELESKFIV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 268 SQDEAVK----QKDSLLMEVNNLQSELQQVRDDRDRHVV---QSQKLAGEILMYKESVGK------SSHELDILIAKSGS 334
Cdd:PLN02939 283 AQEDVSKlsplQYDCWWEKVENLQDLLDRATNQVEKAALvldQNQDLRDKVDKLEASLKEanvskfSSYKVELLQQKLKL 362
|
...
gi 1063721133 335 LEE 337
Cdd:PLN02939 363 LEE 365
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
102-404 |
2.60e-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: 44.58 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 102 QDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSL 181
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 182 REELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQ 261
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 262 LASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRhVVQSQKLAGEILMYKESVGKSshELDILIAKSGSLEETCSL 341
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-EEKEAQLLLELARQLEDLLKE--EKKEELEILEEEEESIEL 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063721133 342 QKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKK 404
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-300 |
2.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 101 VQDKENLSSSLQSAEKRYSDKELDAKTKEE---ELRATITEMKENIESLQE---KLSKEKLSKLD-AIENHRREKDCRVV 173
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELREraaELEAEAEEKREaAAEAEEEAEEAREE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 174 AEKLQVSL------REELDKVkEEKMAAkqkVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSilEN 247
Cdd:PRK02224 574 VAELNSKLaelkerIESLERI-RTLLAA---IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE--AR 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063721133 248 LTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRH 300
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
126-399 |
7.62e-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: 43.13 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 126 KTKEEELRATITEMKENIESLQEKLSK------EKLSKLDAIENH--RREKDCRVVAEKLQvSLREELDKVKEEKMAAKQ 197
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRienrldELSQELSDASRKigEIEKEIEQLEQEEE-KLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 198 KVT----SLEDMYKRLQEYNTSLQQYNTKLQtDLEvAREAHTRAEKekssilenlttLRGHSKSLQDQLASSRVSQDEAV 273
Cdd:TIGR02169 752 EIEnvksELKELEARIEELEEDLHKLEEALN-DLE-ARLSHSRIPE-----------IQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 274 KQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQEL 353
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1063721133 354 AFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGE 399
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-294 |
8.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 121 KELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQvSLREELDKVKEEKMAAKQKVT 200
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-ALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 201 SLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAhtrAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSL- 279
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLe 233
|
170
....*....|....*.
gi 1063721133 280 -LMEVNNLQSELQQVR 294
Cdd:COG4717 234 nELEAAALEERLKEAR 249
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
111-375 |
1.11e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 111 LQSAEKRYSDKELDAKT------KEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLrEE 184
Cdd:COG5022 877 VELAERQLQELKIDVKSisslklVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL-PE 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 185 LDKVKEEKMAAKQKVTSLEDMYKRLQEY-------NTSLQQYNTKLQTDLE--VAREAHTRAEKEKSSILENLTTlrgHS 255
Cdd:COG5022 956 LNKLHEVESKLKETSEEYEDLLKKSTILvregnkaNSELKNFKKELAELSKqyGALQESTKQLKELPVEVAELQS---AS 1032
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 256 KSLQDQLASSRVSQDEAvKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKL--------------AGEILMYKESVGKS 321
Cdd:COG5022 1033 KIISSESTELSILKPLQ-KLKGLLLLENNQLQARYKALKLRRENSLLDDKQLyqlestenllktinVKDLEVTNRNLVKP 1111
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1063721133 322 SHELDILIAKSGSLEetcsLQKERIKMLEQELAFakekLKMVDLSMSHTMTEFE 375
Cdd:COG5022 1112 ANVLQFIVAQMIKLN----LLQEISKFLSQLVNT----LEPVFQKLSVLQLELD 1157
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-397 |
1.26e-03 |
|
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: 42.43 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 126 KTKEEELRATITEMKENIESLQEKLSKEklSKLDAI-ENHRREKDCRVVAEKLQV-SLREELDKVKEEKMAAKQKVTSLE 203
Cdd:pfam07111 323 KAQDLEHRDSVKQLRGQVAELQEQVTSQ--SQEQAIlQRALQDKAAEVEVERMSAkGLQMELSRAQEARRRQQQQTASAE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 204 DMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRG--HSKSLQDQLASSRVSQDEAVKQKDSllm 281
Cdd:pfam07111 401 EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGlmARKVALAQLRQESCPPPPPAPPVDA--- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 282 evnNLQSELQQVRDDRDRHVVQSQKLAGEIlmyKESVGKSSHELDI----LIAKSGSLEETCSLQKERIKMLEQELAFAK 357
Cdd:pfam07111 478 ---DLSLELEQLREERNRLDAELQLSAHLI---QQEVGRAREQGEAerqqLSEVAQQLEQELQRAQESLASVGQQLEVAR 551
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063721133 358 EKLKMVDLSMSHTMTEFEEQKQCMHE-LQDRLADTERQLFE 397
Cdd:pfam07111 552 QGQQESTEEAASLRQELTQQQEIYGQaLQEKVAEVETRLRE 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-419 |
1.71e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 228 EVAREAHT-RAEKEKSSILENLTTLRghskSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQK 306
Cdd:COG1196 210 EKAERYRElKEELKELEAELLLLKLR----ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 307 LAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQD 386
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190
....*....|....*....|....*....|...
gi 1063721133 387 RLADTERQLFEGELLRKKLHNTILELKGNIRVF 419
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
103-392 |
1.76e-03 |
|
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: 41.59 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 103 DKENLSSSLQSAEKRYSDKeldAKTKEEELRATITEMKENiESLQEKLSKEKLSKLDAienhrrEKDCRVVAEKL----Q 178
Cdd:pfam15742 73 DSTKMCSSLTAEWKHCQQK---IRELELEVLKQAQSIKSQ-NSLQEKLAQEKSRVADA------EEKILELQQKLehahK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 179 VSLRE----ELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTdlevareaHTRAEKEKSSILENLTTLRGH 254
Cdd:pfam15742 143 VCLTDtcilEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQ--------QVRSLQDKEAQLEMTNSQQQL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 255 SKSLQD----QLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQsqkLAGEILMYKEsvgKSSHELDILIA 330
Cdd:pfam15742 215 RIQQQEaqlkQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVLKQ---LDVHVRKYNE---KHHHHKAKLRR 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063721133 331 KSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTE 392
Cdd:pfam15742 289 AKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQE 350
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
74-413 |
2.24e-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: 41.35 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 74 GKIEQMTDI--IKKLKVCVrwyqqvdethVQDK-ENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKl 150
Cdd:pfam10174 380 GEIRDLKDMldVKERKINV----------LQKKiENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEK- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 151 skEKLskldaIEN--HRREKDCRVVAEKLQvSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQT--- 225
Cdd:pfam10174 449 --ERI-----IERlkEQREREDRERLEELE-SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSklk 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 226 DLEVAREAHTraekekssilENLTTLRGHSKSLQDQLASSRVSQDEAVKqkdsllmeVNNLQSELQQVRDDRDRHVVQSQ 305
Cdd:pfam10174 521 SLEIAVEQKK----------EECSKLENQLKKAHNAEEAVRTNPEINDR--------IRLLEQEVARYKEESGKAQAEVE 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 306 KLAG---EILMYKESVGKSSHELDILIAKSGSLEET---------CSLQKERIKMLEQELafaKEKLKMVD----LSMSH 369
Cdd:pfam10174 583 RLLGilrEVENEKNDKDKKIAELESLTLRQMKEQNKkvanikhgqQEMKKKGAQLLEEAR---RREDNLADnsqqLQLEE 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1063721133 370 TMTEFEEQKQCMHELQDRLADTERQLFEGE-------LLRKKLHNTILELK 413
Cdd:pfam10174 660 LMGALEKTRQELDATKARLSSTQQSLAEKDghltnlrAERRKQLEEILEMK 710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
110-414 |
2.29e-03 |
|
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: 41.63 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 110 SLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAI-ENHRREKDCRVVAEKLQVSlREELDKV 188
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIkENNATRHLCNLLKETCARS-AEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 189 KEEKMAAKQ-----------KVTSLEDMykRLQEYNTSLQQYnTKLQTDLEVAREAHTRAEKE----------------- 240
Cdd:pfam05483 175 EYEREETRQvymdlnnniekMILAFEEL--RVQAENARLEMH-FKLKEDHEKIQHLEEEYKKEindkekqvsllliqite 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 241 KSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQkdsLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGK 320
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE---LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 321 SSHELDILIAKSGSLE------------ETCSLQkERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQC-------M 381
Cdd:pfam05483 329 LTEEKEAQMEELNKAKaahsfvvtefeaTTCSLE-ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveL 407
|
330 340 350
....*....|....*....|....*....|...
gi 1063721133 382 HELQDRLADTERQLFEgellRKKLHNTILELKG 414
Cdd:pfam05483 408 EELKKILAEDEKLLDE----KKQFEKIAEELKG 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-412 |
2.97e-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: 40.52 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 215 SLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVR 294
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 295 DDRDRHVVQSQKLAG----EILMYKESVGKSSHELDILIAKSGSLE---ETCSLQKERIKMLEQELAFAKEKLKMVDLSM 367
Cdd:COG4942 104 EELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063721133 368 SHTMTEFE----EQKQCMHELQDRLADTERQLFEGELLRKKLHNTILEL 412
Cdd:COG4942 184 EEERAALEalkaERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-405 |
3.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 98 ETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRAT---ITEMKENIESLQEKL--------SKEKLSKLDAIENHRR 166
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELeerIEELKKEIEELEEKVkelkelkeKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 167 EKDCRVvaEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEyntslqqyntkLQTDLEVAREAHTRAEKEKsSILE 246
Cdd:PRK03918 307 DELREI--EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE-----------LEKRLEELEERHELYEEAK-AKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 247 NLTTLRGHSKSLQDQLASSRVsqDEAVKQKDSLLMEVNNLQ---SELQQVRDDRDRHVVQSQKLAGE------------- 310
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKEL--EELEKAKEEIEEEISKITariGELKKEIKELKKAIEELKKAKGKcpvcgrelteehr 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 311 ---ILMYKESVGKSSHELDILIAKSGSL-------EETCSLQKERIKMLE--QELAFAKEKLKMVDLS-MSHTMTEFEEQ 377
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLrkelrelEKVLKKESELIKLKElaEQLKELEEKLKKYNLEeLEKKAEEYEKL 530
|
330 340
....*....|....*....|....*...
gi 1063721133 378 KQCMHELQDRLADTERQLFEGELLRKKL 405
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-272 |
3.00e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 95 QVDETHVQDK-ENLSSSLQSAEKRYSDKELDAKTKEEELRAT---ITEMKENIESLQEKLSK---------EKLSKLDAI 161
Cdd:COG3883 29 QAELEAAQAElDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGEraralyrsgGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 162 EN--------HRREkdcrvVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREA 233
Cdd:COG3883 109 LGsesfsdflDRLS-----ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063721133 234 HTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEA 272
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
102-240 |
4.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 102 QDKENLSSSLQSAEKRYSDKELDAKTKEEElratITEMKENIESLQEKLSKEKLSK-LDA----IENHRREKDcrvVAEK 176
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNKeYEAlqkeIESLKRRIS---DLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063721133 177 LQVSLREELDKVKEEKMAAKQKVTSLEdmyKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKE 240
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
95-377 |
4.72e-03 |
|
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: 40.49 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 95 QVDETHVQdKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKenieslQEKLSKEKLSKLDAIENHRREKDCRVVA 174
Cdd:pfam15921 589 QVEKAQLE-KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE------KVKLVNAGSERLRAVKDIKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 175 EKlqvSLREELDKVKEE----KMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTT 250
Cdd:pfam15921 662 VK---TSRNELNSLSEDyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 251 LRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDrhvvqsqKLAGeilmykesvgksshELDILIA 330
Cdd:pfam15921 739 KRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN-------KMAG--------------ELEVLRS 797
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063721133 331 KSGSLEETCS-----LQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQ 377
Cdd:pfam15921 798 QERRLKEKVAnmevaLDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-417 |
4.88e-03 |
|
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: 40.39 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 106 NLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLS-----KEKLSKLDA--------IENHRREKDcrv 172
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKeleqnNKKIKELEKqlnqlkseISDLNNQKE--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 173 vaEKLQVSLREELDKVKEEKMAAK-------QKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSIL 245
Cdd:TIGR04523 306 --QDWNKELKSELKNQEKKLEEIQnqisqnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 246 ENLTTLRGHSKSLQDQLASsrvsQDEAVKQKDSllmEVNNLQSELQqvrddrdrhvvqsqKLAGEILMYKESVGKSSHEL 325
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQN----QEKLNQQKDE---QIKKLQQEKE--------------LLEKEIERLKETIIKNNSEI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 326 DILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLfegellrKKL 405
Cdd:TIGR04523 443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-------KDL 515
|
330
....*....|..
gi 1063721133 406 HNTILELKGNIR 417
Cdd:TIGR04523 516 TKKISSLKEKIE 527
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
130-293 |
4.93e-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: 40.54 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 130 EELRATITEMKENIESLQEKLSKEKLSKLDAIENHR--------------REKDCRVVAEKLQVSLREELDKVKEE---- 191
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIReleaqiselqedleSERAARNKAEKQRRDLGEELEALKTEledt 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 192 --KMAAKQKVTS-----LEDMYKRLQE----YNTSLQQYNTK-------LQTDLEVAREAHTRAEKEKSSI--------- 244
Cdd:pfam01576 312 ldTTAAQQELRSkreqeVTELKKALEEetrsHEAQLQEMRQKhtqaleeLTEQLEQAKRNKANLEKAKQALesenaelqa 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063721133 245 -LENLTTLRGHS----KSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQV 293
Cdd:pfam01576 392 eLRTLQQAKQDSehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
102-211 |
5.42e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 102 QDKENLS---SSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKlSKLD-----AIENHRREKDcrVV 173
Cdd:PRK00409 513 EDKEKLNeliASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLL-EEAEkeaqqAIKEAKKEAD--EI 589
|
90 100 110
....*....|....*....|....*....|....*...
gi 1063721133 174 AEKLQVSLREELDKVKEEKMAAKQKvtSLEDMYKRLQE 211
Cdd:PRK00409 590 IKELRQLQKGGYASVKAHELIEARK--RLNKANEKKEK 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
139-301 |
5.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 139 MKENIESLqEKLSkEKLSKLDAIENHRRE--------KDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQ 210
Cdd:COG1579 2 MPEDLRAL-LDLQ-ELDSELDRLEHRLKElpaelaelEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 211 EyntslQQYNTK-------LQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSllmEV 283
Cdd:COG1579 80 E-----QLGNVRnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---EL 151
|
170
....*....|....*...
gi 1063721133 284 NNLQSELQQVRDDRDRHV 301
Cdd:COG1579 152 AELEAELEELEAEREELA 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-295 |
5.47e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 103 DKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKenieSLQEKLSKEKlsklDAIENHRREKDcRVVAEKLQvsLR 182
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK----DYREKLEKLK----REINELKRELD-RLQEELQR--LS 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 183 EELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRghsKSLQDQL 262
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ---RELAEAE 496
|
170 180 190
....*....|....*....|....*....|...
gi 1063721133 263 ASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRD 295
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
124-322 |
5.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 124 DAKTKEEELRATITEMKENIESLQEKLSKeklsKLDAIENHRREKDcrvVAEKLQVSLREELDKVKEE--KMAAKQKV-- 199
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEID---KLQAEIAEAEAEIEERREElgERARALYRsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 200 ------------TSLEDMYKRLQeYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRV 267
Cdd:COG3883 100 gsvsyldvllgsESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063721133 268 SQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSS 322
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-417 |
5.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 59 ALLNERAKAGKFDTKGKIEQMTDI------IKKLKVCVRWYQQVdethVQDKENLSSSLQSAEKRYSDKELDAKTKE--- 129
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELkeleeeLKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEkll 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 130 ---------EELRATITEMKENIESLQEKLS--KEKLSKLDAIENHRREKDCRVVAEKLQVSL--REELDKVKEEKMAAK 196
Cdd:COG4717 126 qllplyqelEALEAELAELPERLEELEERLEelRELEEELEELEAELAELQEELEELLEQLSLatEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 197 QKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAE-------------------------------------- 238
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglggsllsliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 239 ---------KEKSSILENLTTLRG-------HSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVV 302
Cdd:COG4717 286 lallflllaREKASLGKEAEELQAlpaleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 303 QSQKLAGEILMykESVGKSSHEldiliaksgSLEETCSLQKERIKmLEQELAFAKEKLKMVDLSMSHTMTEFEEqkqcmH 382
Cdd:COG4717 366 EELEQEIAALL--AEAGVEDEE---------ELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLEALDE-----E 428
|
410 420 430
....*....|....*....|....*....|....*
gi 1063721133 383 ELQDRLADTERQLFEGELLRKKLHNTILELKGNIR 417
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELE 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-264 |
5.96e-03 |
|
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: 40.43 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 3 KKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDI 82
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 83 IKKLKvcvrwyQQVDETHvQDKENLSSSLQSAEKRYSDKELDAKTKE---EELRATITEMKENIESLQEKLSKEKLSKLD 159
Cdd:TIGR02168 798 LKALR------EALDELR-AELTLLNEEAANLRERLESLERRIAATErrlEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 160 AIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQE----YNTSLQQYNTKLQTDLEVAREAHT 235
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREklaqLELRLEGLEVRIDNLQERLSEEYS 950
|
250 260 270
....*....|....*....|....*....|...
gi 1063721133 236 R----AEKEKSSILENLTTLRGHSKSLQDQLAS 264
Cdd:TIGR02168 951 LtleeAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
126-386 |
7.62e-03 |
|
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: 39.70 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 126 KTKEEELRATITEMKENIESLQEKLSK-EKLSKLDAIENHRREKDCRVVAEKLQV-SLREELDKVKEEKMAAKQKVTSL- 202
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSElEEMTKFKNNKEVELEELKKILAEDEKLlDEKKQFEKIAEELKGKEQELIFLl 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 203 EDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSS-----------ILENLTTLRGHS------KSLQDQLASS 265
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieltahcdklLLENKELTQEASdmtlelKKHQEDIINC 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 266 RVSQDEAVKQKDSLLMEVNNLQSELQQVRDD----RDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSL 341
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063721133 342 QKERIKMLEQELAFAKEK-------LKMVDLSMSHTMTEFEEQKQCMHELQD 386
Cdd:pfam05483 606 KNKNIEELHQENKALKKKgsaenkqLNAYEIKVNKLELELASAKQKFEEIID 657
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-416 |
7.87e-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: 39.77 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 183 EELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEkekssilENLTTLRGHSKSLQDQL 262
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE-------EMRARLAARKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 263 A--SSRVSQDEAVKQkdSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCS 340
Cdd:pfam01576 78 HelESRLEEEEERSQ--QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063721133 341 LQKERIKMLEQELAFAKEKLKMVD-LSMSHTMTefeeqkqcMHELQDRLADTERQLFEGELLRKKLHNTILELKGNI 416
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSkLKNKHEAM--------ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
105-312 |
8.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 105 ENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSK--EKLSKLDAIENHRREKDcrvvAEKLQVSLR 182
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELR----EELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 183 EELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQyntkLQTDLEVAREAHTRAEKEKSSILENLT-TLRGHSKSLQDQ 261
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063721133 262 LASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEIL 312
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
61-314 |
8.81e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.65 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 61 LNERAKAGKFDTKGKIEQM--TDIIKKLKVCVRWYQQVDETHVQDKEnlssSLQSAEKRYSDkELDAKTKEEELRATITE 138
Cdd:TIGR01612 1089 IKEKLKHYNFDDFGKEENIkyADEINKIKDDIKNLDQKIDHHIKALE----EIKKKSENYID-EIKAQINDLEDVADKAI 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 139 MKENIESLQEKLsKEKLSKLDAIENHRRE--KDCRVVA--EKLQVSLREE---------------LDKVKEEKMAAKQKV 199
Cdd:TIGR01612 1164 SNDDPEEIEKKI-ENIVTKIDKKKNIYDEikKLLNEIAeiEKDKTSLEEVkginlsygknlgklfLEKIDEEKKKSEHMI 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 200 TSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTrAEKEKSSILENLTTLRGHSKSLQDqlassrvsqdeaVKQKDSL 279
Cdd:TIGR01612 1243 KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISD------------IREKSLK 1309
|
250 260 270
....*....|....*....|....*....|....*
gi 1063721133 280 LMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMY 314
Cdd:TIGR01612 1310 IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLY 1344
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
97-306 |
8.92e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 97 DETHVQDKENLSSSLQSAE--KRYSDKELDAKTKEEELRATITEMKENIESLQE--KLSKEKLSKLDAIE------NHRR 166
Cdd:PRK04863 889 DETLADRVEEIREQLDEAEeaKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQdyQQAQQTQRDAKQQAfaltevVQRR 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 167 -----EKDCRVVAE--KLQVSLREELDKVKEEKMAAKQKVTSLEDmykRLQEYNtslqQYNTKLQTDLEVAREAHTRAEK 239
Cdd:PRK04863 969 ahfsyEDAAEMLAKnsDLNEKLRQRLEQAEQERTRAREQLRQAQA---QLAQYN----QVLASLKSSYDAKRQMLQELKQ 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063721133 240 EkssiLENLTT---------LRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVrdDRD-----RHVVQSQ 305
Cdd:PRK04863 1042 E----LQDLGVpadsgaeerARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL--ERDyhemrEQVVNAK 1115
|
.
gi 1063721133 306 K 306
Cdd:PRK04863 1116 A 1116
|
|
| |
