NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462532900|ref|XP_054228477|]
View 

kinesin-like protein KIF21A isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2462532900    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372     81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372    151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372    228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462532900  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 ...
1315-1628 1.15e-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: 1.15e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1315 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1391
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1392 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1470
Cdd:cd00200     81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1471 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1548
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1549 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1626
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                   ..
gi 2462532900 1627 WK 1628
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 2462532900  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                   ..
gi 2462532900 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 3.43e-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: 3.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 719
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  720 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 790
Cdd:COG4942    101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  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 1.35e-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: 56.37  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKE 587
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  588 EKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENS 667
Cdd:pfam10174  493 EK---ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVA 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  668 QKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLL 746
Cdd:pfam10174  569 RYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRR 644
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  747 KNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEV 821
Cdd:pfam10174  645 EDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEA 713
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2462532900  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 2462532900    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372     81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372    151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372    228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462532900  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372    297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 6.18e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 6.18e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462532900  327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-378 8.19e-138

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: 8.19e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900     9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129  147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900   322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 2.88e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 305.89  E-value: 2.88e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059     53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059    126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059    190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059    249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059    328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  442 MQETVDALRSRITQLVSDQANHVLARaGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059    399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-404 3.89e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.53  E-value: 3.89e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188    94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188   168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188   245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188   313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188   380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458

                   ....*...
gi 2462532900  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 ...
1315-1628 1.15e-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: 1.15e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1315 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1391
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1392 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1470
Cdd:cd00200     81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1471 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1548
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1549 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1626
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                   ..
gi 2462532900 1627 WK 1628
Cdd:cd00200    288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1314-1631 6.58e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 6.58e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1314 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1385
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1386 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1461
Cdd:COG2319    183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1462 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1539
Cdd:COG2319    240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1540 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1617
Cdd:COG2319    311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389
                          330
                   ....*....|....
gi 2462532900 1618 AADDRTVRIWKARN 1631
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 2462532900  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                   ..
gi 2462532900 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 3.43e-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: 3.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 719
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  720 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 790
Cdd:COG4942    101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  791 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 860
Cdd:COG4942    181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-1023 1.93e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 716
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  717 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 794
Cdd:PRK03918   385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 867
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  868 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 931
Cdd:PRK03918   540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  932 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 1006
Cdd:PRK03918   620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
                          410
                   ....*....|....*..
gi 2462532900 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 3.06e-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: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 719
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  720 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 796
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  797 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 871
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  872 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 951
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  952 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1027
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          410
                   ....*....|.
gi 2462532900 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 3.95e-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: 61.61  E-value: 3.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  643 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 722
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  723 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 794
Cdd:TIGR02168  365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  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 1.35e-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: 56.37  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKE 587
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  588 EKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENS 667
Cdd:pfam10174  493 EK---ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVA 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  668 QKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLL 746
Cdd:pfam10174  569 RYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRR 644
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  747 KNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEV 821
Cdd:pfam10174  645 EDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEA 713
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2462532900  822 VL------------------RRKT--EEVTALRRQ 836
Cdd:pfam10174  714 LLaaisekdaniallelsssKKKKtqEEVMALKRE 748
WD40 pfam00400
WD domain, G-beta repeat;
1314-1349 1.13e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462532900 1314 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1349
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
564-1071 2.36e-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: 2.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  564 ESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANY 643
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEK 723
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEE 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  724 KLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQR 803
Cdd:COG1196    443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLR 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  804 KRDHQLRLLeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMR 883
Cdd:COG1196    521 GLAGAVAVL----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  884 IPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRR 961
Cdd:COG1196    597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLE 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  962 EKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLL 1041
Cdd:COG1196    677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELL 748
                          490       500       510
                   ....*....|....*....|....*....|
gi 2462532900 1042 DHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:COG1196    749 EEEALEELPEPPDLEELERELERLEREIEA 778
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1312-1349 3.62e-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: 3.62e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 2462532900  1312 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1349
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
713-1117 7.64e-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: 50.83  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  713 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 788
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  789 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEvvlRRKTEEVTALRRQVRPMSDKVAGKvtRKLSSSDAPAQDTgssaaA 868
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQK--QILRERLANLERQ-----L 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  869 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 948
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  949 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1028
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1029 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1096
Cdd:TIGR02168  465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
                          410       420
                   ....*....|....*....|..
gi 2462532900 1097 -LDALLGHALQeNVEDSTDEDA 1117
Cdd:TIGR02168  538 aIEAALGGRLQ-AVVVENLNAA 558
PTZ00121 PTZ00121
MAEBL; Provisional
557-1021 8.97e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 8.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  557 KRLQKLEESNREERSVAGKEDNTDTDQ-EKKEEKGVSERENNELEVEESQEVSDheDEEEEEEEEEDDIDGGESSDESDS 635
Cdd:PTZ00121  1293 DEAKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADEAEAAEEKAEAAE 1370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  636 ESDEKANYQADLANITCEIAIK-QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 714
Cdd:PTZ00121  1371 KKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  715 KKvrSEYEKKLQAMNKelqrlQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 794
Cdd:PTZ00121  1451 KK--AEEAKKAEEAKK-----KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  795 IAQLKK-DQRKRDHQLRLLEAQKRNQEVVLR---RKTEEVTALRRQVRPMSDKvaGKVTRKLSSSDAPAQDTGSSAAAVE 870
Cdd:PTZ00121  1524 ADEAKKaEEAKKADEAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKLY 1601
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  871 TDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKmtisNMEADMnrl 950
Cdd:PTZ00121  1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK----KAEEDK--- 1674
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532900  951 lKQREELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSIsdcQANIMQMEEAKEEGE 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 9.47e-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: 9.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  446 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsp 525
Cdd:TIGR02168  735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------- 798
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  526 tilssdKETIEIIDLAKKDLEKLKRKEKRKKKrlqklEESNREERSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQ 605
Cdd:TIGR02168  799 ------KALREALDELRAELTLLNEEAANLRE-----RLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELE 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  606 EvsdhedeeeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMML 685
Cdd:TIGR02168  866 E------------------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  686 QHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
717-811 3.51e-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: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  717 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 792
Cdd:cd23703     67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138
                           90
                   ....*....|....*....
gi 2462532900  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 1.61e-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: 1.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   955 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1034
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270
                            90
                    ....*....|...
gi 2462532900  1035 TEARYLLDHFLSM 1047
Cdd:smart00787  271 KEIEKLKEQLKLL 283
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
666-792 9.47e-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: 9.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   666 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 745
Cdd:smart00435  266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2462532900   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 2462532900    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372     81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372    151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372    228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462532900  328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372    297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 6.18e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 6.18e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225  218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462532900  327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-378 8.19e-138

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: 8.19e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900     9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129  147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129  213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900   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 6.88e-121

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: 382.76  E-value: 6.88e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:cd00106      1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   83 TVFAYGQTGAGKTYTMGTGFDvniveEELGIISRAVKHLFKSIEEKKhiaikngLPAPDFKVNAQFLELYNEEVLDLFDt 162
Cdd:cd00106     80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRK-------ETKSSFSVSASYLEIYNEKIYDLLS- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  163 trdidaKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:cd00106    147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV-------- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  243 idadnatDNKIISESAQMnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 322
Cdd:cd00106    213 -------KQRNREKSGES----VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2462532900  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 6.91e-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: 6.91e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGY 80
Cdd:cd01371      2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   81 NATVFAYGQTGAGKTYTMGtGFDVNivEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVldlf 160
Cdd:cd01371     82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIARSQNNQ--------QFLVRVSYLEIYNEEI---- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  161 dttRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 239
Cdd:cd01371    147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  240 cpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 319
Cdd:cd01371    220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  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 3.47e-102

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 331.23  E-value: 3.47e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYI 66
Cdd:cd01370      1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVN 145
Cdd:cd01370     81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKD--------EKEFEVS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  146 AQFLELYNEEVLDLFDTTrdidakSKKSNIRihEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSR 225
Cdd:cd01370    146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  226 SHAIFTIHVCQTrvcpqidadnatdnkiiSESAQMNEfETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 305
Cdd:cd01370    218 SHAVLQITVRQQ-----------------DKTASINQ-QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  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 6.45e-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: 6.45e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYIQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366      4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   86 AYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01366     83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  165 didAKSKKSNIRiHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqid 244
Cdd:cd01366    149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILH----------- 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  245 adnatdnkIISESAQMNEfeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 324
Cdd:cd01366    214 --------ISGRNLQTGE--ISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2462532900  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 5.72e-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: 317.37  E-value: 5.72e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYiQC 68
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVY-ED 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   69 I-EKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvniveEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQ 147
Cdd:cd01365     80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  148 FLELYNEEVLDLFDTtrdiDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSH 227
Cdd:cd01365    147 YMEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSH 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  228 AIFTIhvcqtrVCPQIDADNATDNKiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNV 307
Cdd:cd01365    223 AVFTI------VLTQKRHDAETNLT-----------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKV 285
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  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 7.70e-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: 7.70e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01369      1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   85 FAYGQTGAGKTYTMgtgFDVNIVEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01369     81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIYSMDENL--------EFHVKVSYFEIYMEKIRDLLDVSK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  165 DidakskksNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqid 244
Cdd:cd01369    150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  245 aDNATDNKIisesaqmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 324
Cdd:cd01369    214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2462532900  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 2.34e-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: 2.34e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01364      1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   79 GYNATVFAYGQTGAGKTYTM----GTGFDVNIVEEEL-GIISRAVKHLFKSIEEKKHiaiknglpapDFKVNAQFLELYN 153
Cdd:cd01364     81 GYNCTIFAYGQTGTGKTYTMegdrSPNEEYTWELDPLaGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  154 EEVLDLFDttrdiDAKSKKSNIRIHEDS--TGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 231
Cdd:cd01364    151 EELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  232 IHVcqtrvcpqidadnatdnkIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 311
Cdd:cd01364    226 ITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL 287
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462532900  312 GDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364    288 VERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-511 2.88e-90

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 305.89  E-value: 2.88e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059     53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059    126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059    190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059    249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059    328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  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 2.99e-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: 2.99e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   89 QTGAGKTYTM--GTGFDVNIVEEELGIISRAVKHLFKSI--EEKKHIAIKNglpapdFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01373     83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIqrEKEKAGEGKS------FLCKCSFLEIYNEQIYDLLDPA- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01373    156 -------SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------ 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  245 adnatdnkIISESAQMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVP 322
Cdd:cd01373    217 --------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVC 288
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532900  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 6.30e-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: 292.70  E-value: 6.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01374      1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   85 FAYGQTGAGKTYTMGTGfdvnivEEELGIISRAVKHLFKSIEEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01374     77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDT---------PDREFLLRVSYLEIYNEKINDLLSPT- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01374    141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRI------------ 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  245 adnatdnkIISESAQMNEFE--TLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHVP 322
Cdd:cd01374    202 --------TIESSERGELEEgtVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIP 272
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2462532900  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 3.95e-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: 247.42  E-value: 3.95e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNAT 83
Cdd:cd01376      2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   84 VFAYGQTGAGKTYTMGTGFdvniveEELGIISRAVKHLFKSIEEKkhiaiknglpAPDFKVNAQFLELYNEEVLDLFDtt 163
Cdd:cd01376     81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLLQMTRKE----------AWALSFTMSYLEIYQEKILDLLE-- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  164 rdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqi 243
Cdd:cd01376    143 ------PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  244 dadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 323
Cdd:cd01376    208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2462532900  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 1.90e-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: 1.90e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   10 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01367      2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   79 GYNATVFAYGQTGAGKTYTMGTGFDVNivEEELGIISRAVKHLFksiEEKKHIAIKNGLpapdfKVNAQFLELYNEEVLD 158
Cdd:cd01367     82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVF---RLLNKLPYKDNL-----GVTVSFFEIYGGKVFD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  159 LFdttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFtihvcqtr 238
Cdd:cd01367    152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAIL-------- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  239 vcpQIDADNATDNKiisesaqmnefetLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 317
Cdd:cd01367    215 ---QIILRDRGTNK-------------LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462532900  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 6.29e-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: 6.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   46 DKAFTFDYVFDiDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNIVEEelGIISRAVKHLFKSI 125
Cdd:cd01375     47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENYKHR--GIIPRALQQVFRMI 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  126 EEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKsnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCL 205
Cdd:cd01375    123 EER---------PTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  206 KLGALSRTTASTQMNVQSSRSHAIFTIHVCqtrvcpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375    192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE-------------------AHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  286 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375    253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330

                   ....
gi 2462532900  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 4.86e-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: 4.86e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYIQCIEKLIE 74
Cdd:cd01368      3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   75 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIeekkhiaiknglpaPDFKVNAQFLELYN 153
Cdd:cd01368     83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  154 EEVLDLFDTTRDIDAKSKKSnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 233
Cdd:cd01368    142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  234 VCQtrvcpqidADNATDNKIISESAQMNefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368    221 LVQ--------APGDSDGDVDQDKDQIT-----VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462532900  314 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368    288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-404 3.89e-63

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 237.53  E-value: 3.89e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188    94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188   168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188   245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188   313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188   380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458

                   ....*...
gi 2462532900  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 ...
1315-1628 1.15e-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: 1.15e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1315 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1391
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1392 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1470
Cdd:cd00200     81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1471 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1548
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1549 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1626
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287

                   ..
gi 2462532900 1627 WK 1628
Cdd:cd00200    288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1314-1631 6.58e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 6.58e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1314 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1385
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1386 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1461
Cdd:COG2319    183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1462 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1539
Cdd:COG2319    240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1540 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1617
Cdd:COG2319    311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389
                          330
                   ....*....|....
gi 2462532900 1618 AADDRTVRIWKARN 1631
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 2462532900  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80

                   ..
gi 2462532900 1016 AK 1017
Cdd:cd22263     81 AK 82
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1314-1588 1.04e-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: 1.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1314 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1390
Cdd:cd00200     84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1391 IRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1469
Cdd:cd00200    164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1470 PVMCLTVDQissgqdliitgskDHYIkmfdvtegalgtvspthnfepphydgiealtiqgdnLFSGSRDNGIKKWDLTQK 1549
Cdd:cd00200    221 GVNSVAFSP-------------DGYL------------------------------------LASGSEDGTIRVWDLRTG 251
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462532900 1550 DLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1588
Cdd:cd00200    252 ECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1420-1640 1.20e-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: 1.20e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1420 TVAIPSGENQINQIALNPTGTFLYAASGNA-VRMWDLKRFQSTGKLTGHLGPVmcLTVDQISSGQdLIITGSKDHYIKMF 1498
Cdd:cd00200      2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPV--RDVAASADGT-YLASGSSDKTIRLW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1499 DvtegaLGTVSPTHNFEPpHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLL 1576
Cdd:cd00200     79 D-----LETGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVA 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900 1577 SGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWkarNLQDGQISDT 1640
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 1.37e-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: 1.37e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEgDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22248      1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKD-ESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79

                   ..
gi 2462532900 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 3.84e-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: 3.84e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  936 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1015
Cdd:cd22262      1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80

                   ..
gi 2462532900 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 2.98e-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: 2.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900    9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYiQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796   21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532900   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 ...
1313-1454 1.87e-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: 1.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1313 LQCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1389
Cdd:cd00200    167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900 1390 DIRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWD 1454
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 7.84e-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: 7.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYIQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   91 GAGKTYTMgtgfdvniveeeLGIISRAVKHLFKSIEEKKhiaiknglpapdfkvnaqflelyneevldlfdttrdidaks 170
Cdd:cd01363     62 GAGKTETM------------KGVIPYLASVAFNGINKGE----------------------------------------- 88
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  171 kksnirihEDStggiyTVGVTTRTVNTESEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqidadnatd 250
Cdd:cd01363     89 --------TEG-----WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  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 3.43e-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: 3.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 719
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  720 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 790
Cdd:COG4942    101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  791 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 860
Cdd:COG4942    181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
WD40 COG2319
WD40 repeat [General function prediction only];
1529-1636 2.51e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 64.55  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1529 GDNLFSGSRDNGIKKWDLTQKDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAI 1608
Cdd:COG2319     48 GARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSV 126
                           90       100       110
                   ....*....|....*....|....*....|
gi 2462532900 1609 CV--NSTHIFTAADDRTVRIWkarNLQDGQ 1636
Cdd:COG2319    127 AFspDGKTLASGSADGTVRLW---DLATGK 153
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-1023 1.93e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 716
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  717 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 794
Cdd:PRK03918   385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 867
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  868 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 931
Cdd:PRK03918   540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  932 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 1006
Cdd:PRK03918   620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
                          410
                   ....*....|....*..
gi 2462532900 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 3.06e-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: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 719
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  720 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 796
Cdd:pfam05483  479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  797 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 871
Cdd:pfam05483  558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  872 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 951
Cdd:pfam05483  632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  952 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1027
Cdd:pfam05483  700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
                          410
                   ....*....|.
gi 2462532900 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 3.95e-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: 61.61  E-value: 3.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  643 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 722
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  723 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 794
Cdd:TIGR02168  365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  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 9.09e-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: 9.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  645 ADLANITCEIAIKQKLIDELENSQKRLQTLKKQyEEKLMMLQHKIRDTQlerdqvlqnlGSVESYSEEKAKKVRSEYEKK 724
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYE----------GYELLKEKEALERQKEAIERQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  725 LQAMNKELQ----RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQmkeeqekarltesrrnrEIAQLKK 800
Cdd:TIGR02169  246 LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA-----------------EIASLER 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  801 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQ 880
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  881 KmripvARVQALptpatngnrKKYQRKgltgRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKR 960
Cdd:TIGR02169  388 K-----DYREKL---------EKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  961 REKLSKRREKIVKEngegdknVANINEEMESLTANIDYINDSISDCQANIMQMEEAK-----EEGETLDVTAVINA 1031
Cdd:TIGR02169  450 IKKQEWKLEQLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
668-1170 1.26e-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: 60.13  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  668 QKRLQTLKKQYEEK--LMMLQHKIRDTQLERDQVLQNLGSVEsyseeKAKKVRSEyekkLQAMNKELQRLQaaqkEHARl 745
Cdd:pfam15921  244 EDQLEALKSESQNKieLLLQQHQDRIEQLISEHEVEITGLTE-----KASSARSQ----ANSIQSQLEIIQ----EQAR- 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  746 lkNQ-SQYEKQLKKLQQDVMEMKkTKVRLMKQMKE----EQEK------ARLTESRRNREiaQLKKDQRKRDHQLRLLEA 814
Cdd:pfam15921  310 --NQnSMYMRQLSDLESTVSQLR-SELREAKRMYEdkieELEKqlvlanSELTEARTERD--QFSQESGNLDDQLQKLLA 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  815 --QKRNQEVVLRRKTEEvtalRRQVRPMSDKVA-GKVTRKLSSSDAPAQDTGSSAAAVETDAsrtgaQQKMRIPVARVQA 891
Cdd:pfam15921  385 dlHKREKELSLEKEQNK----RLWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAMKSEC-----QGQMERQMAAIQG 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  892 lptpatnGNRKKYQRKGLTGRVFISKtarmkwQLLERRVTDIIMQKMTISNME---ADMNRLLKQREE-LTKRREKLSKR 967
Cdd:pfam15921  456 -------KNESLEKVSSLTAQLESTK------EMLRKVVEELTAKKMTLESSErtvSDLTASLQEKERaIEATNAEITKL 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  968 REKIvkengegDKNVaninEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETL-----DVTAVINACTLTEARYLLD 1042
Cdd:pfam15921  523 RSRV-------DLKL----QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILrqqieNMTQLVGQHGRTAGAMQVE 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1043 HF-LSMGINKGLQAAQ--------KEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLghalqENVEDST 1113
Cdd:pfam15921  592 KAqLEKEINDRRLELQefkilkdkKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL-----NEVKTSR 666
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532900 1114 DEdapLNSpgsegstLSSDLMKLCGEVKPKNKARRRTTTQMEL-LYADSSELASDTST 1170
Cdd:pfam15921  667 NE---LNS-------LSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNT 714
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 2462532900  642 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVR 718
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  719 SEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 792
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  793 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
PTZ00121 PTZ00121
MAEBL; Provisional
533-830 4.41e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 4.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  533 ETIEIIDLAKKDLEKLKRKekrkKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHED 612
Cdd:PTZ00121  1428 EEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  613 EEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEI--AIKQKLIDELENSQ--KRLQTLKKQYEEKLMMLQHK 688
Cdd:PTZ00121  1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEekKKAEEAKKAEEDKNMALRKA 1583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  689 IRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAmnKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK 768
Cdd:PTZ00121  1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  769 TKVRLMKqmKEEQEKARLTESRRNREiaqlkkDQRKRDHQLRLLEAQKRNQEVVLRRKTEEV 830
Cdd:PTZ00121  1662 KAAEEAK--KAEEDKKKAEEAKKAEE------DEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
640-880 1.31e-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: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 714
Cdd:COG3883     32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  715 KKVrSEYEKKLQAMNkelqRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 794
Cdd:COG3883    112 ESF-SDFLDRLSALS----KIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  795 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDAS 874
Cdd:COG3883    184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263

                   ....*.
gi 2462532900  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 1.35e-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: 56.37  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKE 587
Cdd:pfam10174  423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  588 EKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENS 667
Cdd:pfam10174  493 EK---ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVA 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  668 QKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLL 746
Cdd:pfam10174  569 RYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRR 644
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  747 KNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEV 821
Cdd:pfam10174  645 EDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEA 713
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2462532900  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 2462532900  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDT-QLERDQVLQNLGSvesySEEKAKKVRSEYE 722
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQA----ELSKLEEEVSRIE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  723 KKLQAMNKELQRL----QAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 798
Cdd:TIGR02169  812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462532900  799 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 838
Cdd:TIGR02169  888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
PTZ00121 PTZ00121
MAEBL; Provisional
655-1018 5.38e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 5.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  655 AIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQR 734
Cdd:PTZ00121  1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  735 LQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLtesrRNREIAQLKKDQRKRDHQLRLLEA 814
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI----KAAEEAKKAEEDKKKAEEAKKAEE 1685
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  815 QKRNQEVVLRRKTEEvtalRRQVRPMSDKVAGKVtRKLSSSDAPAQDTGSSAaaveTDASRTGAQQKMRIPVARVQalpt 894
Cdd:PTZ00121  1686 DEKKAAEALKKEAEE----AKKAEELKKKEAEEK-KKAEELKKAEEENKIKA----EEAKKEAEEDKKKAEEAKKD---- 1752
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  895 patNGNRKKYQRkgltgrvfISKTARMKWQLLERRVTDIImqkmtisnmeadmnrllkqREELTKRREKLSKRREKIVKE 974
Cdd:PTZ00121  1753 ---EEEKKKIAH--------LKKEEEKKAEEIRKEKEAVI-------------------EEELDEEDEKRRMEVDKKIKD 1802
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  975 ---NGE-----GDKNVANINEEMESLTANIDYINDSISdcqaniMQMEEAKE 1018
Cdd:PTZ00121  1803 ifdNFAniiegGKEGNLVINDSKEMEDSAIKEVADSKN------MQLEEADA 1848
WD40 pfam00400
WD domain, G-beta repeat;
1314-1349 1.13e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462532900 1314 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1349
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
644-1176 1.24e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  644 QADLANITCEIAIKQKLIDELENsqkRLQTLKKQYEE----KLMMLQHKIRDTQLERDQVLQNLGSVES----------Y 709
Cdd:COG4913    301 RAELARLEAELERLEARLDALRE---ELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAllaalglplpA 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  710 SEEKAKKVRSEYEKKLQAMNKELQRLQAAQkehARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMkeEQEKARLTES 789
Cdd:COG4913    378 SAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDALAEA 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  790 RRNREIA--------QLKKDQRK---------RDHQLRLLEAQKRNQEVV-------LRRK--TEEVTALRRQVRPMSDK 843
Cdd:COG4913    453 LGLDEAElpfvgeliEVRPEEERwrgaiervlGGFALTLLVPPEHYAAALrwvnrlhLRGRlvYERVRTGLPDPERPRLD 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  844 vAGKVTRKLSSSDAPAQD-----TGSSAAAVETDASRTGAQQKMRIpvarvqalpTPA--TNGNRKKYQ---RKGLTGRV 913
Cdd:COG4913    533 -PDSLAGKLDFKPHPFRAwleaeLGRRFDYVCVDSPEELRRHPRAI---------TRAgqVKGNGTRHEkddRRRIRSRY 602
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  914 FISKTARMKWQLLERRVTDIimqkmtisnmEADMNRLLKQREELTKRREKLSKRREKI--VKENGEGDKNVANINEEMES 991
Cdd:COG4913    603 VLGFDNRAKLAALEAELAEL----------EEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAE 672
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  992 LTANIDYINDSISDCQANIMQMEEAKEEGETLDvtAVINACTLTEARylldhflsmginKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:COG4913    673 LEAELERLDASSDDLAALEEQLEELEAELEELE--EELDELKGEIGR------------LEKELEQAEEELDELQDRLEA 738
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1072 TEItsatqnqllfhmlKEKAELNPELDALLGHALQENVEDSTDEDaplnspgsegstLSSDLMKLCGEvkpKNKARRRTT 1151
Cdd:COG4913    739 AED-------------LARLELRALLEERFAAALGDAVERELREN------------LEERIDALRAR---LNRAEEELE 790
                          570       580
                   ....*....|....*....|....*
gi 2462532900 1152 TQMELLYADSSELASDTSTGDASLP 1176
Cdd:COG4913    791 RAMRAFNREWPAETADLDADLESLP 815
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
564-1071 2.36e-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: 2.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  564 ESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANY 643
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEK 723
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEE 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  724 KLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQR 803
Cdd:COG1196    443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLR 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  804 KRDHQLRLLeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMR 883
Cdd:COG1196    521 GLAGAVAVL----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  884 IPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRR 961
Cdd:COG1196    597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLE 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  962 EKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLL 1041
Cdd:COG1196    677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELL 748
                          490       500       510
                   ....*....|....*....|....*....|
gi 2462532900 1042 DHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:COG1196    749 EEEALEELPEPPDLEELERELERLEREIEA 778
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
712-838 2.66e-06

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 47.99  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  712 EKAKKVRSEYEKKLQamnkelqrlqaaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 791
Cdd:pfam20492    2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  792 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 838
Cdd:pfam20492   58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
653-845 3.13e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  653 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE--KAKKVRSEYEKKLQAMN 729
Cdd:PRK03918   148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLE 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  730 KELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARltesrRNREIAQLKKDQRKRDHQL 809
Cdd:PRK03918   228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSEFY 302
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462532900  810 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1312-1349 3.62e-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: 3.62e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 2462532900  1312 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1349
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
PTZ00121 PTZ00121
MAEBL; Provisional
653-970 4.33e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  653 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESysEEKAKKVRSEYEKKlqamnKEL 732
Cdd:PTZ00121  1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKK-----KAD 1293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  733 QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRD-HQLRL 811
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKK 1373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  812 LEAQKRNQEvvLRRKTEEV-TALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAV-ETDASRTGAQQKMRIPVARV 889
Cdd:PTZ00121  1374 EEAKKKADA--AKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkKADEAKKKAEEAKKADEAKK 1451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  890 QALPTPATNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDIIMQKMTISNMEADMnrlLKQREELTKRREKLSKRRE 969
Cdd:PTZ00121  1452 KAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEE 1520

                   .
gi 2462532900  970 K 970
Cdd:PTZ00121  1521 A 1521
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1591-1628 6.79e-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: 6.79e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 2462532900  1591 TFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWK 1628
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
713-1117 7.64e-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: 50.83  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  713 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 788
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  789 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEvvlRRKTEEVTALRRQVRPMSDKVAGKvtRKLSSSDAPAQDTgssaaA 868
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQK--QILRERLANLERQ-----L 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  869 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 948
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  949 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1028
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1029 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1096
Cdd:TIGR02168  465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
                          410       420
                   ....*....|....*....|..
gi 2462532900 1097 -LDALLGHALQeNVEDSTDEDA 1117
Cdd:TIGR02168  538 aIEAALGGRLQ-AVVVENLNAA 558
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
657-826 1.18e-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: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  657 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVRSEYEKKLQaMNKELQRLQ 736
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKAR-QRQELQQAR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  737 AAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 813
Cdd:pfam13868  242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
                          170
                   ....*....|...
gi 2462532900  814 AQKRNQEVVLRRK 826
Cdd:pfam13868  317 GERLREEEAERRE 329
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
695-855 1.23e-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: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  695 ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAaqkeHARLLKNQsqyekqLKKLQQDVMEMKKtKVRLM 774
Cdd:COG2433    385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA----EVEELEAE------LEEKDERIERLER-ELSEA 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  775 KQmkEEQEKARLTE--SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKL 852
Cdd:COG2433    454 RS--EERREIRKDReiSRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKF 519

                   ...
gi 2462532900  853 SSS 855
Cdd:COG2433    520 TKE 522
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
663-845 1.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  663 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQ 739
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  740 KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 816
Cdd:COG4372     94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
                          170       180
                   ....*....|....*....|....*....
gi 2462532900  817 RNQEvvLRRKTEEVTALRRQVRPMSDKVA 845
Cdd:COG4372    174 QALS--EAEAEQALDELLKEANRNAEKEE 200
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
688-1003 2.13e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  688 KIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMK 767
Cdd:COG4372      7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  768 K---TKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 844
Cdd:COG4372     87 EqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  845 AGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQ 924
Cdd:COG4372    167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  925 LLE------RRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDY 998
Cdd:COG4372    247 DKEelleevILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326

                   ....*
gi 2462532900  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 2.36e-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: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  683 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKVRsEYEKKLQAMnKELQRLQAAQKEhARLLKNQSQYEKQLKKLQQD 762
Cdd:pfam13904   38 LTYARKLEGLKLER-------QPLEAYENWLAAKQR-QRQKELQAQ-KEEREKEEQEAE-LRKRLAKEKYQEWLQRKARQ 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462532900  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 3.76e-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: 48.53  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  569 ERSVAGKEDNTDtDQEKKEEKGVSERENNELEVEESQEvsdhedeeeeeeeeeddidggessdesdsesdEKANYQADLA 648
Cdd:TIGR02169  307 ERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELER--------------------------------EIEEERKRRD 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  649 NITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLqnlgsvesyseEKAKKVRSEy 721
Cdd:TIGR02169  354 KLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQ-----------EELQRLSEE- 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  722 ekkLQAMNKELQRLQAAQKE-HARLLKNQSQYEKQLKKLQQDVMEMKktkvrlmkqmKEEQEKARLTEsrrnrEIAQLKK 800
Cdd:TIGR02169  422 ---LADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS----------KYEQELYDLKE-----EYDRVEK 483
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462532900  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 3.89e-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: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE------EKLMMLQHKIRdtQLERDQVLQnlgsvesysEEKAKKV 717
Cdd:pfam17380  326 QAEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqEEIAMEISRMR--ELERLQMER---------QQKNERV 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  718 RSEyekkLQAMNKelQRLQaaQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNREIA 796
Cdd:pfam17380  395 RQE----LEAARK--VKIL--EEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQVE 463
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462532900  797 QLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEE 829
Cdd:pfam17380  464 RLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILE 498
WD40 pfam00400
WD domain, G-beta repeat;
1594-1627 3.95e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 3.95e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462532900 1594 PVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIW 1627
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
653-838 4.38e-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: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  653 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE 722
Cdd:COG4913    669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  723 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 799
Cdd:COG4913    749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462532900  800 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 838
Cdd:COG4913    822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
656-828 4.84e-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: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  656 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKvrseyEKKLQAMNKELQRL 735
Cdd:pfam14988   23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQ-----EREIQDLEEEKEKV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  736 QAA-----QKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 805
Cdd:pfam14988   98 RAEtaekdREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
                          170       180
                   ....*....|....*....|...
gi 2462532900  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 5.03e-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: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  669 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVRSEYEKKlQAMNKELQRL 735
Cdd:pfam02841  155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  736 QAAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 814
Cdd:pfam02841  224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286

                   ....*..
gi 2462532900  815 QKRNQEV 821
Cdd:pfam02841  287 ESLQKEI 293
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
661-815 5.57e-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: 5.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  661 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAM--NKELQrlqAA 738
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYE---AL 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  739 QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 815
Cdd:COG1579     95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
661-899 6.29e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 6.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  661 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseEKAKKVRSEYEKKLQAMNKELQRLQAAQK 740
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------EALQAEIDKLQAEIAEAEAEIEERREELG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  741 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 805
Cdd:COG3883     90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  806 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIP 885
Cdd:COG3883    167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
                          250
                   ....*....|....
gi 2462532900  886 VARVQALPTPATNG 899
Cdd:COG3883    247 AGAGAAGAAGAAAG 260
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
658-789 6.35e-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: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  658 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 736
Cdd:COG3206    266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462532900  737 AAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 789
Cdd:COG3206    334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
644-1039 6.35e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  644 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 714
Cdd:COG4717     94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  715 KKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 794
Cdd:COG4717    174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  795 IA-----QLKKDQRKRDHQLRLLEAQ-------------KRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSD 856
Cdd:COG4717    254 IAaallaLLGLGGSLLSLILTIAGVLflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  857 APAQDTGSS----AAAVETDASRTGAQQKMRIPV--ARVQALPTPATNGNRKKYQRKGLTGRVFISKTARmkWQLLERRV 930
Cdd:COG4717    334 LSPEELLELldriEELQELLREAEELEEELQLEEleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--LEELEEQL 411
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  931 TDI------IMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENG--EGDKNVANINEEMESLTANIDYINDS 1002
Cdd:COG4717    412 EELlgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2462532900 1003 ISDCQANIMQMEEAKEEGETLDVTAVINA-----CTLTEARY 1039
Cdd:COG4717    492 WAALKLALELLEEAREEYREERLPPVLERaseyfSRLTDGRY 533
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
695-1024 6.50e-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: 6.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  695 ERDQVLQNLGSvesyseekAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQyekqlkKLQQDVMEMKKTKVRLM 774
Cdd:pfam12128  605 RLDKAEEALQS--------AREKQAAAEEQLVQANGELEKASREETFARTALKNARL------DLRRLFDEKQSEKDKKN 670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  775 KQMKEEQEKArltesrrNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrkTEEVTALRRQVRPMSDKVAgkvtrklss 854
Cdd:pfam12128  671 KALAERKDSA-------NERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLA--------- 732
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  855 sdapAQDTGSSAAAVETDASRTGAQQKMRIPVArvqALPTPATNGNRKKYQRKGLTGRvfISKTARMKWQLLERRVtdiI 934
Cdd:pfam12128  733 ----LLKAAIAARRSGAKAELKALETWYKRDLA---SLGVDPDVIAKLKREIRTLERK--IERIAVRRQEVLRYFD---W 800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  935 MQ----------KMTISNMEADMNRLlkqREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSIS 1004
Cdd:pfam12128  801 YQetwlqrrprlATQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
                          330       340
                   ....*....|....*....|
gi 2462532900 1005 DCQANimqmEEAKEEGETLD 1024
Cdd:pfam12128  878 DANSE----QAQGSIGERLA 893
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
663-993 6.55e-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: 6.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  663 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNK-------ELQRL 735
Cdd:pfam07888   77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQrvleretELERM 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  736 QAAQKEHARLLKNQSQYEKQLK-KLQQDVMEMKKtkvrlmkqMKEEQEKARLTESRRNREIAQLKKDQRKRdhQLRLLEA 814
Cdd:pfam07888  156 KERAKKAGAQRKEEEAERKQLQaKLQQTEEELRS--------LSKEFQELRNSLAQRDTQVLQLQDTITTL--TQKLTTA 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  815 QkrnqevvlrRKTEEVTALRRQVRPMSDkvagkvtrKLSSSDAPAQDTGSSAAAVETDASRTGAQqkmrIPVARVQAlpt 894
Cdd:pfam07888  226 H---------RKEAENEALLEELRSLQE--------RLNASERKVEGLGEELSSMAAQRDRTQAE----LHQARLQA--- 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  895 patngnrkkyqrKGLTGRVfisktARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSK---RREKI 971
Cdd:pfam07888  282 ------------AQLTLQL-----ADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermEREKL 344
                          330       340
                   ....*....|....*....|...
gi 2462532900  972 VKENG-EGDKNVANINEEMESLT 993
Cdd:pfam07888  345 EVELGrEKDCNRVQLSESRRELQ 367
PRK12704 PRK12704
phosphodiesterase; Provisional
686-829 7.78e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  686 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQY----E 753
Cdd:PRK12704    30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  754 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 829
Cdd:PRK12704   110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
PTZ00121 PTZ00121
MAEBL; Provisional
557-1021 8.97e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 8.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  557 KRLQKLEESNREERSVAGKEDNTDTDQ-EKKEEKGVSERENNELEVEESQEVSDheDEEEEEEEEEDDIDGGESSDESDS 635
Cdd:PTZ00121  1293 DEAKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADEAEAAEEKAEAAE 1370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  636 ESDEKANYQADLANITCEIAIK-QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 714
Cdd:PTZ00121  1371 KKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  715 KKvrSEYEKKLQAMNKelqrlQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 794
Cdd:PTZ00121  1451 KK--AEEAKKAEEAKK-----KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  795 IAQLKK-DQRKRDHQLRLLEAQKRNQEVVLR---RKTEEVTALRRQVRPMSDKvaGKVTRKLSSSDAPAQDTGSSAAAVE 870
Cdd:PTZ00121  1524 ADEAKKaEEAKKADEAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKLY 1601
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  871 TDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKmtisNMEADMnrl 950
Cdd:PTZ00121  1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK----KAEEDK--- 1674
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532900  951 lKQREELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSIsdcQANIMQMEEAKEEGE 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 9.47e-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: 9.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  446 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsp 525
Cdd:TIGR02168  735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------- 798
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  526 tilssdKETIEIIDLAKKDLEKLKRKEKRKKKrlqklEESNREERSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQ 605
Cdd:TIGR02168  799 ------KALREALDELRAELTLLNEEAANLRE-----RLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELE 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  606 EvsdhedeeeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMML 685
Cdd:TIGR02168  866 E------------------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  686 QHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
718-1071 1.11e-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: 46.97  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  718 RSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKktkvRLMKQMKEEQEKARLTESRRNREIAQ 797
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  798 LKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTG 877
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLNEEAANLRERLESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  878 AQQKMripvarvqalptpatngnrkkyqrkgltgrvfisktarmkwqlLERRVTDIIMQkmtISNMEADMNRLLKQREEL 957
Cdd:TIGR02168  831 RRIAA-------------------------------------------TERRLEDLEEQ---IEELSEDIESLAAEIEEL 864
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  958 TKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIM----QMEEAKEEGETLDVTAVINACT 1033
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreKLAQLELRLEGLEVRIDNLQER 944
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2462532900 1034 LTE-ARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1071
Cdd:TIGR02168  945 LSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
662-836 1.11e-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: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  662 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:COG3206    189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELES-QLAEARAELAEAEARLAALRAQLGSGPDALPE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  742 H------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRKR 805
Cdd:COG3206    259 LlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQLA 337
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462532900  806 DHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 836
Cdd:COG3206    338 QLEARLAELPELEAE--LRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
424-788 1.19e-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: 46.97  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  424 ENAMLQTENN--NLRVRIKAMQETVDALRSRITQLVSDQanhvlaragegnEEISNMIHSYIKEIEDLRAKLLESEAVNE 501
Cdd:TIGR02168  669 NSSILERRREieELEEKIEELEEKIAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLA 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  502 NLRKNLTRATARApyfsgsstfsptilssDKETIEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDT 581
Cdd:TIGR02168  737 RLEAEVEQLEERI----------------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  582 DQEKKEEKgvsERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSdesdsesdeKANYQADLANITCEIAIKQKLI 661
Cdd:TIGR02168  801 LREALDEL---RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ---------IEELSEDIESLAAEIEELEELI 868
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  662 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSE 947
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  742 HARL-----LKNQSQYEKQLKKLQQDVMEMKKTKVRL----MKQMKE-EQEKARLTE 788
Cdd:TIGR02168  948 EYSLtleeaEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEyEELKERYDF 1004
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
723-843 1.65e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  723 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 800
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462532900  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 1.66e-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: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  668 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVRSEYEKKLQAMNKELQRLQ-AAQKEHARL 745
Cdd:pfam15709  360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  746 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 825
Cdd:pfam15709  424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498

                   ....*..
gi 2462532900  826 KTEEVTA 832
Cdd:pfam15709  499 QKEEEAA 505
PRK12704 PRK12704
phosphodiesterase; Provisional
656-795 2.04e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  656 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRL 735
Cdd:PRK12704    77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  736 QAAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 795
Cdd:PRK12704   148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
657-838 2.33e-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: 45.29  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  657 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 736
Cdd:pfam13868  125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  737 AAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 809
Cdd:pfam13868  198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
                          170       180
                   ....*....|....*....|....*....
gi 2462532900  810 RLLEAQKRNQevvlrRKTEEVTALRRQVR 838
Cdd:pfam13868  277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
Rabaptin pfam03528
Rabaptin;
657-816 2.91e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 45.48  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  657 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSEEKAKKVRSEYEK 723
Cdd:pfam03528   24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSENTKQEAIDEVKS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  724 KLQamnKELQRLQAAQKE---------HARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQE 782
Cdd:pfam03528  101 QWQ---EEVASLQAIMKEtvreyevqfHRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAE 174
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462532900  783 KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 816
Cdd:pfam03528  175 KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
717-811 3.51e-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: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  717 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 792
Cdd:cd23703     67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138
                           90
                   ....*....|....*....
gi 2462532900  793 REIAQLKKDQRKRDHQLRL 811
Cdd:cd23703    139 REAKELAKKEARADALHEL 157
PRK11637 PRK11637
AmiB activator; Provisional
659-826 4.55e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.68  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  659 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAM 728
Cdd:PRK11637   103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  729 NKELQRLQAAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 803
Cdd:PRK11637   183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
                          170       180
                   ....*....|....*....|....*
gi 2462532900  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 4.81e-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: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  699 VLQNLGSVESYSEEKAKKVRSEyekKLQAMNKELQRLQAAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 774
Cdd:pfam15709  305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  775 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 836
Cdd:pfam15709  380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
662-795 5.21e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  662 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQ-RLQAAQK 740
Cdd:PRK00409   516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  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 6.36e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 6.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  646 DLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE-KAKKVRSEYEKK 724
Cdd:TIGR04523  483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKE 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  725 LQAMNKELQRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRK 804
Cdd:TIGR04523  563 IDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK 628
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462532900  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 6.44e-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: 6.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  663 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNKELQRLQAAQKEH 742
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  743 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 821
Cdd:TIGR00606  771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  822 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSDAPAQdtgssaaavetdasRTGAQQKMRIPVARVQALptpatngnr 901
Cdd:TIGR00606  846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR--------------RQQFEEQLVELSTEVQSL--------- 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  902 kkyqrkgltgrvfisktarmkwqllerrVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENgegDKN 981
Cdd:TIGR00606  901 ----------------------------IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI---KEK 949
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  982 VANINEEMESLTANI-----DYINDSISDCQANIMQMEEAKEEGETLD-----VTAVINACTLTEaRYLLDHFLSMGINK 1051
Cdd:TIGR00606  950 VKNIHGYMKDIENKIqdgkdDYLKQKETELNTVNAQLEECEKHQEKINedmrlMRQDIDTQKIQE-RWLQDNLTLRKREN 1028
                          410       420
                   ....*....|....*....|....*...
gi 2462532900 1052 GLQAAQKEaqIKVLEGRLKQTEITSATQ 1079
Cdd:TIGR00606 1029 ELKEVEEE--LKQHLKEMGQMQVLQMKQ 1054
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
658-838 6.88e-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: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  658 QKLIDELENSQKRLQTLKKQYEeklmMLQHkIRDTQLERDQVLQNLGSVESYSE----EKAKKVRSEYEKKLQAMNKELQ 733
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIE----LLEP-IRELAERYAAARERLAELEYLRAalrlWFAQRRLELLEAELEELRAELA 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  734 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLE 813
Cdd:COG4913    306 RLEAELERLEARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
                          170       180
                   ....*....|....*....|....*.
gi 2462532900  814 AQ-KRNQEVVLRRKtEEVTALRRQVR 838
Cdd:COG4913    380 EEfAALRAEAAALL-EALEEELEALE 404
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
652-820 8.41e-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: 43.51  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  652 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVRSEYEKKL 725
Cdd:pfam15742   54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  726 qamnkELQRlqaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 792
Cdd:pfam15742  132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462532900  793 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 820
Cdd:pfam15742  203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
710-817 8.43e-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: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  710 SEEKAK------KVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 783
Cdd:pfam11600   10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462532900  784 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 817
Cdd:pfam11600   83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
658-974 9.44e-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: 44.01  E-value: 9.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  658 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEEKaKKVRSEY---EKKL 725
Cdd:pfam01576  702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDE-RKQRAQAvaaKKKL 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  726 QAMNKELQ-RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD--- 801
Cdd:pfam01576  776 ELDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaa 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  802 ---QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSdapaqdtg 863
Cdd:pfam01576  852 serARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQ-------- 918
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  864 SSAAAVETDASRTGAQQkmripvarvqalptpaTNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDiiMQKMTISNM 943
Cdd:pfam01576  919 VEQLTTELAAERSTSQK----------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAAL 972
                          330       340       350
                   ....*....|....*....|....*....|....
gi 2462532900  944 EADMNRLLKQREELTKRRE---KLSKRREKIVKE 974
Cdd:pfam01576  973 EAKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
WD40 pfam00400
WD domain, G-beta repeat;
1458-1499 1.05e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 1.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462532900 1458 FQSTGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFD 1499
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
651-815 1.49e-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: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  651 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVRSEY--- 721
Cdd:pfam15619   17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  722 EKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 801
Cdd:pfam15619   87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
                          170
                   ....*....|....
gi 2462532900  802 QRKRDHQLRLLEAQ 815
Cdd:pfam15619  165 HKEAQEEVKILQEE 178
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
640-767 1.52e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsvESYSE- 711
Cdd:PRK00409   508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAE--KEAQQa 578
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  712 -EKAKKVRSEYEKKLQAMNKELQRLQAAQK---EHARLLKNQSQYEKQLKKLQQDVMEMK 767
Cdd:PRK00409   579 iKEAKKEADEIIKELRQLQKGGYASVKAHElieARKRLNKANEKKEKKKKKQKEKQEELK 638
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1557-1588 1.60e-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: 1.60e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462532900  1557 NAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1588
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
955-1047 1.61e-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: 1.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   955 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1034
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270
                            90
                    ....*....|...
gi 2462532900  1035 TEARYLLDHFLSM 1047
Cdd:smart00787  271 KEIEKLKEQLKLL 283
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
642-821 1.73e-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: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  642 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQleRDQVLQNLGSVESYSEEKAKKVRSEY 721
Cdd:pfam12128  351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI--REARDRQLAVAEDDLQALESELREQL 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  722 EKKLQAMNKELQRLQAAQKEhARLLKNQSQYEKQLKklqqdvmEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKK- 800
Cdd:pfam12128  429 EAGKLEFNEEEYRLKSRLGE-LKLRLNQATATPELL-------LQLENFDERIERAREEQEAANAEVERLQSELRQARKr 500
                          170       180
                   ....*....|....*....|....*
gi 2462532900  801 ----DQRKRDHQLRLLEAQKRNQEV 821
Cdd:pfam12128  501 rdqaSEALRQASRRLEERQSALDEL 525
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
670-838 1.74e-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: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  670 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 749
Cdd:COG4913    226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  750 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 827
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
                          170
                   ....*....|.
gi 2462532900  828 EEVTALRRQVR 838
Cdd:COG4913    380 EEFAALRAEAA 390
WD40 pfam00400
WD domain, G-beta repeat;
1552-1588 2.00e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462532900 1552 LQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1588
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
697-832 2.01e-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: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  697 DQVLQNLGSVESYSEEKA--KKVRSEYEKKLQAMNKELQR----LQAAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 770
Cdd:pfam13851   19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  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 2.23e-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: 41.79  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  658 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSEE--KAKKVRSEYEKKL 725
Cdd:cd16269    123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEAilQADQALTEKEKEI 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  726 QAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDVMEMKKTKVRLMKQMKEE-QEKARLTESRRNREIAQLKKDQRK 804
Cdd:cd16269    201 EAERAKAEAAEQERKL----------LEEQQRELEQKLEDQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEA 270
                          170
                   ....*....|....*..
gi 2462532900  805 RDHQLRLLEAQKRNQEV 821
Cdd:cd16269    271 LLEEGFKEQAELLQEEI 287
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
640-831 2.26e-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: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ---LERDQVLQNLGSVE---SYSEEK 713
Cdd:pfam07888  173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlNASERK 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  714 AKKVRSE---------------YEKKLQAMNKELQ---------------------RLQAAQKEHARLLKNQSQYEKQLK 757
Cdd:pfam07888  253 VEGLGEElssmaaqrdrtqaelHQARLQAAQLTLQladaslalregrarwaqeretLQQSAEADKDRIEKLSAELQRLEE 332
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462532900  758 KLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKrnQEV-----VLRRKTEEVT 831
Cdd:pfam07888  333 RLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK--QELleyirQLEQRLETVA 405
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
697-804 2.68e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  697 DQVLQNLGSVESYSEEKAKKV---RSEYEKKLQAMNKELQRLQaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL 773
Cdd:PRK00409   519 NELIASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQ--EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462532900  774 MKQMKEEQEKARLTESRRNREIAQLKKDQRK 804
Cdd:PRK00409   597 QKGGYASVKAHELIEARKRLNKANEKKEKKK 627
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
711-785 2.69e-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: 2.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  711 EEKAKKVRSEYEKKLQAMNKELQRLQAA-QKEhaRLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKAR 785
Cdd:COG2825     45 QKKLEKEFKKRQAELQKLEKELQALQEKlQKE--AATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELL 118
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
671-837 2.69e-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: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  671 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEK-----AKKVRSEYEK-KLQAMNK-ELQRLQAAQKEha 743
Cdd:pfam15665   16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKrriqtLEESLEQHERmKRQALTEfEQYKRRVEERE-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  744 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 809
Cdd:pfam15665   88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
                          170       180
                   ....*....|....*....|....*....
gi 2462532900  810 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 837
Cdd:pfam15665  165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
656-897 2.69e-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: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  656 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDTQ------LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQA 727
Cdd:pfam04747   12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSINDQRkeafasLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQK 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  728 MNKELQRLQAAQKEHARLLKNQSQYEKQlkklqqdvmemkktkvrlmKQMKEEQEKarltesrrnreiaqLKKDQRKRDH 807
Cdd:pfam04747   92 VNAKKAAEKEARRAEAEAKKRAAQEEEH-------------------KQWKAEQER--------------IQKEQEKKEA 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  808 QLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSDAPAQDTGSSAAA--VETDASRTGAQQKM 882
Cdd:pfam04747  139 DLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAepAEQVQEITGKKNKK 218
                          250
                   ....*....|....*
gi 2462532900  883 RIPVARVQALPTPAT 897
Cdd:pfam04747  219 NKKKSESEATAAPAS 233
FliJ pfam02050
Flagellar FliJ protein;
662-797 2.78e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 39.57  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  662 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSvesyseekakkvrSEYEKKLQAMNKELQRLQAAQKE 741
Cdd:pfam02050    1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISA-------------AELRNYQAFISQLDEAIAQQQQE 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  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 3.14e-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: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  776 QMKEEQEKAR--LTESRRNREIA---------QLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 844
Cdd:TIGR02169  167 EFDRKKEKALeeLEEVEENIERLdliidekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  845 AGKvTRKLSSSDAPAQDTGSSAAAVEtdasrtgaqQKMRIPVARVQALptpaTNGNRKKYQRKGLTGRVFISKTAR---- 920
Cdd:TIGR02169  247 ASL-EEELEKLTEEISELEKRLEEIE---------QLLEELNKKIKDL----GEEEQLRVKEKIGELEAEIASLERsiae 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  921 ----MKwQLLERR---VTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLT 993
Cdd:TIGR02169  313 kereLE-DAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  994 ANIDYINDSISDCQANIMQMEEAKEE--GETLDVTAVINActltearylldhfLSMGINKgLQAAQKEAQ--IKVLEGRL 1069
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAG-------------IEAKINE-LEEEKEDKAleIKKQEWKL 457
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2462532900 1070 KQTEITSATQNQLLFHMLKEKAELNPELDAL 1100
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
722-1117 3.23e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  722 EKKLQAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDV----------MEMKKTKVRLMKQmkeEQEKARLTESRR 791
Cdd:COG1196    178 ERKLEATEENLERLEDILGE----------LERQLEPLERQAekaeryrelkEELKELEAELLLL---KLRELEAELEEL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  792 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRpmsdkVAGKVTRKLSSSDAPAQDTGSSAAAVET 871
Cdd:COG1196    245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  872 DASRTGAQQKMRIpVARVQALPTPATNGNRKKYQRKGLTgrvfisKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLL 951
Cdd:COG1196    320 ELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  952 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINA 1031
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1032 CTLTEARYLLDHFLSMGINKG--LQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQENV 1109
Cdd:COG1196    473 ALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552

                   ....*...
gi 2462532900 1110 EDsTDEDA 1117
Cdd:COG1196    553 VE-DDEVA 559
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1458-1499 3.26e-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: 3.26e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 2462532900  1458 FQSTGKLTGHLGPVMCLtvdQISSGQDLIITGSKDHYIKMFD 1499
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 3.65e-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: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  658 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR-DTQL----------------ERDQVLQNLGSVESYSEEKAKKVRSE 720
Cdd:pfam01576   18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQaETELcaeaeemrarlaarkqELEEILHELESRLEEEEERSQQLQNE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  721 yEKKLQAMNKELQRlQAAQKEHARllkNQSQYEK-----QLKKLQQDVMEMKKTKVRLMK--------------QMKEEQ 781
Cdd:pfam01576   98 -KKKMQQHIQDLEE-QLDEEEAAR---QKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKerklleeriseftsNLAEEE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  782 EKARLTESRRNREIAQLKkdqrkrDHQLRLLEAQKRNQEVV-LRRKTE-EVTALRRQVRPMSDKVAgKVTRKLSSSDAPA 859
Cdd:pfam01576  173 EKAKSLSKLKNKHEAMIS------DLEERLKKEEKGRQELEkAKRKLEgESTDLQEQIAELQAQIA-ELRAQLAKKEEEL 245
                          250       260
                   ....*....|....*....|....
gi 2462532900  860 QDTgsSAAAVETDASRTGAQQKMR 883
Cdd:pfam01576  246 QAA--LARLEEETAQKNNALKKIR 267
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
666-799 3.99e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 39.50  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  666 NSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYseekakkvRSEYEKKLQAMNKE-------------L 732
Cdd:COG2882      2 KRSFRLQTLLDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQY--------REEYEQRLQQKLQQglsaaqlrnyqqfI 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532900  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 2462532900  563 EESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIdggessdeSDSESDEKAN 642
Cdd:pfam02029  105 ENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEA--------EEVPTENFAK 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  643 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQvlqnlgsveSYSEEKAKKVRSEYE 722
Cdd:pfam02029  177 EEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ---------SQEREEEAEVFLEAE 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  723 KKLqamnkELQRLQAAQKEharllknqsqyEKQLKKLQQdvmemkktkvrlmKQMKEEQE----KARLTESRRNREIAQL 798
Cdd:pfam02029  248 QKL-----EELRRRRQEKE-----------SEEFEKLRQ-------------KQQEAELEleelKKKREERRKLLEEEEQ 298
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462532900  799 KKDQRKRDHQLRLLEAQKRNQEVVLRRKTEevTALRRQ 836
Cdd:pfam02029  299 RRKQEEAERKLREEEEKRRMKEEIERRRAE--AAEKRQ 334
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
304-513 4.33e-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: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206     96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206    174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  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 4.48e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  560 QKLEESNREERSVAGKEDNTDTDQEKKEEKgvSERENNELEVEESQEVSDHEDEEeeeeeeeddidggessdesdsesde 639
Cdd:pfam17380  316 RKLEEAEKARQAEMDRQAAIYAEQERMAME--RERELERIRQEERKRELERIRQE------------------------- 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 kanyqadlanitcEIAIKQKLIDELEnsqkRLQTLKKQYEEKL---MMLQHKIRDTQLERDQVLQNlgsvesySEEKAKK 716
Cdd:pfam17380  369 -------------EIAMEISRMRELE----RLQMERQQKNERVrqeLEAARKVKILEEERQRKIQQ-------QKVEMEQ 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  717 VRSEYEkklQAMNKELQRLQAAQ-KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLmkqMKEEQEKARLTESRR---N 792
Cdd:pfam17380  425 IRAEQE---EARQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---EKEKRDRKRAEEQRRkilE 498
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532900  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 5.01e-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: 5.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  708 SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHArllknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLT 787
Cdd:pfam14988    7 EYLAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  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 5.35e-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: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  640 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMM---------LQHKIRDTQLER----DQVLQNLGSV 706
Cdd:COG1579     40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRIsdleDEILELMERI 119
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  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 5.68e-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: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  685 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVRSEYEKKLQA-------MNKELQR----LQ 736
Cdd:pfam14073    9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462532900  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 5.95e-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: 5.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  703 LGSVESYS-EEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKK-------LQQD-------VMEMK 767
Cdd:pfam06632  112 LGSVKLQKvPEPAEVIRELISYCLDCIAELQAKNEHLQKENERLQRDWNDVTGRLEKcvkakeeLEADlykrfilVLNEK 191
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462532900  768 KTKVRLMKQMKEEQEKARLTESRRNREIAqlkKDQRKRDHQ 808
Cdd:pfam06632  192 KAKIRSLQKLLNELQESEESTEQKREDPA---TSDRTPDEE 229
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
713-1118 6.19e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  713 KAKKVRSEYEKKLQAMNKELQRLQAAQK----------EHARLLKNQSQYEKQLKKLQQDVMEMKktkVRLmkqmkEEQE 782
Cdd:COG3096    296 GARRQLAEEQYRLVEMARELEELSARESdleqdyqaasDHLNLVQTALRQQEKIERYQEDLEELT---ERL-----EEQE 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  783 KAR--LTESR-RNREIAQLKKDQRKR------DHQLRLLEAQKRN---QEVVLR-RKTEEVTALRrqvrpmsdkvagkvt 849
Cdd:COG3096    368 EVVeeAAEQLaEAEARLEAAEEEVDSlksqlaDYQQALDVQQTRAiqyQQAVQAlEKARALCGLP--------------- 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  850 rKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVArvqalptpATNGNRKKYQR-KGLTGRVFIS---KTARmkwQL 925
Cdd:COG3096    433 -DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA--------ARRQFEKAYELvCKIAGEVERSqawQTAR---EL 500
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  926 LER---------RVTDIIMQKmtisnmeADMNRLLKQREELTKRREKLSKRREKIVKENGEgdknvanINEEMESLTANI 996
Cdd:COG3096    501 LRRyrsqqalaqRLQQLRAQL-------AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-------LEELLAELEAQL 566
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  997 DYINDSISDCQANIMQM----EEAKEEGETLDVTAVI--------------NACTLTEARYLLDHflsMGinkglQAAQK 1058
Cdd:COG3096    567 EELEEQAAEAVEQRSELrqqlEQLRARIKELAARAPAwlaaqdalerlreqSGEALADSQEVTAA---MQ-----QLLER 638
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532900 1059 EAQIKVLEGRLKQTEITSATQ-NQLLFHMLKEKAELNPELDALLGHALQENVEDSTDEDAP 1118
Cdd:COG3096    639 EREATVERDELAARKQALESQiERLSQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAP 699
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
658-778 6.59e-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: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  658 QKLIDELENSQKRLQTLKKQYEEklmmlqhkIRDTQ---LER-DQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNK 730
Cdd:pfam10168  578 QSLEEERKSLSERAEKLAEKYEE--------IKDKQeklMRRcKKVLQRLNSQLpvlSDAEREMKKELETINEQLKHLAN 649
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  731 ELQRLQAAQKEHAR-LLKNQSQY--------EKQLKKLQQDVMEMKKTKVRLMKQMK 778
Cdd:pfam10168  650 AIKQAKKKMNYQRYqIAKSQSIRkksslslsEKQRKTIKEILKQLGSEIDELIKQVK 706
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
670-799 6.60e-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: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  670 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE-KKLQAMNKELQRLQAAQKEHARLL- 746
Cdd:TIGR02473    6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462532900  747 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 799
Cdd:TIGR02473   86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
PRK11637 PRK11637
AmiB activator; Provisional
657-803 7.33e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.83  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  657 KQKLIDELENSQKRLQTLKKQYEEKlmmlqhkirdtQLERDQVLqnlgsvesySEEKAKKvrseyekklqamnkelQRLQ 736
Cdd:PRK11637   168 RQETIAELKQTREELAAQKAELEEK-----------QSQQKTLL---------YEQQAQQ----------------QKLE 211
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  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 8.72e-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: 8.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  661 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDtqlERDQVLQNLGSVESYSEEKakkvrseyEKKLQAMNKELQRLQAAQK 740
Cdd:pfam03938   14 SPEGKAAQAQLEKKFKKRQAELEAKQKELQK---LYEELQKDGALLEEEREEK--------EQELQKKEQELQQLQQKAQ 82
                           90       100
                   ....*....|....*....|....*
gi 2462532900  741 EharllKNQSQYEKQLKKLQQDVME 765
Cdd:pfam03938   83 Q-----ELQKKQQELLQPIQDKINK 102
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
712-838 9.23e-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: 9.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  712 EKAKKVRSEYEKKLQAMNKELQRLqAAQKEHARllKNQSQYEKQL-KKLQQDVMEMKKTKVRLmKQMKEEQEKARLTESR 790
Cdd:cd07652     75 EKLADNGLRFAKALNEMSDELSSL-AKTVEKSR--KSIKETGKRAeKKVQDAEAAAEKAKARY-DSLADDLERVKTGDPG 150
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532900  791 R--------NREIAQLKKD-QRK-----RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 838
Cdd:cd07652    151 KklkfglkgNKSAAQHEDElLRKvqaadQDYASKVNAAQALRQELLSRHRPEAVKDLFDLIL 212
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
728-845 9.24e-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: 9.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  728 MNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKarltesrRNREIAQLKKDqrkrdh 807
Cdd:pfam03938    7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREE-------KEQELQKKEQE------ 73
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462532900  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 9.24e-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: 9.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  655 AIKQKLIDELENSQKRlQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL-----GSVESYSE--EKAKKVRSEYEKKLQA 727
Cdd:pfam01576  303 ALKTELEDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMrqkhtQALEELTEqlEQAKRNKANLEKAKQA 381
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532900  728 MNKELQRLQAaqkeharllknqsqyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNRE 794
Cdd:pfam01576  382 LESENAELQA-----------------ELRTLQQAKQDSEHKRKKLEGQLQELQ--ARLSESERQRA 429
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
666-792 9.47e-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: 9.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900   666 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 745
Cdd:smart00435  266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2462532900   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 ...
450-1121 9.59e-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: 9.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  450 RSRITQLVSDQANHVLARAGEGNEEISNMIHSYIKEIEDLRA---KLLESEAVNENLRKNLTRATArapyfSGSSTFSPT 526
Cdd:pfam02463  182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEeylLYLDYLKLNEERIDLLQELLR-----DEQEEIESS 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  527 ILSSDKETiEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQE 606
Cdd:pfam02463  257 KQEIEKEE-EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  607 VSDHE---------DEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQK-LIDELENSQKRLQTLKK 676
Cdd:pfam02463  336 EIEELekelkeleiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELeLKSEEEKEAQLLLELAR 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  677 QYEEKLMMLQHK---IRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYE 753
Cdd:pfam02463  416 QLEDLLKEEKKEeleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  754 KQLKKLQQDVMEMKKTKVRLMKQMK-------------------------------EEQEKARLTESRRNREIA--QLKK 800
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVggriisahgrlgdlgvavenykvaistavivEVSATADEVEERQKLVRAltELPL 575
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  801 DQRKRDHQLRLLEAQKR---------------NQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSS 865
Cdd:pfam02463  576 GARKLRLLIPKLKLPLKsiavleidpilnlaqLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLE 655
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  866 AA-AVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKMTISNME 944
Cdd:pfam02463  656 EGlAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900  945 ADMNRLL-KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSIS-----DCQANIMQMEEAKE 1018
Cdd:pfam02463  736 EELKLLKqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkaqeeELRALEEELKEEAE 815
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532900 1019 EGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQK------EAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAE 1092
Cdd:pfam02463  816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEElerleeEITKEELLQELLLKEEELEEQKLKDELESKEEKE 895
                          730       740
                   ....*....|....*....|....*....
gi 2462532900 1093 LNPELDALLGHALQENVEDSTDEDAPLNS 1121
Cdd:pfam02463  896 KEEKKELEEESQKLNLLEEKENEIEERIK 924
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH