|
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: 602.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365 160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365 240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767950710 319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365 320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
6-360 |
1.48e-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: 482.84 E-value: 1.48e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129 70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129 148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300
|
330 340 350
....*....|....*....|....*....|....*
gi 767950710 326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129 301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-353 |
5.91e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 461.66 E-value: 5.91e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225 69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225 148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225 227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301
|
330 340
....*....|....*....|....*
gi 767950710 329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225 302 NISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
50-439 |
2.33e-95 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 320.92 E-value: 2.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059 52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059 124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059 201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059 277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059 353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432
|
...
gi 767950710 437 QSS 439
Cdd:COG5059 433 QFL 435
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-379 |
2.10e-77 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 283.36 E-value: 2.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188 153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188 233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188 311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 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 |
4.23e-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: 4.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730 1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
|
90
....*....|....*....
gi 767950710 527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730 81 HHGDRILWGNNHFFRINLP 99
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
1725-1788 |
3.30e-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: 3.30e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950710 1725 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1788
Cdd:pfam01302 2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
1725-1789 |
5.99e-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: 5.99e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 1725 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1789
Cdd:smart01052 2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
357-469 |
4.71e-25 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 103.77 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183 1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183 81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
|
170
....*....|....*
gi 767950710 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 |
1.89e-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: 1.89e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767950710 756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423 1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
1725-1794 |
3.83e-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: 74.72 E-value: 3.83e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1725 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1794
Cdd:COG5244 7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1445-1704 |
1.06e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 70.74 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1445 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1513
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1514 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1590
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1591 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1662
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767950710 1663 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1704
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
471-534 |
3.74e-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: 3.74e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950710 471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1460-1774 |
4.13e-08 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 58.15 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1460 PDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSaSPDIRVTRMEEAQPEMGPDVLV 1539
Cdd:COG5180 174 LPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAAS-SPKVDPPSTSEARSRPATVDAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1540 QTMGAPALKICDKPAKV----PSPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLSDALGPG-LDAAAPPG 1614
Cdd:COG5180 253 PEMRPPADAKERRRAAIgdtpAAEPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRPVRPPGGaRDPGTPRP 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1615 SMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSPFR---VRRVRASELR 1678
Cdd:COG5180 332 GQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLGRRgapGPPMGAGDLV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1679 SFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYVGPADFQEGTWVGVEL 1756
Cdd:COG5180 412 QAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADFVAPVTDATPVDVADV 484
|
330
....*....|....*...
gi 767950710 1757 DLPSGKNDGSIGGKQYFR 1774
Cdd:COG5180 485 LGVRPDAILGGNVAPASG 502
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
1375-1676 |
6.25e-08 |
|
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: 57.10 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1375 LSR-RSISSpnvNRVSVWNQALCCAWDFSPLLF----SWLSGSRqdliPSYSLGSNKGRWESQQDVSQTTVSRGIA---- 1445
Cdd:pfam13254 36 LSRqNSFAS---NRGSVAGPSGSLSPGLSPTKLsregSPESTSR----PSSSHSEATIVRHSKDDERPSTPDEGFVkpal 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1446 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-----PQMPKLLKSLFPVRDEKRGKRPSPLAHQP-----VPRIMVQ 1515
Cdd:pfam13254 109 PRHSRSSSALSNTGSEEDSPSLPTSPPSPSKTMDpkrwsPTKSSWLESALNRPESPKPKAQPSQPAQPawmkeLNKIRQS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1516 SASPDI-RVTRMEEAQPemgpdvlVQTMGAPALKICDKPAKVPSPPPVI-------AVTAVTPAPEAQDGPPSPLSEASS 1587
Cdd:pfam13254 189 RASVDLgRPNSFKEVTP-------VGLMRSPAPGGHSKSPSVSGISADSsptkeepSEEADTLSTDKEQSPAPTSASEPP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1588 GYFSHSVSTATLSDAlgPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRErPDLEAPAPGSP- 1666
Cdd:pfam13254 262 PKTKELPKDSEEPAA--PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRD-PLSPKPKPQSPp 338
|
330
....*....|....*
gi 767950710 1667 --FRV---RRVRASE 1676
Cdd:pfam13254 339 kdFRAnlrSREVPKD 353
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
1221-1278 |
7.91e-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: 50.28 E-value: 7.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950710 1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473 91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1554-1675 |
7.71e-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: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1554 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1625
Cdd:NF040712 200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767950710 1626 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1675
Cdd:NF040712 280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
468-542 |
1.15e-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: 1.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 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 |
1.19e-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: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767950710 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130 66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1445-1666 |
1.71e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1445 APAPALSVSPQNnhspdpglsnlaasylnPVKSFVPQMPKLLKSLFPvRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVT 1524
Cdd:NF033839 294 APKPGMQPSPQP-----------------EKKEVKPEPETPKPEVKP-QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1525 RMEEA-QPEMGPDvlvqtmgaPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASsgyfshsvstatlsdal 1603
Cdd:NF033839 356 PQPEKpKPEVKPQ--------PEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK----------------- 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 1604 gPGLDAAAP---PGSMPTAPEAEPEapishPPPPTAVPAEEPPGPQQLVSPGRERPDLEA-PAPGSP 1666
Cdd:NF033839 411 -PQPEKPKPevkPQPEKPKPEVKPQ-----PEKPKPEVKPQPEKPKPEVKPQPETPKPEVkPQPEKP 471
|
|
| KLF9_13_N-like |
cd21975 |
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
1526-1662 |
3.61e-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: 43.14 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1526 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSV 1594
Cdd:cd21975 12 ISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGS 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950710 1595 STATLSDALGPGLDAAAPPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1662
Cdd:cd21975 88 SLESGDADMGSDSDVAPASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
1600-1684 |
8.01e-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: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1600 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1676
Cdd:NF041121 22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101
|
....*...
gi 767950710 1677 LRSFSRML 1684
Cdd:NF041121 102 PLELARAL 109
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
1553-1720 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1553 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1624
Cdd:TIGR01645 291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1625 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1698
Cdd:TIGR01645 371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
|
170 180
....*....|....*....|...
gi 767950710 1699 PA-PGAGGQALASDSEEADEVPE 1720
Cdd:TIGR01645 448 LAiMGEAAAALALEPKKKKKEKE 470
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1560-1666 |
1.61e-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: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1560 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1635
Cdd:NF040712 194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
|
90 100 110
....*....|....*....|....*....|.
gi 767950710 1636 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1666
Cdd:NF040712 274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
368-444 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950710 368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493 36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-432 |
2.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 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 |
6.60e-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: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913 612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950710 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: 602.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365 160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365 240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767950710 319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365 320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
6-360 |
1.48e-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: 482.84 E-value: 1.48e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129 70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129 148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300
|
330 340 350
....*....|....*....|....*....|....*
gi 767950710 326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129 301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-353 |
5.91e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 461.66 E-value: 5.91e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225 69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225 148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225 227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301
|
330 340
....*....|....*....|....*
gi 767950710 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 |
2.27e-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: 443.62 E-value: 2.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRRETDLhTKCVVDVDANK-VILNPvntnlsKGDARGQPKVFAYDHCFWSMdesvkekyAGQDIVFKCL 83
Cdd:cd00106 1 NVRVAVRVRPLNGREARS-AKSVISVDGGKsVVLDP------PKNRVAPPKTFAFDAVFDST--------STQEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD-QPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPeQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 163 DPKgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHtlYDVKSGTS 242
Cdd:cd00106 146 SPV-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNS 297
|
330 340
....*....|....*....|....*....
gi 767950710 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 |
1.67e-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: 1.67e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 6 VKVAVRIRPMNRRETDLHTKCVVDVDankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmDESVKEkYAGQDIVFKCLGE 85
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVD---EKRGQVSVRNPKATANEPPKTFTFDAVF---DPNSKQ-LDVYDETARPLVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 86 NILQnafdGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01371 76 SVLE----GYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ-FLVRVSYLEIYNEEIRDLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 163 DpKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlYDVKSGTS 242
Cdd:cd01371 151 G-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS-EKGEDGEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01371 229 HIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNS 303
|
330 340 350
....*....|....*....|....*....|.
gi 767950710 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 |
4.33e-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: 359.60 E-value: 4.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNpvntnLSKGDARgqPKVFAYDHCFwSMDESvkekyagQDIVFKCLg 84
Cdd:cd01366 3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIE-----LTSIGAK--QKEFSFDKVF-DPEAS-------QEDVFEEV- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDP 164
Cdd:cd01366 67 SPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 165 KGSRQT-LKVREHSVLGP-YVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvkSGT- 241
Cdd:cd01366 147 GNAPQKkLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------SGRn 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 242 --SGEK-VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdqsagkNKNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01366 219 lqTGEIsVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSL 292
|
330 340 350
....*....|....*....|....*....|....*..
gi 767950710 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 |
4.43e-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: 357.42 E-value: 4.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 6 VKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNP----------VNTNLSKGDARGQPKVFAYDHCFwsmDEsvkekYA 74
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmDNHMLVFDPkdeedgffhgGSNNRDRRKRRNKELKYVFDRVF---DE-----TS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 75 GQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIY 154
Cdd:cd01370 74 TQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK-DEKEFEVSMSYLEIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 155 NEKVRDLLDPKGSRqtLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTl 234
Cdd:cd01370 153 NETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 235 YDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsaGKNKNKFVPYRDSVLTWLL 314
Cdd:cd01370 230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 767950710 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 |
2.48e-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: 2.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 3 DSKVKVAVRIRPMNRRETDLHTKCVVDVDankvilnPVNTNLSKGDARGqpKVFAYDHCFwSMDesvkekyAGQDIVFKC 82
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFD-------PEDTVVIATSETG--KTFSFDRVF-DPN-------TTQEDVYNF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEIYNEKVR 159
Cdd:cd01369 64 AAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSM-DENLEFHVKVSYFEIYMEKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 160 DLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlyDVKS 239
Cdd:cd01369 143 DLLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVET 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 240 GTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLG 319
Cdd:cd01369 219 EKK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLG 291
|
330 340 350
....*....|....*....|....*....|....
gi 767950710 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 |
4.10e-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: 354.33 E-value: 4.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANK--VILnpvntnlskgdarGQPKVFAYDHCFWSMDEsvkekyagQDIVFK 81
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEpqVTV-------------GTDKSFTFDYVFDPSTE--------QEEVYN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA------DQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYN 155
Cdd:cd01372 60 TCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKVSFLEIYN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 156 EKVRDLLDPKG-SRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTL 234
Cdd:cd01372 139 EEIRDLLDPETdKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 235 YDVKSGTSGEK------VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgknKNKFVPYRDS 308
Cdd:cd01372 219 KNGPIAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK---KGAHVPYRDS 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767950710 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 |
1.10e-108 |
|
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: 1.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNlskgdargqpkvFAYDHCFwSMDESVKEkyagqdiVFKCL 83
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLvEPPSTS------------FTFDHVF-GGDSTNRE-------VYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQkeENEEQSFKVEVSYMEIYNEKVRDLLD 163
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKINDLLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 164 PKGsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGtSG 243
Cdd:cd01374 139 PTS--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 244 EKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqSAGKnKNKFVPYRDSVLTWLLKDSLGGNSK 323
Cdd:cd01374 216 VRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGK-VGGHIPYRDSKLTRILQPSLGGNSR 291
|
330 340 350
....*....|....*....|....*....|
gi 767950710 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 |
9.50e-101 |
|
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: 327.93 E-value: 9.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 6 VKVAVRIRPMNRRETDL-HTKCVVDVDANKVILNPVntnlskgdargQPKVFAYDHcfwsmdesVKEKYAGQDIVFKCLG 84
Cdd:cd01373 3 VKVFVRIRPPAEREGDGeYGQCLKKLSSDTLVLHSK-----------PPKTFTFDH--------VADSNTNQESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP--------GLIPRLCSGLFERTQKEEN---EEQSFKVEVSYMEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEkagEGKSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 154 YNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 233
Cdd:cd01373 144 YNEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 234 lYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNkfVPYRDSVLTWL 313
Cdd:cd01373 221 -WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRH--VCYRDSKLTFL 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767950710 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 |
2.17e-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: 312.72 E-value: 2.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 3 DSKVKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNPVNTNLSKGDArgqpKVFAYDHCFWSmdesvkekYAGQDIVFK 81
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVdPVRKEVSVRTGGLADKSST----KTYTFDMVFGP--------EAKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMG-----------TADQPGLIPRLCSGLFERTqkeENEEQSFKVEVSY 150
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKL---EDNGTEYSVKVSY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 151 MEIYNEKVRDLLDPKGS-RQTLKVREHS--VLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFK 227
Cdd:cd01364 146 LEIYNEELFDLLSPSSDvSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 228 ITLthtlYDVKSGTSGE---KVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagknKNKFVP 304
Cdd:cd01364 226 ITI----HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVP 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767950710 305 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01364 296 YRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
50-439 |
2.33e-95 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 320.92 E-value: 2.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059 52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059 124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059 201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059 277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059 353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432
|
...
gi 767950710 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 |
3.69e-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: 265.80 E-value: 3.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRRETDLHTK-CVVDVDANKVILNPVNTNLSKGDARG---QPKVFAYDHCFwSMDESVKEKYAGqdiVF 80
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEgCIEVINSTTVVLHPPKGSAANKSERNggqKETKFSFSKVF-GPNTTQKEFFQG---TA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 81 KCLGENILQnafdGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFertqkeeNEEQSFKVEVSYMEIYNEKVRD 160
Cdd:cd01368 78 LPLVQDLLH----GKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF-------NSIGGYSVFVSYIEIYNEYIYD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 161 LLDPKGS-----RQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL----T 231
Cdd:cd01368 147 LLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 232 HTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdQSAGKNKNKFVPYRDSVLT 311
Cdd:cd01368 227 DSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLR-ENQLQGTNKMVPFRDSKLT 305
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767950710 312 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01368 306 HLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-379 |
2.10e-77 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 283.36 E-value: 2.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188 153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188 233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188 311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 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 |
8.36e-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: 8.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRREtdlHTKCVVDVDaNKVILNPVNTNLSKGDARGQPKVFAYdhcfwSMDESVKEkyAGQDIVFKCLG 84
Cdd:cd01375 1 KVQAFVRVRPTDDFA---HEMIKYGED-GKSISIHLKKDLRRGVVNNQQEDWSF-----KFDGVLHN--ASQELVYETVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD---QPGLIPRLCSGLFErtQKEENEEQSFKVEVSYMEIYNEKVRDL 161
Cdd:cd01375 70 KDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFR--MIEERPTKAYTVHVSYLEIYNEQLYDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 162 LDPK----GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL---THTL 234
Cdd:cd01375 148 LSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeahSRTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 235 YDVKSGTSgekvgKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQsagknKNKFVPYRDSVLTWLL 314
Cdd:cd01375 228 SSEKYITS-----KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHVPFRQSKLTHVL 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 767950710 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 |
2.19e-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: 251.45 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIlnPVNTNLSKGDARGQPKV--FAYDHCFwsmDESVKekyagQDIVFKC 82
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTL--IVHEPKLKVDLTKYIENhtFRFDYVF---DESSS-----NETVYRS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMG----TADQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKV 158
Cdd:cd01367 71 TVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN-LGVTVSFFEIYGGKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 159 RDLLDPKgsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvK 238
Cdd:cd01367 150 FDLLNRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------R 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 239 SGTSGEKVGKLSLVDLAGSERATKTGAAG-DRLKEGSNINKSLTTLGLVISALADQSAgknknkFVPYRDSVLTWLLKDS 317
Cdd:cd01367 220 DRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA------HIPFRGSKLTQVLKDS 293
|
330 340 350
....*....|....*....|....*....|....*
gi 767950710 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 |
5.17e-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: 235.47 E-value: 5.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 6 VKVAVRIRPMNRRETDLHTKCVVDvdankvILNPVNTNLSKGDARGQPKVFAYDHcFWSMDESVKEKYAGQdivFKClge 85
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVS------GIDSCSVELADPRNHGETLKYQFDA-FYGEESTQEDIYARE---VQP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 86 nILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEneeQSFKVEVSYMEIYNEKVRDLLDPK 165
Cdd:cd01376 69 -IVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA---WALSFTMSYLEIYQEKILDLLEPA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 166 GSRqtLKVRE---HSVLGPyvdGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVksgTS 242
Cdd:cd01376 145 SKE--LVIREdkdGNILIP---GLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---PF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqsagKNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01376 217 RQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------NKNLPRIPYRDSKLTRLLQDSLGGGS 290
|
330 340
....*....|....*....|....*....
gi 767950710 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 |
4.23e-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: 4.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730 1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
|
90
....*....|....*....
gi 767950710 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 |
2.46e-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: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANS---QDIQLCGMGILPEHCIIDItSEGQVMLTPQKNTRTFVNGSSVSSP 523
Cdd:cd22706 1 KYYLVNLNADPSLNELLVYYLKEHTLIGRSDAptqQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79
|
90 100
....*....|....*....|..
gi 767950710 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 |
1.45e-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: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22729 1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80
|
90 100
....*....|....*....|....
gi 767950710 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 |
7.99e-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: 7.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22705 4 LVNLNEDPLMSECLLYYIKPgITRVGRADAdvpQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPTR 82
|
90
....*....|....*...
gi 767950710 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 |
3.99e-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: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKE-HTLIGS--ANSQ-DIQLCGMGILPEHCIIdITSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22707 10 LVNLNEDPQLSEMLLYMLKEgQTRVGRskASSShDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88
|
90 100
....*....|....*....|
gi 767950710 526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22707 89 LHHGDRVILGGDHYFRFNHP 108
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
1725-1788 |
3.30e-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: 3.30e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950710 1725 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1788
Cdd:pfam01302 2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
448-545 |
1.59e-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: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 448 CFLVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIdITSEGQVMLTPQKNT-RTFVNGSSVSS 522
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEgETTIGRADAepePDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPGaKVIVNGVPVTG 79
|
90 100
....*....|....*....|...
gi 767950710 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 |
3.86e-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: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 58 YDHCFWSMDeSVKEKYAGQDIVFKcLGENILQNAFDGYN-ACIFAYGQTGSGKSYTMMGtadqpgLIPRLCSGLFERTQK 136
Cdd:cd01363 15 RDSKIIVFY-RGFRRSESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 137 EENEEQsfkvevsymeiynekvrdlldpkgsrqtlkvrehsvlgpyvDGLSKLAVTSYKDIESLMSEGNKSRTvAATNMN 216
Cdd:cd01363 87 GETEGW-----------------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRN 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950710 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 ... |
1725-1789 |
5.99e-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: 5.99e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 1725 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1789
Cdd:smart01052 2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
357-469 |
4.71e-25 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 103.77 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183 1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183 81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
|
170
....*....|....*
gi 767950710 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 |
1.65e-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: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVS 521
Cdd:cd22727 5 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNNNGEVIVTlePCERSETYVNGKRVV 84
|
90 100
....*....|....*....|....*.
gi 767950710 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 |
3.91e-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: 87.68 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQ--VMLTPQKNTRTFVNGSSVS 521
Cdd:cd22726 4 LVNLNEDPLMSECLLYYIKDGiTRVGREDAerrQDIVLSGHFIKEEHCIFrsDTRSGGEavVTLEPCEGADTYVNGKKVT 83
|
90 100 110
....*....|....*....|....*....|...
gi 767950710 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 |
3.77e-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: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 5 KVKVAVRIRPMNRREtdlhtkcvvdvdankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmdesvkEKYAGQDIVFKCLg 84
Cdd:pfam16796 21 NIRVFARVRPELLSE---------------AQIDYPDETSSDGKIGSKNKSFSFDRVF--------PPESEQEDVFQEI- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950710 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 |
1.69e-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: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKEH-TLIGSANSqDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVSSPI 524
Cdd:cd22728 4 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLSGQFIREQHCLFrsIPNPSGEVVVTlePCEGAETYVNGKQVTEPL 82
|
90
....*....|....*....
gi 767950710 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 |
3.91e-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: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22708 11 LIGIDDDLLSTGVVLYHLKEgKTRIGREDApqeQDIVLDGEDIEAEHCIIE-NVGGVVTLHPLPGALCAVNGQVITQPTR 89
|
90 100
....*....|....*....|
gi 767950710 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 |
2.84e-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: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 448 CFLVNLNADPALNellvYYLKEH------TLIGSANS-----QDIQLCGMGILPEHCIIDITsEGQVMLTP-QKNTRTFV 515
Cdd:cd22711 2 PYLLELSPDGSDR----DKPRRHrlqpnvTEVGSERSpansgQFIQLFGPDILPRHCVITHM-EGVVTVTPaSQDAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 767950710 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 |
1.20e-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: 1.20e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950710 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 |
1.89e-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: 1.89e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767950710 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 |
2.39e-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: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 438 SSGIKVGDDKCFLVNLNADPALNELLVYYLKE-HTLIGSANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNtRTFVN 516
Cdd:cd22713 7 GKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGN-LCSVD 84
|
90 100 110
....*....|....*....|....*....|...
gi 767950710 517 GSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKK 549
Cdd:cd22713 85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
1725-1794 |
3.83e-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: 74.72 E-value: 3.83e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1725 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1794
Cdd:COG5244 7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
450-550 |
1.74e-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: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKE-HTLIG---SANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22732 11 LIGIDDDLLSTGIILYHLKEgRTYVGrddATTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEATQ 89
|
90 100
....*....|....*....|....*
gi 767950710 526 LHHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22732 90 LNQGAVILLGRTNMFRFNHPKEAAK 114
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1445-1704 |
1.06e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 70.74 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1445 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1513
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1514 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1590
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1591 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1662
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767950710 1663 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1704
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
471-534 |
3.74e-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: 3.74e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950710 471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1442-1720 |
5.16e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.43 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1442 RGIAPAPAL-SVSPQNNHSPDP---GLSNLAASYLNPVKSFVPQMPKLLKSLFP--VRDEKRGKRPS--PLAHQPVPRIM 1513
Cdd:PHA03247 2605 RGDPRGPAPpSPLPPDTHAPDPpppSPSPAANEPDPHPPPTVPPPERPRDDPAPgrVSRPRRARRLGraAQASSPPQRPR 2684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1514 VQSASPDI-RVTRM-----EEAQPEMGPDVLVQTMGAP-----ALKICDKPAKVPSPPPVIAVTAV------TPAPEAQD 1576
Cdd:PHA03247 2685 RRAARPTVgSLTSLadpppPPPTPEPAPHALVSATPLPpgpaaARQASPALPAAPAPPAVPAGPATpggparPARPPTTA 2764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1577 GPPSPLSEAS-----------SGYFSHSVSTATLSDALGP--------GLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV 1637
Cdd:PHA03247 2765 GPPAPAPPAApaagpprrltrPAVASLSESRESLPSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1638 PAEEPPGPQQLVSPG---RERPDLEAPA--PGSPFR--VRRVRASELRSFSRMLAGDPgcsPGAEgNAPAPGAGGQALAS 1710
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGgdvRRRPPSRSPAakPAAPARppVRRLARPAVSRSTESFALPP---DQPE-RPPQPQAPPPPQPQ 2920
|
330
....*....|
gi 767950710 1711 DSEEADEVPE 1720
Cdd:PHA03247 2921 PQPPPPPQPQ 2930
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
449-539 |
5.25e-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: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 449 FLVNLNADPALNELLVYylKEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNT-RTFVNGSSVSSPIQLH 527
Cdd:cd00060 1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEVD-GGGVYLEDLGSTnGTFVNGKRITPPVPLQ 77
|
90
....*....|..
gi 767950710 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 |
3.12e-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: 59.40 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 450 LVNLNADPALNELLVYYLKEHTL-IGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22731 11 LIAMDDDILSTGVVLYHLREGTTkIGRSDSeqeQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESCR 89
|
90 100
....*....|....*....|
gi 767950710 526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22731 90 LSQGAVIVLGKTHKFRFNHP 109
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
446-540 |
1.01e-09 |
|
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: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 446 DKCFLVNLNADPALNELLVYYLKEHT-LIGS----ANSQDIQLCGMGILPEHCII--------------DITSEGQVMLT 506
Cdd:cd22712 2 DYPYLLTLRGFSPKQDLLVYPLLEQViLVGSrtegARKVDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81
|
90 100 110
....*....|....*....|....*....|....
gi 767950710 507 PQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFF 540
Cdd:cd22712 82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1557-1715 |
2.09e-09 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 62.88 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1557 PSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA 1636
Cdd:PHA03307 114 PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1637 V----PAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRmlagDPGCSPGAEGNAPAPGAGGQALASDS 1712
Cdd:PHA03307 194 PpstpPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE----SSGCGWGPENECPLPRPAPITLPTRI 269
|
...
gi 767950710 1713 EEA 1715
Cdd:PHA03307 270 WEA 272
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1559-1702 |
2.72e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 62.65 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1559 PPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfSHSVSTATLSDA-------LGPGLDAAAPPGSMPTAPeAEPEAPISHP 1631
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSE---PAVTSRARRPDAppqsarpRAPVDDRGDPRGPAPPSP-LPPDTHAPDP 2626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1632 PPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPGAEGNAPAPG 1702
Cdd:PHA03247 2627 PPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLTSLADPPPPP 2705
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1529-1703 |
1.20e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 60.27 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1529 AQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIA-VTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGL 1607
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPaAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAP 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1608 DAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRASELRSFSRMLAGD 1687
Cdd:PRK12323 455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP-EFASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170
....*....|....*.
gi 767950710 1688 PgcSPGAEGNAPAPGA 1703
Cdd:PRK12323 534 P--DDAFETLAPAPAA 547
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
1553-1676 |
1.69e-08 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 59.34 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1553 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGyfshsvstatlsdalgpglDAAAPPGSMPTAPEAEPEAPISHPP 1632
Cdd:PRK14951 389 PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA-------------------PVAAPAAAAPAAAPAAAPAAVALAP 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767950710 1633 PPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASE 1676
Cdd:PRK14951 450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1501-1671 |
1.85e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 59.61 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1501 PSPLAHQPVPrimvQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKicdKPAKVPSPPPVIAVTAVTPAPEAQDGPPS 1580
Cdd:PRK07764 636 PAEASAAPAP----GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA---APPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1581 PLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEA 1660
Cdd:PRK07764 709 PPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788
|
170
....*....|.
gi 767950710 1661 PAPGSPFRVRR 1671
Cdd:PRK07764 789 DAPSMDDEDRR 799
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1501-1820 |
2.03e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 59.80 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1501 PSPLAHQPV---PRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDG 1577
Cdd:PHA03307 28 PGDAADDLLsgsQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1578 PPSPLSEASSGYFSHSVS------TATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA------VPAEEPPGP 1645
Cdd:PHA03307 108 PPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAalplssPEETARAPS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1646 qqlvSPGRERPDLEAPAPGSPfrvrrvRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREG 1725
Cdd:PHA03307 188 ----SPPAEPPPSTPPAAASP------RPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1726 EFVTVGAHKTGVVRYVGpadfqegtWVGVELDLPSGKNDGSIGGK--QYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLR 1803
Cdd:PHA03307 258 PRPAPITLPTRIWEASG--------WNGPSSRPGPASSSSSPRERspSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329
|
330
....*....|....*..
gi 767950710 1804 LGAPEARRSATLSGSAT 1820
Cdd:PHA03307 330 SSSSESSRGAAVSPGPS 346
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
79-290 |
3.97e-08 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 58.21 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 79 VFKCLGENIlQNAFDGynacIFAYGQTGSGKSYTMMgtaDQPGLIPRLC-SGLFERTQKEENEEQSFKVEVSYMEIY-NE 156
Cdd:COG5059 370 VFREQSQLS-QSSLSG----IFAYMQSLKKETETLK---SRIDLIMKSIiSGTFERKKLLKEEGWKYKSTLQFLRIEiDR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 157 KVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLA-VTSYKDIESLMSegnKSRTVAATNMNEESSRSHAVFKitlthtly 235
Cdd:COG5059 442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPeETSDRVESEKAS---KLRSSASTKLNLRSSRSHSKFR-------- 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767950710 236 DVKSG-TSGEKVGKLSLVDLAGSERaTKTGAAGDRLKEGSNINKSLTTLGLVISAL 290
Cdd:COG5059 511 DHLNGsNSSTKELSLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1460-1774 |
4.13e-08 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 58.15 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1460 PDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSaSPDIRVTRMEEAQPEMGPDVLV 1539
Cdd:COG5180 174 LPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAAS-SPKVDPPSTSEARSRPATVDAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1540 QTMGAPALKICDKPAKV----PSPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLSDALGPG-LDAAAPPG 1614
Cdd:COG5180 253 PEMRPPADAKERRRAAIgdtpAAEPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRPVRPPGGaRDPGTPRP 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1615 SMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSPFR---VRRVRASELR 1678
Cdd:COG5180 332 GQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLGRRgapGPPMGAGDLV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1679 SFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYVGPADFQEGTWVGVEL 1756
Cdd:COG5180 412 QAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADFVAPVTDATPVDVADV 484
|
330
....*....|....*...
gi 767950710 1757 DLPSGKNDGSIGGKQYFR 1774
Cdd:COG5180 485 LGVRPDAILGGNVAPASG 502
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1550-1720 |
4.40e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 58.46 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1550 CDKPAKVPSPPPviavtAVTPAPEAQDGPPSPLSEASSGYFSHS--------VSTATLSDALGPGLDAAAPPGSMPTAPE 1621
Cdd:PRK07764 612 AARPAAPAAPAA-----PAAPAPAGAAAAPAEASAAPAPGVAAPehhpkhvaVPDASDGGDGWPAKAGGAAPAAPPPAPA 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1622 AEPEAPISHPPPPTAVPAE--EPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAP 1699
Cdd:PRK07764 687 PAAPAAPAGAAPAQPAPAPaaTPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766
|
170 180
....*....|....*....|.
gi 767950710 1700 APGAGGQALASDSEEADEVPE 1720
Cdd:PRK07764 767 AAAPAAAPPPSPPSEEEEMAE 787
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
1375-1676 |
6.25e-08 |
|
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: 57.10 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1375 LSR-RSISSpnvNRVSVWNQALCCAWDFSPLLF----SWLSGSRqdliPSYSLGSNKGRWESQQDVSQTTVSRGIA---- 1445
Cdd:pfam13254 36 LSRqNSFAS---NRGSVAGPSGSLSPGLSPTKLsregSPESTSR----PSSSHSEATIVRHSKDDERPSTPDEGFVkpal 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1446 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-----PQMPKLLKSLFPVRDEKRGKRPSPLAHQP-----VPRIMVQ 1515
Cdd:pfam13254 109 PRHSRSSSALSNTGSEEDSPSLPTSPPSPSKTMDpkrwsPTKSSWLESALNRPESPKPKAQPSQPAQPawmkeLNKIRQS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1516 SASPDI-RVTRMEEAQPemgpdvlVQTMGAPALKICDKPAKVPSPPPVI-------AVTAVTPAPEAQDGPPSPLSEASS 1587
Cdd:pfam13254 189 RASVDLgRPNSFKEVTP-------VGLMRSPAPGGHSKSPSVSGISADSsptkeepSEEADTLSTDKEQSPAPTSASEPP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1588 GYFSHSVSTATLSDAlgPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRErPDLEAPAPGSP- 1666
Cdd:pfam13254 262 PKTKELPKDSEEPAA--PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRD-PLSPKPKPQSPp 338
|
330
....*....|....*
gi 767950710 1667 --FRV---RRVRASE 1676
Cdd:pfam13254 339 kdFRAnlrSREVPKD 353
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1446-1751 |
8.67e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 57.49 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1446 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTR 1525
Cdd:PHA03307 172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSS-----PISASASSPAPAPGRSAADDAGASSSDSSSSESSG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1526 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEaqDGPPSPLSEASSGyfshSVSTATLSDALGP 1605
Cdd:PHA03307 247 CGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER--SPSPSPSSPGSGP----APSSPRASSSSSS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1606 ----GLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfRVRRVRASELRSFS 1681
Cdd:PHA03307 321 sresSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP-TRRRARAAVAGRAR 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950710 1682 RMLAgdPGCSPGAEGNAPAPGAGGQALASDSEEADEVPewlrEGE-FVTVGAHKTGVVRYVGPADFQEGTW 1751
Cdd:PHA03307 400 RRDA--TGRFPAGRPRPSPLDAGAASGAFYARYPLLTP----SGEpWPGSPPPPPGRVRYGGLGDSRPGLW 464
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1511-1653 |
4.50e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 54.99 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1511 RIMVQSASPDI-----RVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP-PSPLSE 1584
Cdd:PRK07764 361 RMLLPSASDDErgllaRLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPaPAPAPA 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1585 ASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE-APISHPPPPTAVPAEEPPGPQQLVSPGR 1653
Cdd:PRK07764 441 PPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPApAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1416-1707 |
5.28e-07 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 55.07 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1416 LIPSYSLGSNKGRWESQQDVSQ-TTVSRGIAPAPALSVSPqNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLF--PV 1492
Cdd:PHA03378 563 LLPAPGLGPLQIQPLTSPTTSQlASSAPSYAQTPWPVPHP-SQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRmqPI 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1493 RDEKRGkRPSPlaHQPvPRIMVQSASPDIRVTRMEEAQPE-MGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVT----- 1566
Cdd:PHA03378 642 TFNVLV-FPTP--HQP-PQVEITPYKPTWTQIGHIPYQPSpTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGraqrp 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1567 --AVTPAPEAQDGP-------------PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP 1631
Cdd:PHA03378 718 aaATGRARPPAAAPgrarppaaapgraRPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950710 1632 PPPTAVPAEEPPGPQQLvsPGRERPDLEAPAPGSPFRVRRVRASeLRSFSRmlagdpGCSPGAEGNAPAPGAGGQA 1707
Cdd:PHA03378 798 PPPQAGPTSMQLMPRAA--PGQQGPTKQILRQLLTGGVKRGRPS-LKKPAA------LERQAAAGPTPSPGSGTSD 864
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1417-1663 |
7.86e-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: 54.39 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1417 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1496
Cdd:pfam03154 148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1497 rgkrpSPLAhqpvPRIMVQSaSPDIRVTRMEEAQPEMGPdvlvQTMGAPALKICDKPakvpSPPPVIAvTAVTPAPEA-Q 1575
Cdd:pfam03154 223 -----STAA----PHTLIQQ-TPTLHPQRLPSPHPPLQP----MTQPPPPSQVSPQP----LPQPSLH-GQMPPMPHSlQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1576 DGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ-- 1646
Cdd:pfam03154 284 TGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpi 363
|
250 260
....*....|....*....|
gi 767950710 1647 -QLVSPGRER--PDLEAPAP 1663
Cdd:pfam03154 364 pQLPNPQSHKhpPHLSGPSP 383
|
|
| DUF3694 |
pfam12473 |
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ... |
1221-1278 |
7.91e-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: 50.28 E-value: 7.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950710 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 ... |
1490-1663 |
8.24e-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: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1490 FPVRDEKRGKRP----------SPLAHQPVPRIMVQSASPDI-----RVTRMEEAQPEMGPDVLVQTMGAPALKICDKPA 1554
Cdd:pfam15822 16 SAVSNPKPGQPPqgwpgsnpwnNPSAPPAVPSGLPPSTAPSTvpfgpAPTGMYPSIPLTGPSPGPPAPFPPSGPSCPPPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1555 KvPSPPPVIAvtavTPAPEAQDGPPS-PLSEASSGYFSHS--VSTATL-------SDALGPGLDAAAPPGSMPTAPeaep 1624
Cdd:pfam15822 96 G-PYPAPTVP----GPGPIGPYPTPNmPFPELPRPYGAPTdpAAAAPSgpwgsmsSGPWAPGMGGQYPAPNMPYPS---- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767950710 1625 eaPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAP 1663
Cdd:pfam15822 167 --PGPYPaVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDP 204
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1445-1642 |
1.61e-06 |
|
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: 53.23 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1445 APAPALSVSPQNNhSPDPGLSNlAASYLNPVKSFVP---QMPKLLK---SLFPVRDEKRGKRPSplAHQPVPRIMVQSas 1518
Cdd:pfam03154 348 APLSMPHIKPPPT-TPIPQLPN-PQSHKHPPHLSGPspfQMNSNLPpppALKPLSSLSTHHPPS--AHPPPLQLMPQS-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1519 pdirvtrMEEAQPEMGPDVLVQTMGAPALKICDKPA----KVPSPPPVIA---VTAVTPAPEAQDGPPSPLSEASSGYFS 1591
Cdd:pfam03154 422 -------QQLPPPPAQPPVLTQSQSLPPPAASHPPTsglhQVPSQSPFPQhpfVPGGPPPITPPSGPPTSTSSAMPGIQP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767950710 1592 HSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPIShPPPPTAVPAEEP 1642
Cdd:pfam03154 495 PSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPES-PPPPPRSPSPEP 544
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1435-1707 |
3.27e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1435 VSQTTVSRGIAPAP-ALSVSPQNNHSPDPGLSNLA--ASYLNPVKSFVPQMPKLLKSLFPVRDEKRG---------KRPS 1502
Cdd:PHA03247 2788 VASLSESRESLPSPwDPADPPAAVLAPAAALPPAAspAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPP 2867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1503 PLAHQPVPrimvqSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAV-TPAPEAQDGPPSP 1581
Cdd:PHA03247 2868 SRSPAAKP-----AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPP 2942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1582 LS----EASSGYFSHSVSTATLSdALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPA-----------EEP-PGP 1645
Cdd:PHA03247 2943 LApttdPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswasslalhEETdPPP 3021
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1646 ----QQLVSPGR--------------ERPDLEAPAPgspfrvrrvraselrsfsrmLAGDPGCSPGAEGNAPAPGAGGQA 1707
Cdd:PHA03247 3022 vslkQTLWPPDDtedsdadslfdsdsERSDLEALDP--------------------LPPEPHDPFAHEPDPATPEAGARE 3081
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1443-1719 |
3.80e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1443 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPrimvqsASPDI 1521
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPP------AAPDR 2566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1522 RVTRMEEAQPEMGPDVLVQTM--GAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATL 1599
Cdd:PHA03247 2567 SVPPPRPAPRPSEPAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTV 2646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1600 SDALGPGLDAAAPPGSM---------PTAPEAEPEAP--------------ISHPPPPTAVPAEEP-------PGPQQLV 1649
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRprrarrlgrAAQASSPPQRPrrraarptvgsltsLADPPPPPPTPEPAPhalvsatPLPPGPA 2726
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950710 1650 SPGRERPDLE-APAPGSPFRVRRVRASELRSFSRMLAGDPGCS--PGAEGNAPAPGAGGQALASDSEEADEVP 1719
Cdd:PHA03247 2727 AARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLSESRESLP 2799
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1558-1720 |
3.91e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 51.80 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1558 SPPPVIAVTAVTPAPEAQdgPPSPLSEASSGYFSHSVSTATLSDALGPgldAAAPPGSMPTAPEAEPEA-------PISH 1630
Cdd:PRK12323 373 GPATAAAAPVAQPAPAAA--APAAAAPAPAAPPAAPAAAPAAAAAARA---VAAAPARRSPAPEALAAArqasargPGGA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1631 PPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVR-RVRASELRSFSRMLAGDPGcSPGAEGNAPAPGAGGQALA 1709
Cdd:PRK12323 448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAaPAPADDDPPPWEELPPEFA-SPAPAQPDAAPAGWVAESI 526
|
170
....*....|.
gi 767950710 1710 SDSEEADEVPE 1720
Cdd:PRK12323 527 PDPATADPDDA 537
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1554-1675 |
7.71e-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: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1554 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1625
Cdd:NF040712 200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767950710 1626 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1675
Cdd:NF040712 280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1498-1716 |
8.13e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 51.03 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1498 GKRPSPLAHQPVPRIMVQSASPdiRVTRMEEAQPEMGPDVLVQTmGAPALKICDKPAKvPSPPPViavtAVTPAPEAQDG 1577
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAP--AAAAPAPAAPPAAPAAAPAA-AAAARAVAAAPAR-RSPAPE----ALAAARQASAR 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1578 PPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEP-PGPQQL-------- 1648
Cdd:PRK12323 443 GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFAsPAPAQPdaapagwv 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1649 ---------VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAG------GQALASDSE 1713
Cdd:PRK12323 523 aesipdpatADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARlpvrglAQQLARQSE 602
|
...
gi 767950710 1714 EAD 1716
Cdd:PRK12323 603 LAG 605
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1593-1701 |
8.72e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.09 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1593 SVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP----------------------PPPTAVPAEEPPGPQQLVS 1650
Cdd:PHA03247 2490 FAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPvhprmltwirgleelasddagdPPPPLPPAAPPAAPDRSVP 2569
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767950710 1651 PGRERPDLEAPAPGSpfRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAP 1701
Cdd:PHA03247 2570 PPRPAPRPSEPAVTS--RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1594-1752 |
9.92e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 50.75 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1594 VSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVR 1673
Cdd:PRK07764 393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1674 ASEL--RSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAhktgVVRYVGPADFQEGTW 1751
Cdd:PRK07764 473 APEPtaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI----LLPEATVLGVRGDTL 548
|
.
gi 767950710 1752 V 1752
Cdd:PRK07764 549 V 549
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1515-1667 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1515 QSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPeaqdgPPSPLSEASSGYFSHSV 1594
Cdd:pfam03154 142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP-----TPSAPSVPPQGSPATSQ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1595 STATLSDALGP-GLDAAAPPGSMPTAPEAEPE-APISHPPPPTAVPAEE----------PPGPQQLVS-PgrerPDLEAP 1661
Cdd:pfam03154 217 PPNQTQSTAAPhTLIQQTPTLHPQRLPSPHPPlQPMTQPPPPSQVSPQPlpqpslhgqmPPMPHSLQTgP----SHMQHP 292
|
....*.
gi 767950710 1662 APGSPF 1667
Cdd:pfam03154 293 VPPQPF 298
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
468-542 |
1.15e-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: 1.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716 20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
1541-1642 |
1.27e-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: 49.15 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1541 TMGAPALKICDkPAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseassgyfshsvsTATLSDALGPGldaAAPPGSMPTAP 1620
Cdd:pfam07174 30 AVALPAVAHAD-PEPAPPPPSTATAPPAPPPPPPAPAAPAP--------------PPPPAAPNAPN---APPPPADPNAP 91
|
90 100
....*....|....*....|..
gi 767950710 1621 EAEPEAPISHPPPPTAVPAEEP 1642
Cdd:pfam07174 92 PPPPADPNAPPPPAVDPNAPEP 113
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
1410-1666 |
2.23e-05 |
|
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.
Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 48.66 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1410 SGSRQDLI-PSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLaasylNPVKSFVPQMPKLLKS 1488
Cdd:pfam15279 62 AGSSAQLItPDLWLSDCRRKSASPASTRSESVSPGPSSSASPSSSPTSSNSSKPLISVA-----SSSKLLAPKPHEPPSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1489 LFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKicdKPAKVPSPPPV----IA 1564
Cdd:pfam15279 137 PPPPLPPKKGRRHRPGLHPPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPLPAFMEPSSMP---PPFLRPPPSIPqpnsPL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1565 VTAVTPAPEAQDGPPSPLSEASSGY----FS--HSVSTATLSdalGPgldaaaPPGSMPTAPEAEPeaPISHPPPPtavP 1638
Cdd:pfam15279 214 SNPMLPGIGPPPKPPRNLGPPSNPMhrppFSphHPPPPPTPP---GP------PPGLPPPPPRGFT--PPFGPPFP---P 279
|
250 260
....*....|....*....|....*...
gi 767950710 1639 AEEPPGPQQLvspgreRPDLEAPAPGSP 1666
Cdd:pfam15279 280 VNMMPNPPEM------NFGLPSLAPLVP 301
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1529-1711 |
2.65e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 49.08 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1529 AQPEMGPdVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLD 1608
Cdd:PRK07003 395 AVPAVTA-VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPAD 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1609 A---AAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQqlvspGRERPDleAPAPGSPfrvrrvraselrsfsrmla 1685
Cdd:PRK07003 474 SgsaSAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-----AASRED--APAAAAP------------------- 527
|
170 180 190
....*....|....*....|....*....|...
gi 767950710 1686 gdpgcsPGAEGNAPAPGA-------GGQALASD 1711
Cdd:PRK07003 528 ------PAPEARPPTPAAaapaaraGGAAAALD 554
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
1471-1664 |
2.70e-05 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 49.28 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1471 YLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDirvtRMEEAQ--PEM-GP-DVLVQTMGAPA 1546
Cdd:PHA03377 392 YIDPNMEPVQQRPVMFVSRVPWRKPRTLPWPTPKTHPVKRTLVKTSGRSD----EAEQAQstPERpGPsDQPSVPVEPAH 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1547 LKICDKP-AKVPSPPPVIAVTAVTPAPeaqdgPPSPLSEASSGYFSHSV-------STATLSDALGPGLDAAAP------ 1612
Cdd:PHA03377 468 LTPVEHTtVILHQPPQSPPTVAIKPAP-----PPSRRRRGACVVYDDDIievidveTTEEEESVTQPAKPHRKVqdgfqr 542
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767950710 1613 PGSMPTAPEAEPEAPISHPPPPTAVPAEEPP--GPQQLVSPGRERPDLEAPAPG 1664
Cdd:PHA03377 543 SGRRQKRATPPKVSPSDRGPPKASPPVMAPPstGPRVMATPSTGPRDMAPPSTG 596
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1553-1666 |
3.33e-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: 46.02 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1553 PAKVPSPPPVIAVTAVTPAP----EAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPI 1628
Cdd:pfam06346 18 GACIPTPPPLPGGGGPPPPPplpgSAAIPPPPPL----------------------PGGTSIPPPPPLPGAASIPPPPPL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767950710 1629 SH----PPPP-----TAVPAEEPPGPQqlvSPGRERPdlEAPAPGSP 1666
Cdd:pfam06346 76 PGstgiPPPPplpggAGIPPPPPPLPG---GAGVPPP--PPPLPGGP 117
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1556-1719 |
4.30e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1556 VPSPPPVIAVTAVTPaPEAQDG--PPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPISHPPP 1633
Cdd:PHA03247 254 APAPPPVVGEGADRA-PETARGatGPPPPPEAAA-----------------PNGAAAPPDGVWGAALAGAPLALPAPPDP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1634 PTAVPAEEP----------------PGPQQLVS---PGRERP---------DLEA---PAPGSPFRVRRVRASELRS--F 1680
Cdd:PHA03247 316 PPPAPAGDAeeeddedgamevvsplPRPRQHYPlgfPKRRRPtwtppssleDLSAgrhHPKRASLPTRKRRSARHAAtpF 395
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767950710 1681 SRMLAGD--PGCSPGAEGNAPAPGAGGQALASDSEEADEVP 1719
Cdd:PHA03247 396 ARGPGGDdqTRPAAPVPASVPTPAPTPVPASAPPPPATPLP 436
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1562-1719 |
5.05e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1562 VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEE 1641
Cdd:PRK07764 584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950710 1642 PPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADEVP 1719
Cdd:PRK07764 664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--AGQADDPAAQPPQAAQGASAPSPAADDPV 739
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
1431-1664 |
6.11e-05 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 48.07 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1431 SQQDVSQTTVSRGI--APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLF------PVRDEKRGKRPS 1502
Cdd:PHA03369 393 SVPARSPMTAYPPVpqFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPISMANMVypghpqEHGHERKRKRGG 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1503 PL------AHQPVPRIMVQ---SASPDIRVTRMEEAQPEM---GPDVLVQTMGAPALKICDKPA-----KVPSPPPVIAV 1565
Cdd:PHA03369 473 ELkeelieTLKLVKKLKEEqesLAKELEATAHKSEIKKIAeseFKNAGAKTAAANIEPNCSADAaapatKRARPETKTEL 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1566 TAVTPAPEAQDGPPSPLseassgyFSHSVSTATLSDALGPGLDAAA----------------PPGSMPTAPEAEPEAPIS 1629
Cdd:PHA03369 553 EAVVRFPYQIRNMESPA-------FVHSFTSTTLAAAAGQGSDTAEalagaietlltqasaqPAGLSLPAPAVPVNASTP 625
|
250 260 270
....*....|....*....|....*....|....*
gi 767950710 1630 HPPPPTAVPAEEPPgpqqlvsPGRERPDLEAPAPG 1664
Cdd:PHA03369 626 ASTPPPLAPQEPPQ-------PGTSAPSLETSLPQ 653
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
1552-1716 |
7.95e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 47.40 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1552 KP-AKVPSPPPVIAVTAVTPAPEAQDgpPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPish 1630
Cdd:PRK14951 365 KPaAAAEAAAPAEKKTPARPEAAAPA--AAPVAQAAA-----------------APAPAAAPAAAASAPAAPPAAAP--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1631 pPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvrrvrasELRSFSRMLAGDPGCSPGAEGNAPAPGAggqALAS 1710
Cdd:PRK14951 423 -PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP---------ETVAIPVRVAPEPAVASAAPAPAAAPAA---ARLT 489
|
....*.
gi 767950710 1711 DSEEAD 1716
Cdd:PRK14951 490 PTEEGD 495
|
|
| bMERB_dom |
pfam12130 |
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ... |
1099-1143 |
1.19e-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: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767950710 1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130 66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1445-1666 |
1.71e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1445 APAPALSVSPQNnhspdpglsnlaasylnPVKSFVPQMPKLLKSLFPvRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVT 1524
Cdd:NF033839 294 APKPGMQPSPQP-----------------EKKEVKPEPETPKPEVKP-QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1525 RMEEA-QPEMGPDvlvqtmgaPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASsgyfshsvstatlsdal 1603
Cdd:NF033839 356 PQPEKpKPEVKPQ--------PEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK----------------- 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 1604 gPGLDAAAP---PGSMPTAPEAEPEapishPPPPTAVPAEEPPGPQQLVSPGRERPDLEA-PAPGSP 1666
Cdd:NF033839 411 -PQPEKPKPevkPQPEKPKPEVKPQ-----PEKPKPEVKPQPEKPKPEVKPQPETPKPEVkPQPEKP 471
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1500-1721 |
2.74e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.00 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1500 RPSPLAhqpvPRIMVQSASPDIRVTRM---EEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPeaqD 1576
Cdd:PRK07003 411 APKAAA----AAAATRAEAPPAAPAPPataDRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPAS---D 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1577 GPPSPLSEASSgyfshsvSTATLSDALGPGLDAAAPPGSMPTAPEAEPEA-PISHPPPPTavPAEEPPGPQQ-------- 1647
Cdd:PRK07003 484 APPDAAFEPAP-------RAAAPSAATPAAVPDARAPAAASREDAPAAAApPAPEARPPT--PAAAAPAARAggaaaald 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1648 -------LVSPGRERPDLEAPAPGSPfrvrrVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADE-VP 1719
Cdd:PRK07003 555 vlrnagmRVSSDRGARAAAAAKPAAA-----PAAAPKPAAPRVAVQVP--TPRARAATGDAPPNGAARAEQAAESRGaPP 627
|
..
gi 767950710 1720 EW 1721
Cdd:PRK07003 628 PW 629
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1554-1719 |
3.01e-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: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1554 AKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfshSVSTATLSDALGPgldaaaPPGSMPTAPEAEPEAP------ 1627
Cdd:PLN03209 336 ADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPR-----PLSPYTAYEDLKP------PTSPIPTPPSSSPASSksvdav 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1628 --------ISHPPPPTAVPAEEP-PGPQQL---VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAE 1695
Cdd:PLN03209 405 akpaepdvVPSPGSASNVPEVEPaQVEAKKtrpLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAAT 484
|
170 180
....*....|....*....|....
gi 767950710 1696 GNAPAPGAGGQALASDSEEADEVP 1719
Cdd:PLN03209 485 DAAAPPPANMRPLSPYAVYDDLKP 508
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1553-1705 |
3.21e-04 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 45.59 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1553 PAKVPSPPPviavtavTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAP----------PGSMP--- 1617
Cdd:PRK14086 90 PSAGEPAPP-------PPHARRTSEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPaypayqqrpePGAWPraa 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1618 ------------------TAPEAEPEAPISHPPPPTAVPAEEPPGPQQ-------LVSPGRERPDLEAPAPGSPFRVRRV 1672
Cdd:PRK14086 163 ddygwqqqrlgfpprapyASPASYAPEQERDREPYDAGRPEYDQRRRDydhprpdWDRPRRDRTDRPEPPPGAGHVHRGG 242
|
170 180 190
....*....|....*....|....*....|....
gi 767950710 1673 R-ASELRSFSRMLAGDPGCSPGAEGNAPAPGAGG 1705
Cdd:PRK14086 243 PgPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGE 276
|
|
| KLF9_13_N-like |
cd21975 |
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
1526-1662 |
3.61e-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: 43.14 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1526 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSV 1594
Cdd:cd21975 12 ISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGS 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950710 1595 STATLSDALGPGLDAAAPPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1662
Cdd:cd21975 88 SLESGDADMGSDSDVAPASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1544-1719 |
4.76e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.23 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1544 APALKICDKPAKVPSPPPVIAVtavtPAPEAQdgpPSPLSEASSGYFSHSVSTATLSdalgpgldAAAPPGSMPTAPeAE 1623
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARVAGAV----PAPGAR---AAAAVGASAVPAVTAVTGAAGA--------ALAPKAAAAAAA-TR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1624 PEAPISHPPPPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGA 1703
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPA------KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRA 496
|
170
....*....|....*.
gi 767950710 1704 GGQALASDSEEADEVP 1719
Cdd:PRK07003 497 AAPSAATPAAVPDARA 512
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1445-1663 |
4.79e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1445 APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPrimvqSASPdIRVT 1524
Cdd:PRK12323 389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAP-----AAAP-AAAA 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1525 RMEEAQPEmgpdvlvqtmGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALG 1604
Cdd:PRK12323 463 RPAAAGPR----------PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767950710 1605 PGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlVSPGrERPDLEAPAP 1663
Cdd:PRK12323 533 DPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD-MFDG-DWPALAARLP 589
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1497-1668 |
5.39e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1497 RGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPalkiCDKPAKVPSPPPVIAVTAVTPAPEAQD 1576
Cdd:PHA03307 764 VPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAA----SRTASKRKSRSHTPDGGSESSGPARPP 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1577 GP-PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgreR 1655
Cdd:PHA03307 840 GAaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGP---M 916
|
170
....*....|...
gi 767950710 1656 PdLEAPAPGSPFR 1668
Cdd:PHA03307 917 P-PGGPDPRGGFR 928
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
1564-1663 |
7.02e-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: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1564 AVTAVTPAPEAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPgsMPTAPEAEPEAPISHPPPPTAVPAEEPP 1643
Cdd:pfam07174 28 AVAVALPAVAHADPEPAPP----------------------PPSTATAPP--APPPPPPAPAAPAPPPPPAAPNAPNAPP 83
|
90 100
....*....|....*....|
gi 767950710 1644 GPQQLVSPGRERPDLEAPAP 1663
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 ... |
1600-1684 |
8.01e-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: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1600 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1676
Cdd:NF041121 22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101
|
....*...
gi 767950710 1677 LRSFSRML 1684
Cdd:NF041121 102 PLELARAL 109
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
460-540 |
8.63e-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: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 460 NELLVYYL-KEHTLIG---SANSQDIQLCGMGILPEHCII------DITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHG 529
Cdd:cd22733 18 HDCLVYLLnREQHTVGqetPSSKPNISLSAPDILPLHCTIrrvrlpKHRSEEKLVLEPIPGAHVSVNFSEVERTTLLRHG 97
|
90
....*....|.
gi 767950710 530 DRILWGNNHFF 540
Cdd:cd22733 98 DLLSFGAYYLF 108
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1501-1662 |
9.62e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1501 PSPLAHQPVPRImvqSASPDIRVTRMEEAQPEmGPDVLVQTMGAPAlkicdkPAKVPSPPPVIAVTAVTPAPEAQDGPPS 1580
Cdd:PRK07764 651 EHHPKHVAVPDA---SDGGDGWPAKAGGAAPA-APPPAPAPAAPAA------PAGAAPAQPAPAPAATPPAGQADDPAAQ 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1581 PLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEA 1660
Cdd:PRK07764 721 PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
|
..
gi 767950710 1661 PA 1662
Cdd:PRK07764 801 AE 802
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1434-1677 |
9.63e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1434 DVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVksfvPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIM 1513
Cdd:PHA03247 2861 DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP----DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1514 VQSASPdIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKP-AKVPSPPPVIAVTAvTPAPEAQDGPPSPLSEASSGYFSH 1592
Cdd:PHA03247 2937 PRPQPP-LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrFRVPQPAPSREAPA-SSTPPLTGHSLSRVSSWASSLALH 3014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1593 SVST---ATLSDALGP-----GLDAAAPPGSMPTAPEAE--------PEAPISHPPPPTAVPAEEPPGPQQLVSPgrerP 1656
Cdd:PHA03247 3015 EETDpppVSLKQTLWPpddteDSDADSLFDSDSERSDLEaldplppePHDPFAHEPDPATPEAGARESPSSQFGP----P 3090
|
250 260
....*....|....*....|.
gi 767950710 1657 DLEAPAPGSPFRVRRVRASEL 1677
Cdd:PHA03247 3091 PLSANAALSRRYVRSTGRSAL 3111
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
1498-1724 |
1.23e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.70 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1498 GKRPSPLAhqPVPRI---MVqsaspdirVTRM-------EEAQPEMGPDVLVQTMGAPALKicDKPAKVPSPPPVIAVTA 1567
Cdd:PRK07994 335 GRKDLPLA--PDRRMgveMT--------LLRMlafhpaaPLPEPEVPPQSAAPAASAQATA--APTAAVAPPQAPAVPPP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1568 VTPAPEAQdgPPSPLSEAssgyfshsvsTATLSDALgPGLDAAAPPgsmPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQ 1647
Cdd:PRK07994 403 PASAPQQA--PAVPLPET----------TSQLLAAR-QQLQRAQGA---TKAKKSEPAAASRARPVNSALERLASVRPAP 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 1648 LVSPgrerpdlEAPAPGSPFRVRRVRASElrsfsrmLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLRE 1724
Cdd:PRK07994 467 SALE-------KAPAKKEAYRWKATNPVE-------VKKEPVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAL 529
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
1456-1673 |
1.46e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 43.44 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1456 NNHSPDPGLSNLAASylNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGP 1535
Cdd:PRK12727 30 SNRRTAEGIEIVAAS--NYDEELVQRALETARSDTPATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAED 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1536 DVLVQTMGAPALKICDKPAKVP-----SPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSD-ALGPGLDA 1609
Cdd:PRK12727 108 MIAAMALRQPVSVPRQAPAAAPvraasIPSPAAQALAHAAAVRTAPRQEHALSAVPEQLFADFLTTAPVPRaPVQAPVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1610 AAPPGSMPTAPEAEPEAPISH--------------PPPPTAVPAEEPP---GPQQLVSPGRERpdLEAPAPGSPFRVRRV 1672
Cdd:PRK12727 188 APAPVPAIAAALAAHAAYAQDddeqldddgfdlddALPQILPPAALPPivvAPAAPAALAAVA--AAAPAPQNDEELKQL 265
|
.
gi 767950710 1673 R 1673
Cdd:PRK12727 266 R 266
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
1553-1720 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1553 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1624
Cdd:TIGR01645 291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1625 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1698
Cdd:TIGR01645 371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
|
170 180
....*....|....*....|...
gi 767950710 1699 PA-PGAGGQALASDSEEADEVPE 1720
Cdd:TIGR01645 448 LAiMGEAAAALALEPKKKKKEKE 470
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1560-1666 |
1.61e-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: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1560 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1635
Cdd:NF040712 194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
|
90 100 110
....*....|....*....|....*....|.
gi 767950710 1636 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1666
Cdd:NF040712 274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
1566-1663 |
1.77e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 43.26 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1566 TAVTPAPEAQDGPPsplseassgyfshsvsTATLSDALGPGLDAAAPPGSMPTA--PEAEPEAPISHPPPPTAVPAEEPP 1643
Cdd:PRK14950 358 ALLVPVPAPQPAKP----------------TAAAPSPVRPTPAPSTRPKAAAAAniPPKEPVRETATPPPVPPRPVAPPV 421
|
90 100
....*....|....*....|....*...
gi 767950710 1644 GPQQ--------LVSPGRERPDLEAPAP 1663
Cdd:PRK14950 422 PHTPesapkltrAAIPVDEKPKYTPPAP 449
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
368-444 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950710 368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493 36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1603-1720 |
2.03e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1603 LGPGLDAAAPPGSMPTAPEAEPEApiSHPPPPTAVPAEEPPGPqqlvsPGRERPdLEAPAPGSPFRVRRVRASELRSFSR 1682
Cdd:PRK07764 385 LGVAGGAGAPAAAAPSAAAAAPAA--APAPAAAAPAAAAAPAP-----AAAPQP-APAPAPAPAPPSPAGNAPAGGAPSP 456
|
90 100 110
....*....|....*....|....*....|....*...
gi 767950710 1683 MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1720
Cdd:PRK07764 457 PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAP 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-432 |
2.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950710 368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1544-1709 |
3.50e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1544 APALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGldAAAPPGSMPTAPE 1621
Cdd:PHA03307 776 EPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADaaSRTASKRKSRSHTPDGGSESSGPARPPG--AAARPPPARSSES 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1622 AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPG-SPFRVRRVRASELRSFSRMLAGDP---GC---SPGA 1694
Cdd:PHA03307 854 SKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPpAGAPAPRPRPAPRVKLGPMPPGGPdprGGfrrVPPG 933
|
170
....*....|....*
gi 767950710 1695 EGNAPAPGAggQALA 1709
Cdd:PHA03307 934 DLHTPAPSA--AALA 946
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
611-760 |
6.60e-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: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913 612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950710 684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
1442-1663 |
6.75e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 40.99 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1442 RGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDE-------KRGKRPSPLAHQPVPRIMV 1514
Cdd:COG3266 109 LLRAAALLLLKLLLLLLTLLLLVLLLLLALLLALLLDLPLLTLLIVLPLLEEQLlllalqdIQGTLQALGAVAALLGLRK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1515 QSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSP---PPVIAVTAVTPAPEAQDGPPSPLSEASSGYFS 1591
Cdd:COG3266 189 AEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAagaAEVLTARLVLLLLIIGSALKAPSQASSASAPA 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950710 1592 HSVSTATLSDALGPGldAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSP--GRERPDLEAPAP 1663
Cdd:COG3266 269 TTSLGEQQEVSLPPA--VAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKpvVTETAAPAAPAP 340
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
1607-1701 |
8.53e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 40.72 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950710 1607 LDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAG 1686
Cdd:PRK06995 48 LAALAPPAAAAPAAAQPPPAAAPAAVSRPAAPAAEP--APWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125
|
90
....*....|....*
gi 767950710 1687 DPGCSPGAEGNAPAP 1701
Cdd:PRK06995 126 ENAARRLARAAAAAP 140
|
|
| |
