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Conserved domains on  [gi|291167762|ref|NP_001166935|]
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kinesin-like protein KIF21A isoform 1 [Homo sapiens]

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: 625.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 291167762  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 ...
 1339-1652 1.17e-60

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: 210.27  E-value: 1.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1339 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1415
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1416 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1494
Cdd:cd00200    81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1495 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1572
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1573 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1650
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287


                  ..
gi 291167762 1651 WK 1652
Cdd:cd00200   288 WD 289
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 936-1017 1.27e-45

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: 158.94  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80


                  ..
gi 291167762 1016 AK 1017
Cdd:cd22263    81 AK 82
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 640-860 3.37e-11

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: 67.10  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 719
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  720 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 790
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  791 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 860
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
Cast super family cl37807
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 364-836 1.33e-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.


The actual alignment was detected with superfamily member pfam10174:

Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 56.75  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKE 587
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   588 EKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENS 667
Cdd:pfam10174  493 EK---ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVA 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   668 QKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLL 746
Cdd:pfam10174  569 RYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRR 644

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   747 KNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEV 821
Cdd:pfam10174  645 EDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEA 713

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 291167762   822 VL------------------RRKT--EEVTALRRQ 836
Cdd:pfam10174  714 LLaaisekdaniallelsssKKKKtqEEVMALKRE 748
 
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: 625.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 291167762  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 1.06e-139

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.31  E-value: 1.06e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 291167762   327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-378 1.34e-137

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: 429.30  E-value: 1.34e-137
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762      9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762     82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129  147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278

                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762    322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 3.20e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 305.51  E-value: 3.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059   126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059   190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059   249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059   328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  442 MQETVDALRSRITQLVSDQANHVLARaGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059   399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 3-404 4.29e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.53  E-value: 4.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188   94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188  168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188  245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188  313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188  380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458


                  ....*...
gi 291167762  397 QMELMEYK 404
Cdd:PLN03188  459 RDELQRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1339-1652 1.17e-60

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: 210.27  E-value: 1.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1339 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1415
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1416 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1494
Cdd:cd00200    81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1495 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1572
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1573 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1650
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287


                  ..
gi 291167762 1651 WK 1652
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1338-1655 6.70e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 6.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1338 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1409
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1410 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1485
Cdd:COG2319   183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1486 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1563
Cdd:COG2319   240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1564 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1641
Cdd:COG2319   311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389

                         330
                  ....*....|....
gi 291167762 1642 AADDRTVRIWKARN 1655
Cdd:COG2319   390 GSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 936-1017 1.27e-45

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: 158.94  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80


                  ..
gi 291167762 1016 AK 1017
Cdd:cd22263    81 AK 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 640-860 3.37e-11

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: 67.10  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 719
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  720 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 790
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  791 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 860
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-1023 1.69e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 716
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  717 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 794
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 867
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  868 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 931
Cdd:PRK03918  540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  932 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 1006
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699

                         410
                  ....*....|....*..
gi 291167762 1007 QANIMQMEEAKEEGETL 1023
Cdd:PRK03918  700 KEELEEREKAKKELEKL 716
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 640-1038 2.98e-09

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 62.05  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 719
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   720 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 796
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   797 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 871
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   872 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 951
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   952 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1027
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776

                          410
                   ....*....|.
gi 291167762  1028 VINACTLTEAR 1038
Cdd:pfam05483  777 KENTAILKDKK 787
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 643-846 3.79e-09

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: 62.00  E-value: 3.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   643 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 722
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   723 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 794
Cdd:TIGR02168  365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 291167762   795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 846
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 364-836 1.33e-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: 56.75  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKE 587
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   588 EKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENS 667
Cdd:pfam10174  493 EK---ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVA 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   668 QKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLL 746
Cdd:pfam10174  569 RYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRR 644

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   747 KNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEV 821
Cdd:pfam10174  645 EDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEA 713

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 291167762   822 VL------------------RRKT--EEVTALRRQ 836
Cdd:pfam10174  714 LLaaisekdaniallelsssKKKKtqEEVMALKRE 748
WD40 pfam00400
WD domain, G-beta repeat;
1338-1373 1.15e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.15e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 291167762  1338 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1373
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 564-1071 2.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  564 ESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANY 643
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEK 723
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEE 442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  724 KLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQR 803
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLR 520

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  804 KRDHQLRLLeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMR 883
Cdd:COG1196   521 GLAGAVAVL----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  884 IPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRR 961
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLE 676

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  962 EKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLL 1041
Cdd:COG1196   677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELL 748

                         490       500       510
                  ....*....|....*....|....*....|
gi 291167762 1042 DHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:COG1196   749 EEEALEELPEPPDLEELERELERLEREIEA 778
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1336-1373 3.68e-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: 3.68e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 291167762   1336 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1373
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 713-1108 6.62e-06

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: 51.21  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   713 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 788
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   789 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVrpmSDKVAGKvtRKLSSSDAPAQDTgssaaA 868
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQK--QILRERLANLERQ-----L 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   869 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 948
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   949 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1028
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  1029 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1096
Cdd:TIGR02168  465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537

                          410
                   ....*....|...
gi 291167762  1097 -LDALLGHALQDL 1108
Cdd:TIGR02168  538 aIEAALGGRLQAV 550
PTZ00121 PTZ00121
MAEBL; Provisional
 557-1021 8.38e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  557 KRLQKLEESNREERSVAGKEDNTDTDQ-EKKEEKGVSERENNELEVEESQEVSDheDEEEEEEEEEDDIDGGESSDESDS 635
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADEAEAAEEKAEAAE 1370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  636 ESDEKANYQADLANITCEIAIK-QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 714
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  715 KKvrSEYEKKLQAMNKelqrlQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK--QMKEEQEKARLTESRRN 792
Cdd:PTZ00121 1451 KK--AEEAKKAEEAKK-----KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKK 1523

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  793 REIAQLKKDQRKRDhQLRLLEAQKRNQEVVLR---RKTEEVTALRRQVRPMSDKvaGKVTRKLSSSDAPAQDTGSSAAAV 869
Cdd:PTZ00121 1524 ADEAKKAEEAKKAD-EAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKL 1600

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  870 ETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKmtisNMEADMnr 949
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK----KAEEDK-- 1674

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  950 llKQREELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSIsdcQANIMQMEEAKEEGE 1021
Cdd:PTZ00121 1675 --KKAEEAKKAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKKAEELKKAE---EENKIKAEEAKKEAE 1740
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-741 9.54e-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: 47.36  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   446 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsp 525
Cdd:TIGR02168  735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------- 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   526 tilssdKETIEIIDLAKKDLEKLKRKEKRKKKrlqklEESNREERSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQ 605
Cdd:TIGR02168  799 ------KALREALDELRAELTLLNEEAANLRE-----RLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELE 865

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   606 EvsdhedeeeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMML 685
Cdd:TIGR02168  866 E------------------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762   686 QHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
 717-811 3.57e-04

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: 43.31  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  717 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 792
Cdd:cd23703    67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138

                          90
                  ....*....|....*....
gi 291167762  793 REIAQLKKDQRKRDHQLRL 811
Cdd:cd23703   139 REAKELAKKEARADALHEL 157
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 955-1047 1.60e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 1.60e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    955 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1034
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270

                            90
                    ....*....|...
gi 291167762   1035 TEARYLLDHFLSM 1047
Cdd:smart00787  271 KEIEKLKEQLKLL 283
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 666-792 9.45e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 40.41  E-value: 9.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    666 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 745
Cdd:smart00435  266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 291167762    746 LKNQSQYEKQLKKLQQDVMEMKKTkvrlmKQMKEEQEKARLTESRRN 792
Cdd:smart00435  335 KKKEEKKKKQIERLEERIEKLEVQ-----ATDKEENKTVALGTSKIN 376
 
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: 625.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372    81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372   151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372   228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 291167762  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372   297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 1.06e-139

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.31  E-value: 1.06e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 291167762   327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-378 1.34e-137

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: 429.30  E-value: 1.34e-137
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762      9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762     82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129  147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278

                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762    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 1.00e-120

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: 382.37  E-value: 1.00e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:cd00106     1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   83 TVFAYGQTGAGKTYTMGTGFDvniveEELGIISRAVKHLFKSIEEKKhiaikngLPAPDFKVNAQFLELYNEEVLDLFDt 162
Cdd:cd00106    80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRK-------ETKSSFSVSASYLEIYNEKIYDLLS- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  163 trdidaKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:cd00106   147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV-------- 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  243 idadnatDNKIISESAQMnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 322
Cdd:cd00106   213 -------KQRNREKSGES----VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 291167762  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 7.53e-104

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: 335.58  E-value: 7.53e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGY 80
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   81 NATVFAYGQTGAGKTYTMGtGFDVNivEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVldlf 160
Cdd:cd01371    82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIARSQNNQ--------QFLVRVSYLEIYNEEI---- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  161 dttRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 239
Cdd:cd01371   147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  240 cpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 319
Cdd:cd01371   220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291167762  320 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01371   283 HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 9-371 4.39e-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: 4.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYI 66
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVN 145
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKD--------EKEFEVS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  146 AQFLELYNEEVLDLFDTTrdidakSKKSNIRihEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSR 225
Cdd:cd01370   146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  226 SHAIFTIHVCQTrvcpqidadnatdnkiiSESAQMNEfETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 305
Cdd:cd01370   218 SHAVLQITVRQQ-----------------DKTASINQ-QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762  306 NVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01370   280 NCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 10-373 7.76e-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: 329.94  E-value: 7.76e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYIQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366     4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   86 AYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01366    83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  165 didAKSKKSNIRiHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqid 244
Cdd:cd01366   149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILH----------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  245 adnatdnkIISESAQMNEfeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 324
Cdd:cd01366   214 --------ISGRNLQTGE--ISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 291167762  325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 373
Cdd:cd01366   281 NSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 8-378 6.50e-97

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: 316.99  E-value: 6.50e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYiQC 68
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVY-ED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   69 I-EKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvniveEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQ 147
Cdd:cd01365    80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  148 FLELYNEEVLDLFDTtrdiDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSH 227
Cdd:cd01365   147 YMEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSH 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  228 AIFTIhvcqtrVCPQIDADNATDNKiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNV 307
Cdd:cd01365   223 AVFTI------VLTQKRHDAETNLT-----------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKV 285

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762  308 ISALGD-----KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:cd01365   286 ISALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 7-371 8.35e-96

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 312.34  E-value: 8.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   85 FAYGQTGAGKTYTMgtgFDVNIVEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01369    81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIYSMDENL--------EFHVKVSYFEIYMEKIRDLLDVSK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  165 DidakskksNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqid 244
Cdd:cd01369   150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  245 aDNATDNKIisesaqmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 324
Cdd:cd01369   214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 291167762  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 2.33e-93

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


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 306.56  E-value: 2.33e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   79 GYNATVFAYGQTGAGKTYTM----GTGFDVNIVEEEL-GIISRAVKHLFKSIEEKKHiaiknglpapDFKVNAQFLELYN 153
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTMegdrSPNEEYTWELDPLaGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  154 EEVLDLFDttrdiDAKSKKSNIRIHEDS--TGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 231
Cdd:cd01364   151 EELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  232 IHVcqtrvcpqidadnatdnkIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 311
Cdd:cd01364   226 ITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL 287

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167762  312 GDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364   288 VERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 3.20e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 305.51  E-value: 3.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059   126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059   190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059   249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059   328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  442 MQETVDALRSRITQLVSDQANHVLARaGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059   399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 10-380 3.35e-90

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 297.50  E-value: 3.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   89 QTGAGKTYTM--GTGFDVNIVEEELGIISRAVKHLFKSI--EEKKHIAIKNglpapdFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01373    83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIqrEKEKAGEGKS------FLCKCSFLEIYNEQIYDLLDPA- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01373   156 -------SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------ 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  245 adnatdnkIISESAQMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVP 322
Cdd:cd01373   217 --------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVC 288

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 291167762  323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01373   289 YRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 9-371 7.82e-89

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


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 292.31  E-value: 7.82e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   85 FAYGQTGAGKTYTMGTGfdvnivEEELGIISRAVKHLFKSIEEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01374    77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDT---------PDREFLLRVSYLEIYNEKINDLLSPT- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01374   141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRI------------ 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  245 adnatdnkIISESAQMNEFE--TLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHVP 322
Cdd:cd01374   202 --------TIESSERGELEEgtVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIP 272

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 291167762  323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01374   273 YRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 10-369 4.73e-73

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: 247.03  E-value: 4.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNAT 83
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   84 VFAYGQTGAGKTYTMGTGFdvniveEELGIISRAVKHLFKSIEEKkhiaiknglpAPDFKVNAQFLELYNEEVLDLFDtt 163
Cdd:cd01376    81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLLQMTRKE----------AWALSFTMSYLEIYQEKILDLLE-- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  164 rdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqi 243
Cdd:cd01376   143 ------PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  244 dadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 323
Cdd:cd01376   208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 291167762  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 1.95e-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: 239.89  E-value: 1.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   10 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   79 GYNATVFAYGQTGAGKTYTMGTGFDVNivEEELGIISRAVKHLFksiEEKKHIAIKNGLpapdfKVNAQFLELYNEEVLD 158
Cdd:cd01367    82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVF---RLLNKLPYKDNL-----GVTVSFFEIYGGKVFD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  159 LFdttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFtihvcqtr 238
Cdd:cd01367   152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAIL-------- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  239 vcpQIDADNATDNKiisesaqmnefetLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 317
Cdd:cd01367   215 ---QIILRDRGTNK-------------LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291167762  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 6.58e-67

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: 229.77  E-value: 6.58e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   46 DKAFTFDYVFDiDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNIVEEelGIISRAVKHLFKSI 125
Cdd:cd01375    47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENYKHR--GIIPRALQQVFRMI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  126 EEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKsnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCL 205
Cdd:cd01375   123 EER---------PTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  206 KLGALSRTTASTQMNVQSSRSHAIFTIHVCqtrvcpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375   192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE-------------------AHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  286 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375   253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330


                  ....
gi 291167762  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 5.14e-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: 224.97  E-value: 5.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYIQCIEKLIE 74
Cdd:cd01368     3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   75 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIeekkhiaiknglpaPDFKVNAQFLELYN 153
Cdd:cd01368    83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  154 EEVLDLFDTTRDIDAKSKKSnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 233
Cdd:cd01368   142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  234 VCQtrvcpqidADNATDNKIISESAQMNefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368   221 LVQ--------APGDSDGDVDQDKDQIT-----VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 291167762  314 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368   288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 3-404 4.29e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.53  E-value: 4.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188   94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188  168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188  245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188  313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188  380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458


                  ....*...
gi 291167762  397 QMELMEYK 404
Cdd:PLN03188  459 RDELQRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1339-1652 1.17e-60

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: 210.27  E-value: 1.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1339 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1415
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1416 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1494
Cdd:cd00200    81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1495 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1572
Cdd:cd00200   138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1573 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1650
Cdd:cd00200   209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287


                  ..
gi 291167762 1651 WK 1652
Cdd:cd00200   288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1338-1655 6.70e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 6.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1338 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1409
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1410 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1485
Cdd:COG2319   183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1486 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1563
Cdd:COG2319   240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1564 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1641
Cdd:COG2319   311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389

                         330
                  ....*....|....
gi 291167762 1642 AADDRTVRIWKARN 1655
Cdd:COG2319   390 GSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 936-1017 1.27e-45

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: 158.94  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80


                  ..
gi 291167762 1016 AK 1017
Cdd:cd22263    81 AK 82
WD40 COG2319
WD40 repeat [General function prediction only];
1338-1664 3.26e-44

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 166.24  E-value: 3.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1338 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1409
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDgrLLASASADGTVRLWDLATGLLLRTLTGHTGAV--------RSVAFSpdgktlASGSA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1410 ---IKVWDIrDSAKCIRTLTSsgqvtlgdacsastsrtvaipsGENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1485
Cdd:COG2319   141 dgtVRLWDL-ATGKLLRTLTG----------------------HSGAVTSVAFSPDGKLLASGSDdGTVRLWDLATGKLL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1486 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTIQGDN--LFSGSRDN 1563
Cdd:COG2319   198 RTLTGHTGAVRSVA---FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS------GSVRSVAFSPDGrlLASGSADG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1564 GIKKWDLTQKDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1641
Cdd:COG2319   269 TVRLWDLATGELLRTLT-GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347

                         330       340
                  ....*....|....*....|...
gi 291167762 1642 AADDRTVRIWkarNLQDGQISDT 1664
Cdd:COG2319   348 GSDDGTVRLW---DLATGELLRT 367
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1338-1612 1.06e-36

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: 140.93  E-value: 1.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1338 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1414
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1415 IRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1493
Cdd:cd00200   164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1494 PVMCLTVDQissgqdliitgskDHYIkmfdvtegalgtvspthnfepphydgiealtiqgdnLFSGSRDNGIKKWDLTQK 1573
Cdd:cd00200   221 GVNSVAFSP-------------DGYL------------------------------------LASGSEDGTIRVWDLRTG 251

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 291167762 1574 DLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1612
Cdd:cd00200   252 ECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1328-1660 1.22e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.12  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1328 ASKGIRAFPLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKY-CNYTSLVFT 1404
Cdd:COG2319    17 ALALLAAALGALLLLLLGLAAAVASLAasPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFsPDGRLLASA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1405 VSTSYIKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQ 1483
Cdd:COG2319    97 SADGTVRLWDL-ATGLLLRTLTGH----------------------TGAVRSVAFSPDGKTLASGSAdGTVRLWDLATGK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1484 STGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSR 1561
Cdd:COG2319   154 LLRTLTGHSGAVTSVA---FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT------GAVRSVAFspDGKLLASGSA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1562 DNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHI 1639
Cdd:COG2319   225 DGTVRLWDLATGKLLR-TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLL 303

                         330       340
                  ....*....|....*....|.
gi 291167762 1640 FTAADDRTVRIWkarNLQDGQ 1660
Cdd:COG2319   304 ASGSDDGTVRLW---DLATGK 321
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1444-1664 1.22e-34

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: 135.16  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1444 TVAIPSGENQINQIALNPTGTFLYAASGNA-VRMWDLKRFQSTGKLTGHLGPVmcLTVDQISSGQdLIITGSKDHYIKMF 1522
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPV--RDVAASADGT-YLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1523 DvtegaLGTVSPTHNFEPpHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLL 1600
Cdd:cd00200    79 D-----LETGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762 1601 SGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWkarNLQDGQISDT 1664
Cdd:cd00200   152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFspDGEKLLSSSSDGTIKLW---DLSTGKCLGT 214
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
 936-1017 1.25e-29

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: 113.07  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEgDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22248     1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKD-ESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79


                  ..
gi 291167762 1016 AK 1017
Cdd:cd22248    80 SK 81
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
 936-1017 3.68e-29

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: 111.82  E-value: 3.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22262     1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80


                  ..
gi 291167762 1016 AK 1017
Cdd:cd22262    81 TK 82
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 9-159 2.97e-21

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 91.51  E-value: 2.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762     9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYiQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796   21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167762    89 QTGAGKTYTMgtgfdvniveeelgiISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDL 159
Cdd:pfam16796   96 QTGSGSNDGM---------------IPRAREQIFRFISSLK--------KGWKYTIELQFVEIYNESSQDL 143
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1337-1478 1.90e-18

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: 87.78  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1337 LQCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1413
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762 1414 DIRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWD 1478
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 7.52e-13

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: 68.14  E-value: 7.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYIQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   91 GAGKTYTMgtgfdvniveeeLGIISRAVKHLFKSIEEKKhiaiknglpapdfkvnaqflelyneevldlfdttrdidaks 170
Cdd:cd01363    62 GAGKTETM------------KGVIPYLASVAFNGINKGE----------------------------------------- 88

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  171 kksnirihEDStggiyTVGVTTRTVNTESEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqidadnatd 250
Cdd:cd01363    89 --------TEG-----WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  251 nkiisesaqmnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 310
Cdd:cd01363   137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 640-860 3.37e-11

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: 67.10  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 719
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  720 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 790
Cdd:COG4942   101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  791 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 860
Cdd:COG4942   181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-1023 1.69e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 716
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  717 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 794
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 867
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  868 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 931
Cdd:PRK03918  540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  932 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 1006
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699

                         410
                  ....*....|....*..
gi 291167762 1007 QANIMQMEEAKEEGETL 1023
Cdd:PRK03918  700 KEELEEREKAKKELEKL 716
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 640-1038 2.98e-09

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 62.05  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 719
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   720 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 796
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   797 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 871
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   872 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 951
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   952 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1027
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776

                          410
                   ....*....|.
gi 291167762  1028 VINACTLTEAR 1038
Cdd:pfam05483  777 KENTAILKDKK 787
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 643-846 3.79e-09

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: 62.00  E-value: 3.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   643 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 722
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   723 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 794
Cdd:TIGR02168  365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 291167762   795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 846
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 645-1031 8.86e-09

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: 60.47  E-value: 8.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   645 ADLANITCEIAIKQKLIDELENSQKRLQTLKKQyEEKLMMLQHKIRDTQlerdqvlqnlGSVESYSEEKAKKVRSEYEKK 724
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYE----------GYELLKEKEALERQKEAIERQ 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   725 LQAMNKELQ----RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQmkeeqekarltesrrnrEIAQLKK 800
Cdd:TIGR02169  246 LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA-----------------EIASLER 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   801 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQ 880
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   881 KmripvARVQALptpatngnrKKYQRKgltgRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKR 960
Cdd:TIGR02169  388 K-----DYREKL---------EKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762   961 REKLSKRREKIVKEngegdknVANINEEMESLTANIDYINDSISDCQANIMQMEEAK-----EEGETLDVTAVINA 1031
Cdd:TIGR02169  450 IKKQEWKLEQLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 642-845 3.96e-08

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: 58.53  E-value: 3.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   642 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVR 718
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   719 SEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 792
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762   793 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
PTZ00121 PTZ00121
MAEBL; Provisional
 533-830 4.23e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  533 ETIEIIDLAKKDLEKLKRKekrkKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHED 612
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  613 EEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEI--AIKQKLIDELENSQ--KRLQTLKKQYEEKLMMLQHK 688
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEekKKAEEAKKAEEDKNMALRKA 1583

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  689 IRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAmnKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK 768
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  769 TKVRLMKqmKEEQEKARLTESRRNREiaqlkkDQRKRDHQLRLLEAQKRNQEVVLRRKTEEV 830
Cdd:PTZ00121 1662 KAAEEAK--KAEEDKKKAEEAKKAEE------DEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 668-1023 5.82e-08

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: 57.82  E-value: 5.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   668 QKRLQTLKKQYEEK--LMMLQHKIRDTQLERDQVLQNLGSVEsyseeKAKKVRSEyekkLQAMNKELQRLQaaqkEHARl 745
Cdd:pfam15921  244 EDQLEALKSESQNKieLLLQQHQDRIEQLISEHEVEITGLTE-----KASSARSQ----ANSIQSQLEIIQ----EQAR- 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   746 lkNQ-SQYEKQLKKLQQDVMEMKkTKVRLMKQMKE----EQEK------ARLTESRRNREiaQLKKDQRKRDHQLRLLEA 814
Cdd:pfam15921  310 --NQnSMYMRQLSDLESTVSQLR-SELREAKRMYEdkieELEKqlvlanSELTEARTERD--QFSQESGNLDDQLQKLLA 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   815 --QKRNQEVVLRRKTEEvtalRRQVRPMSDKVA-GKVTRKLSSSDAPAQDTGSSAAAVETDAsrtgaQQKMRIPVARVQA 891
Cdd:pfam15921  385 dlHKREKELSLEKEQNK----RLWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAMKSEC-----QGQMERQMAAIQG 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   892 lptpatnGNRKKYQRKGLTGRVFISKtarmkwQLLERRVTDIIMQKMTISNME---ADMNRLLKQREE-LTKRREKLSKR 967
Cdd:pfam15921  456 -------KNESLEKVSSLTAQLESTK------EMLRKVVEELTAKKMTLESSErtvSDLTASLQEKERaIEATNAEITKL 522

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762   968 REKIvkengegDKNVaninEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETL 1023
Cdd:pfam15921  523 RSRV-------DLKL----QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL 567
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 640-880 1.13e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.99  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 714
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  715 KKVrSEYEKKLQAMNkelqRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 794
Cdd:COG3883   112 ESF-SDFLDRLSALS----KIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDAS 874
Cdd:COG3883   184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263


                  ....*.
gi 291167762  875 RTGAQQ 880
Cdd:COG3883   264 AAGAAA 269
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 364-836 1.33e-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: 56.75  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKE 587
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   588 EKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENS 667
Cdd:pfam10174  493 EK---ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVA 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   668 QKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLL 746
Cdd:pfam10174  569 RYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRR 644

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   747 KNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEV 821
Cdd:pfam10174  645 EDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEA 713

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 291167762   822 VL------------------RRKT--EEVTALRRQ 836
Cdd:pfam10174  714 LLaaisekdaniallelsssKKKKtqEEVMALKRE 748
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 644-838 3.11e-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: 55.46  E-value: 3.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDT-QLERDQVLQNLGSvesySEEKAKKVRSEYE 722
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQA----ELSKLEEEVSRIE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   723 KKLQAMNKELQRL----QAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 798
Cdd:TIGR02169  812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 291167762   799 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 838
Cdd:TIGR02169  888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
PTZ00121 PTZ00121
MAEBL; Provisional
 655-1018 4.82e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  655 AIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQR 734
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  735 LQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLtesrRNREIAQLKKDQRKRDHQLRLLEA 814
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI----KAAEEAKKAEEDKKKAEEAKKAEE 1685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  815 QKRNQEVVLRRKTEEvtalRRQVRPMSDKVAGKVtRKLSSSDAPAQDTGSSAaaveTDASRTGAQQKMRIPVARVQalpt 894
Cdd:PTZ00121 1686 DEKKAAEALKKEAEE----AKKAEELKKKEAEEK-KKAEELKKAEEENKIKA----EEAKKEAEEDKKKAEEAKKD---- 1752

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  895 patNGNRKKYQRkgltgrvfISKTARMKWQLLERRVTDIImqkmtisnmeadmnrllkqREELTKRREKLSKRREKIVKE 974
Cdd:PTZ00121 1753 ---EEEKKKIAH--------LKKEEEKKAEEIRKEKEAVI-------------------EEELDEEDEKRRMEVDKKIKD 1802

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291167762  975 ---NGE-----GDKNVANINEEMESLTANIDYINDSISdcqaniMQMEEAKE 1018
Cdd:PTZ00121 1803 ifdNFAniiegGKEGNLVINDSKEMEDSAIKEVADSKN------MQLEEADA 1848
WD40 pfam00400
WD domain, G-beta repeat;
1338-1373 1.15e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.15e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 291167762  1338 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1373
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 712-838 2.27e-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: 48.38  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   712 EKAKKVRSEYEKKLQamnkelqrlqaaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 791
Cdd:pfam20492    2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762   792 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 838
Cdd:pfam20492   58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 564-1071 2.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  564 ESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANY 643
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEK 723
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEE 442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  724 KLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQR 803
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLR 520

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  804 KRDHQLRLLeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMR 883
Cdd:COG1196   521 GLAGAVAVL----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  884 IPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRR 961
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLE 676

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  962 EKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLL 1041
Cdd:COG1196   677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELL 748

                         490       500       510
                  ....*....|....*....|....*....|
gi 291167762 1042 DHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:COG1196   749 EEEALEELPEPPDLEELERELERLEREIEA 778
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
654-870 2.88e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  654 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLgsvESYSEEKaKKVRSeYEKKLQAMNKELQ 733
Cdd:COG4913   612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRL---AEYSWDE-IDVAS-AEREIAELEAELE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  734 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 810
Cdd:COG4913   679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167762  811 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVE 870
Cdd:COG4913   755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
653-845 3.08e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  653 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE--KAKKVRSEYEKKLQAMN 729
Cdd:PRK03918  148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  730 KELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARltesrRNREIAQLKKDQRKRDHQL 809
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSEFY 302

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 291167762  810 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:PRK03918  303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1336-1373 3.68e-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: 3.68e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 291167762   1336 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1373
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
PTZ00121 PTZ00121
MAEBL; Provisional
 653-970 4.09e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  653 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESysEEKAKKVRSEYEKKlqamnKEL 732
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKK-----KAD 1293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  733 QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRD-HQLRL 811
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKK 1373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  812 LEAQKRNQEvvLRRKTEEV-TALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAV-ETDASRTGAQQKMRIPVARV 889
Cdd:PTZ00121 1374 EEAKKKADA--AKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkKADEAKKKAEEAKKADEAKK 1451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  890 QALPTPATNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDIIMQKMTISNMEADMnrlLKQREELTKRREKLSKRRE 969
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEE 1520


                  .
gi 291167762  970 K 970
Cdd:PTZ00121 1521 A 1521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 713-1108 6.62e-06

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: 51.21  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   713 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 788
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   789 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVrpmSDKVAGKvtRKLSSSDAPAQDTgssaaA 868
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQK--QILRERLANLERQ-----L 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   869 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 948
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   949 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1028
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  1029 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1096
Cdd:TIGR02168  465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537

                          410
                   ....*....|...
gi 291167762  1097 -LDALLGHALQDL 1108
Cdd:TIGR02168  538 aIEAALGGRLQAV 550
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1615-1652 6.89e-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: 44.23  E-value: 6.89e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 291167762   1615 TFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWK 1652
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 657-826 1.11e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   657 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVRSEYEKKLQaMNKELQRLQ 736
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKAR-QRQELQQAR 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   737 AAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 813
Cdd:pfam13868  242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316

                          170
                   ....*....|...
gi 291167762   814 AQKRNQEVVLRRK 826
Cdd:pfam13868  317 GERLREEEAERRE 329
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
663-845 1.31e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  663 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQ 739
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  740 KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 816
Cdd:COG4372    94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173

                         170       180
                  ....*....|....*....|....*....
gi 291167762  817 RNQEvvLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:COG4372   174 QALS--EAEAEQALDELLKEANRNAEKEE 200
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
695-855 1.35e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.86  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  695 ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAaqkeHARLLKNQsqyekqLKKLQQDVMEMKKtKVRLM 774
Cdd:COG2433   385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA----EVEELEAE------LEEKDERIERLER-ELSEA 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  775 KQmkEEQEKARLTE--SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKL 852
Cdd:COG2433   454 RS--EERREIRKDReiSRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKF 519


                  ...
gi 291167762  853 SSS 855
Cdd:COG2433   520 TKE 522
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
688-1003 2.04e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  688 KIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMK 767
Cdd:COG4372     7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  768 K---TKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 844
Cdd:COG4372    87 EqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  845 AGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQ 924
Cdd:COG4372   167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  925 LLE------RRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDY 998
Cdd:COG4372   247 DKEelleevILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326


                  ....*
gi 291167762  999 INDSI 1003
Cdd:COG4372   327 KLELA 331
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 683-826 2.20e-05

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: 47.39  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   683 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKVRsEYEKKLQAMnKELQRLQAAQKEhARLLKNQSQYEKQLKKLQQD 762
Cdd:pfam13904   38 LTYARKLEGLKLER-------QPLEAYENWLAAKQR-QRQKELQAQ-KEEREKEEQEAE-LRKRLAKEKYQEWLQRKARQ 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291167762   763 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 826
Cdd:pfam13904  108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 569-830 3.73e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   569 ERSVAGKEDNTDtDQEKKEEKGVSERENNELEVEESQEvsdhedeeeeeeeeeddidggessdesdsesdEKANYQADLA 648
Cdd:TIGR02169  307 ERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELER--------------------------------EIEEERKRRD 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   649 NITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLqnlgsvesyseEKAKKVRSEy 721
Cdd:TIGR02169  354 KLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQ-----------EELQRLSEE- 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   722 ekkLQAMNKELQRLQAAQKE-HARLLKNQSQYEKQLKKLQQDVMEMKktkvrlmkqmKEEQEKARLTEsrrnrEIAQLKK 800
Cdd:TIGR02169  422 ---LADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS----------KYEQELYDLKE-----EYDRVEK 483

                          250       260       270
                   ....*....|....*....|....*....|..
gi 291167762   801 DQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 830
Cdd:TIGR02169  484 ELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 644-829 3.95e-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: 48.58  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE------EKLMMLQHKIRdtQLERDQVLQnlgsvesysEEKAKKV 717
Cdd:pfam17380  326 QAEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqEEIAMEISRMR--ELERLQMER---------QQKNERV 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   718 RSEyekkLQAMNKelQRLQaaQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNREIA 796
Cdd:pfam17380  395 RQE----LEAARK--VKIL--EEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQVE 463

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 291167762   797 QLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEE 829
Cdd:pfam17380  464 RLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILE 498
WD40 pfam00400
WD domain, G-beta repeat;
1618-1651 4.01e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 4.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 291167762  1618 PVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIW 1651
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 656-828 4.36e-05

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


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 46.30  E-value: 4.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   656 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKvrseyEKKLQAMNKELQRL 735
Cdd:pfam14988   23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQ-----EREIQDLEEEKEKV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   736 QAA-----QKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 805
Cdd:pfam14988   98 RAEtaekdREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175

                          170       180
                   ....*....|....*....|...
gi 291167762   806 DHQLRLLEAQKRNQEvvlRRKTE 828
Cdd:pfam14988  176 IQETQALEAIKSKLE---NRKQR 195
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 669-821 4.52e-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: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   669 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVRSEYEKKlQAMNKELQRL 735
Cdd:pfam02841  155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   736 QAAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 814
Cdd:pfam02841  224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286


                   ....*..
gi 291167762   815 QKRNQEV 821
Cdd:pfam02841  287 ESLQKEI 293
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
653-838 4.76e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  653 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE 722
Cdd:COG4913   669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  723 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 799
Cdd:COG4913   749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 291167762  800 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 838
Cdd:COG4913   822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 661-815 5.30e-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: 46.46  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  661 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAM--NKELQrlqAA 738
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYE---AL 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762  739 QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 815
Cdd:COG1579    95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
679-826 5.93e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  679 EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQA----AQKEHARLLKNQSQYEK 754
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEReierLERELEERERRRARLEA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  755 QLKKL-------QQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRN--QEVVLRR 825
Cdd:COG4913   367 LLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipARLLALR 446


                  .
gi 291167762  826 K 826
Cdd:COG4913   447 D 447
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
644-1039 6.08e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 714
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  715 KKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 794
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  795 IA-----QLKKDQRKRDHQLRLLEAQ-------------KRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSD 856
Cdd:COG4717   254 IAaallaLLGLGGSLLSLILTIAGVLflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  857 APAQDTGSS----AAAVETDASRTGAQQKMRIPV--ARVQALPTPATNGNRKKYQRKGLTGRVFISKTARmkWQLLERRV 930
Cdd:COG4717   334 LSPEELLELldriEELQELLREAEELEEELQLEEleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--LEELEEQL 411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  931 TDI------IMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENG--EGDKNVANINEEMESLTANIDYINDS 1002
Cdd:COG4717   412 EELlgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 291167762 1003 ISDCQANIMQMEEAKEEGETLDVTAVINA-----CTLTEARY 1039
Cdd:COG4717   492 WAALKLALELLEEAREEYREERLPPVLERaseyfSRLTDGRY 533
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 661-899 6.17e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  661 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseEKAKKVRSEYEKKLQAMNKELQRLQAAQK 740
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------EALQAEIDKLQAEIAEAEAEIEERREELG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  741 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 805
Cdd:COG3883    90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  806 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIP 885
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246

                         250
                  ....*....|....
gi 291167762  886 VARVQALPTPATNG 899
Cdd:COG3883   247 AGAGAAGAAGAAAG 260
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 663-993 6.83e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.58  E-value: 6.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   663 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNK-------ELQRL 735
Cdd:pfam07888   77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQrvleretELERM 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   736 QAAQKEHARLLKNQSQYEKQLK-KLQQDVMEMKKtkvrlmkqMKEEQEKARLTESRRNREIAQLKKDQRKRdhQLRLLEA 814
Cdd:pfam07888  156 KERAKKAGAQRKEEEAERKQLQaKLQQTEEELRS--------LSKEFQELRNSLAQRDTQVLQLQDTITTL--TQKLTTA 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   815 QkrnqevvlrRKTEEVTALRRQVRPMSDkvagkvtrKLSSSDAPAQDTGSSAAAVETDASRTGAQqkmrIPVARVQAlpt 894
Cdd:pfam07888  226 H---------RKEAENEALLEELRSLQE--------RLNASERKVEGLGEELSSMAAQRDRTQAE----LHQARLQA--- 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   895 patngnrkkyqrKGLTGRVfisktARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSK---RREKI 971
Cdd:pfam07888  282 ------------AQLTLQL-----ADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermEREKL 344

                          330       340
                   ....*....|....*....|...
gi 291167762   972 VKENG-EGDKNVANINEEMESLT 993
Cdd:pfam07888  345 EVELGrEKDCNRVQLSESRRELQ 367
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
658-789 6.84e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  658 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 736
Cdd:COG3206   266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 291167762  737 AAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 789
Cdd:COG3206   334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 695-1024 6.89e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.91  E-value: 6.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   695 ERDQVLQNLGSvesyseekAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQyekqlkKLQQDVMEMKKTKVRLM 774
Cdd:pfam12128  605 RLDKAEEALQS--------AREKQAAAEEQLVQANGELEKASREETFARTALKNARL------DLRRLFDEKQSEKDKKN 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   775 KQMKEEQEKArltesrrNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrkTEEVTALRRQVRPMSDKVAgkvtrklss 854
Cdd:pfam12128  671 KALAERKDSA-------NERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLA--------- 732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   855 sdapAQDTGSSAAAVETDASRTGAQQKMRIPVArvqALPTPATNGNRKKYQRKGLTGRvfISKTARMKWQLLERRVtdiI 934
Cdd:pfam12128  733 ----LLKAAIAARRSGAKAELKALETWYKRDLA---SLGVDPDVIAKLKREIRTLERK--IERIAVRRQEVLRYFD---W 800

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   935 MQ----------KMTISNMEADMNRLlkqREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSIS 1004
Cdd:pfam12128  801 YQetwlqrrprlATQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877

                          330       340
                   ....*....|....*....|
gi 291167762  1005 DCQANimqmEEAKEEGETLD 1024
Cdd:pfam12128  878 DANSE----QAQGSIGERLA 893
PRK12704 PRK12704
phosphodiesterase; Provisional
 686-829 7.51e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  686 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQY----E 753
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762  754 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 829
Cdd:PRK12704  110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
PTZ00121 PTZ00121
MAEBL; Provisional
 557-1021 8.38e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  557 KRLQKLEESNREERSVAGKEDNTDTDQ-EKKEEKGVSERENNELEVEESQEVSDheDEEEEEEEEEDDIDGGESSDESDS 635
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADEAEAAEEKAEAAE 1370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  636 ESDEKANYQADLANITCEIAIK-QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 714
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  715 KKvrSEYEKKLQAMNKelqrlQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK--QMKEEQEKARLTESRRN 792
Cdd:PTZ00121 1451 KK--AEEAKKAEEAKK-----KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKK 1523

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  793 REIAQLKKDQRKRDhQLRLLEAQKRNQEVVLR---RKTEEVTALRRQVRPMSDKvaGKVTRKLSSSDAPAQDTGSSAAAV 869
Cdd:PTZ00121 1524 ADEAKKAEEAKKAD-EAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKL 1600

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  870 ETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKmtisNMEADMnr 949
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK----KAEEDK-- 1674

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  950 llKQREELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSIsdcQANIMQMEEAKEEGE 1021
Cdd:PTZ00121 1675 --KKAEEAKKAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKKAEELKKAE---EENKIKAEEAKKEAE 1740
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-741 9.54e-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: 47.36  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   446 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsp 525
Cdd:TIGR02168  735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------- 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   526 tilssdKETIEIIDLAKKDLEKLKRKEKRKKKrlqklEESNREERSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQ 605
Cdd:TIGR02168  799 ------KALREALDELRAELTLLNEEAANLRE-----RLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELE 865

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   606 EvsdhedeeeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMML 685
Cdd:TIGR02168  866 E------------------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762   686 QHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 424-805 1.08e-04

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: 47.36  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   424 ENAMLQTENN--NLRVRIKAMQETVDALRSRITQLVSDQanhvlaragegnEEISNMIHSYIKEIEDLRAKLLESEAVNE 501
Cdd:TIGR02168  669 NSSILERRREieELEEKIEELEEKIAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   502 NLRKNLTRATARApyfsgsstfsptilssDKETIEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDT 581
Cdd:TIGR02168  737 RLEAEVEQLEERI----------------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   582 DQEKKEEKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSdesdsesdeKANYQADLANITCEIAIKQKLI 661
Cdd:TIGR02168  801 LREALDEL---RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ---------IEELSEDIESLAAEIEELEELI 868

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   662 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSE 947

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   742 HARL-----LKNQSQYEKQLKKLQQDVMEMKKTKVRL----------MKQMKE-----EQEKARLTESRRNRE--IAQLK 799
Cdd:TIGR02168  948 EYSLtleeaEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieeYEELKErydflTAQKEDLTEAKETLEeaIEEID 1027


                   ....*.
gi 291167762   800 KDQRKR 805
Cdd:TIGR02168 1028 REARER 1033
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 718-1071 1.09e-04

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: 47.36  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   718 RSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKktkvRLMKQMKEEQEKARLTESRRNREIAQ 797
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   798 LKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTG 877
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   878 AQQKMripvarvqalptpatngnrkkyqrkgltgrvfisktarmkwqlLERRVTDIIMQkmtISNMEADMNRLLKQREEL 957
Cdd:TIGR02168  831 RRIAA-------------------------------------------TERRLEDLEEQ---IEELSEDIESLAAEIEEL 864

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   958 TKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIM----QMEEAKEEGETLDVTAVINACT 1033
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreKLAQLELRLEGLEVRIDNLQER 944

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 291167762  1034 LTE-ARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:TIGR02168  945 LSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
662-836 1.27e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  662 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:COG3206   189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELES-QLAEARAELAEAEARLAALRAQLGSGPDALPE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  742 H------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRKR 805
Cdd:COG3206   259 LlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQLA 337

                         170       180       190
                  ....*....|....*....|....*....|.
gi 291167762  806 DHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 836
Cdd:COG3206   338 QLEARLAELPELEAE--LRRLEREVEVAREL 366
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
723-843 1.61e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  723 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 800
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291167762  801 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 843
Cdd:COG4717   151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 668-832 1.69e-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: 46.10  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   668 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVRSEYEKKLQAMNKELQRLQ-AAQKEHARL 745
Cdd:pfam15709  360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   746 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 825
Cdd:pfam15709  424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498


                   ....*..
gi 291167762   826 KTEEVTA 832
Cdd:pfam15709  499 QKEEEAA 505
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 657-838 1.95e-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: 45.68  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   657 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 736
Cdd:pfam13868  125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   737 AAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 809
Cdd:pfam13868  198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276

                          170       180
                   ....*....|....*....|....*....
gi 291167762   810 RLLEAQKRNQevvlrRKTEEVTALRRQVR 838
Cdd:pfam13868  277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
PRK12704 PRK12704
phosphodiesterase; Provisional
 656-795 2.03e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  656 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRL 735
Cdd:PRK12704   77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  736 QAAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 795
Cdd:PRK12704  148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
Rabaptin pfam03528
Rabaptin;
657-816 2.85e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 45.48  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   657 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSEEKAKKVRSEYEK 723
Cdd:pfam03528   24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSENTKQEAIDEVKS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   724 KLQamnKELQRLQAAQKE---------HARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQE 782
Cdd:pfam03528  101 QWQ---EEVASLQAIMKEtvreyevqfHRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAE 174

                          170       180       190
                   ....*....|....*....|....*....|....
gi 291167762   783 KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 816
Cdd:pfam03528  175 KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
 717-811 3.57e-04

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: 43.31  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  717 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 792
Cdd:cd23703    67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138

                          90
                  ....*....|....*....
gi 291167762  793 REIAQLKKDQRKRDHQLRL 811
Cdd:cd23703   139 REAKELAKKEARADALHEL 157
PRK11637 PRK11637
AmiB activator; Provisional
 659-826 4.43e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.68  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  659 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAM 728
Cdd:PRK11637  103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  729 NKELQRLQAAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 803
Cdd:PRK11637  183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257

                         170       180
                  ....*....|....*....|....*
gi 291167762  804 KR-DHQLRllEAQK-RNQEVVLRRK 826
Cdd:PRK11637  258 ARaEREAR--EAARvRDKQKQAKRK 280
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 699-836 4.84e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.56  E-value: 4.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   699 VLQNLGSVESYSEEKAKKVRSEyekKLQAMNKELQRLQAAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 774
Cdd:pfam15709  305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762   775 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 836
Cdd:pfam15709  380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 662-795 5.03e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  662 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQ-RLQAAQK 740
Cdd:PRK00409  516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762  741 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 795
Cdd:PRK00409  585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 646-843 5.09e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   646 DLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE-KAKKVRSEYEKK 724
Cdd:TIGR04523  483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKE 562

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   725 LQAMNKELQRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRK 804
Cdd:TIGR04523  563 IDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK 628

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 291167762   805 rdhqlrlLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 843
Cdd:TIGR04523  629 -------LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 663-1079 6.07e-04

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: 44.65  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   663 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNKELQRLQAAQKEH 742
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   743 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 821
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   822 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSDAPAQdtgssaaavetdasRTGAQQKMRIPVARVQALptpatngnr 901
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR--------------RQQFEEQLVELSTEVQSL--------- 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   902 kkyqrkgltgrvfisktarmkwqllerrVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENgegDKN 981
Cdd:TIGR00606  901 ----------------------------IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI---KEK 949

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   982 VANINEEMESLTANI-----DYINDSISDCQANIMQMEEAKEEGETLD-----VTAVINACTLTEaRYLLDHFLSMGINK 1051
Cdd:TIGR00606  950 VKNIHGYMKDIENKIqdgkdDYLKQKETELNTVNAQLEECEKHQEKINedmrlMRQDIDTQKIQE-RWLQDNLTLRKREN 1028

                          410       420
                   ....*....|....*....|....*...
gi 291167762  1052 GLQAAQKEaqIKVLEGRLKQTEITSATQ 1079
Cdd:TIGR00606 1029 ELKEVEEE--LKQHLKEMGQMQVLQMKQ 1054
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
658-838 7.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  658 QKLIDELENSQKRLQTLKKQYEeklmMLQHkIRDTQLERDQVLQNLGSVESYSE----EKAKKVRSEYEKKLQAMNKELQ 733
Cdd:COG4913   231 VEHFDDLERAHEALEDAREQIE----LLEP-IRELAERYAAARERLAELEYLRAalrlWFAQRRLELLEAELEELRAELA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  734 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLE 813
Cdd:COG4913   306 RLEAELERLEARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379

                         170       180
                  ....*....|....*....|....*.
gi 291167762  814 AQ-KRNQEVVLRRKtEEVTALRRQVR 838
Cdd:COG4913   380 EEfAALRAEAAALL-EALEEELEALE 404
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 710-817 7.79e-04

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


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.98  E-value: 7.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   710 SEEKAK------KVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 783
Cdd:pfam11600   10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 291167762   784 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 817
Cdd:pfam11600   83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 652-820 8.04e-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: 8.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   652 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVRSEYEKKL 725
Cdd:pfam15742   54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   726 qamnkELQRlqaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 792
Cdd:pfam15742  132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202

                          170       180       190
                   ....*....|....*....|....*....|..
gi 291167762   793 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 820
Cdd:pfam15742  203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 658-974 8.75e-04

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: 44.40  E-value: 8.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   658 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEEKaKKVRSEY---EKKL 725
Cdd:pfam01576  702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDE-RKQRAQAvaaKKKL 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   726 QAMNKELQ-RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD--- 801
Cdd:pfam01576  776 ELDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaa 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   802 ---QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSdapaqdtg 863
Cdd:pfam01576  852 serARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQ-------- 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   864 SSAAAVETDASRTGAQQkmripvarvqalptpaTNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDiiMQKMTISNM 943
Cdd:pfam01576  919 VEQLTTELAAERSTSQK----------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAAL 972

                          330       340       350
                   ....*....|....*....|....*....|....
gi 291167762   944 EADMNRLLKQREELTKRRE---KLSKRREKIVKE 974
Cdd:pfam01576  973 EAKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
WD40 pfam00400
WD domain, G-beta repeat;
1482-1523 1.07e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 1.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 291167762  1482 FQSTGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFD 1523
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 640-767 1.51e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsvESYSE- 711
Cdd:PRK00409  508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAE--KEAQQa 578

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  712 -EKAKKVRSEYEKKLQAMNKELQRLQAAQK---EHARLLKNQSQYEKQLKKLQQDVMEMK 767
Cdd:PRK00409  579 iKEAKKEADEIIKELRQLQKGGYASVKAHElieARKRLNKANEKKEKKKKKQKEKQEELK 638
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 651-815 1.55e-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: 41.43  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   651 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVRSEY--- 721
Cdd:pfam15619   17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   722 EKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 801
Cdd:pfam15619   87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164

                          170
                   ....*....|....
gi 291167762   802 QRKRDHQLRLLEAQ 815
Cdd:pfam15619  165 HKEAQEEVKILQEE 178
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 955-1047 1.60e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 1.60e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    955 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1034
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270

                            90
                    ....*....|...
gi 291167762   1035 TEARYLLDHFLSM 1047
Cdd:smart00787  271 KEIEKLKEQLKLL 283
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1581-1612 1.63e-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: 37.68  E-value: 1.63e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 291167762   1581 NAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1612
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 642-821 1.76e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   642 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQleRDQVLQNLGSVESYSEEKAKKVRSEY 721
Cdd:pfam12128  351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI--REARDRQLAVAEDDLQALESELREQL 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   722 EKKLQAMNKELQRLQAAQKEhARLLKNQSQYEKQLKklqqdvmEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKK- 800
Cdd:pfam12128  429 EAGKLEFNEEEYRLKSRLGE-LKLRLNQATATPELL-------LQLENFDERIERAREEQEAANAEVERLQSELRQARKr 500

                          170       180
                   ....*....|....*....|....*
gi 291167762   801 ----DQRKRDHQLRLLEAQKRNQEV 821
Cdd:pfam12128  501 rdqaSEALRQASRRLEERQSALDEL 525
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 722-1113 1.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  722 EKKLQAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDV----------MEMKKTKVRLMKQmkeEQEKARLTESRR 791
Cdd:COG1196   178 ERKLEATEENLERLEDILGE----------LERQLEPLERQAekaeryrelkEELKELEAELLLL---KLRELEAELEEL 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  792 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRpmsdkVAGKVTRKLSSSDAPAQDTGSSAAAVET 871
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLE 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  872 DASRTGAQQKMRIpvarvqalptpatngnrkkyqrkgltgrvfISKTARmkwqlLERRVTDIIMQKMTISNMEADMNRLL 951
Cdd:COG1196   320 ELEEELAELEEEL------------------------------EELEEE-----LEELEEELEEAEEELEEAEAELAEAE 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  952 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINA 1031
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762 1032 CTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQDLDSV 1111
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524


                  ..
gi 291167762 1112 PL 1113
Cdd:COG1196   525 AV 526
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
670-838 1.79e-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: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  670 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 749
Cdd:COG4913   226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  750 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 827
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379

                         170
                  ....*....|.
gi 291167762  828 EEVTALRRQVR 838
Cdd:COG4913   380 EEFAALRAEAA 390
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 697-832 1.79e-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: 41.43  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   697 DQVLQNLGSVESYSEEKA--KKVRSEYEKKLQAMNKELQR----LQAAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 770
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762   771 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 832
Cdd:pfam13851   92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 658-821 1.93e-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: 42.18  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  658 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSEE--KAKKVRSEYEKKL 725
Cdd:cd16269   123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEAilQADQALTEKEKEI 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  726 QAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDVMEMKKTKVRLMKQMKEE-QEKARLTESRRNREIAQLKKDQRK 804
Cdd:cd16269   201 EAERAKAEAAEQERKL----------LEEQQRELEQKLEDQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEA 270

                         170
                  ....*....|....*..
gi 291167762  805 RDHQLRLLEAQKRNQEV 821
Cdd:cd16269   271 LLEEGFKEQAELLQEEI 287
WD40 pfam00400
WD domain, G-beta repeat;
1576-1612 2.03e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 2.03e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 291167762  1576 LQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1612
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 640-831 2.31e-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: 42.57  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ---LERDQVLQNLGSVE---SYSEEK 713
Cdd:pfam07888  173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlNASERK 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   714 AKKVRSE---------------YEKKLQAMNKELQ---------------------RLQAAQKEHARLLKNQSQYEKQLK 757
Cdd:pfam07888  253 VEGLGEElssmaaqrdrtqaelHQARLQAAQLTLQladaslalregrarwaqeretLQQSAEADKDRIEKLSAELQRLEE 332

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167762   758 KLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKrnQEV-----VLRRKTEEVT 831
Cdd:pfam07888  333 RLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK--QELleyirQLEQRLETVA 405
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 671-837 2.32e-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: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   671 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEK-----AKKVRSEYEK-KLQAMNK-ELQRLQAAQKEha 743
Cdd:pfam15665   16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKrriqtLEESLEQHERmKRQALTEfEQYKRRVEERE-- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   744 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 809
Cdd:pfam15665   88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164

                          170       180
                   ....*....|....*....|....*....
gi 291167762   810 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 837
Cdd:pfam15665  165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 711-785 2.49e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 40.59  E-value: 2.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762  711 EEKAKKVRSEYEKKLQAMNKELQRLQAA-QKEhaRLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKAR 785
Cdd:COG2825    45 QKKLEKEFKKRQAELQKLEKELQALQEKlQKE--AATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELL 118
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 656-897 2.53e-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: 42.36  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   656 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDTQ------LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQA 727
Cdd:pfam04747   12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSINDQRkeafasLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQK 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   728 MNKELQRLQAAQKEHARLLKNQSQYEKQlkklqqdvmemkktkvrlmKQMKEEQEKarltesrrnreiaqLKKDQRKRDH 807
Cdd:pfam04747   92 VNAKKAAEKEARRAEAEAKKRAAQEEEH-------------------KQWKAEQER--------------IQKEQEKKEA 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   808 QLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSDAPAQDTGSSAAA--VETDASRTGAQQKM 882
Cdd:pfam04747  139 DLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAepAEQVQEITGKKNKK 218

                          250
                   ....*....|....*
gi 291167762   883 RIPVARVQALPTPAT 897
Cdd:pfam04747  219 NKKKSESEATAAPAS 233
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 697-804 2.65e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  697 DQVLQNLGSVESYSEEKAKKV---RSEYEKKLQAMNKELQRLQaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL 773
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQ--EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596

                          90       100       110
                  ....*....|....*....|....*....|.
gi 291167762  774 MKQMKEEQEKARLTESRRNREIAQLKKDQRK 804
Cdd:PRK00409  597 QKGGYASVKAHELIEARKRLNKANEKKEKKK 627
FliJ pfam02050
Flagellar FliJ protein;
662-797 2.88e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 39.57  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   662 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSvesyseekakkvrSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:pfam02050    1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISA-------------AELRNYQAFISQLDEAIAQQQQE 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762   742 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 797
Cdd:pfam02050   68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 776-1100 3.17e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   776 QMKEEQEKAR--LTESRRNREIA---------QLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 844
Cdd:TIGR02169  167 EFDRKKEKALeeLEEVEENIERLdliidekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   845 AGKvTRKLSSSDAPAQDTGSSAAAVEtdasrtgaqQKMRIPVARVQALptpaTNGNRKKYQRKGLTGRVFISKTAR---- 920
Cdd:TIGR02169  247 ASL-EEELEKLTEEISELEKRLEEIE---------QLLEELNKKIKDL----GEEEQLRVKEKIGELEAEIASLERsiae 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   921 ----MKwQLLERR---VTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLT 993
Cdd:TIGR02169  313 kereLE-DAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   994 ANIDYINDSISDCQANIMQMEEAKEE--GETLDVTAVINActltearylldhfLSMGINKgLQAAQKEAQ--IKVLEGRL 1069
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAG-------------IEAKINE-LEEEKEDKAleIKKQEWKL 457

                          330       340       350
                   ....*....|....*....|....*....|.
gi 291167762  1070 KQTEITSATQNQLLFHMLKEKAELNPELDAL 1100
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1482-1523 3.31e-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: 3.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 291167762   1482 FQSTGKLTGHLGPVMCLtvdQISSGQDLIITGSKDHYIKMFD 1523
Cdd:smart00320    2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 658-883 3.47e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   658 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR-DTQL----------------ERDQVLQNLGSVESYSEEKAKKVRSE 720
Cdd:pfam01576   18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQaETELcaeaeemrarlaarkqELEEILHELESRLEEEEERSQQLQNE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   721 yEKKLQAMNKELQRlQAAQKEHARllkNQSQYEK-----QLKKLQQDVMEMKKTKVRLMK--------------QMKEEQ 781
Cdd:pfam01576   98 -KKKMQQHIQDLEE-QLDEEEAAR---QKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKerklleeriseftsNLAEEE 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   782 EKARLTESRRNREIAQLKkdqrkrDHQLRLLEAQKRNQEVV-LRRKTE-EVTALRRQVRPMSDKVAgKVTRKLSSSDAPA 859
Cdd:pfam01576  173 EKAKSLSKLKNKHEAMIS------DLEERLKKEEKGRQELEkAKRKLEgESTDLQEQIAELQAQIA-ELRAQLAKKEEEL 245

                          250       260
                   ....*....|....*....|....
gi 291167762   860 QDTgsSAAAVETDASRTGAQQKMR 883
Cdd:pfam01576  246 QAA--LARLEEETAQKNNALKKIR 267
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
666-799 3.90e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 39.50  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  666 NSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYseekakkvRSEYEKKLQAMNKE-------------L 732
Cdd:COG2882     2 KRSFRLQTLLDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQY--------REEYEQRLQQKLQQglsaaqlrnyqqfI 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291167762  733 QRLQAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 799
Cdd:COG2882    74 ARLDEAIEQQQQQVAQaEQQVEQARQAWLEARQERKALEKLKERRREEERQEENRREQKELDELASRR 141
Caldesmon pfam02029
Caldesmon;
563-836 4.07e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.78  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   563 EESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIdggessdeSDSESDEKAN 642
Cdd:pfam02029  105 ENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEA--------EEVPTENFAK 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   643 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQvlqnlgsveSYSEEKAKKVRSEYE 722
Cdd:pfam02029  177 EEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ---------SQEREEEAEVFLEAE 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   723 KKLqamnkELQRLQAAQKEharllknqsqyEKQLKKLQQdvmemkktkvrlmKQMKEEQE----KARLTESRRNREIAQL 798
Cdd:pfam02029  248 QKL-----EELRRRRQEKE-----------SEEFEKLRQ-------------KQQEAELEleelKKKREERRKLLEEEEQ 298

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 291167762   799 KKDQRKRDHQLRLLEAQKRNQEVVLRRKTEevTALRRQ 836
Cdd:pfam02029  299 RRKQEEAERKLREEEEKRRMKEEIERRRAE--AAEKRQ 334
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
304-513 4.51e-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: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206    96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206   174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  445 ----------TVDALRSRITQLVSDQANhVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 513
Cdd:COG3206   254 dalpellqspVIQQLRAQLAELEAELAE-LSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 560-843 4.59e-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: 41.65  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   560 QKLEESNREERSVAGKEDNTDTDQEKKEEKgvSERENNELEVEESQEVSDHEDEEeeeeeeeddidggessdesdsesde 639
Cdd:pfam17380  316 RKLEEAEKARQAEMDRQAAIYAEQERMAME--RERELERIRQEERKRELERIRQE------------------------- 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   640 kanyqadlanitcEIAIKQKLIDELEnsqkRLQTLKKQYEEKL---MMLQHKIRDTQLERDQVLQNlgsvesySEEKAKK 716
Cdd:pfam17380  369 -------------EIAMEISRMRELE----RLQMERQQKNERVrqeLEAARKVKILEEERQRKIQQ-------QKVEMEQ 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   717 VRSEYEkklQAMNKELQRLQAAQ-KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLmkqMKEEQEKARLTESRR---N 792
Cdd:pfam17380  425 IRAEQE---EARQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---EKEKRDRKRAEEQRRkilE 498

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167762   793 REIAQLKK----DQRKR--------DHQLRLLEAQKRNQEVVLRRKTEEVTALRR---QVRPMSDK 843
Cdd:pfam17380  499 KELEERKQamieEERKRkllekemeERQKAIYEEERRREAEEERRKQQEMEERRRiqeQMRKATEE 564
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 708-862 5.09e-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: 40.14  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   708 SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHArllknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLT 787
Cdd:pfam14988    7 EYLAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762   788 ESrRNREIAQLKKDQRK--RDHQLRLLEAQKRnqevVLRRKteevTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDT 862
Cdd:pfam14988   81 ES-QEREIQDLEEEKEKvrAETAEKDREAHLQ----FLKEK----ALLEKQLQELRILELGERATRELKRKAQALKL 148
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 640-758 5.10e-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: 40.29  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMM---------LQHKIRDTQLER----DQVLQNLGSV 706
Cdd:COG1579    40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRIsdleDEILELMERI 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  707 ESYSEEKA-------------KKVRSEYEKKLQAMNKELQRLQAAQKEHA-----RLLKnqsQYEKQLKK 758
Cdd:COG1579   120 EELEEELAeleaelaeleaelEEKKAELDEELAELEAELEELEAEREELAakippELLA---LYERIRKR 186
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 685-813 5.77e-03

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


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 39.53  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   685 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVRSEYEKKLQA-------MNKELQR----LQ 736
Cdd:pfam14073    9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167762   737 AAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 813
Cdd:pfam14073   89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
XRCC4 pfam06632
DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of ...
 703-808 6.20e-03

DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of several eukaryotic DNA double-strand break repair and V(D)J recombination protein XRCC4 sequences. In the non-homologous end joining pathway of DNA double-strand break repair, the ligation step is catalyzed by a complex of XRCC4 and DNA ligase IV. It is thought that XRCC4 and ligase IV are essential for alignment-based gap filling, as well as for final ligation of the breaks.


Pssm-ID: 369011 [Multi-domain]  Cd Length: 336  Bit Score: 40.86  E-value: 6.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   703 LGSVESYS-EEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKK-------LQQD-------VMEMK 767
Cdd:pfam06632  112 LGSVKLQKvPEPAEVIRELISYCLDCIAELQAKNEHLQKENERLQRDWNDVTGRLEKcvkakeeLEADlykrfilVLNEK 191

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 291167762   768 KTKVRLMKQMKEEQEKARLTESRRNREIAqlkKDQRKRDHQ 808
Cdd:pfam06632  192 KAKIRSLQKLLNELQESEESTEQKREDPA---TSDRTPDEE 229
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 670-799 6.21e-03

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


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.84  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   670 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE-KKLQAMNKELQRLQAAQKEHARLL- 746
Cdd:TIGR02473    6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 291167762   747 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 799
Cdd:TIGR02473   86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 658-778 6.64e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.18  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   658 QKLIDELENSQKRLQTLKKQYEEklmmlqhkIRDTQ---LER-DQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNK 730
Cdd:pfam10168  578 QSLEEERKSLSERAEKLAEKYEE--------IKDKQeklMRRcKKVLQRLNSQLpvlSDAEREMKKELETINEQLKHLAN 649

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762   731 ELQRLQAAQKEHAR-LLKNQSQY--------EKQLKKLQQDVMEMKKTKVRLMKQMK 778
Cdd:pfam10168  650 AIKQAKKKMNYQRYqIAKSQSIRkksslslsEKQRKTIKEILKQLGSEIDELIKQVK 706
PRK11637 PRK11637
AmiB activator; Provisional
 657-803 7.26e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.83  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  657 KQKLIDELENSQKRLQTLKKQYEEKlmmlqhkirdtQLERDQVLqnlgsvesySEEKAKKvrseyekklqamnkelQRLQ 736
Cdd:PRK11637  168 RQETIAELKQTREELAAQKAELEEK-----------QSQQKTLL---------YEQQAQQ----------------QKLE 211

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762  737 AAQKEHARLLknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQR 803
Cdd:PRK11637  212 QARNERKKTL---TGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQK 275
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 661-765 7.39e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 38.71  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   661 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDtqlERDQVLQNLGSVESYSEEKakkvrseyEKKLQAMNKELQRLQAAQK 740
Cdd:pfam03938   14 SPEGKAAQAQLEKKFKKRQAELEAKQKELQK---LYEELQKDGALLEEEREEK--------EQELQKKEQELQQLQQKAQ 82

                           90       100
                   ....*....|....*....|....*
gi 291167762   741 EharllKNQSQYEKQLKKLQQDVME 765
Cdd:pfam03938   83 Q-----ELQKKQQELLQPIQDKINK 102
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 728-845 8.05e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   728 MNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKarltesrRNREIAQLKKDqrkrdh 807
Cdd:pfam03938    7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREE-------KEQELQKKEQE------ 73

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 291167762   808 qlrLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:pfam03938   74 ---LQQLQQKAQQELQKKQQELLQPIQDKINKAIKEVA 108
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 655-794 8.63e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 8.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   655 AIKQKLIDELENSQKRlQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL-----GSVESYSE--EKAKKVRSEYEKKLQA 727
Cdd:pfam01576  303 ALKTELEDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMrqkhtQALEELTEqlEQAKRNKANLEKAKQA 381

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167762   728 MNKELQRLQAaqkeharllknqsqyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNRE 794
Cdd:pfam01576  382 LESENAELQA-----------------ELRTLQQAKQDSEHKRKKLEGQLQELQ--ARLSESERQRA 429
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 712-838 9.38e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 39.64  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762  712 EKAKKVRSEYEKKLQAMNKELQRLqAAQKEHARllKNQSQYEKQL-KKLQQDVMEMKKTKVRLmKQMKEEQEKARLTESR 790
Cdd:cd07652    75 EKLADNGLRFAKALNEMSDELSSL-AKTVEKSR--KSIKETGKRAeKKVQDAEAAAEKAKARY-DSLADDLERVKTGDPG 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167762  791 R--------NREIAQLKKD-QRK-----RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 838
Cdd:cd07652   151 KklkfglkgNKSAAQHEDElLRKvqaadQDYASKVNAAQALRQELLSRHRPEAVKDLFDLIL 212
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 666-792 9.45e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 40.41  E-value: 9.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762    666 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 745
Cdd:smart00435  266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 291167762    746 LKNQSQYEKQLKKLQQDVMEMKKTkvrlmKQMKEEQEKARLTESRRN 792
Cdd:smart00435  335 KKKEEKKKKQIERLEERIEKLEVQ-----ATDKEENKTVALGTSKIN 376
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 365-829 9.50e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   365 ANRARNIKNKVMVNQDRASQQINALRSEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQE 444
Cdd:pfam02463  539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   445 TVDALR--------SRITQLVSDQANHVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARAPY 516
Cdd:pfam02463  619 DKRAKVvegilkdtELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   517 FSGSSTFSPTILSSDKETIEI-------IDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEK 589
Cdd:pfam02463  699 LEIKKKEQREKEELKKLKLEAeelladrVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   590 GVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGessdesdsesdekanYQADLANITCEIAIKQKLIDELENSQK 669
Cdd:pfam02463  779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEL---------------LEEEQLLIEQEEKIKEEELEELALELK 843

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   670 RLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEH------- 742
Cdd:pfam02463  844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEneieeri 923

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167762   743 ARLLKNQSQYEKQLKKL------QQDVMEMKKTKVR-LMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 815
Cdd:pfam02463  924 KEEAEILLKYEEEPEELlleeadEKEKEENNKEEEEeRNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003

                          490
                   ....*....|....
gi 291167762   816 KRNQEVVLRRKTEE 829
Cdd:pfam02463 1004 KKKLIRAIIEETCQ 1017
 
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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