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Conserved domains on  [gi|1039748264|ref|XP_017171939|]
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kinesin-like protein KIF21A isoform X13 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
23-380 0e+00

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


:

Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 610.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGK 102
Cdd:cd01372      8 RVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  103 TYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDidaknKKSN 182
Cdd:cd01372     88 TYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-----KKPT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  183 IRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaenatdnkli 262
Cdd:cd01372    155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA---------- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  263 sESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQD 342
Cdd:cd01372    225 -PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQD 303
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1039748264  343 SLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 380
Cdd:cd01372    304 SLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1314-1627 1.24e-58

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 204.49  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1314 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1390
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1391 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1469
Cdd:cd00200     81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1470 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1547
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1548 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1625
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                   ..
gi 1039748264 1626 WK 1627
Cdd:cd00200    288 WD 289
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
946-1027 4.84e-44

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


:

Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 154.32  E-value: 4.84e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                   ..
gi 1039748264 1026 AK 1027
Cdd:cd22263     81 AK 82
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
650-865 2.73e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.40  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 729
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 800
Cdd:COG4942    101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  801 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 865
Cdd:COG4942    181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Cast super family cl37807
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
372-846 2.32e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


The actual alignment was detected with superfamily member pfam10174:

Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 52.52  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  372 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 445
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  446 RIKAMQETVDALRARITQLVSEQANQvlaragegNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 515
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  516 trataRSPYFSASSAFSPTILSSDKETieiidLAKKDleklkrkekkkkkrlqKLEESGREERSVAGKDDNADTDQEKKE 595
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKE----------------RIIERLKEQREREDRERLEELESLKKE 476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  596 EKG-----------VSEKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEI 664
Cdd:pfam10174  477 NKDlkekvsalqpeLTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI 556
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  665 AIKQKLIdELENSQKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSeekAKKVKCEYEK--KLHAMNKE 741
Cdd:pfam10174  557 NDRIRLL-EQEVARYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLT---LRQMKEQNKKvaNIKHGQQE 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  742 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrd 816
Cdd:pfam10174  630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-- 701
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039748264  817 hqlRLLEAQKRNQEVVL------------------RRKT--EEVTALRRQ 846
Cdd:pfam10174  702 ---QLEEILEMKQEALLaaisekdaniallelsssKKKKtqEEVMALKRE 748
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
23-380 0e+00

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 610.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGK 102
Cdd:cd01372      8 RVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  103 TYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDidaknKKSN 182
Cdd:cd01372     88 TYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-----KKPT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  183 IRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaenatdnkli 262
Cdd:cd01372    155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA---------- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  263 sESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQD 342
Cdd:cd01372    225 -PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQD 303
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1039748264  343 SLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 380
Cdd:cd01372    304 SLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
23-379 2.86e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 435.85  E-value: 2.86e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 95
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   96 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDLFDTTrdid 175
Cdd:pfam00225   81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  176 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 255
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  256 atdnklisesspmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 334
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1039748264  335 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
23-386 3.54e-135

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 422.37  E-value: 3.54e-135
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264    23 RIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 95
Cdd:smart00129    7 RVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAY 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264    96 GQTGAGKTYTMGtGFdvnimEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTrdid 175
Cdd:smart00129   87 GQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNPS---- 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   176 aknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 255
Cdd:smart00129  149 ----SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG--- 221
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   256 atdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHVPYRDSK 335
Cdd:smart00129  222 ----------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSK 284
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1039748264   336 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:smart00129  285 LTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
52-519 1.67e-92

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 312.06  E-value: 1.67e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   52 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLF 130
Cdd:COG5059     53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  131 KSIDEKKTSAiknglpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 210
Cdd:COG5059    126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  211 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefetlTAKFHFVDLAGSERLK 290
Cdd:COG5059    190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK-------------NKVSGTSE--------TSKLSLVDLAGSERAA 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  291 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 370
Cdd:COG5059    249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  371 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 446
Cdd:COG5059    328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039748264  447 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 519
Cdd:COG5059    403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
PLN03188 PLN03188
kinesin-12 family protein; Provisional
55-412 3.10e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.91  E-value: 3.10e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   55 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVRHLF 130
Cdd:PLN03188   132 QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLF 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  131 KSIDEKKtsaIKNGLPPPEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 210
Cdd:PLN03188   212 ARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVT 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  211 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaenatDNKLISESSPMNEFETltAKFHFVDLAGSERLK 290
Cdd:PLN03188   281 QLLIKGLSNRRTGATSINAESSRSHSVFTCVV---------------ESRCKSVADGLSSFKT--SRINLVDLAGSERQK 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  291 RTGATGERAKEGISINCGLLALGNVISALGDKSK--RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLN 368
Cdd:PLN03188   344 LTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFS 423
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1039748264  369 TLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMELMEYK 412
Cdd:PLN03188   424 TLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDELQRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1314-1627 1.24e-58

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 204.49  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1314 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1390
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1391 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1469
Cdd:cd00200     81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1470 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1547
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1548 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1625
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                   ..
gi 1039748264 1626 WK 1627
Cdd:cd00200    288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1308-1630 7.06e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 174.33  E-value: 7.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1308 RASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------ 1379
Cdd:COG2319    106 DLATGLLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkll 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1380 VSTSY---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLK 1455
Cdd:COG2319    178 ASGSDdgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLA 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1456 RFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFS 1533
Cdd:COG2319    235 TGKLLRTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLAS 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1534 GSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NS 1611
Cdd:COG2319    306 GSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDG 384
                          330
                   ....*....|....*....
gi 1039748264 1612 THVFTAADDRTVRIWKAHN 1630
Cdd:COG2319    385 RTLASGSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
946-1027 4.84e-44

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 154.32  E-value: 4.84e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                   ..
gi 1039748264 1026 AK 1027
Cdd:cd22263     81 AK 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
650-865 2.73e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.40  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 729
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 800
Cdd:COG4942    101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  801 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 865
Cdd:COG4942    181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
673-976 1.18e-09

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 63.53  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  673 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 752
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  753 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 831
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  832 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPAPdtgSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGT 910
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR---RQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264  911 RKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 976
Cdd:TIGR00606  921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
650-1033 1.36e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 726
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  727 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 804
Cdd:PRK03918   385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  805 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLrRKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEA 881
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  882 DTSR--------PGTQQKMRIPVARVQALPTPTTNgTRKKYQRKGFT------GRVFTSKTARMKW-------QLLERRV 940
Cdd:PRK03918   540 EIKSlkkeleklEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  941 TDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIVKESGEGDKSVANIIEEMESLTANIDYINDSIAD 1015
Cdd:PRK03918   619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
                          410
                   ....*....|....*...
gi 1039748264 1016 CQANIMQMEEAKEEGETL 1033
Cdd:PRK03918   699 LKEELEEREKAKKELEKL 716
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
650-1048 2.41e-09

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 62.43  E-value: 2.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVKC 729
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 EYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 806
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  807 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAASGEA 881
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAENKQL 631
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  882 DTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 961
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  962 RQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETLDVTA 1037
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          410
                   ....*....|.
gi 1039748264 1038 VINACTLTEAR 1048
Cdd:pfam05483  777 KENTAILKDKK 787
WD40 pfam00400
WD domain, G-beta repeat;
1313-1348 1.13e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1039748264 1313 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1348
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
372-846 2.32e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 52.52  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  372 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 445
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  446 RIKAMQETVDALRARITQLVSEQANQvlaragegNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 515
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  516 trataRSPYFSASSAFSPTILSSDKETieiidLAKKDleklkrkekkkkkrlqKLEESGREERSVAGKDDNADTDQEKKE 595
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKE----------------RIIERLKEQREREDRERLEELESLKKE 476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  596 EKG-----------VSEKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEI 664
Cdd:pfam10174  477 NKDlkekvsalqpeLTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI 556
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  665 AIKQKLIdELENSQKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSeekAKKVKCEYEK--KLHAMNKE 741
Cdd:pfam10174  557 NDRIRLL-EQEVARYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLT---LRQMKEQNKKvaNIKHGQQE 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  742 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrd 816
Cdd:pfam10174  630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-- 701
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039748264  817 hqlRLLEAQKRNQEVVL------------------RRKT--EEVTALRRQ 846
Cdd:pfam10174  702 ---QLEEILEMKQEALLaaisekdaniallelsssKKKKtqEEVMALKRE 748
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1311-1348 3.69e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.00  E-value: 3.69e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1039748264  1311 PLQCVHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1348
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
723-1118 2.62e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  723 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 798
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  799 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPApdtgSSAAS 878
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----ELEAQ 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  879 GEADTSRPGTQQKMripVARVQALPTPTTNgtrkkyQRKGFTGRVftsKTARMKWQLLERRVTDIIMQkmtISNMEADMN 958
Cdd:TIGR02168  325 LEELESKLDELAEE---LAELEEKLEELKE------ELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  959 RLLRQREELTKRREKLSKRREKIvkesgegDKSVANIIEEMESLTANIDY--INDSIADCQANIMQMEEAKEEGETLDVT 1036
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1037 AVINACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE- 1106
Cdd:TIGR02168  463 LEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGy 535
                          410
                   ....*....|....*
gi 1039748264 1107 ---LDALLGHALQDL 1118
Cdd:TIGR02168  536 eaaIEAALGGRLQAV 550
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
312-521 1.91e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  312 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:COG3206     96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  387 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 452
Cdd:COG3206    174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  453 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 521
Cdd:COG3206    254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
668-810 7.44e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 7.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  668 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 727
Cdd:cd16269    123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  728 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 804
Cdd:cd16269    201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279

                   ....*.
gi 1039748264  805 IAQLKK 810
Cdd:cd16269    280 AELLQE 285
PTZ00121 PTZ00121
MAEBL; Provisional
373-1028 1.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  373 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 451
Cdd:PTZ00121  1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  452 ETVDALRARITQLVSEQANQV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARSPyfsass 529
Cdd:PTZ00121  1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKAD------ 1332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  530 afsptilSSDKETIEiidlaKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGVSEKENNELDV 609
Cdd:PTZ00121  1333 -------AAKKKAEE-----AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  610 EENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE 689
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  690 E--KLMMLQHKIRDTQLERDQVLQNLGSVESYSE----EKAKKV----KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 759
Cdd:PTZ00121  1481 EakKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  760 SQYEK-QLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNREIAQLKK--DQRKRDHQLRLLEAQKRNQEVVLR 834
Cdd:PTZ00121  1561 EEKKKaEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKK 1640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  835 RKTEEVTAlRRQVRPMSDKVAGKvTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVAR-VQALPTPTTNGTRKK 913
Cdd:PTZ00121  1641 KEAEEKKK-AEELKKAEEENKIK-AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKA 1718
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  914 YQ-RKGFTGRVFTSKTARMKWQLLERRVTDIIMQkmtisnmEADMNRLLRQREELTKRREKLSKRREKIVKE-------- 984
Cdd:PTZ00121  1719 EElKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedek 1791
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264  985 -SGEGDKSVANIIEEMESL----TANIDYINDS----------IADCQAniMQMEEAKE 1028
Cdd:PTZ00121  1792 rRMEVDKKIKDIFDNFANIieggKEGNLVINDSkemedsaikeVADSKN--MQLEEADA 1848
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
23-380 0e+00

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 610.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGK 102
Cdd:cd01372      8 RVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  103 TYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDidaknKKSN 182
Cdd:cd01372     88 TYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-----KKPT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  183 IRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaenatdnkli 262
Cdd:cd01372    155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA---------- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  263 sESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQD 342
Cdd:cd01372    225 -PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQD 303
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1039748264  343 SLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 380
Cdd:cd01372    304 SLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
23-379 2.86e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 435.85  E-value: 2.86e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 95
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   96 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDLFDTTrdid 175
Cdd:pfam00225   81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  176 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 255
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  256 atdnklisesspmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 334
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1039748264  335 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
23-386 3.54e-135

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 422.37  E-value: 3.54e-135
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264    23 RIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 95
Cdd:smart00129    7 RVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAY 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264    96 GQTGAGKTYTMGtGFdvnimEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTrdid 175
Cdd:smart00129   87 GQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNPS---- 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   176 aknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 255
Cdd:smart00129  149 ----SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG--- 221
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   256 atdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHVPYRDSK 335
Cdd:smart00129  222 ----------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSK 284
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1039748264   336 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:smart00129  285 LTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
23-377 1.66e-118

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: 376.21  E-value: 1.66e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYG 96
Cdd:cd00106      7 RVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGTIFAYG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   97 QTGAGKTYTMGTGFDvnimeEEQGIISRAVRHLFKSIDEKKTsaiknglPPPEFKVNAQFLELYNEEVLDLFDttrdida 176
Cdd:cd00106     86 QTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRKE-------TKSSFSVSASYLEIYNEKIYDLLS------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  177 KNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtDAENA 256
Cdd:cd00106    147 PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV---------KQRNR 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  257 TDNKLISESSpmnefetltaKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKL 336
Cdd:cd00106    218 EKSGESVTSS----------KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIPYRDSKL 285
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1039748264  337 TRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 377
Cdd:cd00106    286 TRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
23-379 2.33e-103

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: 334.04  E-value: 2.33e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 94
Cdd:cd01371      8 RCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYNGTIFA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   95 YGQTGAGKTYTMGtGFDVNimEEEQGIISRAVRHLFKSIdeKKTSAIKNglpppeFKVNAQFLELYNEEVldlfdttRDI 174
Cdd:cd01371     88 YGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHI--ARSQNNQQ------FLVRVSYLEIYNEEI-------RDL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  175 DAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrvcpqtda 253
Cdd:cd01371    150 LGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---------- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  254 enatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRATHVPYRD 333
Cdd:cd01371    220 ---------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRD 288
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1039748264  334 SKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:cd01371    289 SKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
11-381 1.59e-101

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: 328.78  E-value: 1.59e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   11 GCWRVrsydpWSRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYTQcIEKLIEGCFE 86
Cdd:cd01366      2 GNIRV-----FCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   87 GYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQFLELYNEEVL 165
Cdd:cd01366     76 GYNVCIFAYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIR 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  166 DLFDTTRdidAKNKKSNIRiHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqt 245
Cdd:cd01366    142 DLLAPGN---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  246 rvcpqtDAENATDNklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKr 325
Cdd:cd01366    215 ------SGRNLQTG------------EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS- 275
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264  326 atHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 381
Cdd:cd01366    276 --HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
23-379 1.56e-99

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: 323.91  E-value: 1.56e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYTQCIEKL 80
Cdd:cd01370      7 RVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYEETTKPL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   81 IEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAiknglpppEFKVNAQFLEL 159
Cdd:cd01370     87 VDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKDEK--------EFEVSMSYLEI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  160 YNEEVLDLFDTTrdidakNKKSNIRihEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 239
Cdd:cd01370    152 YNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQ 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  240 IHVCQTrvcpqtdaenatdNKLISESSpmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 319
Cdd:cd01370    224 ITVRQQ-------------DKTASINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL 285
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  320 GDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:cd01370    286 ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
23-379 6.45e-96

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: 312.73  E-value: 6.45e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGA 100
Cdd:cd01369      9 RFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  101 GKTYTMgtgFDVNIMEEEQGIISRAVRHLFKSIdEKKTSAIknglpppEFKVNAQFLELYNEEVLDLFDTTRDidaknkk 180
Cdd:cd01369     89 GKTYTM---EGKLGDPESMGIIPRIVQDIFETI-YSMDENL-------EFHVKVSYFEIYMEKIRDLLDVSKT------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  181 sNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqtdaENATDNK 260
Cdd:cd01369    151 -NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ---------ENVETEK 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  261 LisesspmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLL 340
Cdd:cd01369    221 K------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRIL 286
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1039748264  341 QDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:cd01369    287 QDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
23-386 1.12e-95

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: 313.52  E-value: 1.12e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYTQCIEKLIEG 83
Cdd:cd01365      8 RVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVYEDLGEELLQH 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   84 CFEGYNATVFAYGQTGAGKTYTMgTGFDvnimeEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQFLELYNEE 163
Cdd:cd01365     88 AFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVSYMEIYNEK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  164 VLDLFDTtrdiDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVC 243
Cdd:cd01365    155 VRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLT 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  244 QTRVCPQTDAEnatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD-- 321
Cdd:cd01365    231 QKRHDAETNLT-----------------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADms 293
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264  322 ---KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:cd01365    294 sgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
23-388 1.19e-93

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 307.33  E-value: 1.19e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 94
Cdd:cd01364      9 RCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTIFA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   95 YGQTGAGKTYTMgTGFDVNIME------EEQGIISRAVRHLFKSIDEKKTsaiknglpppEFKVNAQFLELYNEEVLDLF 168
Cdd:cd01364     89 YGQTGTGKTYTM-EGDRSPNEEytweldPLAGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYNEELFDLL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  169 DttrdiDAKNKKSNIRIHEDS--TGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 246
Cdd:cd01364    158 S-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITI---- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  247 vcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKra 326
Cdd:cd01364    229 --------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP-- 292
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  327 tHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 388
Cdd:cd01364    293 -HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
52-519 1.67e-92

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 312.06  E-value: 1.67e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   52 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLF 130
Cdd:COG5059     53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  131 KSIDEKKTSAiknglpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 210
Cdd:COG5059    126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  211 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefetlTAKFHFVDLAGSERLK 290
Cdd:COG5059    190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK-------------NKVSGTSE--------TSKLSLVDLAGSERAA 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  291 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 370
Cdd:COG5059    249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  371 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 446
Cdd:COG5059    328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039748264  447 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 519
Cdd:COG5059    403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
23-388 7.71e-90

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: 296.34  E-value: 7.71e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAG 101
Cdd:cd01373      8 RIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYGQTGSG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  102 KTYTM--GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKTSAIKNglppPEFKVNAQFLELYNEEVLDLFDTTrdidaknk 179
Cdd:cd01373     88 KTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEG----KSFLCKCSFLEIYNEQIYDLLDPA-------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  180 KSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenatdn 259
Cdd:cd01373    156 SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------------- 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  260 kLISESSPMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVPYRDSKLT 337
Cdd:cd01373    217 -TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRDSKLT 295
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039748264  338 RLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 388
Cdd:cd01373    296 FLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
55-379 4.07e-89

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 293.08  E-value: 4.07e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   55 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSID 134
Cdd:cd01374     39 TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQ 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  135 EKKTSaiknglpppEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLK 214
Cdd:cd01374    113 DTPDR---------EFLLRVSYLEIYNEKINDLLSPT--------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  215 LGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaenatdnklisESSPMNEFETLTAKF---HFVDLAGSERLKR 291
Cdd:cd01374    176 RGEKNRHVGETDMNERSSRSHTIFRITI---------------------ESSERGELEEGTVRVstlNLIDLAGSERAAQ 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  292 TGATGERAKEGISINCGLLALGNVISALGDkSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLK 371
Cdd:cd01374    235 TGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLK 313

                   ....*...
gi 1039748264  372 YANRARNI 379
Cdd:cd01374    314 FASRAKKI 321
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
56-375 1.02e-69

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: 237.58  E-value: 1.02e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   56 AFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNimEEEQGIISRAVRHLFKSIde 135
Cdd:cd01367     51 TFRFDYVFDESSSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVFRLL-- 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  136 kKTSAIKNGLpppefKVNAQFLELYNEEVLDLFdttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKL 215
Cdd:cd01367    127 -NKLPYKDNL-----GVTVSFFEIYGGKVFDLL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIES 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  216 GALSRTTASTQMNVQSSRSHAIFTIhVCQTRvcpqtdaenatdnklisesspmnEFETLTAKFHFVDLAGSER-LKRTGA 294
Cdd:cd01367    192 GSSLRTTGQTSANSQSSRSHAILQI-ILRDR-----------------------GTNKLHGKLSFVDLAGSERgADTSSA 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  295 TGERAKEGISINCGLLALGNVISALGDKSkraTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYA 373
Cdd:cd01367    248 DRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYA 324

                   ..
gi 1039748264  374 NR 375
Cdd:cd01367    325 DR 326
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
14-377 4.53e-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: 4.53e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   14 RVRSYdpwSRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEG 87
Cdd:cd01376      1 NVRVA---VRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   88 YNATVFAYGQTGAGKTYTMGTGFdvnimeEEQGIISRAVRHLFkSIDEKKTSAiknglpppeFKVNAQFLELYNEEVLDL 167
Cdd:cd01376     77 QNATVFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLL-QMTRKEAWA---------LSFTMSYLEIYQEKILDL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  168 FDTtrdidaknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrv 247
Cdd:cd01376    141 LEP--------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV----- 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  248 cpqtdaenatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRAT 327
Cdd:cd01376    208 ---------------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLP 269
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039748264  328 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 377
Cdd:cd01376    270 RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
54-377 6.16e-69

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 235.55  E-value: 6.16e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   54 DKAFTFDYVFDiDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNImeEEQGIISRAVRHLFKSI 133
Cdd:cd01375     47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENY--KHRGIIPRALQQVFRMI 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  134 DEKKTSAIKnglpppefkVNAQFLELYNEEVLDLFDTTRDIDAKNKKsnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCL 213
Cdd:cd01375    123 EERPTKAYT---------VHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  214 KLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTG 293
Cdd:cd01375    192 FLGETNRIIASHTMNKNSSRSHCIFTIH-------------------LEAHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  294 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 373
Cdd:cd01375    253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330

                   ....
gi 1039748264  374 NRAR 377
Cdd:cd01375    331 SRVK 334
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
23-373 1.26e-64

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: 223.81  E-value: 1.26e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEG 87
Cdd:cd01368      8 RVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQDLLHG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   88 YNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIdekktsaiknglppPEFKVNAQFLELYNEEVLD 166
Cdd:cd01368     88 KNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNEYIYD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  167 LFDTTRDIDAKNKKSnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTR 246
Cdd:cd01368    147 LLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAP 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  247 VCPQTDAENATDNKLISESSpmnefetltakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRA 326
Cdd:cd01368    226 GDSDGDVDQDKDQITVSQLS-------------LVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQG 292
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039748264  327 T--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 373
Cdd:cd01368    293 TnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
55-412 3.10e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.91  E-value: 3.10e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   55 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVRHLF 130
Cdd:PLN03188   132 QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLF 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  131 KSIDEKKtsaIKNGLPPPEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 210
Cdd:PLN03188   212 ARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVT 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  211 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaenatDNKLISESSPMNEFETltAKFHFVDLAGSERLK 290
Cdd:PLN03188   281 QLLIKGLSNRRTGATSINAESSRSHSVFTCVV---------------ESRCKSVADGLSSFKT--SRINLVDLAGSERQK 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  291 RTGATGERAKEGISINCGLLALGNVISALGDKSK--RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLN 368
Cdd:PLN03188   344 LTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFS 423
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1039748264  369 TLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMELMEYK 412
Cdd:PLN03188   424 TLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDELQRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1314-1627 1.24e-58

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 204.49  E-value: 1.24e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1314 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1390
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1391 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1469
Cdd:cd00200     81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1470 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1547
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1548 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1625
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                   ..
gi 1039748264 1626 WK 1627
Cdd:cd00200    288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1308-1630 7.06e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 174.33  E-value: 7.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1308 RASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------ 1379
Cdd:COG2319    106 DLATGLLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkll 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1380 VSTSY---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLK 1455
Cdd:COG2319    178 ASGSDdgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLA 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1456 RFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFS 1533
Cdd:COG2319    235 TGKLLRTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLAS 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1534 GSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NS 1611
Cdd:COG2319    306 GSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDG 384
                          330
                   ....*....|....*....
gi 1039748264 1612 THVFTAADDRTVRIWKAHN 1630
Cdd:COG2319    385 RTLASGSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
946-1027 4.84e-44

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 154.32  E-value: 4.84e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                   ..
gi 1039748264 1026 AK 1027
Cdd:cd22263     81 AK 82
WD40 COG2319
WD40 repeat [General function prediction only];
1307-1639 6.76e-44

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 165.47  E-value: 6.76e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1307 VRASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT----- 1379
Cdd:COG2319     63 LDAAAGALLATLLGHTAAVLSVAFSPDgrLLASASADGTVRLWDLATGLLLRTLTGHTGAV--------RSVAFSpdgkt 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1380 -VSTSY---IKVWDIrESAKCIRTLTssgqvtlgeacsastsrtvaipSGESQINQIALNPTGTFLYAASG-NAVRMWDL 1454
Cdd:COG2319    135 lASGSAdgtVRLWDL-ATGKLLRTLT----------------------GHSGAVTSVAFSPDGKLLASGSDdGTVRLWDL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1455 KRFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LF 1532
Cdd:COG2319    192 ATGKLLRTLTGHTGAVRSVAFS--PDGK-LLASGSADGTVRLWDLATGKLLRTLTGHS------GSVRSVAFSPDGrlLA 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1533 SGSRDNGIKKWDLaQKGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--N 1610
Cdd:COG2319    263 SGSADGTVRLWDL-ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspD 341
                          330       340
                   ....*....|....*....|....*....
gi 1039748264 1611 STHVFTAADDRTVRIWkahNLQDGQLSDT 1639
Cdd:COG2319    342 GKTLASGSDDGTVRLW---DLATGELLRT 367
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1313-1544 1.30e-35

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 137.85  E-value: 1.30e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1313 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1389
Cdd:cd00200     84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1390 IReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1468
Cdd:cd00200    164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 1469 PVMCLTVdqiSNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LFSGSRDNGIKKWD 1544
Cdd:cd00200    221 GVNSVAF---SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT------NSVTSLAWSPDGkrLASGSADGTIRIWD 289
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
946-1027 1.48e-28

regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410202 [Multi-domain]  Cd Length: 81  Bit Score: 109.99  E-value: 1.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKEsGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22248      1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDE-GKDESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79

                   ..
gi 1039748264 1026 AK 1027
Cdd:cd22248     80 SK 81
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
946-1027 2.46e-28

regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.


Pssm-ID: 410203 [Multi-domain]  Cd Length: 82  Bit Score: 109.51  E-value: 2.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22262      1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80

                   ..
gi 1039748264 1026 AK 1027
Cdd:cd22262     81 TK 82
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
23-167 8.00e-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: 84.58  E-value: 8.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   23 RIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYtQCIEKLIEGCFEGYNATVFAYGQTGAGK 102
Cdd:pfam16796   27 RVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYGQTGSGS 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264  103 TYTMgtgfdvnimeeeqgiISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDL 167
Cdd:pfam16796  102 NDGM---------------IPRAREQIFRFISSLKKG--------WKYTIELQFVEIYNESSQDL 143
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1312-1453 3.07e-17

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 83.92  E-value: 3.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1312 LQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1388
Cdd:cd00200    167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264 1389 DIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWD 1453
Cdd:cd00200    247 DLR-TGECVQTLSGH----------------------TNSVTSLAWSPDGKRLASGSAdGTIRIWD 289
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
54-318 1.01e-12

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: 67.76  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264   54 DKAFTFDYVFDIDSQQEQIYTQCiEKLIEGCFEGYN-ATVFAYGQTGAGKTYTMgtgfdvnimeeeQGIISRAVRHLFKS 132
Cdd:cd01363     17 SKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAFNG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  133 IDEKKTSAiknglpppefkvnaqflelyneevldlfdttrdidaknkksnirihedstggiyTVGVTTRTVNTEPEMMQC 212
Cdd:cd01363     84 INKGETEG------------------------------------------------------WVYLTEITVTLEDQILQA 109
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  213 LKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenatdnklisesspmnefetltakfhFVDLAGSERlkrt 292
Cdd:cd01363    110 NPILEAFG-NAKTTRNENSSRFGKFIEI---------------------------------------LLDIAGFEI---- 145
                          250       260
                   ....*....|....*....|....*.
gi 1039748264  293 gatgerakegisINCGLLALGNVISA 318
Cdd:cd01363    146 ------------INESLNTLMNVLRA 159
WD40 COG2319
WD40 repeat [General function prediction only];
1523-1639 1.06e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.78  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1523 ALAIQGDNLFSGSRDNGIKKWDLAQKGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDS 1602
Cdd:COG2319     43 AASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1039748264 1603 PINAICV--NSTHVFTAADDRTVRIWkahNLQDGQLSDT 1639
Cdd:COG2319    122 AVRSVAFspDGKTLASGSADGTVRLW---DLATGKLLRT 157
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
650-865 2.73e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.40  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 729
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 800
Cdd:COG4942    101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  801 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 865
Cdd:COG4942    181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
673-976 1.18e-09

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 63.53  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  673 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 752
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  753 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 831
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  832 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPAPdtgSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGT 910
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR---RQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264  911 RKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 976
Cdd:TIGR00606  921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
650-1033 1.36e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 726
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  727 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 804
Cdd:PRK03918   385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  805 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLrRKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEA 881
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  882 DTSR--------PGTQQKMRIPVARVQALPTPTTNgTRKKYQRKGFT------GRVFTSKTARMKW-------QLLERRV 940
Cdd:PRK03918   540 EIKSlkkeleklEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  941 TDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIVKESGEGDKSVANIIEEMESLTANIDYINDSIAD 1015
Cdd:PRK03918   619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
                          410
                   ....*....|....*...
gi 1039748264 1016 CQANIMQMEEAKEEGETL 1033
Cdd:PRK03918   699 LKEELEEREKAKKELEKL 716
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
650-1048 2.41e-09

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 62.43  E-value: 2.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVKC 729
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 EYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 806
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  807 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAASGEA 881
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAENKQL 631
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  882 DTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 961
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  962 RQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETLDVTA 1037
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          410
                   ....*....|.
gi 1039748264 1038 VINACTLTEAR 1048
Cdd:pfam05483  777 KENTAILKDKK 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
655-1041 8.82e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  655 ADLANITCEIAIKQKLIDELENSQKRLQTlkkqyeeklmmlqhkirdtqlERDQvlqnlgsVESYSEEKAKKVKCEYEKK 734
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRR---------------------EREK-------AERYQALLKEKREYEGYEL 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  735 LHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE--EQEKARLTESRRN--REIAQLKK 810
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGEleAEIASLER 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  811 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSEspapdtgssaasgeadtsrpgtqQ 890
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELK-----------------------E 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  891 KMRIPVARVQALPTP--TTNGTRKKYQRK--GFTGRVFTSKTARMKWQLLERRVTdiimqkMTISNMEADMNRLLRQREE 966
Cdd:TIGR02169  365 ELEDLRAELEEVDKEfaETRDELKDYREKleKLKREINELKRELDRLQEELQRLS------EELADLNAAIAGIEAKINE 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  967 LTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK-----EEGETLDVTAVINA 1041
Cdd:TIGR02169  439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
650-890 1.59e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.61  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 724
Cdd:COG3883     32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  725 KKvkceyekkLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 804
Cdd:COG3883    112 ES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  805 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTS 884
Cdd:COG3883    184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263

                   ....*.
gi 1039748264  885 RPGTQQ 890
Cdd:COG3883    264 AAGAAA 269
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
652-855 4.01e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  652 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVK 728
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  729 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 802
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  803 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 855
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
590-856 5.16e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 5.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  590 DQEKKEEKGVS-------EKENNELDVEENQEVSDHEDeeeeEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 662
Cdd:TIGR02168  220 AELRELELALLvlrleelREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNkel 742
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELE--- 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  743 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---REIAQLKKDQRK 814
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAELEELEEELEE 451
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1039748264  815 RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 856
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
WD40 pfam00400
WD domain, G-beta repeat;
1313-1348 1.13e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1039748264 1313 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1348
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
372-846 2.32e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 52.52  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  372 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 445
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  446 RIKAMQETVDALRARITQLVSEQANQvlaragegNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 515
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  516 trataRSPYFSASSAFSPTILSSDKETieiidLAKKDleklkrkekkkkkrlqKLEESGREERSVAGKDDNADTDQEKKE 595
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKE----------------RIIERLKEQREREDRERLEELESLKKE 476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  596 EKG-----------VSEKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEI 664
Cdd:pfam10174  477 NKDlkekvsalqpeLTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI 556
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  665 AIKQKLIdELENSQKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSeekAKKVKCEYEK--KLHAMNKE 741
Cdd:pfam10174  557 NDRIRLL-EQEVARYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLT---LRQMKEQNKKvaNIKHGQQE 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  742 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrd 816
Cdd:pfam10174  630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-- 701
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039748264  817 hqlRLLEAQKRNQEVVL------------------RRKT--EEVTALRRQ 846
Cdd:pfam10174  702 ---QLEEILEMKQEALLaaisekdaniallelsssKKKKtqEEVMALKRE 748
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
663-1027 2.74e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKE 741
Cdd:PRK03918   148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREIN-EISSELPELREE 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  742 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNR--EIAQLKKDQRKRDHQL 819
Cdd:PRK03918   223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFY 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  820 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA--GKVTRKLSssespapdtgssaasgeadtsrpgtqqkmripva 897
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErlEELKKKLK---------------------------------- 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  898 rvqalptpttnGTRKKYQRkgFTGRVftsktarmkwQLLERrvtdiIMQKMTisnmeadmnrllrQREELTKRREKLSKr 977
Cdd:PRK03918   349 -----------ELEKRLEE--LEERH----------ELYEE-----AKAKKE-------------ELERLKKRLTGLTP- 386
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039748264  978 rEKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK 1027
Cdd:PRK03918   387 -EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1311-1348 3.69e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.00  E-value: 3.69e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1039748264  1311 PLQCVHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1348
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
722-848 3.99e-06

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 47.61  E-value: 3.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  722 EKAKKVKCEYEKKLHamnkelqrlqtaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 801
Cdd:pfam20492    2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  802 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 848
Cdd:pfam20492   58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
654-848 5.72e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 5.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  654 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRD-TQLERDQVLQNLGSvesySEEKAKKVKCEYE 732
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  733 KKLHAMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 808
Cdd:TIGR02169  812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1039748264  809 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 848
Cdd:TIGR02169  888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
548-1102 5.98e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.51  E-value: 5.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  548 LAKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKgvSEKENNELDVEENQEVSDHEDEEEEEED 627
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE--KLAQVLKENKEEEKEKKLQEEELKLLAK 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  628 EEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRL--QTLKKQYEEKLMMLQHKIRDTQLE 705
Cdd:pfam02463  294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELeiKREAEEEEEEELEKLQEKLEQLEE 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  706 RDQVLQNLGSVESYSEEKakkvkcEYEKKLHAMNKELQRLQTAQKeharlLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK 785
Cdd:pfam02463  374 ELLAKKKLESERLSSAAK------LKEEELELKSEEEKEAQLLLE-----LARQLEDLLKEEKKEELEILEEEEESIELK 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  786 QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRR-KTEEVTALRRQVRPMSDK----VAGKVTR 860
Cdd:pfam02463  443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVllalIKDGVGG 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  861 KLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIpvarVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERRV 940
Cdd:pfam02463  523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT----ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  941 TDIIMQKMTI--SNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANidyINDSIADCQA 1018
Cdd:pfam02463  599 IDPILNLAQLdkATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVK---ASLSELTKEL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1019 NIMQMEEAKEEGETLdvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLK 1098
Cdd:pfam02463  676 LEIQELQEKAESELA---------KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746

                   ....
gi 1039748264 1099 EKAE 1102
Cdd:pfam02463  747 EEEE 750
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
583-882 7.25e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 7.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  583 KDDNADTDQEKKEEkgvsEKENNELDVEENQevsdhedeeeeeeDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 662
Cdd:COG1196    233 KLRELEAELEELEA----ELEELEAELEELE-------------AELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKEL 742
Cdd:COG1196    296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAEL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  743 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLL 822
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  823 EAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEAD 882
Cdd:COG1196    455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
669-1033 1.02e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  669 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQR---- 744
Cdd:COG4372      3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEELEQARSELEQleee 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  745 -------LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRK 814
Cdd:COG4372     82 leelneqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLES 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  815 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQVRPMSDKVagKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKmri 894
Cdd:COG4372    162 LQEELAALEQELQALS--EAEAEQALDELLKEANRNAEKE--EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA--- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  895 pvarVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLRQREELTKRREKL 974
Cdd:COG4372    235 ----LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264  975 SKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAKEEGETL 1033
Cdd:COG4372    311 GALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1590-1627 1.15e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.84  E-value: 1.15e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1039748264  1590 TFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIWK 1627
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
671-825 1.20e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  671 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAM--NKELQRLQta 748
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYEALQ-- 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  749 qKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 825
Cdd:COG1579     96 -KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
667-836 1.36e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.15  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  667 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVKCEYEKKLhAMNKELQRLQ 746
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKA-RQRQELQQAR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  747 TAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 823
Cdd:pfam13868  242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
                          170
                   ....*....|...
gi 1039748264  824 AQKRNQEVVLRRK 836
Cdd:pfam13868  317 GERLREEEAERRE 329
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
723-1118 2.62e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  723 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 798
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  799 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPApdtgSSAAS 878
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----ELEAQ 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  879 GEADTSRPGTQQKMripVARVQALPTPTTNgtrkkyQRKGFTGRVftsKTARMKWQLLERRVTDIIMQkmtISNMEADMN 958
Cdd:TIGR02168  325 LEELESKLDELAEE---LAELEEKLEELKE------ELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  959 RLLRQREELTKRREKLSKRREKIvkesgegDKSVANIIEEMESLTANIDY--INDSIADCQANIMQMEEAKEEGETLDVT 1036
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1037 AVINACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE- 1106
Cdd:TIGR02168  463 LEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGy 535
                          410
                   ....*....|....*
gi 1039748264 1107 ---LDALLGHALQDL 1118
Cdd:TIGR02168  536 eaaIEAALGGRLQAV 550
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
679-831 2.95e-05

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 48.05  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  679 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVKCEYEKKlHAMNKELQRL 745
Cdd:pfam02841  155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  746 QTAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 824
Cdd:pfam02841  224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286

                   ....*..
gi 1039748264  825 QKRNQEV 831
Cdd:pfam02841  287 ESLQKEI 293
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
721-866 3.06e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  721 EEKAKKVKCEYEKKLHAMNKELQRLQtaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKtKVRLMKQmkEEQEKARLTE-- 798
Cdd:COG2433    394 EPEAEREKEHEERELTEEEEEIRRLE---EQVERLEAEVEELEAELEEKDERIERLER-ELSEARS--EERREIRKDRei 467
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264  799 SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 866
Cdd:COG2433    468 SRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKFTKEA 523
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
667-861 4.57e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.20  E-value: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  667 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHKIR--------DTQLERDQVLQNLGSVESYSEEKAKKVK 728
Cdd:pfam17380  305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAMERERelerirqeERKRELERIRQEEIAMEISRMRELERLQ 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  729 CEYEKKLHAMNKELQ---RLQTAQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNRE 804
Cdd:pfam17380  385 MERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQ 461
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264  805 IAQLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEEVTALRRQVRPMSDKVAGKVTRK 861
Cdd:pfam17380  462 VERLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILEKELEERKQAMIEEERKRKLLEK 520
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
686-839 4.69e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  686 KQYEEKLMMLQ-HKIRDTQLERDQVLQNLgsVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQyEK 764
Cdd:pfam13868    9 RELNSKLLAAKcNKERDAQIAEKKRIKAE--EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-ER 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264  765 QLKKlQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEE 839
Cdd:pfam13868   86 EQKR-QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
664-880 6.24e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 6.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  664 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLGSVESYSEEKAkkvkcEYEKKLHAMNKELQ 743
Cdd:COG4913    612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELE 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  744 RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 820
Cdd:COG4913    679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039748264  821 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGE 880
Cdd:COG4913    755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
WD40 pfam00400
WD domain, G-beta repeat;
1591-1626 6.85e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 6.85e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1039748264 1591 FVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIW 1626
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
663-853 8.42e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 8.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKLIDELEnsqkRLQTLKKQYEEKLMM-----LQHKIRDTQLERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLH 736
Cdd:pfam17380  369 EIAMEISRMRELE----RLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKVEMEQIRAEqEEARQREVRRLEEER 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  737 AMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQE----KARLTESRRNREIaqLKKDQ 812
Cdd:pfam17380  445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKL--LEKEM 522
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039748264  813 RKRdhQLRLLEAQKRNQEVVLRRKTEEVTALRR---QVRPMSDK 853
Cdd:pfam17380  523 EER--QKAIYEEERRREAEEERRKQQEMEERRRiqeQMRKATEE 564
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
666-838 9.16e-05

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 45.53  E-value: 9.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  666 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSeekakKVKCEYEKKLHAMNKELQRL 745
Cdd:pfam14988   23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFA-----KLKESQEREIQDLEEEKEKV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  746 Q-----TAQKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 815
Cdd:pfam14988   98 RaetaeKDREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
                          170       180
                   ....*....|....*....|...
gi 1039748264  816 DHQLRLLEAQKRNQEvvlRRKTE 838
Cdd:pfam14988  176 IQETQALEAIKSKLE---NRKQR 195
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
693-836 1.71e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 44.70  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  693 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKvKCEYEKKLhaMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQD 772
Cdd:pfam13904   38 LTYARKLEGLKLER-------QPLEAYENWLAAK-QRQRQKEL--QAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264  773 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 836
Cdd:pfam13904  108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
663-836 1.78e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV-LQNLGSVEsyseekakkvkceyekklhamnke 741
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLE------------------------ 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  742 lQRLQTAQKEHARLLKNQSQYEKQLKKL-------QQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRK 814
Cdd:COG4913    345 -REIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
                          170       180
                   ....*....|....*....|....
gi 1039748264  815 RDHQLRLLEAQKRN--QEVVLRRK 836
Cdd:COG4913    424 LEAEIASLERRKSNipARLLALRD 447
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
312-521 1.91e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  312 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:COG3206     96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  387 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 452
Cdd:COG3206    174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  453 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 521
Cdd:COG3206    254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
PRK12704 PRK12704
phosphodiesterase; Provisional
696-839 2.40e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  696 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQY----E 763
Cdd:PRK12704    30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264  764 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 839
Cdd:PRK12704   110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
733-853 3.07e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  733 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 810
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1039748264  811 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 853
Cdd:COG4717    151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
667-848 3.21e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 3.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  667 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 746
Cdd:pfam13868  125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  747 TAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 819
Cdd:pfam13868  198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
                          170       180
                   ....*....|....*....|....*....
gi 1039748264  820 RLLEAQKRNQevvlrRKTEEVTALRRQVR 848
Cdd:pfam13868  277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
653-840 4.00e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  653 YQADLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAk 725
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELA- 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  726 kvkcEYEKKLHAMNKELQRLQTAQKEHARLLKNQsqyEKQLKKLQQDVmemkktkvrlmkqMKEEQEKARLTEsrrnrEI 805
Cdd:TIGR02169  424 ----DLNAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADL-------------SKYEQELYDLKE-----EY 478
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039748264  806 AQLKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 840
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
654-798 4.31e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  654 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 724
Cdd:COG4717     94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039748264  725 KKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTE 798
Cdd:COG4717    174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
662-830 5.55e-04

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 44.28  E-value: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  662 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVKCEYEKKL 735
Cdd:pfam15742   54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  736 hamnkELQRlqtaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 802
Cdd:pfam15742  132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039748264  803 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 830
Cdd:pfam15742  203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
709-846 6.10e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.56  E-value: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  709 VLQNLGSVESYSEEKAKKVKCEyekKLHAMNKELQRLQTAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 784
Cdd:pfam15709  305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  785 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 846
Cdd:pfam15709  380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
668-842 6.31e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 44.29  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  668 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQT 747
Cdd:pfam05622  310 QQLLEDANRRKNELETQNRLANQRILELQQQVEELQKA----LQEQGSKAEDSSLLKQKLE-EHLEKLHEAQSELQKKKE 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  748 AQKEHARllKNQSQYEKQLKKLQqdvmEMKKTKVRLMKQMKEEQ----EKARLT----ESRRNR----EIAQLKKDQRKR 815
Cdd:pfam05622  385 QIEELEP--KQDSNLAQKIDELQ----EALRKKDEDMKAMEERYkkyvEKAKSViktlDPKQNPasppEIQALKNQLLEK 458
                          170       180       190
                   ....*....|....*....|....*....|
gi 1039748264  816 DHQLRLLEAQKrnQEVVLRRKTEE---VTA 842
Cdd:pfam05622  459 DKKIEHLERDF--EKSKLQREQEEkliVTA 486
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
668-810 7.44e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 7.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  668 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 727
Cdd:cd16269    123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  728 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 804
Cdd:cd16269    201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279

                   ....*.
gi 1039748264  805 IAQLKK 810
Cdd:cd16269    280 AELLQE 285
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-614 8.13e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 8.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  370 LKYANRARNIKNKVMVNQDR-ASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIK 448
Cdd:COG1196    216 RELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEE-----------LRLELEELELELE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  449 AMQETVDALRARITQLVSE---------QANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 519
Cdd:COG1196    285 EAQAEEYELLAELARLEQDiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  520 ARspYFSASSAFSPTILSSDKETIEIIDLAKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGV 599
Cdd:COG1196    365 EA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
                          250
                   ....*....|....*
gi 1039748264  600 SEKENNELDVEENQE 614
Cdd:COG1196    443 ALEEAAEEEAELEEE 457
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
707-842 8.27e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.59  E-value: 8.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  707 DQVLQNLGSVESYSEEKA--KKVKCEYEKKLHAMNKELQR----LQTAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 780
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  781 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 842
Cdd:pfam13851   92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
661-825 8.57e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 42.20  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  661 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVKCEY--- 731
Cdd:pfam15619   17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  732 EKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 811
Cdd:pfam15619   87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
                          170
                   ....*....|....
gi 1039748264  812 QRKRDHQLRLLEAQ 825
Cdd:pfam15619  165 HKEAQEEVKILQEE 178
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
663-848 8.64e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 8.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE 732
Cdd:COG4913    669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  733 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 809
Cdd:COG4913    749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039748264  810 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 848
Cdd:COG4913    822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
PTZ00121 PTZ00121
MAEBL; Provisional
373-1028 1.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  373 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 451
Cdd:PTZ00121  1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  452 ETVDALRARITQLVSEQANQV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARSPyfsass 529
Cdd:PTZ00121  1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKAD------ 1332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  530 afsptilSSDKETIEiidlaKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGVSEKENNELDV 609
Cdd:PTZ00121  1333 -------AAKKKAEE-----AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  610 EENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE 689
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  690 E--KLMMLQHKIRDTQLERDQVLQNLGSVESYSE----EKAKKV----KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 759
Cdd:PTZ00121  1481 EakKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  760 SQYEK-QLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNREIAQLKK--DQRKRDHQLRLLEAQKRNQEVVLR 834
Cdd:PTZ00121  1561 EEKKKaEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKK 1640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  835 RKTEEVTAlRRQVRPMSDKVAGKvTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVAR-VQALPTPTTNGTRKK 913
Cdd:PTZ00121  1641 KEAEEKKK-AEELKKAEEENKIK-AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKA 1718
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  914 YQ-RKGFTGRVFTSKTARMKWQLLERRVTDIIMQkmtisnmEADMNRLLRQREELTKRREKLSKRREKIVKE-------- 984
Cdd:PTZ00121  1719 EElKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedek 1791
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264  985 -SGEGDKSVANIIEEMESL----TANIDYINDS----------IADCQAniMQMEEAKE 1028
Cdd:PTZ00121  1792 rRMEVDKKIKDIFDNFANIieggKEGNLVINDSkemedsaikeVADSKN--MQLEEADA 1848
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
664-847 1.24e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  664 IAIKQKLIDELENSQKRL-QTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAKKVKCEYEKKL---HAMN 739
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLdEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEKLqerEQMD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  740 KELQRLQTAQKEharllknqsQYEKQLKK---LQQDVMEMKKTKVRLMKQMKEEQEKarltESRRNREiAQLKKDQRKrd 816
Cdd:pfam13868  105 EIVERIQEEDQA---------EAEEKLEKqrqLREEIDEFNEEQAEWKELEKEEERE----EDERILE-YLKEKAERE-- 168
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039748264  817 hqlrllEAQKRNQEVVLRRKTEEVTALRRQV 847
Cdd:pfam13868  169 ------EEREAEREEIEEEKEREIARLRAQQ 193
46 PHA02562
endonuclease subunit; Provisional
659-861 1.32e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.46  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  659 NITCEIAIKQKLIDELENSQK-RLQTLKKQYEEKL-MMLQHKIRDTQLErDQVLQNLGSVESYSEEKAK--------KVK 728
Cdd:PHA02562   192 HIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVeEAKTIKAEIEELT-DELLNLVMDIEDPSAALNKlntaaakiKSK 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  729 CEYEKKLHAMNKE-------LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEkarltesrR 801
Cdd:PHA02562   271 IEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE--------L 342
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  802 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRK 861
Cdd:PHA02562   343 KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
663-866 1.32e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKEL 742
Cdd:TIGR04523  413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  743 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL-----------------MKQMKEEQEKARLTESRR--NR 803
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLesekkekeskisdledeLNKDDFELKKENLEKEIDekNK 568
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039748264  804 EIAQLKKDQRKrdhqlrLLEAQKRNQEvVLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 866
Cdd:TIGR04523  569 EIEELKQTQKS------LKKKQEEKQE-LIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAK 623
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
680-848 1.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  680 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 759
Cdd:COG4913    226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  760 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 837
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
                          170
                   ....*....|.
gi 1039748264  838 EEVTALRRQVR 848
Cdd:COG4913    380 EEFAALRAEAA 390
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
678-842 1.39e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.40  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  678 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVKCEYEKKLHAMNKELQRLQ-TAQKEHARL 755
Cdd:pfam15709  360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  756 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 835
Cdd:pfam15709  424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498

                   ....*..
gi 1039748264  836 KTEEVTA 842
Cdd:pfam15709  499 QKEEEAA 505
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
745-871 1.42e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.35  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  745 LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEA 824
Cdd:pfam07888  310 QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  825 QKrnQEV-----VLRRKTEEVTALRRQVRPMSDKvaGKVTRKLSSSESPAPD 871
Cdd:pfam07888  386 EK--QELleyirQLEQRLETVADAKWSEAALTST--ERPDSPLSDSEDENPE 433
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
666-891 1.48e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 43.13  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  666 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDtqlERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLHAMNKEL 742
Cdd:pfam04747   12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSIND---QRKEAFASLELTEQPQQvEKVKKSEKKKAQKQIAKDHEA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  743 QRLQTAQKEHArllKNQSQYEKQLKKlqqdvmemKKTKVRLMKQMKEEQEKarltesrrnreiaqLKKDQRKRDHQLRLL 822
Cdd:pfam04747   89 EQKVNAKKAAE---KEARRAEAEAKK--------RAAQEEEHKQWKAEQER--------------IQKEQEKKEADLKKL 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  823 EAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQK 891
Cdd:pfam04747  144 QAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKK 215
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
672-846 1.55e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  672 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVES-YSEEKAKKVkcEYEKKLHAMNKELQRLQTAQK 750
Cdd:COG3206    189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESqLAEARAELA--EAEARLAALRAQLGSGPDALP 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  751 EH------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRK 814
Cdd:COG3206    258 ELlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQL 336
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039748264  815 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 846
Cdd:COG3206    337 AQLEARLAELPELEAE--LRRLEREVEVAREL 366
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
720-827 1.55e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.21  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  720 SEEKAK------KVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 793
Cdd:pfam11600   10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039748264  794 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 827
Cdd:pfam11600   83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
734-848 1.58e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  734 KLHAMNKELQRLQTAQKEH----ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-----ARLTESRRNR- 803
Cdd:COG1579     11 DLQELDSELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVRNNKe 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039748264  804 ------EIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 848
Cdd:COG1579     91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
WD40 pfam00400
WD domain, G-beta repeat;
1457-1498 1.64e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1039748264 1457 FQSTGKLTGHLGPVMCLTvdqISNGQDLIITGSKDHYIKMFD 1498
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
681-847 1.80e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 41.57  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  681 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEKAKKVKCE-----YEK-KLHAMNK-ELQRLQTAQKEha 753
Cdd:pfam15665   16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKRRIQTLEesleqHERmKRQALTEfEQYKRRVEERE-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  754 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 819
Cdd:pfam15665   88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
                          170       180
                   ....*....|....*....|....*....
gi 1039748264  820 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 847
Cdd:pfam15665  165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
671-910 1.86e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  671 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsveSYSEEKAKKVkceyEKKLHAMNKELQRLQTAQK 750
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKL----QAEIAEAEAEIEERREELG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  751 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 815
Cdd:COG3883     90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  816 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIP 895
Cdd:COG3883    167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
                          250
                   ....*....|....*
gi 1039748264  896 VARVQALPTPTTNGT 910
Cdd:COG3883    247 AGAGAAGAAGAAAGS 261
Rabaptin pfam03528
Rabaptin;
667-826 2.17e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 42.40  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  667 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSE----EKAKKVKC 729
Cdd:pfam03528   24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSEntkqEAIDEVKS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 EYEKK---LHAMNKELQRLQTAQKeHARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQEKA 794
Cdd:pfam03528  101 QWQEEvasLQAIMKETVREYEVQF-HRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAEKL 176
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039748264  795 RLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 826
Cdd:pfam03528  177 RSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
672-805 2.18e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  672 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVKCEYEKKLHAMNKELQ-RLQTAQK 750
Cdd:PRK00409   516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  751 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 805
Cdd:PRK00409   585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
650-780 2.30e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  650 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEE 722
Cdd:PRK00409   508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEA-------EK 573
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  723 KAKKV----KCEYEKKLHAMNKELQRLQTAQKEHaRLLKNQSQYEKQLKKLQQDVMEMKKTK 780
Cdd:PRK00409   574 EAQQAikeaKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQ 634
PRK12704 PRK12704
phosphodiesterase; Provisional
666-805 2.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  666 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKCEYEKKLHAMNKELQRL 745
Cdd:PRK12704    77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  746 QTAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 805
Cdd:PRK12704   148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
672-815 2.49e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  672 DELENsQKRLQTLKKQYEEKLmmlQHKIRDTQLERDQVL---QNLGSVESYSEEKAKKVkCEYEKKLHAMNKELQRLQTA 748
Cdd:pfam17380  454 EEQER-QQQVERLRQQEEERK---RKKLELEKEKRDRKRaeeQRRKILEKELEERKQAM-IEEERKRKLLEKEMEERQKA 528
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264  749 QKEHARLLKNQSQYEKQLKklqqdvMEMKKtkvRLMKQM-KEEQEKARLTESRRNREIA-QLKKDQRKR 815
Cdd:pfam17380  529 IYEEERRREAEEERRKQQE------MEERR---RIQEQMrKATEERSRLEAMEREREMMrQIVESEKAR 588
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
668-799 2.98e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  668 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 746
Cdd:COG3206    266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039748264  747 TAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 799
Cdd:COG3206    334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
711-821 3.15e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 40.23  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  711 QNLgsVESYSEEKAKKVKCEyekklhamNKELQRLQTAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkq 786
Cdd:cd23703     61 QNL--REGLRELEERKLKTE--------ELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT--- 124
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039748264  787 mkEEQEKARLTESRRNREIAQLKKDQRKRDHQLRL 821
Cdd:cd23703    125 --DPEREERAAKRRANREAKELAKKEARADALHEL 157
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
357-1110 3.26e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  357 SPSDRDFMETL-NTLKYANRARNIKNKVMVNqdrASQQINALRSEITRLQMELMEYKT---------GKRIIDEEGVES- 425
Cdd:pfam15921  137 SQSQEDLRNQLqNTVHELEAAKCLKEDMLED---SNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasGKKIYEHDSMSTm 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  426 --------INDMFHEnamLQTENNNLRVRIKAMQETVDALRaritqlvSEQANQVLARAGEGNEEISNMIHSYIKEIEDL 497
Cdd:pfam15921  214 hfrslgsaISKILRE---LDTEISYLKGRIFPVEDQLEALK-------SESQNKIELLLQQHQDRIEQLISEHEVEITGL 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  498 RAKlleseavnenlrknltratarspyfsASSAFSPTilSSDKETIEIIdlakkdleklkrkekkkkkrlqklEESGREE 577
Cdd:pfam15921  284 TEK--------------------------ASSARSQA--NSIQSQLEII------------------------QEQARNQ 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  578 RSVAGKddnadtdQEKKEEKGVSEkenneLDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADL 657
Cdd:pfam15921  312 NSMYMR-------QLSDLESTVSQ-----LRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  658 anitceiaikQKLIDELENSQKRLqTLKKQYEEKL--------MMLQHKIRDTQlERDQVLQNLGSVesyseEKAKKVKC 729
Cdd:pfam15921  380 ----------QKLLADLHKREKEL-SLEKEQNKRLwdrdtgnsITIDHLRRELD-DRNMEVQRLEAL-----LKAMKSEC 442
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  730 --EYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrRNREIAQ 807
Cdd:pfam15921  443 qgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA-TNAEITK 521
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  808 LkkdqRKRdHQLRLLEAQK-RNQEVVLRRKTEEVTALRRQVRPmSDKVAGKVTRKLSSSESPAPDTGSSAASgeadtsrp 886
Cdd:pfam15921  522 L----RSR-VDLKLQELQHlKNEGDHLRNVQTECEALKLQMAE-KDKVIEILRQQIENMTQLVGQHGRTAGA-------- 587
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  887 gtqqkMRIPVARVQAlptpTTNGTRKKYQRKgftgRVFTSKTaRMKWQLLERRVTDIIMQKMTISNMEADMNRLLRQree 966
Cdd:pfam15921  588 -----MQVEKAQLEK----EINDRRLELQEF----KILKDKK-DAKIRELEARVSDLELEKVKLVNAGSERLRAVKD--- 650
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  967 ltkrrekLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANI-MQMEEAKEEGETldvtaviNACTLT 1045
Cdd:pfam15921  651 -------IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkMQLKSAQSELEQ-------TRNTLK 716
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 1046 EARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTE--ITSATQNQllfHMLK-EKAELNPELDAL 1110
Cdd:pfam15921  717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeaMTNANKEK---HFLKeEKNKLSQELSTV 781
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1457-1498 3.49e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.91  E-value: 3.49e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1039748264  1457 FQSTGKLTGHLGPVMCLtvdQISNGQDLIITGSKDHYIKMFD 1498
Cdd:smart00320    2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
PRK11637 PRK11637
AmiB activator; Provisional
669-836 3.56e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.60  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  669 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAM 738
Cdd:PRK11637   103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  739 NKELQRLQTAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 813
Cdd:PRK11637   183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
                          170       180
                   ....*....|....*....|....*
gi 1039748264  814 KR-DHQLRllEAQK-RNQEVVLRRK 836
Cdd:PRK11637   258 ARaEREAR--EAARvRDKQKQAKRK 280
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
722-848 4.19e-03

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 41.12  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  722 EKAKKVKCEYEKKLHAMNK-ELQRLQ--TAQKEHARLLKNQSQYEKQLKKLQQDVMEmkktkvrlmkqmkEEQEKARLTE 798
Cdd:pfam12037   29 ERAAKAARELESSPHAKKAlELMKKQeqTRQAELQAKIKEYEAAQEQLKIERQRVEY-------------EERRKTLQEE 95
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039748264  799 SRRNREIAQlKKDQ--RKRdHQLRLLEAQKRNQEVVlrRKTEEVTALRRQVR 848
Cdd:pfam12037   96 TKQKQQRAQ-YQDElaRKR-YQDQLEAQRRRNEELL--RKQEESVAKQEAMR 143
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
668-984 4.21e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  668 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEE--KAKKVKCEYEKKLH 736
Cdd:pfam01576  702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDerKQRAQAVAAKKKLE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  737 AMNKELQ-RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD---- 811
Cdd:pfam01576  777 LDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaas 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  812 --QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSEspapDTGS 874
Cdd:pfam01576  853 erARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQV----EQLT 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  875 SAASGEADTSrpgtqQKmripvarvqalptptTNGTRKKYQRKgftgrvftSKTARMKWQLLERRVTDiiMQKMTISNME 954
Cdd:pfam01576  924 TELAAERSTS-----QK---------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAALE 973
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1039748264  955 ADMNRLLRQREELTKRRE---KLSKRREKIVKE 984
Cdd:pfam01576  974 AKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
695-823 5.32e-03

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 39.53  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  695 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVKCEYEKKLHA-------MNKELQR----LQ 746
Cdd:pfam14073    9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264  747 TAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 823
Cdd:pfam14073   89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
448-1081 5.40e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  448 KAMQETVDALRARITQLVSEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARspYFSA 527
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--EYEL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  528 SSAFSPTILSSDKETIEIIDLAKKdleklkrkekkkkkrlqkLEESGREERSVAGKDDNADTD-QEKKEEKGVSEKENNE 606
Cdd:COG1196    294 LAELARLEQDIARLEERRRELEER------------------LEELEEELAELEEELEELEEElEELEEELEEAEEELEE 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  607 LDVEENQEVSDHEDEEEEEEdeeeeddiegeessdesDSESDEKANYQADLANITcEIAIKQKLIDELENSQKRLQTLKK 686
Cdd:COG1196    356 AEAELAEAEEALLEAEAELA-----------------EAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLE 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  687 QYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseekakkvkceyEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQL 766
Cdd:COG1196    418 RLEEELEELEEALAELEEEEEEEEEAL------------------EEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  767 KKLQQDVMEmKKTKVRLMKQMKEEQE-----KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQkRNQEVVLRRKTEEVT 841
Cdd:COG1196    480 AELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDE 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  842 ALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVARvqalptpttngtrkkYQRKGFTG 921
Cdd:COG1196    558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------------YYVLGDTL 622
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  922 RVFTSKTARMKWQLLERRVTD----IIMQKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIE 997
Cdd:COG1196    623 LGRTLVAARLEAALRRAVTLAgrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  998 EMESLTANIDYINDSIADCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEG 1077
Cdd:COG1196    703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEELPEPPDLEELERELERLER 774

                   ....
gi 1039748264 1078 RLKQ 1081
Cdd:COG1196    775 EIEA 778
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
748-876 5.42e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 39.67  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  748 AQKEHARLLKNQSQYEKQLKKLQQdvmemKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK---------KDQRKRDHQ 818
Cdd:pfam11600   11 EEKEKQRLEKDKERLRRQLKLEAE-----KEEKERLKEEAKAEKERAKEEARRKKEEEKELKekerrekkeKDEKEKAEK 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264  819 LRLLEAQKRNQEVVL------RRKTEEVTALRRQVRPMSDKVAGkVTRKLSSSESP-APDTGSSA 876
Cdd:pfam11600   86 LRLKEEKRKEKQEALeakleeKRKKEEEKRLKEEEKRIKAEKAE-ITRFLQKPKTQqAPKTLAGS 149
FliJ pfam02050
Flagellar FliJ protein;
672-807 6.17e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 38.42  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  672 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAkkvkceYEKKLHAMNKELQRLQtaqKE 751
Cdd:pfam02050    1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQ----QQLSGAGQGISAAELRN------YQAFISQLDEAIAQQQ---QE 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264  752 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 807
Cdd:pfam02050   68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
680-809 6.41e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.84  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  680 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE-KKLHAMNKELQRLQTAQKEHARLL- 756
Cdd:TIGR02473    6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039748264  757 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 809
Cdd:TIGR02473   86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
725-827 7.55e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 39.75  E-value: 7.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  725 KKVKCEYEKKLHAMNKelQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrRNRE 804
Cdd:pfam14988   10 AKKTEEKQKKIEKLWN--QYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKES-QERE 86
                           90       100
                   ....*....|....*....|....*
gi 1039748264  805 IAQLKKDQRK--RDHQLRLLEAQKR 827
Cdd:pfam14988   87 IQDLEEEKEKvrAETAEKDREAHLQ 111
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
690-913 7.79e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  690 EKLMMLQHKIRDTQLERDQvLQNLGSVESYSEEKAK---KVKCEYEKKLHAMNKElQRLQTAQKEHARLLKNQSQYEKQL 766
Cdd:PTZ00108  1102 EKVEKLNAELEKKEKELEK-LKNTTPKDMWLEDLDKfeeALEEQEEVEEKEIAKE-QRLKSKTKGKASKLRKPKLKKKEK 1179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  767 KKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 846
Cdd:PTZ00108  1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264  847 VRPMSDKVAGKVTRKLSSSE---------SPAPDTGSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGTRKK 913
Cdd:PTZ00108  1260 FSSDDLSKEGKPKNAPKRVSavqysppppSKRPDGESNGGSKPSSPTKKKVKKRLEgSLAALKKKKKSEKKTARKKK 1336
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
671-853 8.67e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  671 IDELENSQKRLQTLKKQYEEKLMMLQHKIrdtqLERDQVLQNlgsvesyseEKAKKVKCEYekklhamNKELQRLQTAQK 750
Cdd:TIGR04523  519 ISSLKEKIEKLESEKKEKESKISDLEDEL----NKDDFELKK---------ENLEKEIDEK-------NKEIEELKQTQK 578
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  751 EharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRKrdhqlrlLEAQKRNQE 830
Cdd:TIGR04523  579 S---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK-------LSSIIKNIK 637
                          170       180
                   ....*....|....*....|...
gi 1039748264  831 VVLRRKTEEVTALRRQVRPMSDK 853
Cdd:TIGR04523  638 SKKNKLKQEVKQIKETIKEIRNK 660
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
380-848 8.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 8.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  380 KNKVMVNQDRASQQINALRSEITRLqmELMEYKTGKRIIDEEGVESINDMFHENAMLQTEnnnlrvrIKAMQETVDALRA 459
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKEL--EEKEERLEELKKKLKELEKRLEELEERHELYEE-------AKAKKEELERLKK 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  460 RITQLVSEQANQVLARAGEGNEEISnmihsyiKEIEDLRAKLLESEAVNENLRKN---LTRATARSPYFSAS-------- 528
Cdd:PRK03918   380 RLTGLTPEKLEKELEELEKAKEEIE-------EEISKITARIGELKKEIKELKKAieeLKKAKGKCPVCGRElteehrke 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  529 --SAFSPTILSSDKETIEIIDLAKKdleklkrkekkKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGVSEKENNE 606
Cdd:PRK03918   453 llEEYTAELKRIEKELKEIEEKERK-----------LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  607 LDVEENQEVSDhedeeeeeedeeeeddiegeessdesdsesdekanyqaDLANITCEIAIKQKLIDELENSQKRLQTLKK 686
Cdd:PRK03918   522 KKAEEYEKLKE--------------------------------------KLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  687 QY---EEKLMMLQHKIRDTQLER-DQVLQNLGSVESYSEE--KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQS 760
Cdd:PRK03918   564 KLdelEEELAELLKELEELGFESvEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264  761 QYEKQLKKLQQ--DVMEMKKTKVRLMKQMKE-EQEKARLTESRRNREiaQLKKDQRKRDHQLRLLEAQKRNQEvVLRRKT 837
Cdd:PRK03918   644 ELRKELEELEKkySEEEYEELREEYLELSRElAGLRAELEELEKRRE--EIKKTLEKLKEELEEREKAKKELE-KLEKAL 720
                          490
                   ....*....|.
gi 1039748264  838 EEVTALRRQVR 848
Cdd:PRK03918   721 ERVEELREKVK 731
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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