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Conserved domains on  [gi|157823761|ref|NP_001102511|]
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kinesin-like protein KIF21A isoform 2 [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 ...
 8-372 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: 623.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   88 GQTGAGKTYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  168 aknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA--- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  248 atdnklisESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   225 --------PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 157823761  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1293-1606 1.23e-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: 1.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1293 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1369
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1370 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1448
Cdd:cd00200    81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1449 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1526
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1527 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1604
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287


                  ..
gi 157823761 1605 WK 1606
Cdd:cd00200   288 WD 289
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 925-1006 7.25e-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: 153.93  E-value: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80


                  ..
gi 157823761 1005 AK 1006
Cdd:cd22263    81 AK 82
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 629-844 3.77e-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: 63.63  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 708
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  709 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 779
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761  780 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 844
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 389-1027 3.95e-10

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.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 64.74  E-value: 3.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARITQLVSEQANQvla 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQ--- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   467 raGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArspyfsassafspTI--LSSDKETIeiIDLAKKD 544
Cdd:pfam05483  281 --DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TIcqLTEEKEAQ--MEELNKA 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   545 LEKLKRKEKKKKKSVAGKDDNADTDQEKKEEkgvSEKENNELDVEENQEVSDhedeeeeeedeeeeddiegeessdeSDS 624
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-------------------------LEE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   625 ESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAK 704
Cdd:pfam05483  396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   705 KVKCEYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRN 781
Cdd:pfam05483  475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESV 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   782 REIAQLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAA 856
Cdd:pfam05483  554 REEFIQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAE 627

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   857 SGEADTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADM 936
Cdd:pfam05483  628 NKQLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK 696

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   937 nRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETL 1012
Cdd:pfam05483  697 -RCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKL 772

                          650
                   ....*....|....*
gi 157823761  1013 DVTAVINACTLTEAR 1027
Cdd:pfam05483  773 KMEAKENTAILKDKK 787
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 8-372 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: 623.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   88 GQTGAGKTYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  168 aknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA--- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  248 atdnklisESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   225 --------PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 157823761  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 4.99e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 4.99e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    88 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   168 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   248 atdnklisesspmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 157823761   327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-378 7.94e-139

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: 432.00  E-value: 7.94e-139
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761      9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761     82 ATVFAYGQTGAGKTYTMGtGFdvnimEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    162 TTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCP 241
Cdd:smart00129  147 PS--------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS 218

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    242 QTDaenatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  219 SSG-------------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278

                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761    322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 6.30e-92

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 310.52  E-value: 6.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   44 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLF 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  123 KSIDEKKTSAiknglpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 202
Cdd:COG5059   126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefetlTAKFHFVDLAGSERLK 282
Cdd:COG5059   190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK-------------NKVSGTSE--------TSKLSLVDLAGSERAA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059   249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 438
Cdd:COG5059   328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823761  439 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059   403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 7-404 7.35e-65

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 243.30  E-value: 7.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    7 ESSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 86
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   87 YGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaIKNGLPPPEFKVNAQFLELYNEEVLDLFDT 162
Cdd:PLN03188  172 YGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDP 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  163 TrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:PLN03188  249 S--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV-------- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  243 tdaenatDNKLISESSPMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK--RATH 320
Cdd:PLN03188  313 -------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRH 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  321 VPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMEL 400
Cdd:PLN03188  384 IPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDEL 462


                  ....
gi 157823761  401 MEYK 404
Cdd:PLN03188  463 QRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1293-1606 1.23e-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: 1.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1293 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1369
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1370 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1448
Cdd:cd00200    81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1449 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1526
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1527 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1604
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287


                  ..
gi 157823761 1605 WK 1606
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1287-1609 6.95e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 174.33  E-value: 6.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1287 RASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------ 1358
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkll 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1359 VSTSY---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLK 1434
Cdd:COG2319   178 ASGSDdgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLA 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1435 RFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFS 1512
Cdd:COG2319   235 TGKLLRTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLAS 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1513 GSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NS 1590
Cdd:COG2319   306 GSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDG 384

                         330
                  ....*....|....*....
gi 157823761 1591 THVFTAADDRTVRIWKAHN 1609
Cdd:COG2319   385 RTLASGSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 925-1006 7.25e-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: 153.93  E-value: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80


                  ..
gi 157823761 1005 AK 1006
Cdd:cd22263    81 AK 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 629-844 3.77e-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: 63.63  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 708
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  709 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 779
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761  780 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 844
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 389-1027 3.95e-10

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: 64.74  E-value: 3.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARITQLVSEQANQvla 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQ--- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   467 raGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArspyfsassafspTI--LSSDKETIeiIDLAKKD 544
Cdd:pfam05483  281 --DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TIcqLTEEKEAQ--MEELNKA 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   545 LEKLKRKEKKKKKSVAGKDDNADTDQEKKEEkgvSEKENNELDVEENQEVSDhedeeeeeedeeeeddiegeessdeSDS 624
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-------------------------LEE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   625 ESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAK 704
Cdd:pfam05483  396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   705 KVKCEYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRN 781
Cdd:pfam05483  475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESV 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   782 REIAQLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAA 856
Cdd:pfam05483  554 REEFIQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAE 627

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   857 SGEADTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADM 936
Cdd:pfam05483  628 NKQLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK 696

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   937 nRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETL 1012
Cdd:pfam05483  697 -RCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKL 772

                          650
                   ....*....|....*
gi 157823761  1013 DVTAVINACTLTEAR 1027
Cdd:pfam05483  773 KMEAKENTAILKDKK 787
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 652-955 1.57e-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: 63.14  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   652 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 731
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   732 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 810
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   811 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPAPdtgSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGT 889
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR---RQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823761   890 RKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 955
Cdd:TIGR00606  921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
629-1012 2.14e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 705
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  706 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 783
Cdd:PRK03918  385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  784 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLrRKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEA 860
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  861 DTSR--------PGTQQKMRIPVARVQALPTPTTNgTRKKYQRKGFT------GRVFTSKTARMKW-------QLLERRV 919
Cdd:PRK03918  540 EIKSlkkeleklEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  920 TDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIVKESGEGDKSVANIIEEMESLTANIDYINDSIAD 994
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698

                         410
                  ....*....|....*...
gi 157823761  995 CQANIMQMEEAKEEGETL 1012
Cdd:PRK03918  699 LKEELEEREKAKKELEKL 716
WD40 pfam00400
WD domain, G-beta repeat;
1292-1327 1.12e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157823761  1292 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1327
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1290-1327 3.65e-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: 3.65e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 157823761   1290 PLQCVHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1327
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 701-827 4.97e-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: 47.22  E-value: 4.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   701 EKAKKVKCEYEKKLHamnkelqrlqtaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 780
Cdd:pfam20492    2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761   781 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 827
Cdd:pfam20492   58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 702-1097 4.01e-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: 48.51  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   702 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 777
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   778 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPApdtgSSAAS 857
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----ELEAQ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   858 GEADTSRPGTQQKMripVARVQALPTPTTNgtrkkyQRKGFTGRVftsKTARMKWQLLERRVTDIIMQkmtISNMEADMN 937
Cdd:TIGR02168  325 LEELESKLDELAEE---LAELEEKLEELKE------ELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   938 RLLRQREELTKRREKLSKRREKIvkesgegDKSVANIIEEMESLTANIDY--INDSIADCQANIMQMEEAKEEGETLDVT 1015
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  1016 AVINACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE- 1085
Cdd:TIGR02168  463 LEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGy 535

                          410
                   ....*....|....*
gi 157823761  1086 ---LDALLGHALQDL 1097
Cdd:TIGR02168  536 eaaIEAALGGRLQAV 550
PTZ00121 PTZ00121
MAEBL; Provisional
 365-1007 2.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  365 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 443
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  444 ETVDALRARITQLVSEQANQV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARSPYFSASS 521
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  522 AFSPTILSSDKETIEIidlAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNEldVEENQEVSDHEDEE 601
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKADELKKA 1413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  602 EEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE--KLMMLQHKIR 679
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAE 1493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  680 DTQLERDQVLQNLGSVESYSE----EKAKKV----KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEK-QLKKLQQ 750
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEakkaEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAE 1573

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  751 DVMEMKKTKVRLMKQMKEE--QEKARLTESRRNREIAQLKK--DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTAlRRQV 826
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEEL 1652

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  827 RPMSDKVAGKvTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVAR-VQALPTPTTNGTRKKYQ-RKGFTGRVFT 904
Cdd:PTZ00121 1653 KKAEEENKIK-AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKAEElKKAEEENKIK 1731

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  905 SKTARMKWQLLERRVTDIIMQkmtisnmEADMNRLLRQREELTKRREKLSKRREKIVKE---------SGEGDKSVANII 975
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedekrRMEVDKKIKDIF 1804

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 157823761  976 EEMESL----TANIDYINDS----------IADCQAniMQMEEAKE 1007
Cdd:PTZ00121 1805 DNFANIieggKEGNLVINDSkemedsaikeVADSKN--MQLEEADA 1848
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
304-513 3.57e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206    96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206   174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  445 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 513
Cdd:COG3206   254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 647-789 1.05e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  647 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 706
Cdd:cd16269   123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  707 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 783
Cdd:cd16269   201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279


                  ....*.
gi 157823761  784 IAQLKK 789
Cdd:cd16269   280 AELLQE 285
 
Name Accession Description Interval E-value
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 8-372 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: 623.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   88 GQTGAGKTYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  168 aknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA--- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  248 atdnklisESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   225 --------PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 157823761  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 4.99e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 4.99e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    88 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   168 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   248 atdnklisesspmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 157823761   327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-378 7.94e-139

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: 432.00  E-value: 7.94e-139
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761      9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761     82 ATVFAYGQTGAGKTYTMGtGFdvnimEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    162 TTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCP 241
Cdd:smart00129  147 PS--------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS 218

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    242 QTDaenatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  219 SSG-------------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278

                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761    322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 9-369 5.62e-122

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: 385.46  E-value: 5.62e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNA 82
Cdd:cd00106     1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   83 TVFAYGQTGAGKTYTMGTGFDvnimeEEQGIISRAVRHLFKSIDEKKTsaiknglPPPEFKVNAQFLELYNEEVLDLFDt 162
Cdd:cd00106    80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRKE-------TKSSFSVSASYLEIYNEKIYDLLS- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  163 trdidaKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRvcPQ 242
Cdd:cd00106   147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN--RE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  243 TDAENATDNKLisesspmnefetltakfHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 322
Cdd:cd00106   219 KSGESVTSSKL-----------------NLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 157823761  323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd00106   280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 9-371 5.03e-106

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: 341.75  E-value: 5.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGY 80
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   81 NATVFAYGQTGAGKTYTMGtGFDVNimEEEQGIISRAVRHLFKSIdeKKTSAIKNglpppeFKVNAQFLELYNEEVldlf 160
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHI--ARSQNNQQ------FLVRVSYLEIYNEEI---- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  161 dttRDIDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 239
Cdd:cd01371   147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  240 cpqtdaenatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 319
Cdd:cd01371   220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157823761  320 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01371   283 HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 10-373 3.83e-102

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: 330.33  E-value: 3.83e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYTQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366     4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   86 AYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01366    83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  165 didAKNKKSNIRiHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtD 244
Cdd:cd01366   149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI---------S 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  245 AENATDNklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 324
Cdd:cd01366   216 GRNLQTG------------EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 157823761  325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 373
Cdd:cd01366   281 NSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 9-371 3.89e-102

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: 331.23  E-value: 3.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYT 66
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAiknglpppEFKVN 145
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKDEK--------EFEVS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  146 AQFLELYNEEVLDLFDTTrdidakNKKSNIRihEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSR 225
Cdd:cd01370   146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  226 SHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 305
Cdd:cd01370   218 SHAVLQITVRQQ-------------DKTASINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823761  306 NVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01370   280 NCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 8-378 2.74e-99

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 323.54  E-value: 2.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYTQC 68
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   69 IEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvnimeEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQF 148
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVSY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  149 LELYNEEVLDLFDTtrdiDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHA 228
Cdd:cd01365   148 MEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  229 IFTIHVCQTRVCPQTDAEnatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVI 308
Cdd:cd01365   224 VFTIVLTQKRHDAETNLT-----------------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVI 286

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823761  309 SALGD-----KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:cd01365   287 SALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 7-371 3.12e-98

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: 319.28  E-value: 3.12e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATV 84
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   85 FAYGQTGAGKTYTMgtgFDVNIMEEEQGIISRAVRHLFKSIdEKKTSAIknglpppEFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01369    81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETI-YSMDENL-------EFHVKVSYFEIYMEKIRDLLDVSK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  165 DidaknkksNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqtd 244
Cdd:cd01369   150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  245 aENATDNKLisesspmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 324
Cdd:cd01369   214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 157823761  325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01369   279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 7-380 3.85e-96

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: 314.26  E-value: 3.85e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFE 78
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   79 GYNATVFAYGQTGAGKTYTMgTGFDVNIME------EEQGIISRAVRHLFKSIDEKKTsaiknglpppEFKVNAQFLELY 152
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTM-EGDRSPNEEytweldPLAGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  153 NEEVLDLFDttrdiDAKNKKSNIRIHEDS--TGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIF 230
Cdd:cd01364   150 NEELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  231 TIHVcqtrvcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 310
Cdd:cd01364   225 SITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITA 286

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  311 LGDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364   287 LVERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 6.30e-92

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 310.52  E-value: 6.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   44 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLF 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  123 KSIDEKKTSAiknglpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 202
Cdd:COG5059   126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefetlTAKFHFVDLAGSERLK 282
Cdd:COG5059   190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK-------------NKVSGTSE--------TSKLSLVDLAGSERAA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059   249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 438
Cdd:COG5059   328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823761  439 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059   403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 10-380 1.33e-91

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: 301.35  E-value: 1.33e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   89 QTGAGKTYTM--GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKTSAIKNglppPEFKVNAQFLELYNEEVLDLFDTTrdi 166
Cdd:cd01373    83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEG----KSFLCKCSFLEIYNEQIYDLLDPA--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  167 daknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdae 246
Cdd:cd01373   156 -----SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC-------------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  247 natdnkLISESSPMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVPYR 324
Cdd:cd01373   217 ------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYR 290

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157823761  325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01373   291 DSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 9-371 4.23e-90

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: 295.78  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATV 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   85 FAYGQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglpppEFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01374    77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDR---------EFLLRVSYLEIYNEKINDLLSPT- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  165 didaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtd 244
Cdd:cd01374   141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI---------- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  245 aenatdnklisESSPMNEFETLTAKF---HFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHV 321
Cdd:cd01374   204 -----------ESSERGELEEGTVRVstlNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHI 271

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 157823761  322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01374   272 PYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 10-369 5.38e-72

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: 243.95  E-value: 5.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNAT 83
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   84 VFAYGQTGAGKTYTMGTGFdvnimeEEQGIISRAVRHLFkSIDEKKTSAiknglpppeFKVNAQFLELYNEEVLDLFDTt 163
Cdd:cd01376    81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLL-QMTRKEAWA---------LSFTMSYLEIYQEKILDLLEP- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  164 rdidaknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqt 243
Cdd:cd01376   144 -------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  244 daenatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 323
Cdd:cd01376   208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 157823761  324 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd01376   274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 10-367 1.52e-70

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: 240.28  E-value: 1.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   10 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYTQCIEKLIEGCFE 78
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   79 GYNATVFAYGQTGAGKTYTMGTGFDVNimEEEQGIISRAVRHLFKSIdekKTSAIKNGLpppefKVNAQFLELYNEEVLD 158
Cdd:cd01367    82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVFRLL---NKLPYKDNL-----GVTVSFFEIYGGKVFD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  159 LFdttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhVCQTR 238
Cdd:cd01367   152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI-ILRDR 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  239 vcpqtdaenatdnklisesspmnEFETLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 317
Cdd:cd01367   222 -----------------------GTNKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157823761  318 aTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 367
Cdd:cd01367   277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 46-369 1.21e-68

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: 234.78  E-value: 1.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   46 DKAFTFDYVFDiDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNImeEEQGIISRAVRHLFKSI 125
Cdd:cd01375    47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENY--KHRGIIPRALQQVFRMI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  126 DEKKTSAIKnglpppefkVNAQFLELYNEEVLDLFDTTRDIDAKNKKsnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCL 205
Cdd:cd01375   123 EERPTKAYT---------VHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  206 KLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375   192 FLGETNRIIASHTMNKNSSRSHCIFTIH-------------------LEAHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  286 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375   253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330


                  ....
gi 157823761  366 NRAR 369
Cdd:cd01375   331 SRVK 334
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 10-365 1.01e-65

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: 226.89  E-value: 1.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYTQCIEKLIE 74
Cdd:cd01368     3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   75 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIdekktsaiknglppPEFKVNAQFLELYN 153
Cdd:cd01368    83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  154 EEVLDLFDTTRDIDAKNKKSnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 233
Cdd:cd01368   142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  234 VCQTRVCPQTDAENATDNKLISESSpmnefetltakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368   221 LVQAPGDSDGDVDQDKDQITVSQLS-------------LVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157823761  314 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368   288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 7-404 7.35e-65

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 243.30  E-value: 7.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761    7 ESSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 86
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   87 YGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaIKNGLPPPEFKVNAQFLELYNEEVLDLFDT 162
Cdd:PLN03188  172 YGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDP 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  163 TrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:PLN03188  249 S--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV-------- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  243 tdaenatDNKLISESSPMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK--RATH 320
Cdd:PLN03188  313 -------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRH 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  321 VPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMEL 400
Cdd:PLN03188  384 IPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDEL 462


                  ....
gi 157823761  401 MEYK 404
Cdd:PLN03188  463 QRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1293-1606 1.23e-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: 1.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1293 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1369
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1370 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1448
Cdd:cd00200    81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1449 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1526
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1527 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1604
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287


                  ..
gi 157823761 1605 WK 1606
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1287-1609 6.95e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 174.33  E-value: 6.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1287 RASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------ 1358
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkll 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1359 VSTSY---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLK 1434
Cdd:COG2319   178 ASGSDdgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLA 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1435 RFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFS 1512
Cdd:COG2319   235 TGKLLRTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLAS 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1513 GSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NS 1590
Cdd:COG2319   306 GSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDG 384

                         330
                  ....*....|....*....
gi 157823761 1591 THVFTAADDRTVRIWKAHN 1609
Cdd:COG2319   385 RTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
1286-1618 6.65e-44

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 165.47  E-value: 6.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1286 VRASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT----- 1358
Cdd:COG2319    63 LDAAAGALLATLLGHTAAVLSVAFSPDgrLLASASADGTVRLWDLATGLLLRTLTGHTGAV--------RSVAFSpdgkt 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1359 -VSTSY---IKVWDIrESAKCIRTLTssgqvtlgeacsastsrtvaipSGESQINQIALNPTGTFLYAASG-NAVRMWDL 1433
Cdd:COG2319   135 lASGSAdgtVRLWDL-ATGKLLRTLT----------------------GHSGAVTSVAFSPDGKLLASGSDdGTVRLWDL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1434 KRFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LF 1511
Cdd:COG2319   192 ATGKLLRTLTGHTGAVRSVAFS--PDGK-LLASGSADGTVRLWDLATGKLLRTLTGHS------GSVRSVAFSPDGrlLA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1512 SGSRDNGIKKWDLaQKGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--N 1589
Cdd:COG2319   263 SGSADGTVRLWDL-ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspD 341

                         330       340
                  ....*....|....*....|....*....
gi 157823761 1590 STHVFTAADDRTVRIWkahNLQDGQLSDT 1618
Cdd:COG2319   342 GKTLASGSDDGTVRLW---DLATGELLRT 367
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 925-1006 7.25e-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: 153.93  E-value: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80


                  ..
gi 157823761 1005 AK 1006
Cdd:cd22263    81 AK 82
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1292-1523 1.28e-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: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1292 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1368
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1369 IReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1447
Cdd:cd00200   164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823761 1448 PVMCLTVdqiSNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LFSGSRDNGIKKWD 1523
Cdd:cd00200   221 GVNSVAF---SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT------NSVTSLAWSPDGkrLASGSADGTIRIWD 289
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
 925-1006 1.94e-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: 109.60  E-value: 1.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKEsGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22248     1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDE-GKDESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79


                  ..
gi 157823761 1005 AK 1006
Cdd:cd22248    80 SK 81
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
 925-1006 3.28e-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: 109.13  E-value: 3.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22262     1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80


                  ..
gi 157823761 1005 AK 1006
Cdd:cd22262    81 TK 82
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 9-159 1.76e-20

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 89.20  E-value: 1.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761     9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYtQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796   21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823761    89 QTGAGKTYTMgtgfdvnimeeeqgiISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDL 159
Cdd:pfam16796   96 QTGSGSNDGM---------------IPRAREQIFRFISSLKKG--------WKYTIELQFVEIYNESSQDL 143
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1291-1432 3.02e-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: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1291 LQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1367
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823761 1368 DIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWD 1432
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 ...
 12-310 6.81e-14

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 71.22  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYTQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   91 GAGKTYTMgtgfdvnimeeeQGIISRAVRHLFKSIDEKKTSAiknglpppefkvnaqflelyneevldlfdttrdidakn 170
Cdd:cd01363    62 GAGKTETM------------KGVIPYLASVAFNGINKGETEG-------------------------------------- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  171 kksnirihedstggiyTVGVTTRTVNTEPEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenatd 250
Cdd:cd01363    92 ----------------WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  251 nklisesspmnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 310
Cdd:cd01363   137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
WD40 COG2319
WD40 repeat [General function prediction only];
1502-1618 1.04e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.78  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761 1502 ALAIQGDNLFSGSRDNGIKKWDLAQKGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDS 1581
Cdd:COG2319    43 AASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 157823761 1582 PINAICV--NSTHVFTAADDRTVRIWkahNLQDGQLSDT 1618
Cdd:COG2319   122 AVRSVAFspDGKTLASGSADGTVRLW---DLATGKLLRT 157
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 629-844 3.77e-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: 63.63  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 708
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  709 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 779
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761  780 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 844
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 389-1027 3.95e-10

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: 64.74  E-value: 3.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARITQLVSEQANQvla 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQ--- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   467 raGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArspyfsassafspTI--LSSDKETIeiIDLAKKD 544
Cdd:pfam05483  281 --DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TIcqLTEEKEAQ--MEELNKA 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   545 LEKLKRKEKKKKKSVAGKDDNADTDQEKKEEkgvSEKENNELDVEENQEVSDhedeeeeeedeeeeddiegeessdeSDS 624
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-------------------------LEE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   625 ESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAK 704
Cdd:pfam05483  396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   705 KVKCEYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRN 781
Cdd:pfam05483  475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESV 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   782 REIAQLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAA 856
Cdd:pfam05483  554 REEFIQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAE 627

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   857 SGEADTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADM 936
Cdd:pfam05483  628 NKQLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK 696

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   937 nRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETL 1012
Cdd:pfam05483  697 -RCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKL 772

                          650
                   ....*....|....*
gi 157823761  1013 DVTAVINACTLTEAR 1027
Cdd:pfam05483  773 KMEAKENTAILKDKK 787
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 652-955 1.57e-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: 63.14  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   652 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 731
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   732 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 810
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   811 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPAPdtgSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGT 889
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR---RQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823761   890 RKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 955
Cdd:TIGR00606  921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
629-1012 2.14e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 705
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  706 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 783
Cdd:PRK03918  385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  784 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLrRKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEA 860
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  861 DTSR--------PGTQQKMRIPVARVQALPTPTTNgTRKKYQRKGFT------GRVFTSKTARMKW-------QLLERRV 919
Cdd:PRK03918  540 EIKSlkkeleklEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  920 TDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIVKESGEGDKSVANIIEEMESLTANIDYINDSIAD 994
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698

                         410
                  ....*....|....*...
gi 157823761  995 CQANIMQMEEAKEEGETL 1012
Cdd:PRK03918  699 LKEELEEREKAKKELEKL 716
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 634-1020 1.24e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   634 ADLANITCEIAIKQKLIDELENSQKRLQTlkkqyeeklmmlqhkirdtqlERDQvlqnlgsVESYSEEKAKKVKCEYEKK 713
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRR---------------------EREK-------AERYQALLKEKREYEGYEL 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   714 LHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE--EQEKARLTESRRN--REIAQLKK 789
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGEleAEIASLER 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   790 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSEspapdtgssaasgeadtsrpgtqQ 869
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELK-----------------------E 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   870 KMRIPVARVQALPTP--TTNGTRKKYQRK--GFTGRVFTSKTARMKWQLLERRVTdiimqkMTISNMEADMNRLLRQREE 945
Cdd:TIGR02169  365 ELEDLRAELEEVDKEfaETRDELKDYREKleKLKREINELKRELDRLQEELQRLS------EELADLNAAIAGIEAKINE 438

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   946 LTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK-----EEGETLDVTAVINA 1020
Cdd:TIGR02169  439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 629-869 3.03e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.45  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 703
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  704 KKvkceyekkLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 783
Cdd:COG3883   112 ES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  784 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTS 863
Cdd:COG3883   184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263


                  ....*.
gi 157823761  864 RPGTQQ 869
Cdd:COG3883   264 AAGAAA 269
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 631-834 5.44e-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: 5.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   631 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVK 707
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   708 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 781
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761   782 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 834
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 569-835 6.72e-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: 54.29  E-value: 6.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   569 DQEKKEEKGVS-------EKENNELDVEENQEVSDHEDeeeeEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 641
Cdd:TIGR02168  220 AELRELELALLvlrleelREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNkel 721
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELE--- 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   722 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---REIAQLKKDQRK 793
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAELEELEEELEE 451

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 157823761   794 RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 835
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 364-825 9.62e-07

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: 53.67  E-value: 9.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   438 RIKAMQETVDALRARITQLVSEQANQvlaragegNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   508 trataRSPYFSASSAFSPTILSSDKETieiidLAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEK--------GVS 579
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKekvsalqpELT 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   580 EKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENSQKR 659
Cdd:pfam10174  493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVARYK 571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   660 LQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSeekAKKVKCEYEK--KLHAMNKELQRLQTAQKEHARLLK 736
Cdd:pfam10174  572 EESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLT---LRQMKEQNKKvaNIKHGQQEMKKKGAQLLEEARRRE 645

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   737 NQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEVV 811
Cdd:pfam10174  646 DNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEAL 714

                          490       500       510
                   ....*....|....*....|....*....|....
gi 157823761   812 L------------------RRKT--EEVTALRRQ 825
Cdd:pfam10174  715 LaaisekdaniallelsssKKKKtqEEVMALKRE 748
WD40 pfam00400
WD domain, G-beta repeat;
1292-1327 1.12e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157823761  1292 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1327
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1290-1327 3.65e-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: 3.65e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 157823761   1290 PLQCVHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1327
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
642-1006 3.66e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  642 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKE 720
Cdd:PRK03918  148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREIN-EISSELPELREE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  721 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNR--EIAQLKKDQRKRDHQL 798
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFY 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  799 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA--GKVTRKLSssespapdtgssaasgeadtsrpgtqqkmripva 876
Cdd:PRK03918  303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErlEELKKKLK---------------------------------- 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  877 rvqalptpttnGTRKKYQRkgFTGRVftsktarmkwQLLERrvtdiIMQKMTisnmeadmnrllrQREELTKRREKLSKr 956
Cdd:PRK03918  349 -----------ELEKRLEE--LEERH----------ELYEE-----AKAKKE-------------ELERLKKRLTGLTP- 386

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 157823761  957 rEKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK 1006
Cdd:PRK03918  387 -EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 349-956 3.73e-06

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: 52.04  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   349 SPSDRDFMETL-NTLKYANRARNIKNKVMVNqdrASQQINALRSEITRLQMELMEYKT---------GKRIIDEEGVES- 417
Cdd:pfam15921  137 SQSQEDLRNQLqNTVHELEAAKCLKEDMLED---SNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasGKKIYEHDSMSTm 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   418 --------INDMFHEnamLQTENNNLRVRIKAMQETVDALRA---------------RITQLVSEQANQV--LARAGEGN 472
Cdd:pfam15921  214 hfrslgsaISKILRE---LDTEISYLKGRIFPVEDQLEALKSesqnkielllqqhqdRIEQLISEHEVEItgLTEKASSA 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   473 EEISNMIHSYIKeiedlrakLLESEAVNEN---LRK----NLTRATARSPYFSASSAFSPTILSSDKETIeiidLAKKDL 545
Cdd:pfam15921  291 RSQANSIQSQLE--------IIQEQARNQNsmyMRQlsdlESTVSQLRSELREAKRMYEDKIEELEKQLV----LANSEL 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   546 EKLKRKEKKKKKSVAGKDDNAD---TDQEKKEEKGVSEKENNE--LDVEENQEVS-DHEDEEEEEEDEEEEDDIEGEESS 619
Cdd:pfam15921  359 TEARTERDQFSQESGNLDDQLQkllADLHKREKELSLEKEQNKrlWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAM 438

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   620 desdsesdeKANYQADLANITCEIAIKQK-------LIDELENSQKRLQTLKKQYEEKLMMLQHKIRdtqlerdqVLQNL 692
Cdd:pfam15921  439 ---------KSECQGQMERQMAAIQGKNEslekvssLTAQLESTKEMLRKVVEELTAKKMTLESSER--------TVSDL 501

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   693 GSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEK-QLKKLQQD-VMEMKKTKVRLMKQMKEEQ 770
Cdd:pfam15921  502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDkVIEILRQQIENMTQLVGQH 581

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   771 ---------EKARLTESRRNR--EIAQLKKDQRKRDHQLRLLEA---------------------------QKRNQ---E 809
Cdd:pfam15921  582 grtagamqvEKAQLEKEINDRrlELQEFKILKDKKDAKIRELEArvsdlelekvklvnagserlravkdikQERDQllnE 661

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   810 VVLRRK-----TEEVTALRRQVRPMSDKV---AGKVTRKLSSSESPAPDTGSS-----AASGEADTSRPGTQQKMRIPVA 876
Cdd:pfam15921  662 VKTSRNelnslSEDYEVLKRNFRNKSEEMettTNKLKMQLKSAQSELEQTRNTlksmeGSDGHAMKVAMGMQKQITAKRG 741

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   877 RVQALPT-------PTTNGTRKKY----QRKGFTGRVFTSKTARMKW----QLL---ERRVtdiimqKMTISNMEADMNR 938
Cdd:pfam15921  742 QIDALQSkiqfleeAMTNANKEKHflkeEKNKLSQELSTVATEKNKMagelEVLrsqERRL------KEKVANMEVALDK 815

                          730       740
                   ....*....|....*....|.
gi 157823761   939 LLRQREE---LTKRREKLSKR 956
Cdd:pfam15921  816 ASLQFAEcqdIIQRQEQESVR 836
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 701-827 4.97e-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: 47.22  E-value: 4.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   701 EKAKKVKCEYEKKLHamnkelqrlqtaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 780
Cdd:pfam20492    2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761   781 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 827
Cdd:pfam20492   58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 562-861 7.03e-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: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  562 KDDNADTDQEKKEEkgvsEKENNELDVEENQevsdhedeeeeeeDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 641
Cdd:COG1196   233 KLRELEAELEELEA----ELEELEAELEELE-------------AELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKEL 721
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  722 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLL 801
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  802 EAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEAD 861
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 633-827 7.14e-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: 7.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   633 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRD-TQLERDQVLQNLGSvesySEEKAKKVKCEYE 711
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA----ELSKLEEEVSRIE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   712 KKLHAMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 787
Cdd:TIGR02169  812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 157823761   788 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 827
Cdd:TIGR02169  888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1569-1606 1.14e-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: 1.14e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 157823761   1569 TFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIWK 1606
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 650-804 1.49e-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: 48.00  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  650 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAM--NKELQRLQta 727
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYEALQ-- 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761  728 qKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 804
Cdd:COG1579    96 -KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 646-815 1.70e-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: 48.76  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   646 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVKCEYEKKLhAMNKELQRLQ 725
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKA-RQRQELQQAR 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   726 TAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 802
Cdd:pfam13868  242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316

                          170
                   ....*....|...
gi 157823761   803 AQKRNQEVVLRRK 815
Cdd:pfam13868  317 GERLREEEAERRE 329
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
648-834 2.27e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  648 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQR---- 723
Cdd:COG4372     3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEELEQARSELEQleee 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  724 -------LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRK 793
Cdd:COG4372    82 leelneqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLES 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157823761  794 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQVRPMSDKVA 834
Cdd:COG4372   162 LQEELAALEQELQALS--EAEAEQALDELLKEANRNAEKEE 200
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
700-845 3.31e-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: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  700 EEKAKKVKCEYEKKLHAMNKELQRLQtaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKtKVRLMKQmkEEQEKARLTE-- 777
Cdd:COG2433   394 EPEAEREKEHEERELTEEEEEIRRLE---EQVERLEAEVEELEAELEEKDERIERLER-ELSEARS--EERREIRKDRei 467

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823761  778 SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 845
Cdd:COG2433   468 SRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKFTKEA 523
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 702-1097 4.01e-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: 48.51  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   702 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 777
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   778 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPApdtgSSAAS 857
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----ELEAQ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   858 GEADTSRPGTQQKMripVARVQALPTPTTNgtrkkyQRKGFTGRVftsKTARMKWQLLERRVTDIIMQkmtISNMEADMN 937
Cdd:TIGR02168  325 LEELESKLDELAEE---LAELEEKLEELKE------ELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   938 RLLRQREELTKRREKLSKRREKIvkesgegDKSVANIIEEMESLTANIDY--INDSIADCQANIMQMEEAKEEGETLDVT 1015
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  1016 AVINACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE- 1085
Cdd:TIGR02168  463 LEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGy 535

                          410
                   ....*....|....*
gi 157823761  1086 ---LDALLGHALQDL 1097
Cdd:TIGR02168  536 eaaIEAALGGRLQAV 550
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 658-810 4.04e-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: 47.28  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   658 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVKCEYEKKlHAMNKELQRL 724
Cdd:pfam02841  155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   725 QTAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 803
Cdd:pfam02841  224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286


                   ....*..
gi 157823761   804 QKRNQEV 810
Cdd:pfam02841  287 ESLQKEI 293
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 646-818 4.54e-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: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   646 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHKIR--------DTQLERDQVLQNLGSVESYSEEKAKKVK 707
Cdd:pfam17380  305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAMERERelerirqeERKRELERIRQEEIAMEISRMRELERLQ 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   708 CEYEKKLHAMNKELQ---RLQTAQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNRE 783
Cdd:pfam17380  385 MERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQ 461

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 157823761   784 IAQLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEE 818
Cdd:pfam17380  462 VERLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILE 498
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 665-818 5.51e-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: 47.22  E-value: 5.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   665 KQYEEKLMMLQ-HKIRDTQLERDQVLQNLgsVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQyEK 743
Cdd:pfam13868    9 RELNSKLLAAKcNKERDAQIAEKKRIKAE--EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-ER 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823761   744 QLKKlQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEE 818
Cdd:pfam13868   86 EQKR-QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159
WD40 pfam00400
WD domain, G-beta repeat;
1570-1605 6.76e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 6.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157823761  1570 FVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIW 1605
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
643-859 7.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  643 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLGSVESYSEEKAkkvkcEYEKKLHAMNKELQ 722
Cdd:COG4913   612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  723 RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 799
Cdd:COG4913   679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823761  800 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGE 859
Cdd:COG4913   755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 632-1033 9.23e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.74  E-value: 9.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   632 YQADLANITCEIA--IKQKLIDELENSQKrLQTLKKQYEEKLMMLQHkirdtqLERDQVLQNLGSVESySEEKAKKVKCE 709
Cdd:TIGR01612  669 YEDDIDALYNELSsiVKENAIDNTEDKAK-LDDLKSKIDKEYDKIQN------METATVELHLSNIEN-KKNELLDIIVE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   710 YEKKLHA-----MNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNR 782
Cdd:TIGR01612  741 IKKHIHGeinkdLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNhyNDQINIDNIKDEDAKQNYDKSKEYI 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   783 EIAQLKKDQ-RKRDHQLRLLEAQ---KRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVT-RKLSSSESPAPDTGS--- 853
Cdd:TIGR01612  821 KTISIKEDEiFKIINEMKFMKDDflnKVDKFINFENNcKEKIDSEHEQFAELTNKIKAEISdDKLNDYEKKFNDSKSlin 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   854 -SAASGEADTSRPGTQQKmripVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMK-WQLLERRVT----------- 920
Cdd:TIGR01612  901 eINKSIEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKeSNLIEKSYKdkfdntlidki 976

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   921 ---DIIMQKMTISNMEADMNRLLRQREELtkrREKLSKRREKIV-KESGEGDKSVANIIEEMESLTANIDYINDSIADCQ 996
Cdd:TIGR01612  977 nelDKAFKDASLNDYEAKNNELIKYFNDL---KANLGKNKENMLyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI 1053

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 157823761   997 ANIMQmEEAKEEGETLDvtaVINACTLTEARYLLDHF 1033
Cdd:TIGR01612 1054 YNIID-EIEKEIGKNIE---LLNKEILEEAEINITNF 1086
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 645-817 1.10e-04

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: 45.14  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   645 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSeekakKVKCEYEKKLHAMNKELQRL 724
Cdd:pfam14988   23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFA-----KLKESQEREIQDLEEEKEKV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   725 Q-----TAQKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 794
Cdd:pfam14988   98 RaetaeKDREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175

                          170       180
                   ....*....|....*....|...
gi 157823761   795 DHQLRLLEAQKRNQEvvlRRKTE 817
Cdd:pfam14988  176 IQETQALEAIKSKLE---NRKQR 195
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 672-815 1.47e-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: 45.08  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   672 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKvKCEYEKKLhaMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQD 751
Cdd:pfam13904   38 LTYARKLEGLKLER-------QPLEAYENWLAAK-QRQRQKEL--QAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823761   752 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 815
Cdd:pfam13904  108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
642-815 1.86e-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: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV-LQNLGSVEsyseekakkvkceyekklhamnke 720
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLE------------------------ 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  721 lQRLQTAQKEHARLLKNQSQYEKQLKKL-------QQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRK 793
Cdd:COG4913   345 -REIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423

                         170       180
                  ....*....|....*....|....
gi 157823761  794 RDHQLRLLEAQKRN--QEVVLRRK 815
Cdd:COG4913   424 LEAEIASLERRKSNipARLLALRD 447
PTZ00121 PTZ00121
MAEBL; Provisional
 365-1007 2.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  365 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 443
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  444 ETVDALRARITQLVSEQANQV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARSPYFSASS 521
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  522 AFSPTILSSDKETIEIidlAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNEldVEENQEVSDHEDEE 601
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKADELKKA 1413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  602 EEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE--KLMMLQHKIR 679
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAE 1493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  680 DTQLERDQVLQNLGSVESYSE----EKAKKV----KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEK-QLKKLQQ 750
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEakkaEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAE 1573

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  751 DVMEMKKTKVRLMKQMKEE--QEKARLTESRRNREIAQLKK--DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTAlRRQV 826
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEEL 1652

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  827 RPMSDKVAGKvTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVAR-VQALPTPTTNGTRKKYQ-RKGFTGRVFT 904
Cdd:PTZ00121 1653 KKAEEENKIK-AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKAEElKKAEEENKIK 1731

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  905 SKTARMKWQLLERRVTDIIMQkmtisnmEADMNRLLRQREELTKRREKLSKRREKIVKE---------SGEGDKSVANII 975
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedekrRMEVDKKIKDIF 1804

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 157823761  976 EEMESL----TANIDYINDS----------IADCQAniMQMEEAKE 1007
Cdd:PTZ00121 1805 DNFANIieggKEGNLVINDSkemedsaikeVADSKN--MQLEEADA 1848
PRK12704 PRK12704
phosphodiesterase; Provisional
 675-818 2.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  675 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQY----E 742
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823761  743 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 818
Cdd:PRK12704  110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
712-832 3.52e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  712 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 789
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157823761  790 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 832
Cdd:COG4717   151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
304-513 3.57e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206    96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206   174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  445 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 513
Cdd:COG3206   254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 646-827 4.08e-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: 44.52  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   646 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 725
Cdd:pfam13868  125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   726 TAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 798
Cdd:pfam13868  198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276

                          170       180
                   ....*....|....*....|....*....
gi 157823761   799 RLLEAQKRNQevvlrRKTEEVTALRRQVR 827
Cdd:pfam13868  277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
633-777 5.12e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  633 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 703
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823761  704 KKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTE 777
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 632-819 5.39e-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: 45.06  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   632 YQADLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAk 704
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELA- 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   705 kvkcEYEKKLHAMNKELQRLQTAQKEHARLLKNQsqyEKQLKKLQQDVmemkktkvrlmkqMKEEQEKARLTEsrrnrEI 784
Cdd:TIGR02169  424 ----DLNAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADL-------------SKYEQELYDLKE-----EY 478

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 157823761   785 AQLKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 819
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 688-825 6.33e-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: 44.17  E-value: 6.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   688 VLQNLGSVESYSEEKAKKVKCEyekKLHAMNKELQRLQTAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 763
Cdd:pfam15709  305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823761   764 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 825
Cdd:pfam15709  380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 641-809 7.40e-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: 43.90  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   641 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVKCEYEKKL 714
Cdd:pfam15742   54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   715 hamnkELQRlqtaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 781
Cdd:pfam15742  132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202

                          170       180       190
                   ....*....|....*....|....*....|..
gi 157823761   782 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 809
Cdd:pfam15742  203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 647-821 7.58e-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: 43.91  E-value: 7.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   647 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQT 726
Cdd:pfam05622  310 QQLLEDANRRKNELETQNRLANQRILELQQQVEELQKA----LQEQGSKAEDSSLLKQKLE-EHLEKLHEAQSELQKKKE 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   727 AQKEHARllKNQSQYEKQLKKLQqdvmEMKKTKVRLMKQMKEEQ----EKARLT----ESRRNR----EIAQLKKDQRKR 794
Cdd:pfam05622  385 QIEELEP--KQDSNLAQKIDELQ----EALRKKDEDMKAMEERYkkyvEKAKSViktlDPKQNPasppEIQALKNQLLEK 458

                          170       180       190
                   ....*....|....*....|....*....|
gi 157823761   795 DHQLRLLEAQKrnQEVVLRRKTEE---VTA 821
Cdd:pfam05622  459 DKKIEHLERDF--EKSKLQREQEEkliVTA 486
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 367-846 8.01e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   367 RARNIKNKVMVNQDRAS-----------------QQINALRSEITRLQMELMEyktgkriIDEEGVESINDMFHENAMLQ 429
Cdd:TIGR04523   83 QIKDLNDKLKKNKDKINklnsdlskinseikndkEQKNKLEVELNKLEKQKKE-------NKKNIDKFLTEIKKKEKELE 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   430 TENNNLRVRIKAMQETVDALRARITQLVSEQANQVLARAGEGNEE--ISNmIHSYIKEIEDLRAKLLESEAVNENLRKNL 507
Cdd:TIGR04523  156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEllLSN-LKKKIQKNKSLESQISELKKQNNQLKDNI 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   508 TRATarspyfSASSAFSPTILSSDKETIEIIDLAKKDLeklkrkekkkkksvagKDDNADTDQEKKEEKGVSEKENN--- 584
Cdd:TIGR04523  235 EKKQ------QEINEKTTEISNTQTQLNQLKDEQNKIK----------------KQLSEKQKELEQNNKKIKELEKQlnq 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   585 ---ELDVEENQEVSDHEDEEEEEEdeeeeddiegeessdesdsesdekANYQADLANITCEIAIKQKLIDELENSQKRL- 660
Cdd:TIGR04523  293 lksEISDLNNQKEQDWNKELKSEL------------------------KNQEKKLEEIQNQISQNNKIISQLNEQISQLk 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   661 ----------QTLKKQYEEKlmmlQHKIRDTQLERDQVLQNLGSVESYSE------EKAKKVKCEYEKKLHAMNKELQRL 724
Cdd:TIGR04523  349 keltnsesenSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINdleskiQNQEKLNQQKDEQIKKLQQEKELL 424

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   725 qtaQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKarltesrrnrEIAQLKKDQRKRDHQLrlleaQ 804
Cdd:TIGR04523  425 ---EKEIERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNTRESLET----------QLKVLSRSINKIKQNL-----E 485

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 157823761   805 KRNQEvvLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSES 846
Cdd:TIGR04523  486 QKQKE--LKSKEKELKKLNEEKKELEEKVK-DLTKKISSLKE 524
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
642-827 9.42e-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: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  642 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE 711
Cdd:COG4913   669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  712 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 788
Cdd:COG4913   749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 157823761  789 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 827
Cdd:COG4913   822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 647-789 1.05e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  647 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 706
Cdd:cd16269   123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  707 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 783
Cdd:cd16269   201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279


                  ....*.
gi 157823761  784 IAQLKK 789
Cdd:cd16269   280 AELLQE 285
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 640-804 1.07e-03

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: 41.81  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   640 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVKCEY--- 710
Cdd:pfam15619   17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   711 EKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 790
Cdd:pfam15619   87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164

                          170
                   ....*....|....
gi 157823761   791 QRKRDHQLRLLEAQ 804
Cdd:pfam15619  165 HKEAQEEVKILQEE 178
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 686-821 1.19e-03

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: 41.82  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   686 DQVLQNLGSVESYSEEKA--KKVKCEYEKKLHAMNKELQR----LQTAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 759
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823761   760 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 821
Cdd:pfam13851   92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 657-821 1.45e-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: 43.02  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   657 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVKCEYEKKLHAMNKELQRLQ-TAQKEHARL 734
Cdd:pfam15709  360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   735 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 814
Cdd:pfam15709  424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498


                   ....*..
gi 157823761   815 KTEEVTA 821
Cdd:pfam15709  499 QKEEEAA 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
659-827 1.46e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  659 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 738
Cdd:COG4913   226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  739 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 816
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379

                         170
                  ....*....|.
gi 157823761  817 EEVTALRRQVR 827
Cdd:COG4913   380 EEFAALRAEAA 390
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 724-850 1.54e-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: 42.96  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   724 LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEA 803
Cdd:pfam07888  310 QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157823761   804 QKrnQEV-----VLRRKTEEVTALRRQVRPMSDKvaGKVTRKLSSSESPAPD 850
Cdd:pfam07888  386 EK--QELleyirQLEQRLETVADAKWSEAALTST--ERPDSPLSDSEDENPE 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-730 1.56e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   446 VDALRARItqlvsEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARspyfsassafsp 525
Cdd:TIGR02168  735 LARLEAEV-----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE------------ 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   526 tiLSSDKETIEiidlAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNELDVEE-NQEVSDhedeeeee 604
Cdd:TIGR02168  798 --LKALREALD----ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlAAEIEE-------- 863

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   605 edeeeeDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLE 684
Cdd:TIGR02168  864 ------LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 157823761   685 RDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKE 730
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 643-826 1.60e-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: 42.60  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   643 IAIKQKLIDELENSQKRL-QTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAKKVKCEYEKKL---HAMN 718
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLdEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEKLqerEQMD 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   719 KELQRLQTAQKEharllknqsQYEKQLKK---LQQDVMEMKKTKVRLMKQMKEEQEKarltESRRNREiAQLKKDQRKrd 795
Cdd:pfam13868  105 EIVERIQEEDQA---------EAEEKLEKqrqLREEIDEFNEEQAEWKELEKEEERE----EDERILE-YLKEKAERE-- 168

                          170       180       190
                   ....*....|....*....|....*....|.
gi 157823761   796 hqlrllEAQKRNQEVVLRRKTEEVTALRRQV 826
Cdd:pfam13868  169 ------EEREAEREEIEEEKEREIARLRAQQ 193
WD40 pfam00400
WD domain, G-beta repeat;
1436-1477 1.62e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 1.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 157823761  1436 FQSTGKLTGHLGPVMCLTvdqISNGQDLIITGSKDHYIKMFD 1477
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
46 PHA02562
endonuclease subunit; Provisional
 638-840 1.71e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  638 NITCEIAIKQKLIDELENSQK-RLQTLKKQYEEKL-MMLQHKIRDTQLErDQVLQNLGSVESYSEEKAK--------KVK 707
Cdd:PHA02562  192 HIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVeEAKTIKAEIEELT-DELLNLVMDIEDPSAALNKlntaaakiKSK 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  708 CEYEKKLHAMNKE-------LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEkarltesrR 780
Cdd:PHA02562  271 IEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE--------L 342

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  781 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRK 840
Cdd:PHA02562  343 KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 645-870 1.81e-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: 42.74  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   645 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDtqlERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLHAMNKEL 721
Cdd:pfam04747   12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSIND---QRKEAFASLELTEQPQQvEKVKKSEKKKAQKQIAKDHEA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   722 QRLQTAQKEHArllKNQSQYEKQLKKlqqdvmemKKTKVRLMKQMKEEQEKarltesrrnreiaqLKKDQRKRDHQLRLL 801
Cdd:pfam04747   89 EQKVNAKKAAE---KEARRAEAEAKK--------RAAQEEEHKQWKAEQER--------------IQKEQEKKEADLKKL 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823761   802 EAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQK 870
Cdd:pfam04747  144 QAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKK 215
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 699-806 1.82e-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: 40.83  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   699 SEEKAK------KVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 772
Cdd:pfam11600   10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 157823761   773 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 806
Cdd:pfam11600   83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 713-827 1.99e-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: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  713 KLHAMNKELQRLQTAQKEH----ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-----ARLTESRRNR- 782
Cdd:COG1579    11 DLQELDSELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVRNNKe 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157823761  783 ------EIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 827
Cdd:COG1579    91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 642-808 2.02e-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: 42.70  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKEL 721
Cdd:TIGR04523  413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   722 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkvrlmKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLR-- 799
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKVKDLTKKI-----------SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKke 557


                   ....*....
gi 157823761   800 LLEAQKRNQ 808
Cdd:TIGR04523  558 NLEKEIDEK 566
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 651-784 2.36e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  651 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVKCEYEKKLHAMNKELQ-RLQTAQK 729
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761  730 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 784
Cdd:PRK00409  585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 651-794 2.48e-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: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   651 DELENsQKRLQTLKKQYEEKLmmlQHKIRDTQLERDQVL---QNLGSVESYSEEKAKKVkCEYEKKLHAMNKELQRLQTA 727
Cdd:pfam17380  454 EEQER-QQQVERLRQQEEERK---RKKLELEKEKRDRKRaeeQRRKILEKELEERKQAM-IEEERKRKLLEKEMEERQKA 528

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823761   728 QKEHARLLKNQSQYEKQLKklqqdvMEMKKtkvRLMKQM-KEEQEKARLTESRRNREIA-QLKKDQRKR 794
Cdd:pfam17380  529 IYEEERRREAEEERRKQQE------MEERR---RIQEQMrKATEERSRLEAMEREREMMrQIVESEKAR 588
Rabaptin pfam03528
Rabaptin;
646-805 2.48e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 42.40  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   646 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSE----EKAKKVKC 708
Cdd:pfam03528   24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSEntkqEAIDEVKS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   709 EYEKK---LHAMNKELQRLQTAQKeHARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQEKA 773
Cdd:pfam03528  101 QWQEEvasLQAIMKETVREYEVQF-HRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAEKL 176

                          170       180       190
                   ....*....|....*....|....*....|..
gi 157823761   774 RLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 805
Cdd:pfam03528  177 RSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 660-826 2.51e-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: 41.18  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   660 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEKAKKVKCE-----YEK-KLHAMNK-ELQRLQTAQKEha 732
Cdd:pfam15665   16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKRRIQTLEesleqHERmKRQALTEfEQYKRRVEERE-- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   733 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 798
Cdd:pfam15665   88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164

                          170       180
                   ....*....|....*....|....*....
gi 157823761   799 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 826
Cdd:pfam15665  165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
651-825 2.67e-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: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  651 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVES-YSEEKAKKVkcEYEKKLHAMNKELQRLQTAQK 729
Cdd:COG3206   189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESqLAEARAELA--EAEARLAALRAQLGSGPDALP 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  730 EH------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRK 793
Cdd:COG3206   258 ELlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQL 336

                         170       180       190
                  ....*....|....*....|....*....|..
gi 157823761  794 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 825
Cdd:COG3206   337 AQLEARLAELPELEAE--LRRLEREVEVAREL 366
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 629-759 2.68e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  629 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEE 701
Cdd:PRK00409  508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEA-------EK 573

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823761  702 KAKKV----KCEYEKKLHAMNKELQRLQTAQKEHaRLLKNQSQYEKQLKKLQQDVMEMKKTK 759
Cdd:PRK00409  574 EAQQAikeaKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQ 634
PRK12704 PRK12704
phosphodiesterase; Provisional
 645-784 2.98e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  645 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKCEYEKKLHAMNKELQRL 724
Cdd:PRK12704   77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  725 QTAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 784
Cdd:PRK12704  148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
 690-800 3.35e-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: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  690 QNLgsVESYSEEKAKKVKCEyekklhamNKELQRLQTAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkq 765
Cdd:cd23703    61 QNL--REGLRELEERKLKTE--------ELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT--- 124

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 157823761  766 mkEEQEKARLTESRRNREIAQLKKDQRKRDHQLRL 800
Cdd:cd23703   125 --DPEREERAAKRRANREAKELAKKEARADALHEL 157
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 650-889 3.42e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  650 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsveSYSEEKAKKVkceyEKKLHAMNKELQRLQTAQK 729
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKL----QAEIAEAEAEIEERREELG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  730 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 794
Cdd:COG3883    90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  795 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIP 874
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246

                         250
                  ....*....|....*
gi 157823761  875 VARVQALPTPTTNGT 889
Cdd:COG3883   247 AGAGAAGAAGAAAGS 261
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1436-1477 3.45e-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: 3.45e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 157823761   1436 FQSTGKLTGHLGPVMCLtvdQISNGQDLIITGSKDHYIKMFD 1477
Cdd:smart00320    2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
PRK11637 PRK11637
AmiB activator; Provisional
 648-815 4.09e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.60  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  648 KLIDELENSQKRLQTLKKQYEEKLMML--------QHKirDTQL----ERDQVLQNLGSVESYSEEKAKKVKCEYEKKLH 715
Cdd:PRK11637  103 KQIDELNASIAKLEQQQAAQERLLAAQldaafrqgEHT--GLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTRE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  716 AMNKELQRLQTAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKD 790
Cdd:PRK11637  181 ELAAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAERE 255

                         170       180
                  ....*....|....*....|....*..
gi 157823761  791 QRKR-DHQLRllEAQK-RNQEVVLRRK 815
Cdd:PRK11637  256 AKARaEREAR--EAARvRDKQKQAKRK 280
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
647-778 4.23e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  647 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 725
Cdd:COG3206   266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157823761  726 TAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 778
Cdd:COG3206   334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 701-827 4.72e-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: 40.74  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   701 EKAKKVKCEYEKKLHAMNK-ELQRLQ--TAQKEHARLLKNQSQYEKQLKKLQQDVMEmkktkvrlmkqmkEEQEKARLTE 777
Cdd:pfam12037   29 ERAAKAARELESSPHAKKAlELMKKQeqTRQAELQAKIKEYEAAQEQLKIERQRVEY-------------EERRKTLQEE 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157823761   778 SRRNREIAQlKKDQ--RKRdHQLRLLEAQKRNQEVVlrRKTEEVTALRRQVR 827
Cdd:pfam12037   96 TKQKQQRAQ-YQDElaRKR-YQDQLEAQRRRNEELL--RKQEESVAKQEAMR 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 362-593 4.81e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  362 LKYANRARNIKNKVMVNQDR-ASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIK 440
Cdd:COG1196   216 RELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEE-----------LRLELEELELELE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  441 AMQETVDALRARITQLVSE---------QANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG1196   285 EAQAEEYELLAELARLEQDiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  512 ARspYFSASSAFSPTILSSDKETIEIIDLAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNELDVEEN 591
Cdd:COG1196   365 EA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442


                  ..
gi 157823761  592 QE 593
Cdd:COG1196   443 AL 444
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 727-855 6.16e-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: 39.29  E-value: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   727 AQKEHARLLKNQSQYEKQLKKLQQdvmemKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK---------KDQRKRDHQ 797
Cdd:pfam11600   11 EEKEKQRLEKDKERLRRQLKLEAE-----KEEKERLKEEAKAEKERAKEEARRKKEEEKELKekerrekkeKDEKEKAEK 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823761   798 LRLLEAQKRNQEVVL------RRKTEEVTALRRQVRPMSDKVAGkVTRKLSSSESP-APDTGSSA 855
Cdd:pfam11600   86 LRLKEEKRKEKQEALeakleeKRKKEEEKRLKEEEKRIKAEKAE-ITRFLQKPKTQqAPKTLAGS 149
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 647-963 6.17e-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: 41.31  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   647 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEE--KAKKVKCEYEKKLH 715
Cdd:pfam01576  702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDerKQRAQAVAAKKKLE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   716 AMNKELQ-RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD---- 790
Cdd:pfam01576  777 LDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaas 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   791 --QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSEspapDTGS 853
Cdd:pfam01576  853 erARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQV----EQLT 923

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   854 SAASGEADTSrpgtqQKmripvarvqalptptTNGTRKKYQRKgftgrvftSKTARMKWQLLERRVTDiiMQKMTISNME 933
Cdd:pfam01576  924 TELAAERSTS-----QK---------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAALE 973

                          330       340       350
                   ....*....|....*....|....*....|...
gi 157823761   934 ADMNRLLRQREELTKRRE---KLSKRREKIVKE 963
Cdd:pfam01576  974 AKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 674-802 6.26e-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: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   674 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVKCEYEKKLHA-------MNKELQR----LQ 725
Cdd:pfam14073    9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823761   726 TAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 802
Cdd:pfam14073   89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 440-1060 6.52e-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: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  440 KAMQETVDALRARITQLVSEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARspYFSA 519
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--EYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  520 SSAfsptiLSSDKETIEIIDLAKKDLEKLKRKEKKKKKSVAGKDDNADTD-QEKKEEKGVSEKENNELDVEENQEVSDHE 598
Cdd:COG1196   294 LAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  599 DEEEEEEdeeeeddiegeessdesDSESDEKANYQADLANITcEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKI 678
Cdd:COG1196   369 EAEAELA-----------------EAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  679 RDTQLERDQVLQNLgsvesyseekakkvkceyEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKT 758
Cdd:COG1196   431 AELEEEEEEEEEAL------------------EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAA 491

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  759 KVRLMKQMKEEQE-----KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQkRNQEVVLRRKTEEVTALRRQVRPMSDKV 833
Cdd:COG1196   492 RLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAK 570

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  834 AGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVARvqalptpttngtrkkYQRKGFTGRVFTSKTARMKWQ 913
Cdd:COG1196   571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------------YYVLGDTLLGRTLVAARLEAA 635

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  914 LLERRVTD----IIMQKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYIN 989
Cdd:COG1196   636 LRRAVTLAgrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823761  990 DSIADCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1060
Cdd:COG1196   716 RLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 669-892 7.68e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  669 EKLMMLQHKIRDTQLERDQvLQNLGSVESYSEEKAK---KVKCEYEKKLHAMNKElQRLQTAQKEHARLLKNQSQYEKQL 745
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEK-LKNTTPKDMWLEDLDKfeeALEEQEEVEEKEIAKE-QRLKSKTKGKASKLRKPKLKKKEK 1179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761  746 KKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 825
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823761  826 VRPMSDKVAGKVTRKLSSSE---------SPAPDTGSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGTRKK 892
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRVSavqysppppSKRPDGESNGGSKPSSPTKKKVKKRLEgSLAALKKKKKSEKKTARKKK 1336
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 704-806 7.87e-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: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   704 KKVKCEYEKKLHAMNKelQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrRNRE 783
Cdd:pfam14988   10 AKKTEEKQKKIEKLWN--QYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKES-QERE 86

                           90       100
                   ....*....|....*....|....*
gi 157823761   784 IAQLKKDQRK--RDHQLRLLEAQKR 806
Cdd:pfam14988   87 IQDLEEEKEKvrAETAEKDREAHLQ 111
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 659-788 8.26e-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: 38.45  E-value: 8.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   659 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE-KKLHAMNKELQRLQTAQKEHARLL- 735
Cdd:TIGR02473    6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157823761   736 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 788
Cdd:TIGR02473   86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
FliJ pfam02050
Flagellar FliJ protein;
651-786 8.45e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 38.03  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823761   651 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAkkvkceYEKKLHAMNKELQRLQtaqKE 730
Cdd:pfam02050    1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQ----QQLSGAGQGISAAELRN------YQAFISQLDEAIAQQQ---QE 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157823761   731 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 786
Cdd:pfam02050   68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
 
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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