|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
4-360 |
0e+00 |
|
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: 602.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365 160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365 240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530387683 319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365 320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
6-360 |
1.71e-156 |
|
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: 482.07 E-value: 1.71e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129 70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129 148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300
|
330 340 350
....*....|....*....|....*....|....*
gi 530387683 326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129 301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-353 |
6.53e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 461.27 E-value: 6.53e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225 69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225 148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225 227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301
|
330 340
....*....|....*....|....*
gi 530387683 329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225 302 NISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
50-439 |
8.55e-95 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 318.99 E-value: 8.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059 52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059 124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059 201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059 277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059 353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432
|
...
gi 530387683 437 QSS 439
Cdd:COG5059 433 QFL 435
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-379 |
3.32e-77 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 282.59 E-value: 3.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188 153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188 233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188 311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188 390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
447-545 |
4.13e-68 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438782 [Multi-domain] Cd Length: 99 Bit Score: 224.02 E-value: 4.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730 1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
|
90
....*....|....*....
gi 530387683 527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730 81 HHGDRILWGNNHFFRINLP 99
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
1683-1746 |
3.22e-30 |
|
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 114.42 E-value: 3.22e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683 1683 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1746
Cdd:pfam01302 2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
1683-1747 |
5.85e-26 |
|
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 102.28 E-value: 5.85e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 1683 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1747
Cdd:smart01052 2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
357-469 |
5.41e-25 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 103.77 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183 1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183 81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
|
170
....*....|....*
gi 530387683 455 ADPALNELLVYYLKE 469
Cdd:pfam16183 161 EDPLMSECLLYYIKD 175
|
|
| KIF1B |
pfam12423 |
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ... |
756-802 |
1.85e-13 |
|
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.
Pssm-ID: 463574 Cd Length: 43 Bit Score: 66.09 E-value: 1.85e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530387683 756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423 1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
1683-1752 |
4.58e-13 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 74.34 E-value: 4.58e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1683 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1752
Cdd:COG5244 7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
471-534 |
3.66e-11 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 60.28 E-value: 3.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530387683 471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1422-1660 |
5.10e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.43 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1422 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEmGPDVLVQTm 1500
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPPA-APDRSVPP- 2570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 gapalkicDKPAKVPSPPpviAVTAVTPAPEAqdgPPSPLSEASsgyfshsvstatlsdalgPGLDAAAPPGSMPTAPeA 1580
Cdd:PHA03247 2571 --------PRPAPRPSEP---AVTSRARRPDA---PPQSARPRA------------------PVDDRGDPRGPAPPSP-L 2617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1581 EPEAPISHPPPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPG 1651
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLT 2696
|
....*....
gi 530387683 1652 AEGNAPAPG 1660
Cdd:PHA03247 2697 SLADPPPPP 2705
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1396-1621 |
2.62e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 55.93 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1396 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1475
Cdd:pfam03154 148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1476 rgkrpSPLAHQAQPEMGPDVLVQTMGAPALKIcdKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLS-EASSGYFSHSVST 1554
Cdd:pfam03154 223 -----STAAPHTLIQQTPTLHPQRLPSPHPPL--QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSlQTGPSHMQHPVPP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1555 ATLSDA---------LGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ---QLVSPGRER-- 1613
Cdd:pfam03154 296 QPFPLTpqssqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpipQLPNPQSHKhp 375
|
....*...
gi 530387683 1614 PDLEAPAP 1621
Cdd:pfam03154 376 PHLSGPSP 383
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
1221-1278 |
7.36e-07 |
|
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.
Pssm-ID: 463599 Cd Length: 149 Bit Score: 50.66 E-value: 7.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530387683 1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473 91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1479-1732 |
1.60e-06 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 52.76 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPAlkICDKPAKvpsPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLS 1558
Cdd:COG5180 243 RSRPATVDAQPEMRPPADAKERRRAA--IGDTPAA---EPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1559 DALGPG-LDAAAPPGSMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSP 1624
Cdd:COG5180 317 VRPPGGaRDPGTPRPGQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1625 FR---VRRVRASELRSFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYV 1699
Cdd:COG5180 397 RRgapGPPMGAGDLVQAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADF 469
|
250 260 270
....*....|....*....|....*....|...
gi 530387683 1700 GPADFQEGTWVGVELDLPSGKNDGSIGGKQYFR 1732
Cdd:COG5180 470 VAPVTDATPVDVADVLGVRPDAILGGNVAPASG 502
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1512-1633 |
7.26e-06 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 50.15 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1512 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1583
Cdd:NF040712 200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 530387683 1584 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1633
Cdd:NF040712 280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
468-542 |
1.13e-05 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 45.72 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716 20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
|
|
| bMERB_dom |
pfam12130 |
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ... |
1099-1143 |
1.26e-04 |
|
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.
Pssm-ID: 463467 [Multi-domain] Cd Length: 131 Bit Score: 43.66 E-value: 1.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530387683 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130 66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
|
|
| KLF9_13_N-like |
cd21975 |
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
1501-1620 |
5.54e-04 |
|
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.
Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 42.37 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 GAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSVSTATLSDALGPGLDAAA 1569
Cdd:cd21975 29 GLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGSSLESGDADMGSDSDVAP 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1570 PPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1620
Cdd:cd21975 105 ASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
1558-1642 |
7.17e-04 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 44.22 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1558 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1634
Cdd:NF041121 22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101
|
....*...
gi 530387683 1635 LRSFSRML 1642
Cdd:NF041121 102 PLELARAL 109
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1518-1624 |
1.51e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 42.83 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1518 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1593
Cdd:NF040712 194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
|
90 100 110
....*....|....*....|....*....|.
gi 530387683 1594 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1624
Cdd:NF040712 274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
1511-1678 |
1.74e-03 |
|
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.
Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 43.14 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1582
Cdd:TIGR01645 291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1583 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1656
Cdd:TIGR01645 371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
|
170 180
....*....|....*....|...
gi 530387683 1657 PA-PGAGGQALASDSEEADEVPE 1678
Cdd:TIGR01645 448 LAiMGEAAAALALEPKKKKKEKE 470
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
368-444 |
2.01e-03 |
|
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];
Pssm-ID: 444244 [Multi-domain] Cd Length: 239 Bit Score: 41.89 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530387683 368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493 36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-432 |
2.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
611-760 |
7.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913 612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
4-360 |
0e+00 |
|
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: 602.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365 160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365 240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530387683 319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365 320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
6-360 |
1.71e-156 |
|
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: 482.07 E-value: 1.71e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129 70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129 148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300
|
330 340 350
....*....|....*....|....*....|....*
gi 530387683 326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129 301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-353 |
6.53e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 461.27 E-value: 6.53e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225 69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225 148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225 227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301
|
330 340
....*....|....*....|....*
gi 530387683 329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225 302 NISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
5-351 |
2.69e-142 |
|
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: 443.24 E-value: 2.69e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRRETDLhTKCVVDVDANK-VILNPvntnlsKGDARGQPKVFAYDHCFWSMdesvkekyAGQDIVFKCL 83
Cdd:cd00106 1 NVRVAVRVRPLNGREARS-AKSVISVDGGKsVVLDP------PKNRVAPPKTFAFDAVFDST--------STQEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD-QPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPeQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 163 DPKgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHtlYDVKSGTS 242
Cdd:cd00106 146 SPV-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNS 297
|
330 340
....*....|....*....|....*....
gi 530387683 323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd00106 298 KTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
6-353 |
1.40e-119 |
|
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: 380.65 E-value: 1.40e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 6 VKVAVRIRPMNRRETDLHTKCVVDVDankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmDESVKEkYAGQDIVFKCLGE 85
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVD---EKRGQVSVRNPKATANEPPKTFTFDAVF---DPNSKQ-LDVYDETARPLVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 86 NILQnafdGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01371 76 SVLE----GYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ-FLVRVSYLEIYNEEIRDLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 163 DpKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlYDVKSGTS 242
Cdd:cd01371 151 G-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS-EKGEDGEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01371 229 HIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNS 303
|
330 340 350
....*....|....*....|....*....|.
gi 530387683 323 KTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01371 304 KTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
5-355 |
5.00e-112 |
|
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: 359.22 E-value: 5.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNpvntnLSKGDARgqPKVFAYDHCFwSMDESvkekyagQDIVFKCLg 84
Cdd:cd01366 3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIE-----LTSIGAK--QKEFSFDKVF-DPEAS-------QEDVFEEV- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDP 164
Cdd:cd01366 67 SPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 165 KGSRQT-LKVREHSVLGP-YVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvkSGT- 241
Cdd:cd01366 147 GNAPQKkLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------SGRn 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 242 --SGEK-VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdqsagkNKNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01366 219 lqTGEIsVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSL 292
|
330 340 350
....*....|....*....|....*....|....*..
gi 530387683 319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVN 355
Cdd:cd01366 293 GGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
6-353 |
6.76e-111 |
|
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: 356.65 E-value: 6.76e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 6 VKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNP----------VNTNLSKGDARGQPKVFAYDHCFwsmDEsvkekYA 74
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmDNHMLVFDPkdeedgffhgGSNNRDRRKRRNKELKYVFDRVF---DE-----TS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 75 GQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIY 154
Cdd:cd01370 74 TQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK-DEKEFEVSMSYLEIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 155 NEKVRDLLDPKGSRqtLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTl 234
Cdd:cd01370 153 NETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 235 YDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsaGKNKNKFVPYRDSVLTWLL 314
Cdd:cd01370 230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 530387683 315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01370 307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
3-353 |
2.23e-110 |
|
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: 354.33 E-value: 2.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 3 DSKVKVAVRIRPMNRRETDLHTKCVVDVDankvilnPVNTNLSKGDARGqpKVFAYDHCFwSMDesvkekyAGQDIVFKC 82
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFD-------PEDTVVIATSETG--KTFSFDRVF-DPN-------TTQEDVYNF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEIYNEKVR 159
Cdd:cd01369 64 AAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSM-DENLEFHVKVSYFEIYMEKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 160 DLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlyDVKS 239
Cdd:cd01369 143 DLLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVET 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 240 GTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLG 319
Cdd:cd01369 219 EKK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLG 291
|
330 340 350
....*....|....*....|....*....|....
gi 530387683 320 GNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01369 292 GNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
4-353 |
6.00e-110 |
|
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: 353.56 E-value: 6.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANK--VILnpvntnlskgdarGQPKVFAYDHCFWSMDEsvkekyagQDIVFK 81
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEpqVTV-------------GTDKSFTFDYVFDPSTE--------QEEVYN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA------DQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYN 155
Cdd:cd01372 60 TCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKVSFLEIYN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 156 EKVRDLLDPKG-SRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTL 234
Cdd:cd01372 139 EEIRDLLDPETdKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 235 YDVKSGTSGEK------VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgknKNKFVPYRDS 308
Cdd:cd01372 219 KNGPIAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK---KGAHVPYRDS 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530387683 309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01372 296 KLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
5-353 |
9.98e-109 |
|
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: 349.32 E-value: 9.98e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNlskgdargqpkvFAYDHCFwSMDESVKEkyagqdiVFKCL 83
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLvEPPSTS------------FTFDHVF-GGDSTNRE-------VYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQkeENEEQSFKVEVSYMEIYNEKVRDLLD 163
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKINDLLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 164 PKGsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGtSG 243
Cdd:cd01374 139 PTS--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 244 EKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqSAGKnKNKFVPYRDSVLTWLLKDSLGGNSK 323
Cdd:cd01374 216 VRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGK-VGGHIPYRDSKLTRILQPSLGGNSR 291
|
330 340 350
....*....|....*....|....*....|
gi 530387683 324 TAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01374 292 TAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
6-362 |
1.35e-100 |
|
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: 327.54 E-value: 1.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 6 VKVAVRIRPMNRRETDL-HTKCVVDVDANKVILNPVntnlskgdargQPKVFAYDHcfwsmdesVKEKYAGQDIVFKCLG 84
Cdd:cd01373 3 VKVFVRIRPPAEREGDGeYGQCLKKLSSDTLVLHSK-----------PPKTFTFDH--------VADSNTNQESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP--------GLIPRLCSGLFERTQKEEN---EEQSFKVEVSYMEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEkagEGKSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 154 YNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 233
Cdd:cd01373 144 YNEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 234 lYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNkfVPYRDSVLTWL 313
Cdd:cd01373 221 -WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRH--VCYRDSKLTFL 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530387683 314 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01373 298 LRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
3-362 |
4.93e-95 |
|
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: 311.57 E-value: 4.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 3 DSKVKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNPVNTNLSKGDArgqpKVFAYDHCFWSmdesvkekYAGQDIVFK 81
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVdPVRKEVSVRTGGLADKSST----KTYTFDMVFGP--------EAKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMG-----------TADQPGLIPRLCSGLFERTqkeENEEQSFKVEVSY 150
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKL---EDNGTEYSVKVSY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 151 MEIYNEKVRDLLDPKGS-RQTLKVREHS--VLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFK 227
Cdd:cd01364 146 LEIYNEELFDLLSPSSDvSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 228 ITLthtlYDVKSGTSGE---KVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagknKNKFVP 304
Cdd:cd01364 226 ITI----HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVP 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 305 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01364 296 YRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
50-439 |
8.55e-95 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 318.99 E-value: 8.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059 52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059 124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059 201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059 277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059 353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432
|
...
gi 530387683 437 QSS 439
Cdd:COG5059 433 QFL 435
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
5-351 |
4.83e-79 |
|
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: 265.41 E-value: 4.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRRETDLHTK-CVVDVDANKVILNPVNTNLSKGDARG---QPKVFAYDHCFwSMDESVKEKYAGqdiVF 80
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEgCIEVINSTTVVLHPPKGSAANKSERNggqKETKFSFSKVF-GPNTTQKEFFQG---TA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 81 KCLGENILQnafdGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFertqkeeNEEQSFKVEVSYMEIYNEKVRD 160
Cdd:cd01368 78 LPLVQDLLH----GKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF-------NSIGGYSVFVSYIEIYNEYIYD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 161 LLDPKGS-----RQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL----T 231
Cdd:cd01368 147 LLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 232 HTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdQSAGKNKNKFVPYRDSVLT 311
Cdd:cd01368 227 DSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLR-ENQLQGTNKMVPFRDSKLT 305
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530387683 312 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01368 306 HLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-379 |
3.32e-77 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 282.59 E-value: 3.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188 153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188 233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188 311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188 390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
5-351 |
8.14e-75 |
|
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: 252.89 E-value: 8.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRREtdlHTKCVVDVDaNKVILNPVNTNLSKGDARGQPKVFAYdhcfwSMDESVKEkyAGQDIVFKCLG 84
Cdd:cd01375 1 KVQAFVRVRPTDDFA---HEMIKYGED-GKSISIHLKKDLRRGVVNNQQEDWSF-----KFDGVLHN--ASQELVYETVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD---QPGLIPRLCSGLFErtQKEENEEQSFKVEVSYMEIYNEKVRDL 161
Cdd:cd01375 70 KDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFR--MIEERPTKAYTVHVSYLEIYNEQLYDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 162 LDPK----GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL---THTL 234
Cdd:cd01375 148 LSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeahSRTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 235 YDVKSGTSgekvgKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQsagknKNKFVPYRDSVLTWLL 314
Cdd:cd01375 228 SSEKYITS-----KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHVPFRQSKLTHVL 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 530387683 315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01375 298 RDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-351 |
2.28e-74 |
|
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: 251.06 E-value: 2.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIlnPVNTNLSKGDARGQPKV--FAYDHCFwsmDESVKekyagQDIVFKC 82
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTL--IVHEPKLKVDLTKYIENhtFRFDYVF---DESSS-----NETVYRS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMG----TADQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKV 158
Cdd:cd01367 71 TVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN-LGVTVSFFEIYGGKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 159 RDLLDPKgsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvK 238
Cdd:cd01367 150 FDLLNRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------R 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 239 SGTSGEKVGKLSLVDLAGSERATKTGAAG-DRLKEGSNINKSLTTLGLVISALADQSAgknknkFVPYRDSVLTWLLKDS 317
Cdd:cd01367 220 DRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA------HIPFRGSKLTQVLKDS 293
|
330 340 350
....*....|....*....|....*....|....*
gi 530387683 318 L-GGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01367 294 FiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
6-351 |
6.34e-69 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 235.09 E-value: 6.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 6 VKVAVRIRPMNRRETDLHTKCVVDvdankvILNPVNTNLSKGDARGQPKVFAYDHcFWSMDESVKEKYAGQdivFKClge 85
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVS------GIDSCSVELADPRNHGETLKYQFDA-FYGEESTQEDIYARE---VQP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 86 nILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEneeQSFKVEVSYMEIYNEKVRDLLDPK 165
Cdd:cd01376 69 -IVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA---WALSFTMSYLEIYQEKILDLLEPA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 166 GSRqtLKVRE---HSVLGPyvdGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVksgTS 242
Cdd:cd01376 145 SKE--LVIREdkdGNILIP---GLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---PF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqsagKNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01376 217 RQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------NKNLPRIPYRDSKLTRLLQDSLGGGS 290
|
330 340
....*....|....*....|....*....
gi 530387683 323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01376 291 RCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
447-545 |
4.13e-68 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438782 [Multi-domain] Cd Length: 99 Bit Score: 224.02 E-value: 4.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730 1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
|
90
....*....|....*....
gi 530387683 527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730 81 HHGDRILWGNNHFFRINLP 99
|
|
| FHA_KIF13 |
cd22706 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ... |
447-545 |
2.40e-59 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438758 [Multi-domain] Cd Length: 101 Bit Score: 199.06 E-value: 2.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANS---QDIQLCGMGILPEHCIIDItSEGQVMLTPQKNTRTFVNGSSVSSP 523
Cdd:cd22706 1 KYYLVNLNADPSLNELLVYYLKEHTLIGRSDAptqQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79
|
90 100
....*....|....*....|..
gi 530387683 524 IQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22706 80 TQLRHGDRILWGNNHFFRLNCP 101
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
447-550 |
1.41e-55 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438781 [Multi-domain] Cd Length: 109 Bit Score: 188.56 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22729 1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80
|
90 100
....*....|....*....|....
gi 530387683 527 HHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22729 81 WHGDRILWGNNHFFRINLPKRKRR 104
|
|
| FHA_KIF1 |
cd22705 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
450-543 |
7.81e-34 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438757 [Multi-domain] Cd Length: 101 Bit Score: 126.19 E-value: 7.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22705 4 LVNLNEDPLMSECLLYYIKPgITRVGRADAdvpQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPTR 82
|
90
....*....|....*...
gi 530387683 526 LHHGDRILWGNNHFFRLN 543
Cdd:cd22705 83 LKTGSRVILGKNHVFRFN 100
|
|
| FHA_KIF14 |
cd22707 |
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ... |
450-545 |
3.90e-31 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438759 [Multi-domain] Cd Length: 108 Bit Score: 118.52 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKE-HTLIGS--ANSQ-DIQLCGMGILPEHCIIdITSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22707 10 LVNLNEDPQLSEMLLYMLKEgQTRVGRskASSShDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88
|
90 100
....*....|....*....|
gi 530387683 526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22707 89 LHHGDRVILGGDHYFRFNHP 108
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
1683-1746 |
3.22e-30 |
|
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 114.42 E-value: 3.22e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683 1683 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1746
Cdd:pfam01302 2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
448-545 |
1.55e-28 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438761 [Multi-domain] Cd Length: 102 Bit Score: 110.77 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 448 CFLVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIdITSEGQVMLTPQKNT-RTFVNGSSVSS 522
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEgETTIGRADAepePDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPGaKVIVNGVPVTG 79
|
90 100
....*....|....*....|...
gi 530387683 523 PIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22709 80 ETELHHLDRVILGSNHLYVFVGP 102
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
58-289 |
3.76e-28 |
|
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: 112.44 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 58 YDHCFWSMDeSVKEKYAGQDIVFKcLGENILQNAFDGYN-ACIFAYGQTGSGKSYTMMGtadqpgLIPRLCSGLFERTQK 136
Cdd:cd01363 15 RDSKIIVFY-RGFRRSESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 137 EENEEQsfkvevsymeiynekvrdlldpkgsrqtlkvrehsvlgpyvDGLSKLAVTSYKDIESLMSEGNKSRTvAATNMN 216
Cdd:cd01363 87 GETEGW-----------------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRN 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530387683 217 EESSRSHAVFKItlthtlydvksgtsgekvgklsLVDLAGSERatktgaagdrlkegsnINKSLTTLGLVISA 289
Cdd:cd01363 125 ENSSRFGKFIEI----------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
1683-1747 |
5.85e-26 |
|
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 102.28 E-value: 5.85e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 1683 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1747
Cdd:smart01052 2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
357-469 |
5.41e-25 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 103.77 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183 1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183 81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
|
170
....*....|....*
gi 530387683 455 ADPALNELLVYYLKE 469
Cdd:pfam16183 161 EDPLMSECLLYYIKD 175
|
|
| FHA_KIF1B |
cd22727 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ... |
450-547 |
1.62e-23 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438779 [Multi-domain] Cd Length: 110 Bit Score: 97.03 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVS 521
Cdd:cd22727 5 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNNNGEVIVTlePCERSETYVNGKRVV 84
|
90 100
....*....|....*....|....*.
gi 530387683 522 SPIQLHHGDRILWGNNHFFRLNLPKK 547
Cdd:cd22727 85 QPVQLRSGNRIIMGKNHVFRFNHPEQ 110
|
|
| FHA_KIF1A |
cd22726 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
450-554 |
4.25e-20 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438778 [Multi-domain] Cd Length: 115 Bit Score: 87.29 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQ--VMLTPQKNTRTFVNGSSVS 521
Cdd:cd22726 4 LVNLNEDPLMSECLLYYIKDGiTRVGREDAerrQDIVLSGHFIKEEHCIFrsDTRSGGEavVTLEPCEGADTYVNGKKVT 83
|
90 100 110
....*....|....*....|....*....|...
gi 530387683 522 SPIQLHHGDRILWGNNHFFRLNLPKKKKKaERE 554
Cdd:cd22726 84 EPSILRSGNRIIMGKSHVFRFNHPEQARQ-ERE 115
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
5-162 |
3.68e-19 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 85.73 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 5 KVKVAVRIRPMNRREtdlhtkcvvdvdankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmdesvkEKYAGQDIVFKCLg 84
Cdd:pfam16796 21 NIRVFARVRPELLSE---------------AQIDYPDETSSDGKIGSKNKSFSFDRVF--------PPESEQEDVFQEI- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 85 ENILQNAFDGYNACIFAYGQTGSGKSytmmgtadqPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:pfam16796 77 SQLVQSCLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGWK-YTIELQFVEIYNESSQDLL 144
|
|
| FHA_KIF1C |
cd22728 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
450-543 |
1.65e-17 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 79.53 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKEH-TLIGSANSqDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVSSPI 524
Cdd:cd22728 4 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLSGQFIREQHCLFrsIPNPSGEVVVTlePCEGAETYVNGKQVTEPL 82
|
90
....*....|....*....
gi 530387683 525 QLHHGDRILWGNNHFFRLN 543
Cdd:cd22728 83 VLKSGNRIVMGKNHVFRFN 101
|
|
| FHA_KIF16 |
cd22708 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ... |
450-545 |
3.82e-17 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438760 [Multi-domain] Cd Length: 109 Bit Score: 78.85 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22708 11 LIGIDDDLLSTGVVLYHLKEgKTRIGREDApqeQDIVLDGEDIEAEHCIIE-NVGGVVTLHPLPGALCAVNGQVITQPTR 89
|
90 100
....*....|....*....|
gi 530387683 526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22708 90 LTQGDVILLGKTNMFRFNHP 109
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
448-545 |
2.77e-15 |
|
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438763 [Multi-domain] Cd Length: 106 Bit Score: 73.51 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 448 CFLVNLNADPALNellvYYLKEH------TLIGSANS-----QDIQLCGMGILPEHCIIDITsEGQVMLTP-QKNTRTFV 515
Cdd:cd22711 2 PYLLELSPDGSDR----DKPRRHrlqpnvTEVGSERSpansgQFIQLFGPDILPRHCVITHM-EGVVTVTPaSQDAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 530387683 516 NGSSVSSPIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
468-539 |
1.17e-13 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 68.39 E-value: 1.17e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530387683 468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTP-QKNTRTFVNGSSVSSPIQLHHGDRILWGNNHF 539
Cdd:cd22673 20 KKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGRSF 92
|
|
| KIF1B |
pfam12423 |
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ... |
756-802 |
1.85e-13 |
|
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.
Pssm-ID: 463574 Cd Length: 43 Bit Score: 66.09 E-value: 1.85e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530387683 756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423 1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
|
|
| FHA_PHLB1 |
cd22713 |
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ... |
438-549 |
2.34e-13 |
|
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438765 Cd Length: 120 Bit Score: 68.12 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 438 SSGIKVGDDKCFLVNLNADPALNELLVYYLKE-HTLIGSANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNtRTFVN 516
Cdd:cd22713 7 GKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGN-LCSVD 84
|
90 100 110
....*....|....*....|....*....|...
gi 530387683 517 GSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKK 549
Cdd:cd22713 85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
1683-1752 |
4.58e-13 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 74.34 E-value: 4.58e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1683 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1752
Cdd:COG5244 7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
450-550 |
1.70e-12 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438784 [Multi-domain] Cd Length: 117 Bit Score: 65.73 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKE-HTLIG---SANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22732 11 LIGIDDDLLSTGIILYHLKEgRTYVGrddATTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEATQ 89
|
90 100
....*....|....*....|....*
gi 530387683 526 LHHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22732 90 LNQGAVILLGRTNMFRFNHPKEAAK 114
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
471-534 |
3.66e-11 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 60.28 E-value: 3.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530387683 471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1422-1660 |
5.10e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.43 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1422 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEmGPDVLVQTm 1500
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPPA-APDRSVPP- 2570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 gapalkicDKPAKVPSPPpviAVTAVTPAPEAqdgPPSPLSEASsgyfshsvstatlsdalgPGLDAAAPPGSMPTAPeA 1580
Cdd:PHA03247 2571 --------PRPAPRPSEP---AVTSRARRPDA---PPQSARPRA------------------PVDDRGDPRGPAPPSP-L 2617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1581 EPEAPISHPPPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPG 1651
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLT 2696
|
....*....
gi 530387683 1652 AEGNAPAPG 1660
Cdd:PHA03247 2697 SLADPPPPP 2705
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
449-539 |
5.12e-11 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 60.75 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 449 FLVNLNADPALNELLVYylKEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNT-RTFVNGSSVSSPIQLH 527
Cdd:cd00060 1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEVD-GGGVYLEDLGSTnGTFVNGKRITPPVPLQ 77
|
90
....*....|..
gi 530387683 528 HGDRILWGNNHF 539
Cdd:cd00060 78 DGDVIRLGDTTF 89
|
|
| FHA_KIF16A_STARD9 |
cd22731 |
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ... |
450-545 |
3.56e-10 |
|
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 59.02 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 450 LVNLNADPALNELLVYYLKEHTL-IGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22731 11 LIAMDDDILSTGVVLYHLREGTTkIGRSDSeqeQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESCR 89
|
90 100
....*....|....*....|
gi 530387683 526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22731 90 LSQGAVIVLGKTHKFRFNHP 109
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1417-1662 |
4.54e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.34 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1417 TTVSRGIAPAPALSVSPqnNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPlahqaqPEMGPDVL 1496
Cdd:PHA03247 2738 APAPPAVPAGPATPGGP--ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP------WDPADPPA 2809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1497 VQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF-----------SHSVSTATLSDALGPGL 1565
Cdd:PHA03247 2810 AVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrppSRSPAAKPAAPARPPVR 2884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1566 DAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPAPGSPFRVRRVRASElrsfsrmlaGD 1645
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPPPPPPPRPQPPLAPT---------TD 2948
|
250
....*....|....*..
gi 530387683 1646 PGCSPGAEGNAPAPGAG 1662
Cdd:PHA03247 2949 PAGAGEPSGAVPQPWLG 2965
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1459-1678 |
8.59e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1459 PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAV------TPAPEA 1532
Cdd:PHA03247 2683 PRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpggparPARPPT 2762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1533 QDGPPSPLSEAS-----------SGYFSHSVSTATLSDALGP--------GLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1593
Cdd:PHA03247 2763 TAGPPAPAPPAApaagpprrltrPAVASLSESRESLPSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1594 AVPAEEPPGPQQLVSPG---RERPDLEAPA--PGSPFR--VRRVRASELRSFSRMLAGDPgcsPGAEgNAPAPGAGGQAL 1666
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPGgdvRRRPPSRSPAakPAAPARppVRRLARPAVSRSTESFALPP---DQPE-RPPQPQAPPPPQ 2918
|
250
....*....|..
gi 530387683 1667 ASDSEEADEVPE 1678
Cdd:PHA03247 2919 PQPQPPPPPQPQ 2930
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
446-540 |
9.89e-10 |
|
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438764 [Multi-domain] Cd Length: 120 Bit Score: 58.08 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 446 DKCFLVNLNADPALNELLVYYLKEHT-LIGS----ANSQDIQLCGMGILPEHCII--------------DITSEGQVMLT 506
Cdd:cd22712 2 DYPYLLTLRGFSPKQDLLVYPLLEQViLVGSrtegARKVDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81
|
90 100 110
....*....|....*....|....*....|....
gi 530387683 507 PQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFF 540
Cdd:cd22712 82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1515-1673 |
1.82e-09 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 62.88 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1515 PSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA 1594
Cdd:PHA03307 114 PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1595 V----PAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRmlagDPGCSPGAEGNAPAPGAGGQALASDS 1670
Cdd:PHA03307 194 PpstpPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE----SSGCGWGPENECPLPRPAPITLPTRI 269
|
...
gi 530387683 1671 EEA 1673
Cdd:PHA03307 270 WEA 272
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1479-1629 |
1.99e-09 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 62.70 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAK---VPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTA 1555
Cdd:PRK07764 646 GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAApppAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683 1556 TLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRR 1629
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRR 799
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1479-1661 |
6.47e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 61.05 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQP---EMGPDVLVQTMGAPALKICDKPAKVPSPPPVIA-VTAVTPAPEAQDGPPSPLSEASSGYFSHSVST 1554
Cdd:PRK12323 364 RPGQSGGGAGPataAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPaAAAAARAVAAAPARRSPAPEALAAARQASARG 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1555 ATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRASE 1634
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP-EFASPAPAQPDAAPAGWV 522
|
170 180
....*....|....*....|....*..
gi 530387683 1635 LRSFSRMLAGDPgcSPGAEGNAPAPGA 1661
Cdd:PRK12323 523 AESIPDPATADP--DDAFETLAPAPAA 547
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
1511-1634 |
1.63e-08 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 59.34 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGyfshsvstatlsdalgpglDAAAPPGSMPTAPEAEPEAPISHPP 1590
Cdd:PRK14951 389 PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA-------------------PVAAPAAAAPAAAPAAAPAAVALAP 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530387683 1591 PPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASE 1634
Cdd:PRK14951 450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1475-1678 |
3.22e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 58.84 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1475 KRGKRPSPLAHQAQPEMGPdvlvqtmgAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVST 1554
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPA--------APAAPAAPAPAGAAAAP---AEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1555 ATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV------PAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvr 1628
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPagqaddPAAQPPQAAQGASAPSPAADDPVPLPPEP---- 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530387683 1629 rvraselrSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1678
Cdd:PRK07764 746 --------DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE 787
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1511-1778 |
3.51e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 59.03 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQ---DGPPSPLSEASSGYFSHSVS------TATLSDALGPGLDAAAPPGSMPTAPEAE 1581
Cdd:PHA03307 80 PANESRSTPTWSLSTLAPASPARegsPTPPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1582 PEAPISHPPPPTA------VPAEEPPGPqqlvSPGRERPDLEAPAPGSPfrvrrvRASELRSFSRMLAGDPGCSPGAEGN 1655
Cdd:PHA03307 160 AAVASDAASSRQAalplssPEETARAPS----SPPAEPPPSTPPAAASP------RPPRRSSPISASASSPAPAPGRSAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1656 APAPGAGGQALASDSEEADEVPEWLREGEFVTVGAHKTGVVRYVGpadfqegtWVGVELDLPSGKNDGSIGGK--QYFRC 1733
Cdd:PHA03307 230 DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASG--------WNGPSSRPGPASSSSSPRERspSPSPS 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530387683 1734 NPGYGLLVRPSRVRRATGPVRRRSTGLRLGAPEARRSATLSGSAT 1778
Cdd:PHA03307 302 SPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
79-290 |
5.79e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 57.83 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 79 VFKCLGENIlQNAFDGynacIFAYGQTGSGKSYTMMgtaDQPGLIPRLC-SGLFERTQKEENEEQSFKVEVSYMEIY-NE 156
Cdd:COG5059 370 VFREQSQLS-QSSLSG----IFAYMQSLKKETETLK---SRIDLIMKSIiSGTFERKKLLKEEGWKYKSTLQFLRIEiDR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 157 KVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLA-VTSYKDIESLMSegnKSRTVAATNMNEESSRSHAVFKitlthtly 235
Cdd:COG5059 442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPeETSDRVESEKAS---KLRSSASTKLNLRSSRSHSKFR-------- 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530387683 236 DVKSG-TSGEKVGKLSLVDLAGSERaTKTGAAGDRLKEGSNINKSLTTLGLVISAL 290
Cdd:COG5059 511 DHLNGsNSSTKELSLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1371-1665 |
1.61e-07 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 56.61 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1371 GKGKLSRRSISSPNVNRLSGSrqdlIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASY 1450
Cdd:PHA03378 568 GLGPLQIQPLTSPTTSQLASS----APSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITF 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1451 LNPVKSFVPQMPKLLKSLFP---VRDEKRGKRPSPLAHQAQ------------PEMGPDVLVQTMGAPALKICDKPAKVP 1515
Cdd:PHA03378 644 NVLVFPTPHQPPQVEITPYKptwTQIGHIPYQPSPTGANTMlpiqwapgtmqpPPRAPTPMRPPAAPPGRAQRPAAATGR 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1516 SPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV 1595
Cdd:PHA03378 724 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAG 803
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1596 PAEEPPGPQQLvsPGRERPDLEAPAPGSPFRVRRVRASeLRSFSRmlagdpGCSPGAEGNAPAPGAGGQA 1665
Cdd:PHA03378 804 PTSMQLMPRAA--PGQQGPTKQILRQLLTGGVKRGRPS-LKKPAA------LERQAAAGPTPSPGSGTSD 864
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1396-1621 |
2.62e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 55.93 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1396 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1475
Cdd:pfam03154 148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1476 rgkrpSPLAHQAQPEMGPDVLVQTMGAPALKIcdKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLS-EASSGYFSHSVST 1554
Cdd:pfam03154 223 -----STAAPHTLIQQTPTLHPQRLPSPHPPL--QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSlQTGPSHMQHPVPP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1555 ATLSDA---------LGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ---QLVSPGRER-- 1613
Cdd:pfam03154 296 QPFPLTpqssqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpipQLPNPQSHKhp 375
|
....*...
gi 530387683 1614 PDLEAPAP 1621
Cdd:pfam03154 376 PHLSGPSP 383
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
1221-1278 |
7.36e-07 |
|
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.
Pssm-ID: 463599 Cd Length: 149 Bit Score: 50.66 E-value: 7.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530387683 1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473 91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
1424-1621 |
8.11e-07 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 52.30 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1424 APAPALSVS-PQNNHSPD--PG---LSNLAASYLNPvkSFVPqmPKLLKSLFPVRDEKRGKRPSplahqaQPEMGPDVLV 1497
Cdd:pfam15822 11 SPAKTSAVSnPKPGQPPQgwPGsnpWNNPSAPPAVP--SGLP--PSTAPSTVPFGPAPTGMYPS------IPLTGPSPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1498 QTMGAPALKICDKPAKvPSPPPVIAvtavTPAPEAQDGPPS-PLSEASSGYFSHS--VSTATL-------SDALGPGLDA 1567
Cdd:pfam15822 81 PAPFPPSGPSCPPPGG-PYPAPTVP----GPGPIGPYPTPNmPFPELPRPYGAPTdpAAAAPSgpwgsmsSGPWAPGMGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1568 AAPPGSMPTAPeaepeaPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAP 1621
Cdd:pfam15822 156 QYPAPNMPYPS------PGPYPaVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDP 204
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1425-1709 |
1.13e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.02 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1425 PAPALSVSPQNNHSPDPGLSNL-------AASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEMGPDVLV 1497
Cdd:PHA03307 172 AALPLSSPEETARAPSSPPAEPppstppaAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1498 QTM------GAPALKICDKPAKVPSPPPVIAVTAVTPAPE-AQDGPPSPLSEASSGyfshSVSTATLSDALGP----GLD 1566
Cdd:PHA03307 252 ENEcplprpAPITLPTRIWEASGWNGPSSRPGPASSSSSPrERSPSPSPSSPGSGP----APSSPRASSSSSSsresSSS 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1567 AAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfRVRRVRASELRSFSRMLAgdP 1646
Cdd:PHA03307 328 STSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP-TRRRARAAVAGRARRRDA--T 404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683 1647 GCSPGAEGNAPAPGAGGQALASDSEEADEVPewlrEGE-FVTVGAHKTGVVRYVGPADFQEGTW 1709
Cdd:PHA03307 405 GRFPAGRPRPSPLDAGAASGAFYARYPLLTP----SGEpWPGSPPPPPGRVRYGGLGDSRPGLW 464
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1479-1732 |
1.60e-06 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 52.76 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPAlkICDKPAKvpsPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLS 1558
Cdd:COG5180 243 RSRPATVDAQPEMRPPADAKERRRAA--IGDTPAA---EPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1559 DALGPG-LDAAAPPGSMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSP 1624
Cdd:COG5180 317 VRPPGGaRDPGTPRPGQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1625 FR---VRRVRASELRSFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYV 1699
Cdd:COG5180 397 RRgapGPPMGAGDLVQAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADF 469
|
250 260 270
....*....|....*....|....*....|...
gi 530387683 1700 GPADFQEGTWVGVELDLPSGKNDGSIGGKQYFR 1732
Cdd:COG5180 470 VAPVTDATPVDVADVLGVRPDAILGGNVAPASG 502
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1476-1669 |
3.13e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 52.16 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1476 RGKRPSPLAHQAQPEMGPdVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTA 1555
Cdd:PRK07003 384 GARAAAAVGASAVPAVTA-VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1556 TLSDALGPGLDA---AAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQqlvspGRERPDleAPAPGSPfrvrrvra 1632
Cdd:PRK07003 463 CDERDAQPPADSgsaSAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-----AASRED--APAAAAP-------- 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530387683 1633 selrsfsrmlagdpgcsPGAEGNAPAPGA-------GGQALASD 1669
Cdd:PRK07003 528 -----------------PAPEARPPTPAAaapaaraGGAAAALD 554
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
1500-1634 |
4.87e-06 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 50.94 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1500 MGAPALKICDKPAKVPSPPPVI-------AVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDAlgPGLDAAAPPG 1572
Cdd:pfam13254 209 MRSPAPGGHSKSPSVSGISADSsptkeepSEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAA--PSKSAEASTE 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 1573 SMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRErPDLEAPAPGSP---FRV---RRVRASE 1634
Cdd:pfam13254 287 KKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRD-PLSPKPKPQSPpkdFRAnlrSREVPKD 353
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1476-1677 |
5.31e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1476 RGKRPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPP----VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHS 1551
Cdd:PHA03247 2585 RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPpspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP 2664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1552 VSTATLSDALGPGLDA------AAPPGSMPTAPEAEPEAPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1624
Cdd:PHA03247 2665 RRARRLGRAAQASSPPqrprrrAARPTVGSLTSLADPPPPPPTPePAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1625 FRVRRVRASELRSFSRMLAGDPGCS--PGAEGNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PHA03247 2745 PAGPATPGGPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLSESRESLP 2799
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1512-1633 |
7.26e-06 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 50.15 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1512 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1583
Cdd:NF040712 200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 530387683 1584 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1633
Cdd:NF040712 280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1551-1659 |
8.57e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.09 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1551 SVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP----------------------PPPTAVPAEEPPGPQQLVS 1608
Cdd:PHA03247 2490 FAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPvhprmltwirgleelasddagdPPPPLPPAAPPAAPDRSVP 2569
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 530387683 1609 PGRERPDLEAPAPGSpfRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAP 1659
Cdd:PHA03247 2570 PPRPAPRPSEPAVTS--RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1552-1710 |
9.50e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 50.75 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1552 VSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVR 1631
Cdd:PRK07764 393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1632 ASEL--RSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAhktgVVRYVGPADFQEGTW 1709
Cdd:PRK07764 473 APEPtaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI----LLPEATVLGVRGDTL 548
|
.
gi 530387683 1710 V 1710
Cdd:PRK07764 549 V 549
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1423-1600 |
1.07e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 50.54 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1423 IAPAPALSVSPQNN---HSPDPGLSNLAASYLNpvkSFVPQMPKL--LKSLFPVRDEKRGKRPSPLAHQAQ----PEMGP 1493
Cdd:pfam03154 355 IKPPPTTPIPQLPNpqsHKHPPHLSGPSPFQMN---SNLPPPPALkpLSSLSTHHPPSAHPPPLQLMPQSQqlppPPAQP 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1494 DVLVQTMGAPALKICDKPA----KVPSPPPVIA---VTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLD 1566
Cdd:pfam03154 432 PVLTQSQSLPPPAASHPPTsglhQVPSQSPFPQhpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVS 511
|
170 180 190
....*....|....*....|....*....|....
gi 530387683 1567 AAAPPGSMPTAPEAEPEAPIShPPPPTAVPAEEP 1600
Cdd:pfam03154 512 CPLPPVQIKEEALDEAEEPES-PPPPPRSPSPEP 544
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
1499-1600 |
1.09e-05 |
|
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.
Pssm-ID: 429334 Cd Length: 301 Bit Score: 49.54 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1499 TMGAPALKICDkPAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseassgyfshsvsTATLSDALGPGldaAAPPGSMPTAP 1578
Cdd:pfam07174 30 AVALPAVAHAD-PEPAPPPPSTATAPPAPPPPPPAPAAPAP--------------PPPPAAPNAPN---APPPPADPNAP 91
|
90 100
....*....|....*....|..
gi 530387683 1579 EAEPEAPISHPPPPTAVPAEEP 1600
Cdd:pfam07174 92 PPPPADPNAPPPPAVDPNAPEP 113
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
468-542 |
1.13e-05 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 45.72 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716 20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1511-1624 |
2.22e-05 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 46.40 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAP----EAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPI 1586
Cdd:pfam06346 18 GACIPTPPPLPGGGGPPPPPplpgSAAIPPPPPL----------------------PGGTSIPPPPPLPGAASIPPPPPL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530387683 1587 SH----PPPP-----TAVPAEEPPGPQqlvSPGRERPdlEAPAPGSP 1624
Cdd:pfam06346 76 PGstgiPPPPplpggAGIPPPPPPLPG---GAGVPPP--PPPLPGGP 117
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1424-1621 |
3.19e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1424 APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEMGPDVLVQTMGAP 1503
Cdd:PRK12323 389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAG 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1504 ALKicdkPAKVPSPPPVIAVTAVTPAPEAQDGPP---------SPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSM 1574
Cdd:PRK12323 469 PRP----VAAAAAAAPARAAPAAAPAPADDDPPPweelppefaSPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPA 544
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530387683 1575 PTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlVSPGrERPDLEAPAP 1621
Cdd:PRK12323 545 PAAAPAPRAAAATEPVVAPRPPRASASGLPD-MFDG-DWPALAARLP 589
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1520-1677 |
5.00e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1520 VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEE 1599
Cdd:PRK07764 584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 1600 PPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PRK07764 664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--AGQADDPAAQPPQAAQGASAPSPAADDPV 739
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1511-1611 |
5.17e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQDGP---PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE-API 1586
Cdd:PRK07764 406 PAAAPAPAAAAPAAAAAPAPAAAPQPapaPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPApAPP 485
|
90 100
....*....|....*....|....*
gi 530387683 1587 SHPPPPTAVPAEEPPGPQQLVSPGR 1611
Cdd:PRK07764 486 AAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1514-1677 |
6.44e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1514 VPSPPPVI----------AVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDalgpgldaAAPPGSMPTAPEAEPE 1583
Cdd:PHA03247 254 APAPPPVVgegadrapetARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLAL--------PAPPDPPPPAPAGDAE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1584 A------------PISHPP-------PPTAVPAEEPPGPQQLVSPGRERPDLEAPapgsPFRVRRVRASELRSFSRMLAG 1644
Cdd:PHA03247 326 EeddedgamevvsPLPRPRqhyplgfPKRRRPTWTPPSSLEDLSAGRHHPKRASL----PTRKRRSARHAATPFARGPGG 401
|
170 180 190
....*....|....*....|....*....|....*
gi 530387683 1645 D--PGCSPGAEGNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PHA03247 402 DdqTRPAAPVPASVPTPAPTPVPASAPPPPATPLP 436
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
1510-1674 |
7.68e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 47.40 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1510 KP-AKVPSPPPVIAVTAVTPAPEAQDgpPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPish 1588
Cdd:PRK14951 365 KPaAAAEAAAPAEKKTPARPEAAAPA--AAPVAQAAA-----------------APAPAAAPAAAASAPAAPPAAAP--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1589 pPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvrrvrasELRSFSRMLAGDPGCSPGAEGNAPAPGAggqALAS 1668
Cdd:PRK14951 423 -PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP---------ETVAIPVRVAPEPAVASAAPAPAAAPAA---ARLT 489
|
....*.
gi 530387683 1669 DSEEAD 1674
Cdd:PRK14951 490 PTEEGD 495
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1428-1626 |
8.80e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.86 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1428 ALSVSPQNNHSPD----PGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPlahqaqpEMGPDVLVQTMGAP 1503
Cdd:PHA03307 730 ARTVAPLVRYSPRraraRASAWDITDALFSNPSLVPAKLAEALALLEPAEPQRGAGSSP-------PVRAEAAFRRPGRL 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1504 ALKICDKPAKVP------SPPPVIAVTAVTPAPEAQDGP-PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPT 1576
Cdd:PHA03307 803 RRSGPAADAASRtaskrkSRSHTPDGGSESSGPARPPGAaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRAR 882
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530387683 1577 APEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgreRPdLEAPAPGSPFR 1626
Cdd:PHA03307 883 PGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGP---MP-PGGPDPRGGFR 928
|
|
| bMERB_dom |
pfam12130 |
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ... |
1099-1143 |
1.26e-04 |
|
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.
Pssm-ID: 463467 [Multi-domain] Cd Length: 131 Bit Score: 43.66 E-value: 1.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530387683 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130 66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1511-1633 |
2.20e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPP 1590
Cdd:PRK07764 398 APSAAAAAPAAAPAPAAAAPAAAAAPAPA---AAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP 474
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530387683 1591 PPTAVPAEEPPGPQQlvSPGRERPDLEAPAPGSPFRVRRVRAS 1633
Cdd:PRK07764 475 EPTAAPAPAPPAAPA--PAAAPAAPAAPAAPAGADDAATLRER 515
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1479-1674 |
2.86e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.64 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAvtAVTPAPEAQDGPPSPLSEASSgyfshsvSTATLS 1558
Cdd:PRK12323 416 ARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPA--AAARPAAAGPRPVAAAAAAAP-------ARAAPA 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1559 DALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlvsPGRERPDLEAPAPGSPFRVRRVRASELRSF 1638
Cdd:PRK12323 487 AAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD---PDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530387683 1639 SRMLAGDPGCSPGAEGNAPAPGAG------GQALASDSEEAD 1674
Cdd:PRK12323 564 RPPRASASGLPDMFDGDWPALAARlpvrglAQQLARQSELAG 605
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1512-1677 |
2.93e-04 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 45.69 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1512 AKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfshSVSTATLSDALGPgldaaaPPGSMPTAPEAEPEAP------ 1585
Cdd:PLN03209 336 ADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPR-----PLSPYTAYEDLKP------PTSPIPTPPSSSPASSksvdav 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1586 --------ISHPPPPTAVPAEEP-PGPQQL---VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAE 1653
Cdd:PLN03209 405 akpaepdvVPSPGSASNVPEVEPaQVEAKKtrpLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAAT 484
|
170 180
....*....|....*....|....
gi 530387683 1654 GNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PLN03209 485 DAAAPPPANMRPLSPYAVYDDLKP 508
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1511-1663 |
3.35e-04 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 45.59 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPviavtavTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAP----------PGSMP--- 1575
Cdd:PRK14086 90 PSAGEPAPP-------PPHARRTSEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPaypayqqrpePGAWPraa 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1576 ------------------TAPEAEPEAPISHPPPPTAVPAEEPPGPQQ-------LVSPGRERPDLEAPAPGSPFRVRRV 1630
Cdd:PRK14086 163 ddygwqqqrlgfpprapyASPASYAPEQERDREPYDAGRPEYDQRRRDydhprpdWDRPRRDRTDRPEPPPGAGHVHRGG 242
|
170 180 190
....*....|....*....|....*....|....
gi 530387683 1631 R-ASELRSFSRMLAGDPGCSPGAEGNAPAPGAGG 1663
Cdd:PRK14086 243 PgPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGE 276
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1414-1665 |
3.40e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1414 VSQTTVSRGIAPAP-ALSVSPQNNHSPDPGLSNLA--ASYLNPVKSFVPQMPKLLKSLFPVRDEKRG---------KRPS 1481
Cdd:PHA03247 2788 VASLSESRESLPSPwDPADPPAAVLAPAAALPPAAspAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPP 2867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1482 PLAHQAQPEMGPDVLVQTMGAPALKIC--------DKPAKVPSP---------PPVIAVTAVTPAPEAQDGPPSPLS--- 1541
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVRRLARPAVSRStesfalppDQPERPPQPqappppqpqPQPPPPPQPQPPPPPPPRPQPPLAptt 2947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1542 -EASSGYFSHSVSTATLSdALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPA-----------EEP-PGP----Q 1604
Cdd:PHA03247 2948 dPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswasslalhEETdPPPvslkQ 3026
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1605 QLVSPGR--------------ERPDLEAPAPgspfrvrrvraselrsfsrmLAGDPGCSPGAEGNAPAPGAGGQA 1665
Cdd:PHA03247 3027 TLWPPDDtedsdadslfdsdsERSDLEALDP--------------------LPPEPHDPFAHEPDPATPEAGARE 3081
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1477-1678 |
3.63e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1477 GKRPSPLA-HQAQPEMGPDVL--VQTMGAPALKicdkPAKVPSPPPVIAVTA------------VTPAPEAQD------- 1534
Cdd:PHA03247 277 GPPPPPEAaAPNGAAAPPDGVwgAALAGAPLAL----PAPPDPPPPAPAGDAeeeddedgamevVSPLPRPRQhyplgfp 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1535 -------GPPSPLSEASSGyfSHSVSTATLSD-------------ALGPGLD-----AAAPPGSMPTaPEAEPeAPISHP 1589
Cdd:PHA03247 353 krrrptwTPPSSLEDLSAG--RHHPKRASLPTrkrrsarhaatpfARGPGGDdqtrpAAPVPASVPT-PAPTP-VPASAP 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1590 PPP-TAVPAEEPPGPQQLVSPGRERPDLEA--PAPGSPFRVRRVRASELRsfSRMLAGDPGCSPgAE--GNAPAPGAGGQ 1664
Cdd:PHA03247 429 PPPaTPLPSAEPGSDDGPAPPPERQPPAPAtePAPDDPDDATRKALDALR--ERRPPEPPGADL-AEllGRHPDTAGTVV 505
|
250
....*....|....*
gi 530387683 1665 ALAS-DSEEADEVPE 1678
Cdd:PHA03247 506 RLAArEAAIAREVAE 520
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1480-1674 |
3.66e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1480 PSPLAHQAQPEMGPDVLVQTMGAPA-LKICDKPAKVPSPPPVIAVTAVTPA-----------------PEAQDGPPSPLS 1541
Cdd:PHA03307 131 APDLSEMLRPVGSPGPPPAASPPAAgASPAAVASDAASSRQAALPLSSPEEtarapssppaepppstpPAAASPRPPRRS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1542 EASSGYFSHSVSTATLSDALGPG--LDAAAPPGSMPTAPEAEPEAPISHPPPPT-------AVPAEEP---PGPQQLVSP 1609
Cdd:PHA03307 211 SPISASASSPAPAPGRSAADDAGasSSDSSSSESSGCGWGPENECPLPRPAPITlptriweASGWNGPssrPGPASSSSS 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 1610 GRER-PDLEAPAPGSPFRVRRVRASELRSFSR--MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEAD 1674
Cdd:PHA03307 291 PRERsPSPSPSSPGSGPAPSSPRASSSSSSSResSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1502-1677 |
4.45e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.23 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1502 APALKICDKPAKVPSPPPVIAVtavtPAPEAQdgpPSPLSEASSGYFSHSVSTATLSdalgpgldAAAPPGSMPTAPeAE 1581
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARVAGAV----PAPGAR---AAAAVGASAVPAVTAVTGAAGA--------ALAPKAAAAAAA-TR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1582 PEAPISHPPPPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGA 1661
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPA------KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRA 496
|
170
....*....|....*.
gi 530387683 1662 GGQALASDSEEADEVP 1677
Cdd:PRK07003 497 AAPSAATPAAVPDARA 512
|
|
| KLF9_13_N-like |
cd21975 |
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
1501-1620 |
5.54e-04 |
|
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.
Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 42.37 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 GAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSVSTATLSDALGPGLDAAA 1569
Cdd:cd21975 29 GLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGSSLESGDADMGSDSDVAP 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1570 PPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1620
Cdd:cd21975 105 ASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
|
|
| Tymo_45kd_70kd |
pfam03251 |
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ... |
1421-1626 |
5.69e-04 |
|
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.
Pssm-ID: 281269 [Multi-domain] Cd Length: 468 Bit Score: 44.40 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1421 RGIAPAPA-------LSV----SPQNNHSPDPGLSNLAASYLNPVKSFVPQMP--KLLKS--LFPVRDEKRGKRPSPLAH 1485
Cdd:pfam03251 257 RPITPGPSnthdlrpLSVlprtSPRRGLLPNPRRHRTSTGHIPPTTTSRPTGPpsRLQRPvhLYQSSPHTPNFRPSSIRK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1486 QAQPEMGPDV-LVQTMGAPA-LKICDKpakvpSPPpviaVTAVTPAPEAQDGPPSPLSEAS-SGYFSHSVSTATLSDalg 1562
Cdd:pfam03251 337 DALLQTGPRLgHLERLGQPAnLRTSER-----SPP----TKRRLPRSSEPNRLPKPLPEATlAPSYRHRRPYPLLPN--- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1563 pgldaaaPPGSMPTAPEAEPEAPISHPPPPTAVPAE-EPPGPQQLVSPgrerpdleAPAPGSPFR 1626
Cdd:pfam03251 405 -------PPAALPSIAYTSSRGKIHHSLPKGALPKEgAPPPPRRLPSP--------APRPQLPLR 454
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
1522-1621 |
6.32e-04 |
|
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.
Pssm-ID: 429334 Cd Length: 301 Bit Score: 43.76 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1522 AVTAVTPAPEAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPgsMPTAPEAEPEAPISHPPPPTAVPAEEPP 1601
Cdd:pfam07174 28 AVAVALPAVAHADPEPAPP----------------------PPSTATAPP--APPPPPPAPAAPAPPPPPAAPNAPNAPP 83
|
90 100
....*....|....*....|
gi 530387683 1602 GPQQLVSPGRERPDLEAPAP 1621
Cdd:pfam07174 84 PPADPNAPPPPPADPNAPPP 103
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
1558-1642 |
7.17e-04 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 44.22 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1558 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1634
Cdd:NF041121 22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101
|
....*...
gi 530387683 1635 LRSFSRML 1642
Cdd:NF041121 102 PLELARAL 109
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
460-540 |
8.84e-04 |
|
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438785 Cd Length: 113 Bit Score: 40.94 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 460 NELLVYYL-KEHTLIG---SANSQDIQLCGMGILPEHCII------DITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHG 529
Cdd:cd22733 18 HDCLVYLLnREQHTVGqetPSSKPNISLSAPDILPLHCTIrrvrlpKHRSEEKLVLEPIPGAHVSVNFSEVERTTLLRHG 97
|
90
....*....|.
gi 530387683 530 DRILWGNNHFF 540
Cdd:cd22733 98 DLLSFGAYYLF 108
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
1482-1682 |
1.08e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.70 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1482 PLAHQAQPEMGPDVLVQTMGAPALKicDKPAKVPSPPPVIAVTAVTPAPEAQdgPPSPLSEAssgyfshsvsTATLSDAL 1561
Cdd:PRK07994 361 PAAPLPEPEVPPQSAAPAASAQATA--APTAAVAPPQAPAVPPPPASAPQQA--PAVPLPET----------TSQLLAAR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1562 gPGLDAAAPPgsmPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgrerpdlEAPAPGSPFRVRRVRASElrsfsrm 1641
Cdd:PRK07994 427 -QQLQRAQGA---TKAKKSEPAAASRARPVNSALERLASVRPAPSALE-------KAPAKKEAYRWKATNPVE------- 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 530387683 1642 LAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLRE 1682
Cdd:PRK07994 489 VKKEPVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAL 529
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
1497-1622 |
1.11e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 43.83 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1497 VQTMGAPALKICDKPA-----KVPSPPPVIAVTAVTPAPEAQDGPPSPLseassgyFSHSVSTATLSDALGPGLDAAA-- 1569
Cdd:PHA03369 521 AKTAAANIEPNCSADAaapatKRARPETKTELEAVVRFPYQIRNMESPA-------FVHSFTSTTLAAAAGQGSDTAEal 593
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 1570 --------------PPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPgpqqlvsPGRERPDLEAPAPG 1622
Cdd:PHA03369 594 agaietlltqasaqPAGLSLPAPAVPVNASTPASTPPPLAPQEPPQ-------PGTSAPSLETSLPQ 653
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1518-1624 |
1.51e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 42.83 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1518 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1593
Cdd:NF040712 194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
|
90 100 110
....*....|....*....|....*....|.
gi 530387683 1594 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1624
Cdd:NF040712 274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
1511-1678 |
1.74e-03 |
|
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.
Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 43.14 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1582
Cdd:TIGR01645 291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1583 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1656
Cdd:TIGR01645 371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
|
170 180
....*....|....*....|...
gi 530387683 1657 PA-PGAGGQALASDSEEADEVPE 1678
Cdd:TIGR01645 448 LAiMGEAAAALALEPKKKKKEKE 470
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
1524-1621 |
1.74e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 43.26 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1524 TAVTPAPEAQDGPPsplseassgyfshsvsTATLSDALGPGLDAAAPPGSMPTA--PEAEPEAPISHPPPPTAVPAEEPP 1601
Cdd:PRK14950 358 ALLVPVPAPQPAKP----------------TAAAPSPVRPTPAPSTRPKAAAAAniPPKEPVRETATPPPVPPRPVAPPV 421
|
90 100
....*....|....*....|....*...
gi 530387683 1602 GPQQ--------LVSPGRERPDLEAPAP 1621
Cdd:PRK14950 422 PHTPesapkltrAAIPVDEKPKYTPPAP 449
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1561-1678 |
1.98e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1561 LGPGLDAAAPPGSMPTAPEAEPEApiSHPPPPTAVPAEEPPGPqqlvsPGRERPdLEAPAPGSPFRVRRVRASELRSFSR 1640
Cdd:PRK07764 385 LGVAGGAGAPAAAAPSAAAAAPAA--APAPAAAAPAAAAAPAP-----AAAPQP-APAPAPAPAPPSPAGNAPAGGAPSP 456
|
90 100 110
....*....|....*....|....*....|....*...
gi 530387683 1641 MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1678
Cdd:PRK07764 457 PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAP 494
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
368-444 |
2.01e-03 |
|
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];
Pssm-ID: 444244 [Multi-domain] Cd Length: 239 Bit Score: 41.89 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530387683 368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493 36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1511-1636 |
2.26e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAvTPAPEAQDGPPSPLSEASSGyfshsvstatlsdALGPGLDAAAPPGSMPTAPEAEPEAPISHPP 1590
Cdd:PRK07764 415 AAPAAAAAPAPAAAP-QPAPAPAPAPAPPSPAGNAP-------------AGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530387683 1591 PPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELR 1636
Cdd:PRK07764 481 APAPPAAPAPAAAPAAPAAP------AAPAGADDAATLRERWPEIL 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-432 |
2.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1502-1667 |
2.93e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1502 APALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGldAAAPPGSMPTAPE 1579
Cdd:PHA03307 776 EPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADaaSRTASKRKSRSHTPDGGSESSGPARPPG--AAARPPPARSSES 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1580 AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPG-SPFRVRRVRASELRSFSRMLAGDP---GC---SPGA 1652
Cdd:PHA03307 854 SKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPpAGAPAPRPRPAPRVKLGPMPPGGPdprGGfrrVPPG 933
|
170
....*....|....*
gi 530387683 1653 EGNAPAPGAggQALA 1667
Cdd:PHA03307 934 DLHTPAPSA--AALA 946
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1528-1803 |
5.12e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1528 PAPEAQDGPPSPLSeASSGYFShsVSTATLSDALGPGLDAAAPPGSMPTAPEAEPeapishpppptavPAEEPPGPQQLV 1607
Cdd:PHA03307 24 PPATPGDAADDLLS-GSQGQLV--SDSAELAAVTVVAGAAACDRFEPPTGPPPGP-------------GTEAPANESRST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1608 SPGRERPDLEAPAPGSPFRVRRVRASelrsfsrmlagDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVT 1687
Cdd:PHA03307 88 PTWSLSTLAPASPAREGSPTPPGPSS-----------PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1688 V--GAHKTGVVRYVGPADFqegtwvgveLDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRR---ATGPVRRRSTGLRL 1762
Cdd:PHA03307 157 AspAAVASDAASSRQAALP---------LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSspiSASASSPAPAPGRS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530387683 1763 GAPEARRSATLSGSATNLASLTAALAKADRSHKNPENRKSW 1803
Cdd:PHA03307 228 AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
611-760 |
7.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913 612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
1565-1659 |
8.61e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 40.72 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1565 LDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAG 1644
Cdd:PRK06995 48 LAALAPPAAAAPAAAQPPPAAAPAAVSRPAAPAAEP--APWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125
|
90
....*....|....*
gi 530387683 1645 DPGCSPGAEGNAPAP 1659
Cdd:PRK06995 126 ENAARRLARAAAAAP 140
|
|
| |
